|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
6-649 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1328.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 6 KHAIPSAIAERALINPAQYQQYYQQSVQDPEAFWGEHGKILDWIKPYTKVkntsFDPGHVSIRWFEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPFDTV----LDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 86 LAERGDQTAIIWEGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 166 FSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALKNPGVVSVANVvvFQRTGKPGYWQEGRDLWWHELTQGVS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIV--VRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 246 ADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 326 TTLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNA 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 406 KCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 486 QTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 566 NHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTsNLGDTSTLADPAVVDKLLEEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
gi 727190822 646 QSMK 649
Cdd:PRK00174 634 QNRK 637
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
31-644 |
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: 1158.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGK-ILDWIKPYTKVKNTSFDPghvSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTQSKKVT 109
Cdd:TIGR02188 14 SIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEGDEPGEVRKIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 110 YKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEG 189
Cdd:TIGR02188 91 YRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 190 LRAGRAVPLKKNVDDALKNPGVVSVANVVvFQRTGKP-GYWQEGRDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGST 268
Cdd:TIGR02188 171 LRGGKVIPLKAIVDEALEKCPVSVEHVLV-VRRTGNPvVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGST 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 269 GKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDK 348
Cdd:TIGR02188 250 GKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 349 HQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKCPIVDTWWQTETGGFMITPLPG 428
Cdd:TIGR02188 330 HKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 429 ATELKAGSATRPFFGVQPALVDNVGTPQEGACEGN-LVIVDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDED 507
Cdd:TIGR02188 410 ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKD 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEI 587
Cdd:TIGR02188 490 GYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEI 569
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 588 GPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPAVVDKLLEE 644
Cdd:TIGR02188 570 GPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-634 |
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: 1147.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGKILDWIKPYTKVKNTSFDPGHvsIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTQSKKVTY 110
Cdd:cd05966 10 SIEDPEEFWGEIAKELDWFKPWDKVLDWSKGPPF--IKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPDQSRTITY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 111 KQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGL 190
Cdd:cd05966 88 RELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 191 RAGRAVPLKKNVDDALKNpgVVSVANVVVFQRTGKPGYWQEGRDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGK 270
Cdd:cd05966 168 RGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 271 PKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDKHQ 350
Cdd:cd05966 246 PKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 351 VNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKCPIVDTWWQTETGGFMITPLPGAT 430
Cdd:cd05966 326 VTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGAT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 431 ELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYY 510
Cdd:cd05966 406 PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYY 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 511 WITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPI 590
Cdd:cd05966 486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPI 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 727190822 591 ATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdTSNLGDTSTLAD 634
Cdd:cd05966 566 ATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-611 |
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: 959.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGKILDWIKPYTKVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTQSKKVTY 110
Cdd:cd17634 8 SINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTSQSRTISY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 111 KQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGL 190
Cdd:cd17634 88 RELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 191 RAGRAVPLKKNVDDALkNPGVVSVANVVVFQRTGKPGYWQEGRDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGK 270
Cdd:cd17634 168 RAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 271 PKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDKHQ 350
Cdd:cd17634 247 PKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 351 VNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKCPIVDTWWQTETGGFMITPLPGAT 430
Cdd:cd17634 327 VNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 431 ELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYY 510
Cdd:cd17634 407 ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 511 WITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPI 590
Cdd:cd17634 487 WITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPL 566
|
570 580
....*....|....*....|.
gi 727190822 591 ATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 567 ATPDVVHWVDSLPKTRSGKIM 587
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
68-643 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 921.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 68 RWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGEDGE-ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 148 AMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALKnpGVVSVANVVVFQRTGKPG 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE--ELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 228 YWQEgrDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 GWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 388 EPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPLPGaTELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIV 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 DSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 548 VGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 727190822 628 DTSTLADPAVVDKLLE 643
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
10-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 828.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 10 PSA-IAERALI-NPAQYQQYYQQSVQDPEAFWGEHGKILDWIKPYTKVK----NTSFDPGHVSIRWFEDGTLNLAANCLD 83
Cdd:PLN02654 16 PSKdFSAQALVsSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEvcseNLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHL-AERGDQTAIIWEGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PLN02654 96 RNVeAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 FGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALKNPGVVSVAN--------VVVFQRTGKPgyWQEGRD 234
Cdd:PLN02654 176 FAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVgicltyenQLAMKREDTK--WQEGRD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 235 LWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHS 314
Cdd:PLN02654 254 VWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 YLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEA 394
Cdd:PLN02654 334 YVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 395 WEWYYNKIGNAKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQA 474
Cdd:PLN02654 414 WRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAF 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 475 RTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNI 554
Cdd:PLN02654 494 RTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 555 KGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLAD 634
Cdd:PLN02654 574 KGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLAD 653
|
....*....
gi 727190822 635 PAVVDKLLE 643
Cdd:PLN02654 654 PGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-641 |
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: 642.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGKILDWIKPYTKVKNTSFDPGHvsiRWFEDGTLNLAANCLDRH-LAERGDQTAIIWEGDDPTQSKKVT 109
Cdd:cd05967 8 SIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFT---RWFVGGRLNTCYNALDRHvEAGRGDQIALIYDSPVTGTERTYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 110 YKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEG 189
Cdd:cd05967 85 YAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 190 LRAGRAVPLKKNVDDALKNPGvVSVANVVVFQRTGKP-GYWQEGRDLWWHELTQGV-SADCPPeeVNAEDPLFILYTSGS 267
Cdd:cd05967 165 IEPGKVVPYKPLLDKALELSG-HKPHHVLVLNRPQVPaDLTKPGRDLDWSELLAKAePVDCVP--VAATDPLYILYTSGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVP-NYPGVNRLSQVI 346
Cdd:cd05967 242 TGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPGAFWRVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 347 DKHQVNILYTAPTAIRALMAEGDKAIEGTRRD--SLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMIT 424
Cdd:cd05967 322 EKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDlsSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTETGWPITA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 425 PLPGATEL--KAGSATRPFFGVQPALVDNVGTPQEGACEGNLVI-VDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDG 501
Cdd:cd05967 399 NPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIkLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPE-LYAEVR 580
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEeLEKELV 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADPAVVDKL 641
Cdd:cd05967 559 ALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-641 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 594.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGKILDWIKPYTKVKNTSFDPghvSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTQSKKVTY 110
Cdd:PRK10524 11 SIDDPEAFWAEQARRIDWQTPFTQVLDYSNPP---FARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDEERTYTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 111 KQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGL 190
Cdd:PRK10524 88 RQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 191 RAGRAVPLKKNVDDALKNpGVVSVANVVVFQRTGKPGYWQEGRDLWWHELTQGV-SADCPPEEVNAEDPLFILYTSGSTG 269
Cdd:PRK10524 168 RGGKVVPYKPLLDEAIAL-AQHKPRHVLLVDRGLAPMARVAGRDVDYATLRAQHlGARVPVEWLESNEPSYILYTSGTTG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 270 KPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVIDKH 349
Cdd:PRK10524 247 KPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 350 QVNILYTAPTAIRALMAEGDKAIegTRRD--SLRIMGSVGEPINPEAWEWYYNKIGNakcPIVDTWWQTETGGFMITPLP 427
Cdd:PRK10524 327 KVNRMFSAPTAIRVLKKQDPALL--RKHDlsSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 428 G--ATELKAGSATRPFFGVQPALVDNV-GTPQEGACEGNLVIVDSW-PGQARTLFGDHDRFEQTYFSTFKGM-YFSGDGA 502
Cdd:PRK10524 402 GveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFGRQvYSTFDWG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHG-----EEPTPELYA 577
Cdd:PRK10524 482 IRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsladREARLALEK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 578 EVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAG-DTsnlGDTSTLADPAVVDKL 641
Cdd:PRK10524 562 EIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
31-635 |
0e+00 |
|
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: 527.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEHGKILD--WIKPYTKVKNTSfdPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPTqSKKV 108
Cdd:cd05968 16 SAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEGEDGT-SRTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADE 188
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 GLRAGRAVPLKKNVDDALKN-PGVVSVANVvvfQRTGKPGYWQEGRDLWWHELTQGvsADCPPEEVNAEDPLFILYTSGS 267
Cdd:cd05968 173 FTRRGREVNLKEEADKACAQcPTVEKVVVV---RHLGNDFTPAKGRDLSYDEEKET--AGDGAERTESEDPLMIIYTSGT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGD-IYWCTaDVGWVTGhSYLLYGPLACGATTLMFEGVPNYPGVNRLSQVI 346
Cdd:cd05968 248 TGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 347 DKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKCPIVDTWWQTETGGFMITPL 426
Cdd:cd05968 326 EDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 427 PgATELKAGSATRPFFGVQPALVDNVGTPQEGAcEGNLVIVDSWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDE 506
Cdd:cd05968 406 L-IKPIKPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKE 586
Cdd:cd05968 484 EGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADP 635
Cdd:cd05968 564 LGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
32-628 |
2.71e-174 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 508.28 E-value: 2.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 32 VQDPEAFWGEHgkildWIKPYTKVKNT-SFDPGHVSIRWFEDGTLNLAANCLDRHLA-ERGDQTAIIWEGDDPTQskKVT 109
Cdd:PRK04319 3 VETLPVIKGEP-----NLKDYEETYATfSWEEVEKEFSWLETGKVNIAYEAIDRHADgGRKDKVALRYLDASRKE--KYT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 110 YKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEG 189
Cdd:PRK04319 76 YKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 190 LR---AGRAVPLKKN--VDDALKNPgvvsvanvvvfqrtgkPGYWQegrdlwWHELTQGVSADCPPEEVNAEDPLFILYT 264
Cdd:PRK04319 156 LErkpADDLPSLKHVllVGEDVEEG----------------PGTLD------FNALMEQASDEFDIEWTDREDGAILHYT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGVLHttggylVYAAM-----TFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGvpnypgv 339
Cdd:PRK04319 214 SGSTGKPKGVLH------VHNAMlqhyqTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 340 nRLS-----QVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNakcPIVDTWW 414
Cdd:PRK04319 281 -RFSperwyRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWW 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 415 QTETGGFMITPLPgATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFEQtYFStfKG 494
Cdd:PRK04319 357 MTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPE 574
Cdd:PRK04319 433 WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 575 LYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK----IAAGDTSNLGD 628
Cdd:PRK04319 513 LKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
109-619 |
4.87e-145 |
|
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: 428.84 E-value: 4.87e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 GLragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppEEVNAEDPLFILYTSGST 268
Cdd:cd05969 82 LY------------------------------------------------------------ERTDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 269 GKPKGVLHTTGGYLVYAaMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNypgVNRLSQVIDK 348
Cdd:cd05969 102 GTPKGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 349 HQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPLPG 428
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 429 aTELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFEQtYFSTfkGMYFSGDGARRDEDG 508
Cdd:cd05969 255 -MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIG 588
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLG 410
|
490 500 510
....*....|....*....|....*....|.
gi 727190822 589 PIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
108-617 |
2.43e-118 |
|
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: 359.73 E-value: 2.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITad 187
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 eglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevNAEDPLFILYTSGS 267
Cdd:cd05972 79 ------------------------------------------------------------------DAEDPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGgYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPgvNRLSQVID 347
Cdd:cd05972 93 TGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDA--ERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 348 KHQVNILYTAPTAIRALMAEGdkaIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGgFMITPLP 427
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 428 GaTELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDHDRFEqtyfSTFKG-MYFSGDGARRDE 506
Cdd:cd05972 243 D-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTE----ASIRGdYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKE 586
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKV 397
|
490 500 510
....*....|....*....|....*....|.
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 398 LAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
5.09e-107 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 330.04 E-value: 5.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAiiWEGDDPTqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGEGR---RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEglragravPLKKNVDDALKNPGVVSVANVVVFQRtgkpgyWQEGRDLWWHELT 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEVVKLVLVLDRDP------VLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 QGVsADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAAMTFKYV----FDYHDGDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 142 ADV-PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 318 YGPLACGATTLMFEGVPNYPgVNRLSQVIDKHQVNILYTAPTAIRALMAEGdkAIEGTRRDSLRIMGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 398 YYNKIGnakCPIVDTWWQTETGGFMITPLPGATEL-KAGSATRPFFGVQPALVD-NVGTPQEGACEGNLVIvdSWPGQAR 475
Cdd:pfam00501 297 FRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 727190822 476 TLFGDHDRFEQTYFStfKGMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:pfam00501 372 GYLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-623 |
6.40e-99 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 310.20 E-value: 6.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITAdeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwhelt 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgvsadcppeevnaedplFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 322 ACGATTLMfegvpnYPGVN--RLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINPEAWEWYY 399
Cdd:COG0318 165 LAGATLVL------LPRFDpeRVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 400 NKIGnakCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARTLFG 479
Cdd:COG0318 237 ERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 480 DHDRFEQTyfstFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQA 558
Cdd:COG0318 312 DPEATAEA----FRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGER 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 559 IYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:COG0318 388 VVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-611 |
3.74e-94 |
|
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: 293.81 E-value: 3.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYvFDYHDGDIYWCTADVGWVtGHSYLLYGPLACGATTLMFEGVPny 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 337 PGvnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQT 416
Cdd:cd04433 77 PE--AALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 417 ETGGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQartlfGDHDRFEQTYFSTFKGMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK-----GYWNNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPEly 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 727190822 577 aEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
109-617 |
2.73e-88 |
|
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: 282.10 E-value: 2.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITade 188
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 glragravplkkNVDdalknpgvvsvanvvvfQRtgkpgywqegrdlwwHELTqgvsadcppeevnaEDPLFILYTSGST 268
Cdd:cd05973 79 ------------DAA-----------------NR---------------HKLD--------------SDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 269 GKPKGVLHTTGGYLVYAAMtFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGVNRlsqVIDK 348
Cdd:cd05973 101 GLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWR---VIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 349 HQVNILYTAPTAIRALMAEGdKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPLPG 428
Cdd:cd05973 177 LGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHAL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 429 ATELKAGSATRPFFGVQPALVDNVG-TPQEGAcEGNLVI-VDSWPgqaRTLFGDHDRFEQTYFStfKGMYFSGDGARRDE 506
Cdd:cd05973 253 EHPVHAGSAGRAMPGWRVAVLDDDGdELGPGE-PGRLAIdIANSP---LMWFRGYQLPDTPAID--GGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKE 586
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
31-639 |
2.72e-82 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 271.84 E-value: 2.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEhgkILDWI-----KPYTKV---KNTSFDPghvsiRWFEDGTLNLAANCLdRHlAERGDQTAIIWEGDDP 102
Cdd:cd05943 26 SVDDPGAFWAA---VWDFSgvrgsKPYDVVvvsGRIMPGA-----RWFPGARLNYAENLL-RH-ADADDPAAIYAAEDGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 103 TQskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKL 182
Cdd:cd05943 96 RT--EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 183 VITADEGLRAGRAVPLKKNVDDALKN-PGVVSVANVVVFQRTGKPGYWQEGRDLWWHE-LTQGVSADCPPEEVNAEDPLF 260
Cdd:cd05943 174 LFAVDAYTYNGKRHDVREKVAELVKGlPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDfLATGAAGELEFEPLPFDHPLY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 261 ILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSylLYGPLACGATTLMFEGVPNYPGVN 340
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLAVGATIVLYDGSPFYPDTN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 341 RLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNakcpivDTWWQTETGG 420
Cdd:cd05943 332 ALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 421 ------FMIT-PL----PGatELKAgsatrPFFGVQPALVDNVGTPQEGAcEGNLVIVDSWPGQARTLFGDHD--RFEQT 487
Cdd:cd05943 406 tdiiscFVGGnPLlpvyRG--EIQC-----RGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPSMPVGFWNDPDgsRYRAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 488 YFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNH 567
Cdd:cd05943 478 YFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727190822 568 GEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdtSNLGDTSTLADPAVVD 639
Cdd:cd05943 558 GVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPESLD 627
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
31-639 |
2.37e-79 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 264.73 E-value: 2.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWGEhgkILDWI-----KPYTKVKNTSFDPGhvsIRWFEDGTLNLAANCLdRHlaERGDQTAIIWEGDDpTQS 105
Cdd:PRK03584 43 SVEDLEAFWQS---VWDFFgvigsTPYTVVLAGRRMPG---ARWFPGARLNYAENLL-RH--RRDDRPAIIFRGED-GPR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 ADeGLR-AGRAVPLKKNVD---DALKNPGVVSVANVVVFQRTGKPGywqeGRDLWWHELTQGVSADCP-PEEVNAEDPLF 260
Cdd:PRK03584 193 VD-GYRyGGKAFDRRAKVAelrAALPSLEHVVVVPYLGPAAAAAAL----PGALLWEDFLAPAEAAELeFEPVPFDHPLW 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 261 ILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGD-IYWCTAdVGW------VTGhsyllygpLACGATTLMFEGV 333
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGATLVLYDGS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 PNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNakcpivDTW 413
Cdd:PRK03584 339 PFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVW 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 414 WQTETGG------FMI-TPL----PGatELKAgsatrPFFGVQPALVDNVGTPQEGAcEGNLVIVDSWPGQARTLFGDHD 482
Cdd:PRK03584 413 LASISGGtdicscFVGgNPLlpvyRG--EIQC-----RGLGMAVEAWDEDGRPVVGE-VGELVCTKPFPSMPLGFWNDPD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 483 --RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:PRK03584 485 gsRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMP 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 561 AYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIM----RRILRKIAAGDTSNLGdtsTLADPA 636
Cdd:PRK03584 565 LFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAVNRD---ALANPE 641
|
...
gi 727190822 637 VVD 639
Cdd:PRK03584 642 ALD 644
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-616 |
4.86e-77 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 252.74 E-value: 4.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 105 SKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 TaDEglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGVLHTTG---GYLVYAAMTFKyvFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPGvnR 341
Cdd:cd05971 97 SGTTGPPKGALHAHRvllGHLPGVQFPFN--LFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPK--A 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 342 LSQVIDKHQVNILYTAPTAIRaLMAEGDKAIEGTRRdSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTEtGGF 421
Cdd:cd05971 173 ALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQV-KLRAIATGGESLGEELLGWAREQFG---VEVNEFYGQTE-CNL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 422 MITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQARTLFGDhdrfEQTYFSTFKGMYF-SGD 500
Cdd:cd05971 247 VIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNN----PSATEKKMAGDWLlTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 501 GARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVR 580
Cdd:cd05971 323 LGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQ 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 727190822 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 403 ELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
74-616 |
2.45e-74 |
|
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: 248.56 E-value: 2.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 74 TLNLAANCLDRHLAERGDQTAIIWeGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:cd05970 15 NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 154 RIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGLragravpLKKNVDDALKNPGVVSVANVVVfqrtgkpgywQEGR 233
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAAPECPSKPKLVWVG----------DPVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 DLW--WHELTQGVSADCPPEEVNA----EDPLFILYTSGSTGKPKGVLHTTG---GYLVyaamTFKYVFDYHDGDIYWCT 304
Cdd:cd05970 157 EGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQNVREGGLHLTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 305 ADVGWVTGHSYLLYGPLACGATTLMFEGVPNYPgvNRLSQVIDKHQVNILYTAPTAIRALMAEgdkaiEGTRRD--SLRI 382
Cdd:cd05970 233 ADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDP--KALLEKLSKYGVTTFCAPPTIYRFLIRE-----DLSRYDlsSLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 383 MGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGgFMITPLPGaTELKAGSATRPFFGVQPALVDNVGTPQEGACEG 462
Cdd:cd05970 306 CTTAGEALNPEVFNTFKEKTG---IKLMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 463 NLVIVDSwPGQARTLFGDHDRFEQTYFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:cd05970 381 EIVIRTS-KGKPVGLFGGYYKDAEKTAEVWHdGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 542 IAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05970 460 VLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
34-617 |
8.57e-73 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 246.96 E-value: 8.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 34 DPEAFWGEHG-KILDWIKPYTKVkntsFDPGHVSIRWFEDGTLNLAANCLDRHL--AERGDQTAIIWEGDDPTQSKKVTY 110
Cdd:PTZ00237 20 NPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVknPLKRDQDALIYECPYLKKTIKLTY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 111 KQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGL 190
Cdd:PTZ00237 96 YQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 191 RAGRAVPLKKNVDDALKnpgvvsvanvvvfQRTGKPGY--------WQEGRDL--------------WWHELTQGVSADC 248
Cdd:PTZ00237 176 LNDEIITFTPNLKEAIE-------------LSTFKPSNvitlfrndITSESDLkkietiptipntlsWYDEIKKIKENNQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 249 PP--EEVNAED--PLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYlLYGPLACG 324
Cdd:PTZ00237 243 SPfyEYVPVESshPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYGSLSLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 ATTLMFEG--VPNYPGVNRLSQVIDKHQVNILYTAPTAIRALM---AEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYY 399
Cdd:PTZ00237 322 NTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIktdPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 400 NKIgNAKCPIVdtWWQTETGgfmITPLPGATELKAGSAT--RPFFGVQPALVDNVGTPQEGACEGNLVI-VDSWPGQART 476
Cdd:PTZ00237 402 NKL-KIKSSRG--YGQTEIG---ITYLYCYGHINIPYNAtgVPSIFIKPSILSEDGKELNVNEIGEVAFkLPMPPSFATT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 477 LFGDHDRFEQTyFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKG 556
Cdd:PTZ00237 476 FYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 557 QAIYAYITLNHGEEPTP----ELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 555 NVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-616 |
1.21e-69 |
|
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: 234.96 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 78 AANCLDRHLAE-RGDQTAIIwegdDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEgRGDKTAFI----DDAGS--LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 157 AVHSVIFGGFSPEAVAGRIIDSNAKLVITADE-----GLRAGRAVPLKKNVDdalknpgvvsvanvvvfqRTGKPGywQE 231
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGElapvlAAALTKSEHTLVVLI------------------VSGGAG--PE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 232 GRDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTF-KYVFDYHDGDIYWCTADVGWV 310
Cdd:cd05959 139 AGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 311 TGHSYLLYGPLACGATTLMFegvPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAegDKAIEGTRRDSLRIMGSVGEPI 390
Cdd:cd05959 218 YGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 391 NPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSW 470
Cdd:cd05959 293 PAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYV--RG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 PGQARTLFGdhdRFEQTYfSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05959 366 PSSATMYWN---NRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 550 IPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 442 VEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
4.41e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 225.84 E-value: 4.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 72 DGTLNLAaNCLDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 152 CARIGAV-HSV-IFggFSPEAVAGRIIDSNAKLVITADEGlragraVPLKKNVDDALknPGVVSVANVVVFQRTGKPGYW 229
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEF------VPLLAAILPQL--PTVRTVIVEGDGPAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 230 QEgrdlwWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTtggY--LVYAAMTFKYVFDYHDGDIYwctadv 307
Cdd:PRK06187 146 GE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS---HrnLFLHSLAVCAWLKLSRDDVY------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 gwvtghsyLLYGPLA-CGATTL----MFEGVPN-YPG---VNRLSQVIDKHQVNILYTAPTAIRALMaegdKAIEGTRRD 378
Cdd:PRK06187 212 --------LVIVPMFhVHAWGLpylaLMAGAKQvIPRrfdPENLLDLIETERVTFFFAVPTIWQMLL----KAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 379 --SLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFM-ITPLP---GATELKAGSATRPFFGVQPALVDNV 452
Cdd:PRK06187 280 fsSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPEdqlPGQWTKRRSAGRPLPGVEARIVDDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 453 GTPQEGACE--GNLVIVDSWPGQArtLFGDHDRFEQTYFstfKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK06187 357 GDELPPDGGevGEIIVRGPWLMQG--YWNRPEATAETID---GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 531 EIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK06187 432 ELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKI 508
|
570
....*....|...
gi 727190822 611 MRRILR-KIAAGD 622
Cdd:PRK06187 509 LKRVLReQYAEGK 521
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
92-616 |
5.27e-66 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 223.11 E-value: 5.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 92 QTAIIwegdDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV 171
Cdd:cd05919 1 KTAFY----AADRS--VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 172 AGRIIDSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppe 251
Cdd:cd05919 75 AYIARDCEARLVVT------------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 252 evNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADV--GWVTGHSylLYGPLACGATTLM 329
Cdd:cd05919 89 --SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 330 FegvPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRrdSLRIMGSVGEPINPEAWEWYYNKIGnakCPI 409
Cdd:cd05919 165 N---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALR--SLRLCVSAGEALPRGLGERWMEHFG---GPI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 410 VDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARtlfGDHDRFEQTYF 489
Cdd:cd05919 237 LDGIGATEVGHIFLSNRPGAWRL--GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLV--RGPSAAV---GYWNNPEKSRA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 490 STFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGE 569
Cdd:cd05919 310 TFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 727190822 570 EPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 390 APQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-617 |
3.83e-65 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 223.50 E-value: 3.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 76 NLAANCLD-----RHLAERGDQTAIIWEGDDPTQSKkVTYKQLHHDVCQFANVLKKL-GVKKGDVVAIYMPMVPEAAVAM 149
Cdd:cd05928 6 NFASDVLDqwadkEKAGKRPPNPALWWVNGKGDEVK-WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 150 LACARIGAVhsVIFGGFSPEA--VAGRIIDSNAKLVITADEglragravpLKKNVDD-ALKNPGVVSVANVVVFQRTGkp 226
Cdd:cd05928 85 VACIRTGLV--FIPGTIQLTAkdILYRLQASKAKCIVTSDE---------LAPEVDSvASECPSLKTKLLVSEKSRDG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 227 gyWqegrdLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTAD 306
Cdd:cd05928 152 --W-----LNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 307 VGWVTGHSYLLYGPLACGATTLMFEgVPNYpGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIegtRRDSLRIMGSV 386
Cdd:cd05928 225 TGWIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSY---KFPSLQHCVTG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 387 GEPINPEAWEWYYNKIGnakCPIVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVI 466
Cdd:cd05928 300 GEPLNPEVLEKWKAQTG---LDIYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 VDSwPGQARTLFGDH-DRFEQTYfSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd05928 375 RVK-PIRPFGLFSGYvDNPEKTA-ATIRGdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 545 AAVVGIPHNIKGQAIYAYITLN-----HGEEptpELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 453 SAVVSSPDPIRGEVVKAFVVLApqflsHDPE---QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
1.57e-63 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 216.71 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVItadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwhelt 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgvsadcppeevnaEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 322 ACGATTLMFEGvpnyPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDkaIEGTRRDSLRIMGSVGEPINP---EAWEWY 398
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPMPErllRALQAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 399 YnkignakCPIVDTWWQTETGGfMITPL-PGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARtl 477
Cdd:cd17631 237 G-------VKFVQGYGMTETSP-GVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA-- 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 478 fGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQ 557
Cdd:cd17631 305 -GYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGE 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 558 AIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 384 AVVAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-616 |
3.34e-62 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 213.96 E-value: 3.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGgfsPEAVAGRIIDSNAKLVITAdeglragraVPLKknvdDALKNPGVVSvanvvvfqrtgkpgywqegrdlwwh 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIVA---------VSFT----DLLAAGAPLG------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 239 eltqgvsadcPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGD-----------IYWCTAdv 307
Cdd:cd05936 118 ----------ERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDdvvlaalplfhVFGLTV-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 gwvtghSYLLygPLACGATTLMfegVPNyPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRrdSLRIMGSVG 387
Cdd:cd05936 186 ------ALLL--PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFS--SLRLCISGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 388 EPINPEAWEWYYNKIGnakCPIVDTWWQTETG-GFMITPLPGATelKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVI 466
Cdd:cd05936 252 APLPVEVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 vdswPGQARTLfGDHDRFEQTYfSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd05936 327 ----RGPQVMK-GYWNRPEETA-EAFVdGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 546 AVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
102-617 |
5.67e-57 |
|
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: 200.62 E-value: 5.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 102 PTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAK 181
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 182 LVITADEGLraGRAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGywqegrdlwwheLTQGVSADCPPEEVNAEDPLFI 261
Cdd:cd05926 89 LVLTPKGEL--GPASRAASKLGLAILELALDVGVLIRAPSAESLSN------------LLADKKNAKSEGVPLPDDLALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 262 LYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegvPnyPGVNR 341
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL----P--PRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 342 LS--QVIDKHQVNiLYTA-PTAIRALMAEgDKAIEGTRRDSLRIMGSVGEPINP---EAWEWYYnkignaKCPIVDTWWQ 415
Cdd:cd05926 228 STfwPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIRSCSASLPPavlEALEATF------GAPVLEAYGM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 416 TETGGFMIT-PLPGATElKAGSATRPFfGVQPALVDNVGTPQEGACEGNLVIVDswPGQARTLFGDHdrfEQTYFSTFKG 494
Cdd:cd05926 300 TEAAHQMTSnPLPPGPR-KPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNP---EANAEAAFKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 495 MYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTP 573
Cdd:cd05926 373 GWFrTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 727190822 574 ElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 453 E---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-616 |
7.78e-57 |
|
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: 198.28 E-value: 7.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 107 KVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITa 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 deglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 267 STGKPKGVLhTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegVPNYPGVNRLSQVi 346
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRFSASRFWSDV- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 347 DKHQVNILYTAPTAIRALMAEGDKAIEgtRRDSLRIMGsvGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPL 426
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSPDD--RAHRLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 427 PGATelKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvDSWPGQARTLfGDHDRFEQTYFSTFKGMYFSGDGARRDE 506
Cdd:cd05934 240 DEPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI-RGLRGWGFFK-GYYNMPEATAEAMRNGWFHTGDLGYRDA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKE 586
Cdd:cd05934 316 DGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCEGQ 392
|
490 500 510
....*....|....*....|....*....|
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 393 LAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
100-611 |
9.92e-57 |
|
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: 199.75 E-value: 9.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 100 DDPTqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSN 179
Cdd:cd05911 4 DADT-GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 180 AKLVITADEGLragravplkKNVDDALKNPGvvsvANVVVFQRTGKPGYWQEGRDLWWHELTQGVSADCPPEEVNAEDPL 259
Cdd:cd05911 83 PKVIFTDPDGL---------EKVKEAAKELG----PKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 260 FILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFD-YHDGDIYWCTADVGWVTGHSYLLYGPLaCGATTLMFegvpNYPG 338
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM----PKFD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 339 VNRLSQVIDKHQVNILYTAPtAIRALMAEGDKAiegTRRD--SLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVDTWWQT 416
Cdd:cd05911 225 SELFLDLIEKYKITFLYLVP-PIAAALAKSPLL---DKYDlsSLRVILSGGAPLSKELQELLAKRFPNAT--IKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 417 ETGGfMITPLPGaTELKAGSATRPFFGVQPALVD-----NVGTPQEGacEgnlVIVDS---WPGQartlfgdHDRFEQTY 488
Cdd:cd05911 299 ETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDddgkdSLGPNEPG--E---ICVRGpqvMKGY-------YNNPEATK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 489 FSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNH 567
Cdd:cd05911 365 ETFDEDGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 727190822 568 GEEPTPElyaEVRNWVRKEIgpiatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 445 GEKLTEK---EVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-624 |
2.15e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 199.77 E-value: 2.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITADEglragravpLKKNVDDALKNPGVVSVANVVVFQRTGKPGYWQEGRDLwwhelTQGVSADCPP 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADW-----AEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 EEVNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaAMTFKYVFDYHDGDIywcTADVgwVTGHSYLLY---------GP- 320
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVSCIVAGDM---SADD--IPLHALPLYhcaqldvflGPy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 321 LACGATTLMFEGvpnyPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDkaIEGTRRDSLR-------IMGsvGEPIN-- 391
Cdd:PRK08316 235 LYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRkgyygasIMP--VEVLKel 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 392 ----PEAweWYYNKIGnakcpivdtwwQTEtggfmITPL-----PGATELKAGSATRPFFGVQPALVDN------VGTPQ 456
Cdd:PRK08316 307 rerlPGL--RFYNCYG-----------QTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDdgndvaPGEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 457 EgacegnlvIVDSWPgQArtLFGDHDRFEQTYfSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK08316 369 E--------IVHRSP-QL--MLGYWDDPEKTA-EAFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 536 LVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08316 437 LYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
....*....
gi 727190822 616 RKIAAGDTS 624
Cdd:PRK08316 514 RERYAGAFT 522
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
31-617 |
5.06e-55 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 199.92 E-value: 5.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 31 SVQDPEAFWG---EHGKILDWIKPYTKVKNTSF-DPGHvsiRWFEDGTLNLAANCLDRHLAERGDQTAIIW--EGDDPTQ 104
Cdd:PLN03052 129 SVENPEVYWSivlDELSLVFSVPPRCILDTSDEsNPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSDDLP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 105 SKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVI 184
Cdd:PLN03052 206 VNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 TADEGLRAGRAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGywqegrDLWWHELTQGVSADCPPEEVNA-----EDPL 259
Cdd:PLN03052 286 TQDVIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSVRVKLREG------DMSWDDFLARANGLRRPDEYKAveqpvEAFT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 260 FILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVfDYHDGDIY-WCTaDVGWVTGHsYLLYGPLACGATTLMFEGVPNYPG 338
Cdd:PLN03052 360 NILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 339 VNRLSQvidKHQVNILYTAPTAIRALMAEGdkAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAkcPIVDTWWQTET 418
Cdd:PLN03052 437 FAKFVQ---DAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTEL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 419 GG-FMITPLPGATELKAGSAtrPFFGVQPALVDNVGT--PQEGACEGNLVIVDSWPGQARTLF-GDHDrfeQTYfstFKG 494
Cdd:PLN03052 510 GGgFVTGSLLQPQAFAAFST--PAMGCKLFILDDSGNpyPDDAPCTGELALFPLMFGASSTLLnADHY---KVY---FKG 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 495 M-YFSGDGARRDED-------GYYWITGRVDDVLNVSGHRLGTAEIESAL-VSHPKIAEAAVVGIPHNIKGQ---AIYAY 562
Cdd:PLN03052 582 MpVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPeqlVIAAV 661
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 563 ITLNHGEEPTPELYAEVRN-WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 662 LKDPPGSNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
3.90e-54 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 191.24 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhsVIfggfspeavagriidsNAKLVITAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV--VI----------------PATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EglragravpLKKNVDdalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltQGVSADCPPEEVN-AEDPLFILYTSG 266
Cdd:cd05974 63 D---------LRDRVD--------------------------------------RGGAVYAAVDENThADDPMLLYFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 267 STGKPKGVLHTTGGYLVYAAMTFkYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFegvpNYPGVN--RLSQ 344
Cdd:cd05974 96 TTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYARFDakRVLA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 345 VIDKHQVNILYTAPTAIRALMAEGDKAIegtrRDSLRIMGSVGEPINPEAWEWYYNKIGNAkcpIVDTWWQTETGGfMIT 424
Cdd:cd05974 171 ALVRYGVTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWGLT---IRDGYGQTETTA-LVG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 425 PLPGATeLKAGSATRPFFGVQPALVDNVGTP-QEGacEGNLVIVDSWP-GQARTLFGDHDRfeqTYFSTFKGMYFSGDGA 502
Cdd:cd05974 243 NSPGQP-VKAGSMGRPLPGYRVALLDPDGAPaTEG--EVALDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNW 582
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 727190822 583 VRKEIGPIATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
5.55e-54 |
|
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: 192.75 E-value: 5.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 73 GTLNLAANCLDRHLAE-RGDQTAIIwegdDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI----DDISS--LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 152 CARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGL-----RAGRAVPLKKNVDDALKNPGVVSVANvvvFQRTGKP 226
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLpvikaALGKSPHLEHRVVVGRPEAGEVQLAE---LLATESE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 227 GYwqegrdlwwheltqgvsadcPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTAD 306
Cdd:TIGR02262 152 QF--------------------KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 307 VGWVTGHSYLLYGPLACGATTLMFegvPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEgtRRDSLRIMGSV 386
Cdd:TIGR02262 212 LFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSE--DQVRLRLCTSA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 387 GEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPLPGAteLKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVI 466
Cdd:TIGR02262 287 GEALPAEVGQRWQARFG---VDIVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 vdSWPGQARTLFGDHDRFEqtyfSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:TIGR02262 362 --SGPSSATMYWNNRAKSR----DTFQGEWTrSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEA 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 546 AVVGIP---HNIKGQaiyAYITLNHGEEptpELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 436 AVVGVAdedGLIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
8.97e-54 |
|
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: 190.43 E-value: 8.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRII----DSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsa 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 247 dcppeevNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAmTFKYVFDYHDGDIYWCTA----DVGWVTghsylLYGPLA 322
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WMQEAYPLTPGDRVLQFTsfsfDVSVWE-----IFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 323 CGATTLMF-EGVPNYPGvnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtRRDSLRIMGSVGEPINPEAWEWYYNK 401
Cdd:cd05930 158 AGATLVVLpEEVRKDPE--ALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWREL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 402 IGNAKcpIVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNVGTPQ-EGAcEGNLVIvdSWPGQARTLF 478
Cdd:cd05930 232 LPGAR--LVNLYGPTEATVDATYYRVPPDDEEDGRVPigRPIPNTRVYVLDENLRPVpPGV-PGELYI--GGAGLARGYL 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 479 GDHD----RFEQTYFSTFKGMYFSGDGARRDEDG--YYwiTGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd05930 307 NRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARED 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 553 NIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 385 GDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-617 |
3.58e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 182.41 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGD------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGL----RAGRAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGywqegrdlww 237
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLgvdySATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAG---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 238 heltqgvSADCPPEEVNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAAMTFKYVFDYHDGDIYWCTA--------DVGW 309
Cdd:PRK07656 155 -------DPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANpffhvfgyKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 310 VTghsyllygPLACGATTLMfegVPNYpGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRrdSLRIMGSVGEP 389
Cdd:PRK07656 227 NA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLS--SLRLAVTGAAS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 390 INPEAWEWYYNKIGnakCPIVDTWWQ-TETGGFM-ITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVI- 466
Cdd:PRK07656 293 MPVALLERFESELG---VDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVr 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 --------VDSWPGQARTLFGDhdrfeqtyfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVS 538
Cdd:PRK07656 370 gpnvmkgyYDDPEATAAAIDAD-------------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 539 HPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 437 HPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
106-616 |
1.41e-49 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 178.83 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLK-KLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAgRIIDsnaklvi 184
Cdd:cd05958 9 REWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA-YILD------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 tadeglRAGRAVPLkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadCPPEEVNAEDPLFILYT 264
Cdd:cd05958 81 ------KARITVAL-------------------------------------------------CAHALTASDDICILAFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEG-VPNypgvnRLS 343
Cdd:cd05958 106 SGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEaTPD-----LLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 344 QVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMI 423
Cdd:cd05958 181 SAIARYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 424 TPLPGatELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdswpgQARTLF-GDHDRFEQTYFStfKGMYFSGDGA 502
Cdd:cd05958 256 SARPG--DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV------RGPTGCrYLADKRQRTYVQ--GGWNITGDTY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNW 582
Cdd:cd05958 326 SRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDH 405
|
490 500 510
....*....|....*....|....*....|....
gi 727190822 583 VRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 406 AKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-624 |
6.43e-48 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 176.78 E-value: 6.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlnp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 -------HSV----------------IFGGFSPEAVAgriidsnaklvitadEGLRagRAVPlkknvddALKNPGVVSVA 215
Cdd:PRK13295 110 lmpifreRELsfmlkhaeskvlvvpkTFRGFDHAAMA---------------RRLR--PELP-------ALRHVVVVGGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 216 NVVVFQRTGKPGYWQEGRDLwwhelTQGVSADCPpeevNAEDPLFILYTSGSTGKPKGVLHTT----GGYLVYAAMtfky 291
Cdd:PRK13295 166 GADSFEALLITPAWEQEPDA-----PAILARLRP----GPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 292 vFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgVPNypgVNRLSQVIDKHQVNilYT-APTAIRALMAEgdk 370
Cdd:PRK13295 233 -LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD-IWD---PARAAELIRTEGVT--FTmASTPFLTDLTR--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 371 AIEGTRRD--SLRIMGSVGEPINP----EAWEwyynkIGNAKcpIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGV 444
Cdd:PRK13295 303 AVKESGRPvsSLRTFLCAGAPIPGalveRARA-----ALGAK--IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 445 QPALVDNVGTPQEGACEGNLVIvdswpgQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK13295 376 EVRVVDADGAPLPAGQIGRLQV------RGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 525 HRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTpelYAEVRNWVR-KEIGPIATPDVLHWTDSLP 603
Cdd:PRK13295 450 ENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD---FEEMVEFLKaQKVAKQYIPERLVVRDALP 526
|
570 580
....*....|....*....|.
gi 727190822 604 KTRSGKIMRRILRKIAAGDTS 624
Cdd:PRK13295 527 RTPSGKIQKFRLREMLRGEDA 547
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
4.98e-47 |
|
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: 170.91 E-value: 4.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKL-GVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGfSPEAVAGRII-DSNAKLVITA 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-YPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 DEG-LRAGRAVPLKKNVDDalknpgvvsvanvvvfqrtgkpgywqegrdLWWHELTQGVSADCPPEEVNAEDPLFILYTS 265
Cdd:TIGR01733 80 SALaSRLAGLVLPVILLDP------------------------------LELAALDDAPAPPPPDAPSGPDDLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWvtGHSYL-LYGPLACGATTLMFEGVPNYPGVNRLSQ 344
Cdd:TIGR01733 130 GSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSF--DASVEeIFGALLAGATLVVPPEDEERDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 345 VIDKHQVNILYTAPTAIRALMAEGDkaiegTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAkcPIVDTWWQTE-TGGFMI 423
Cdd:TIGR01733 207 LIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALVDRWRARGPGA--RLINLYGPTEtTVWSTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 424 TPLPGATELKAGSAT--RPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARTLFGDHD----RFEQTYFSTFKG--M 495
Cdd:TIGR01733 280 TLVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVPVGVVGELYI--GGPGVARGYLNRPEltaeRFVPDPFAGGDGarL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 727190822 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
108-617 |
1.21e-46 |
|
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: 170.64 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EgLRAGRAVPLkknvddalknpgvvsvanvvvfqrtgkPGywqegrdlwwheltqgvsadcppeevnaeDPLFILYTSGS 267
Cdd:cd05903 82 R-FRQFDPAAM---------------------------PD-----------------------------AVALLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATT-LMFEGVPNypgvnRLSQVI 346
Cdd:cd05903 105 TGEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVvLQDIWDPD-----KALALM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 347 DKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINP----EAWEwyynkIGNAKcpIVDTWWQTETGGFM 422
Cdd:cd05903 179 REHGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRslarRAAE-----LLGAK--VCSAYGSTECPGAV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 423 ITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdswpgQARTLF-GDHDRFEQTYFSTFKGMYFSGDG 501
Cdd:cd05903 250 TSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS------RGPSVFlGYLDRPDLTADAAPEGWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVrn 581
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY-- 401
|
490 500 510
....*....|....*....|....*....|....*.
gi 727190822 582 WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 402 LDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
1.52e-44 |
|
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: 166.26 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 87 AERGDQTAIIwegdDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 167 SPEAVAGRIIDSNAKLVITADEGL----RAGRAVPLkknVDDALKNPGVVsvanvvvfqrtgkpgywqegrdlwWHELTQ 242
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELAeklaSLALPVVL---LDSAEFDSLSF------------------------SDLLFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 243 GVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGylvYAAMTFKYVFD----YHDGDIYWCTADVGWVTGHSYLLY 318
Cdd:cd05904 145 ADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN---LIAMVAQFVAGegsnSDSEDVFLCVLPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 319 GPLACGATTLMfegVPNYPGVNRLSqVIDKHQVNILYTAPTAIRALMaegdKAIEGTRRD--SLRIMGSVGEPINPEAWE 396
Cdd:cd05904 222 GLLRLGATVVV---MPRFDLEELLA-AIERYKVTHLPVVPPIVLALV----KSPIVDKYDlsSLRQIMSGAAPLGKELIE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 397 WYYNKIGNAKcpIVDTWWQTE-TGGFMITPLPGATELKAGSATRPFFGVQPALVDnvgtPQEGACEGnlvivdswPGQAR 475
Cdd:cd05904 294 AFRAKFPNVD--LGQGYGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVD----PETGESLP--------PNQTG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 476 TL-----------FGDHDRFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd05904 360 ELwirgpsimkgyLNNPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 545 AAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 438 AAVIPYPDEEAGEVPMAFVVRKPGSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
82-617 |
1.67e-44 |
|
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: 166.50 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERG-DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHS 160
Cdd:TIGR03098 5 LLEDAAARLpDATALVHHD------RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 161 VIFGGFSPEAVAGRIIDSNAKLVITADEGLragravplkknvdDALKnPGVVSVANVVVFQRTGKPGYWQEGRD----LW 236
Cdd:TIGR03098 79 PINPLLKAEQVAHILADCNVRLLVTSSERL-------------DLLH-PALPGCHDLRTLIIVGDPAHASEGHPgeepAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 237 WHELtQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHS 314
Cdd:TIGR03098 145 WPKL-LALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 YLLYGPLACGATTLMfegvpNYPGVNRLSQVIDKHQVNILYTAPtAIRALMAEGDKAIEGTRrdSLRIMGSVGEPINPEA 394
Cdd:TIGR03098 221 QLTTAFYVGATVVLH-----DYLLPRDVLKALEKHGITGLAAVP-PLWAQLAQLDWPESAAP--SLRYLTNSGGAMPRAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 395 WEWYYNKIGNAKcpIVDTWWQTEtgGFMITPL-PGATELKAGSATR--PFFGVQPALVDN----VGTPQEGACEGNLVIV 467
Cdd:TIGR03098 293 LSRLRSFLPNAR--LFLMYGLTE--AFRSTYLpPEEVDRRPDSIGKaiPNAEVLVLREDGsecaPGEEGELVHRGALVAM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 DSWPGQARTlfgdHDRFE----QTYFSTFKGM-YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:TIGR03098 369 GYWNDPEKT----AERFRplppFPGELHLPELaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 543 AEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 445 AEAVAFGVPDPTLGQAIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
3.18e-44 |
|
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: 165.14 E-value: 3.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDdalknpgvvsvanvvvfqrtgkpgywqegrdlwwHELT 241
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLG----------------------------------DEAL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 QGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGW-VTGhsYLLYGP 320
Cdd:cd17646 124 AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFWP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 321 LACGATTLMFEgvpnyPGVNR----LSQVIDKHQVNILYTAPTAIRALMAEGDkaieGTRRDSLRIMGSVGEPINPEAWE 396
Cdd:cd17646 201 LVAGARLVVAR-----PGGHRdpayLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 397 WY--------YNKIGNAKCPIVDTWWQTeTGGFMITPLP-GatelkagsatRPFFGVQPALVDNVGTPQEGACEGNLVIv 467
Cdd:cd17646 272 RFlalpgaelHNLYGPTEAAIDVTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGELYL- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 dSWPGQARtlfGDHDRFEQTY-------FSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:cd17646 340 -GGVQLAR---GYLGRPALTAerfvpdpFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHP 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 541 KIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17646 416 AVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
1.39e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 165.90 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIW--EGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 160 SvIFGGFSPEAVAGRIIDSNAKLVIT---------ADEGLRAGRAVP-LKKNVDDALKNPGVVSVANVVVFQRtGKPGyw 229
Cdd:PRK07529 111 P-INPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiWQKVAEVLAALPeLRTVVEVDLARYLPGPKRLAVPLIR-RKAH-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 230 qeGRDLWWHELTQGVSADC--PPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADV 307
Cdd:PRK07529 187 --ARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 GWVTGHSYLLYGPLACGATtLMFEGVPNY--PGV-NRLSQVIDKHQVNILYTAPTAIRALMaegDKAIEGTRRDSLRIMG 384
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAH-VVLATPQGYrgPGViANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 385 SVGEPINPEAWEWYYNKIGnakCPIVDTWWQTE-TGGFMITPLPGatELKAGSATRPFFG--VQPALVDNVGT-PQEGAC 460
Cdd:PRK07529 340 CGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGRyLRDCAV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 461 E--GNLVIvdSWPGQART-LFGDHDR---FEQTYFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK07529 415 DevGVLCI--AGPNVFSGyLEAAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 535 ALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIG-PIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKP 562
|
....*..
gi 727190822 614 ILRKIAA 620
Cdd:PRK07529 563 ALRRDAI 569
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
2.25e-43 |
|
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: 163.57 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDDPTQskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGEVH--RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITaDEGLragraVPLKKNVDDALKNpgvvsvaNVVVFQRTGKPGYWQEGRDLWWH--E 239
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFV-DRDF-----LPLLEAIAPRLPT-------VEHVVVMTDDAAMPEPAGVGVLAyeE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 240 LTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGV--------LHTTGgylvyAAMTFkyVFDYHDGDIY---------- 301
Cdd:cd12119 147 LLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHAMA-----ALLTD--GLGLSESDVVlpvvpmfhvn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 302 -WCTADVGWVTGHSYLLYGPLACGATtlmfegvpnypgvnrLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSL 380
Cdd:cd12119 220 aWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 381 R---IMGSVGEPINPEAWEWYYNKIGNAkcpivdtWWQTETG--GFMITPLPGATELKAG-------SATRPFFGVQPAL 448
Cdd:cd12119 283 RrvvIGGSAVPRSLIEAFEERGVRVIHA-------WGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 449 VDNVGT--PQEGACEGNLVIVDSWpgQARTLFGDHDR----FEQTYFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNV 522
Cdd:cd12119 356 VDDDGRelPWDGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLRT-------GDVATIDEDGYLTITDRSKDVIKS 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 523 SGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSL 602
Cdd:cd12119 427 GGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEI 503
|
570
....*....|....*
gi 727190822 603 PKTRSGKIMRRILRK 617
Cdd:cd12119 504 PKTSTGKIDKKALRE 518
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
2.49e-42 |
|
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: 159.01 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcpp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 eevNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTfKYVFDYHDGDIywctadvgWVTGHSYL-------LYGPLAC 323
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT-QRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 324 GATTLMfegVPNypGVNR----LSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLR--IMGsvGEPINPEAWEW 397
Cdd:cd17643 159 GGRLVV---VPY--EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRP 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 398 YYNKIGNAKCPIVDTWWQTETGGFM-ITPLpGATELKAGSAT---RPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQ 473
Cdd:cd17643 230 WAGRFGLDRPQLVNMYGITETTVHVtFRPL-DAADLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAGV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 474 ARtlfGDHDRFEQT--YF--STFKG----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd17643 307 AR---GYLGRPELTaeRFvaNPFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDA 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 546 AVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 384 AVIVREDEPGDTRLVAYVVADDGAAADI---AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-616 |
2.62e-42 |
|
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: 159.82 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERGDQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 164 GGFSPEAVAGRIIDSNAKLVITADE--GLRAGRAVPlkknvddalknpgvvsvanvvvfqrtgkpgywqeGRDLWWHELT 241
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlaGELAVELVA----------------------------------VTLLDQPGAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 QGVSADcPPEEVNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAAmtfKYVFDYHDGDIYWCTADVGW-VTGHSylLY 318
Cdd:cd17651 123 AGADAE-PDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQ---ARASSLGPGARTLQFAGLGFdVSVQE--IF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 319 GPLACGATtLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEP--INPEAWE 396
Cdd:cd17651 197 STLCAGAT-LVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTEDLRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 397 WY--------YNKIGNAKCPIVDTWWQT-ETGGFMITPLPGatelkagsatRPFFGVQPALVDNVGTPQEGACEGNLVIv 467
Cdd:cd17651 274 FCaglpglrlHNHYGPTETHVVTALSLPgDPAAWPAPPPIG----------RPIDNTRVYVLDAALRPVPPGVPGELYI- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 dSWPGQARTLFGD----HDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:cd17651 343 -GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727190822 544 EAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAYVVGDPEAPVDA---AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-615 |
1.30e-41 |
|
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: 157.75 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 83 DRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:cd12117 4 EEQAARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 FGGFSPEAVAGRIIDSNAKLVITaDEGLRAGRAVPLKKNVDDALKNPGvvsvanvvvfqrtgkpgywqegrdlwwheltq 242
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT-DRSLAGRAGGLEVAVVIDEALDAG-------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 243 gvSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVfDYHDGDIYWCTADVGWvTGHSYLLYGPLA 322
Cdd:cd12117 125 --PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 323 CGAT-TLMFEGVPNYPgvNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRdslRIMGsvGEPINPEAwewyYNK 401
Cdd:cd12117 200 NGARlVLAPKGTLLDP--DALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRE---LLTG--GEVVSPPH----VRR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 402 IgNAKCP---IVDTWWQTETGGF----MITPL-PGATELKAGsatRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQ 473
Cdd:cd12117 269 V-LAACPglrLVNGYGPTENTTFttshVVTELdEVAGSIPIG---RPIANTRVYVLDEDGRPVPPGVPGELYV--GGDGL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 474 ARTLFGDHD----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd12117 343 ALGYLNRPAltaeRFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 550 IPHNIKGQAIYAYITlnhGEEPTPelYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 423 REDAGGDKRLVAYVV---AEGALD--AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
3.88e-41 |
|
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: 155.60 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17649 2 DAVALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywQEGRDLWWheltqgvsadcpp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQLAY------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 eevnaedplfILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYvFDYHDGDIYWCTADVGWVTGHSYLlYGPLACGATTLMf 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 331 EGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGtRRDSLRIMGSVGEPINPEAWEwyynKIGNAKCPIV 410
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELLR----RWLKAPVRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 411 DTWWQTETggfMITPL--PGATELKAGSAT----RPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARtlfGDHDRF 484
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASmpigRPLGGRSAYILDADLNPVPVGVTGELYI--GGEGLAR---GYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 485 EQT--------YFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkG 556
Cdd:cd17649 313 ELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 557 QAIYAYITLNHGEEpTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 392 KQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-615 |
4.64e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 157.43 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 87 AER-GDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLK-KLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK08314 20 ARRyPDKTAIVFYG------RAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 165 GFSPEAVAGRIIDSNAKLVITADEglRAGRAVPLKK----------NVDDALKNPGVVSVANVVVfQRTGKPGYWQEGRD 234
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSE--LAPKVAPAVGnlrlrhvivaQYSDYLPAEPEIAVPAWLR-AEPPLQALAPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 235 LWWHELTQGVSAdcPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHS 314
Cdd:PRK08314 171 AWKEALAAGLAP--PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRT-VMANAVGSVLWSNSTPESVVLAVLPLFHVTGMV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 YLLYGPLACGATTLMFegvpnyPGVNR--LSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtRRD--SLRIMGSVGEPI 390
Cdd:PRK08314 248 HSMNAPIYAGATVVLM------PRWDReaAARLIERYRVTHWTNIPTMVVDFLASPGLA----ERDlsSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 391 nPEA-----WEWYynkignaKCPIVDTWWQTETGGFMITPLPGATELK-AGSatrPFFGVQPALVDNVgTPQEGAC--EG 462
Cdd:PRK08314 318 -PEAvaerlKELT-------GLDYVEGYGLTETMAQTHSNPPDRPKLQcLGI---PTFGVDARVIDPE-TLEELPPgeVG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 463 NLVIvdSWPGQARTLFGDHDRFEQTyFSTFKGMYF--SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK08314 386 EIVV--HGPQVFKGYWNRPEATAEA-FIEIDGKRFfrTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 541 KIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08314 463 AIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
9.71e-41 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 155.74 E-value: 9.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 139 MPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDAlknpgvvSVANVV 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA-------APAKAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 219 VFQRTGKPGYWQ-EGRDLWWHEL-----TQGVSADCPPEEV--NAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFlgvaaAQGSVGGNEYSPVyaPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 291 YVfDYHDGDIYWCTADVGWVTGhSYLLYGPLACGATTLMFEGVPNYPGvnrLSQVIDKHQVNILYTAPTAIRALMAEGDK 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 371 AIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKcPIVDTWWQTETGGFMI--TPL-PGAtelkAGSATRPFFGVQPA 447
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLqPQA----PGAFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 448 LVDN--VGTPQEGACEGNLVIVDSWPGQA-RTLFGDHDrfeQTYfstFKGM--YFS--------GDGARRDEDGYYWITG 514
Cdd:PLN03051 304 LLNDngVPYPDDQPCVGEVALAPPMLGASdRLLNADHD---KVY---YKGMpmYGSkgmplrrhGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 515 RVDDVLNVSGHRLGTAEIESALVSHPK-IAEAAVVGIPhNIKGQAIYAYITLNHGEEPT-------PELYAEVRNWVRKE 586
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTN 456
|
490 500 510
....*....|....*....|....*....|
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 457 LNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
1.56e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 148.96 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITADEglragravplkknvddalknpgvvsvanvvvFQRTGKPGYWQEgrdlwWHELTQGVSADCPP 250
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDD-------------------------------FEAKLIPGISVK-----FAELMNGPKEEAEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 -EEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLL----YG-PLacg 324
Cdd:PRK03640 135 qEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMrsviYGmRV--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 atTLM--FEgvpnypgVNRLSQVIDKHQVNILYTAPTAIRALMAEGDkaiEGTRRDSLRIMGSVGEPINPEAWEwyynki 402
Cdd:PRK03640 211 --VLVekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLG---EGTYPSSFRCMLLGGGPAPKPLLE------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 403 gnaKC-----PIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNvGTPQEGACEGNLVIvdswpgQARTL 477
Cdd:PRK03640 273 ---QCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV------KGPNV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 478 FGDHDRFEQTYFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKG 556
Cdd:PRK03640 343 TKGYLNREDATRETFQdGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727190822 557 QAIYAYITLnhgEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 423 QVPVAFVVK---SGEVTE--EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
84-616 |
4.30e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.21 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERGDQTAIIWeGDDptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:PRK06188 20 SALKRYPDRPALVL-GDT-----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 164 GGFSPEAVAGRIIDSNAKLVItADEGLRAGRAVPLKKNVDdALKN-----PGVvsvanvvvfqrtgkpgywqEGRDLWWH 238
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP-SLKHvltlgPVP-------------------DGVDLLAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 239 ELTQG----VSADCPPeevnaeDPLFILYTSGSTGKPKGVLHTTGGYlvyAAMTfkyvfdyhdgdiYWCTADVGWVTGHS 314
Cdd:PRK06188 153 AAKFGpaplVAAALPP------DIAGLAYTGGTTGKPKGVMGTHRSI---ATMA------------QIQLAEWEWPADPR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 YLLYGPL--ACGAT---TLMFEG----VPNY-PGvnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtRRD--SLRI 382
Cdd:PRK06188 212 FLMCTPLshAGGAFflpTLLRGGtvivLAKFdPA--EVLRAIEEQRITATFLVPTMIYALLDHPDLR----TRDlsSLET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 383 MGSVGEPINP----EAWEwyynKIGnakcPI-VDTWWQTETGGFmITPLP-----GATELKAGSATRPFFGVQPALVDN- 451
Cdd:PRK06188 286 VYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEd 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 452 -----VGTPQEGACEGNLVIVDSWpgqartlfgdhDRFEQTYfSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK06188 357 grevaQGEVGEICVRGPLVMDGYW-----------NRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGF 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 526 RLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKT 605
Cdd:PRK06188 425 NVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLT 501
|
570
....*....|.
gi 727190822 606 RSGKIMRRILR 616
Cdd:PRK06188 502 ALGKPDKKALR 512
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
6.27e-38 |
|
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: 146.31 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERGDQTAIIwegddpTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 164 GGFSPEAVAGRIIDSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqg 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 244 vsadcppeevNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAAMTFkyvfdyhdgdiywcTADV--GWVTGHS---- 314
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAF--------------SAEElaGVLASTSicfd 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 ---YLLYGPLACGATTLMFEGVPNYPGVNRLSQVidkhqvNILYTAPTAIRALMAEGdkAIEGtrrdSLRIMGSVGEPIN 391
Cdd:cd12115 159 lsvFELFGPLATGGKVVLADNVLALPDLPAAAEV------TLINTVPSAAAELLRHD--ALPA----SVRVVNLAGEPLP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 392 PEAWEWYYNKIGNAKcpIVDTWWQTETGGF-MITPLPGATElKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSW 470
Cdd:cd12115 227 RDLVQRLYARLQVER--VVNLYGPSEDTTYsTVAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYI--GG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 PGQARTLFGD----HDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:cd12115 302 AGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAV 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 547 VVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 382 VVAIGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
9.53e-38 |
|
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: 145.90 E-value: 9.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIwegddpTQSKKVTYKQLHHDVCQFANVL-KKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspe 169
Cdd:cd05941 1 DRIAIV------DDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 170 avagriidsnaklvitadeglragrAVPLkknvddALKNPGvvsvanvvvfqrtgkpgywqegrdlwwHELtQGVSADCP 249
Cdd:cd05941 64 -------------------------AVPL------NPSYPL---------------------------AEL-EYVITDSE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 250 PEEVnaEDPLFILYTSGSTGKPKGVLHTTGgylVYAAMTFKYVfDYHDgdiyWCTADV-----------GWVTGhsylLY 318
Cdd:cd05941 85 PSLV--LDPALILYTSGTTGRPKGVVLTHA---NLAANVRALV-DAWR----WTEDDVllhvlplhhvhGLVNA----LL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 319 GPLACGATTLMfegVPNYpGVNRLSQVIDKHQVNILYTAPT-------AIRALMAEGDKAIEGTRRdSLRIMGSVGEPIN 391
Cdd:cd05941 151 CPLFAGASVEF---LPKF-DPKEVAISRLMPSITVFMGVPTiytrllqYYEAHFTDPQFARAAAAE-RLRLMVSGSAALP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 392 PEAWEWYYNKIGNakcPIVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVD-NVGTPQEGACEGNLVIvdsw 470
Cdd:cd05941 226 VPTLEEWEAITGH---TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQV---- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 pgQARTLFgdhdrfeQTYFS---------TFKGMYFSGDGARRDEDGYYWITGRV-DDVLNVSGHRLGTAEIESALVSHP 540
Cdd:cd05941 297 --RGPSVF-------KEYWNkpeatkeefTDDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHP 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 541 KIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05941 368 GVSECAVIGVPDPDWGERVVAVVVLRAGAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
1.68e-37 |
|
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: 145.08 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 86 LAERGDQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 166 FSPEAVAgRIIDSNAKLVITADEGlragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvs 245
Cdd:cd05945 75 SPAERIR-EILDAAKPALLIADGD-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 246 adcppeevnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYvFDYHDGDIYWCTADVGW---VTGhsylLYGPLA 322
Cdd:cd05945 98 -----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFdlsVMD----LYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 323 CGATTLMfegVPN--YPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTrrDSLRIMGSVGEPI-NPEAWEWyy 399
Cdd:cd05945 162 SGATLVP---VPRdaTADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESL--PSLRHFLFCGEVLpHKTARAL-- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 400 nkIGNA-KCPIVDTWWQTET----GGFMITPLP--GATELKAGsatRPFFGVQPALVDNVGTPQEGACEGNLVIVDswPG 472
Cdd:cd05945 235 --QQRFpDARIYNTYGPTEAtvavTYIEVTPEVldGYDRLPIG---YAKPGAKLVILDEDGRPVPPGEKGELVISG--PS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 473 QARTLFGDHDRFEQTYFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:cd05945 308 VSKGYLNNPEKTAAAFFPDEGqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKY 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 552 HNIKGQAIYAYITLNHGEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 388 KGEKVTELIAFVVPKPGAEAGLT--KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
108-615 |
2.71e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 145.13 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 E---GLRAGRAVPLKKNVDDAlknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgVSADCPPEEVNAEDPLFILYT 264
Cdd:cd12116 93 AlpdRLPAGLPVLLLALAAAA--------------------------------------AAPAAPRTPVSPDDLAYVIYT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGV----------LHTTGGYL-------VYAAMTfkYVFDYhdgdiywctadvgwvtghSYL-LYGPLACGAT 326
Cdd:cd12116 135 SGSTGRPKGVvvshrnlvnfLHSMRERLglgpgdrLLAVTT--YAFDI------------------SLLeLLLPLLAGAR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 327 TLMFEGVPNYpGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtrRDSLRIM-GsvGEPINPEAWEWYYNKIGNA 405
Cdd:cd12116 195 VVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG--GEALPPDLAARLLSRVGSL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 406 kcpivdtwWQ----TETggfmiTPLPGATELKAGSAT----RPFFGVQPALVDNVGTP-QEGACeGNLVIvdSWPGQART 476
Cdd:cd12116 267 --------WNlygpTET-----TIWSTAARVTAAAGPipigRPLANTQVYVLDAALRPvPPGVP-GELYI--GGDGVAQG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 477 LFGDHD----RFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:cd12116 331 YLGRPAltaeRFVPDPFAGPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 552 HNIKGQaIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12116 411 DGGDRR-LVAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
108-616 |
2.82e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.43 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EGLRAGRAVP--LKKNVDDALKNPGvvsvanvvvfqrtGKPGYwqegRDlwWHELTQGVSADCPPEEVNAEDplfILYTS 265
Cdd:PRK08276 92 ALADTAAELAaeLPAGVPLLLVVAG-------------PVPGF----RS--YEEALAAQPDTPIADETAGAD---MLYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYAA---MTFKYVFDYH--DGDIYWCTADvgwvtghsylLY--GPLACGATTLMFEGV----P 334
Cdd:PRK08276 150 GTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYggPDSVYLSPAP----------LYhtAPLRFGMSALALGGTvvvmE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 335 NYPGVNRLsQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRD--SLRIMGSVGEPINPEA----WEWYynkiGnakcP 408
Cdd:PRK08276 220 KFDAEEAL-ALIERYRVTHSQLVPTMFVRMLKLPEEV--RARYDvsSLRVAIHAAAPCPVEVkramIDWW----G----P 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 409 IVD-TWWQTETGGF-MITPLPGATelKAGSATRPFFGVQPALVDN---VGTPQEGacegnLVIVdSWPGQARTLFGDHDR 483
Cdd:PRK08276 289 IIHeYYASSEGGGVtVITSEDWLA--HPGSVGKAVLGEVRILDEDgneLPPGEIG-----TVYF-EMDGYPFEYHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 484 FEQTYFStfKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYI 563
Cdd:PRK08276 361 TAAARNP--HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 727190822 564 TLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 439 QPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
101-615 |
4.34e-37 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 144.96 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 101 DPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNA 180
Cdd:cd05923 22 DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 181 KLVITAD-----EGLRAGRAVPLKKNVDDALKNPgvvsvanvvvfqrtgkpgywqegrdlwwheLTQGVSADCPPEEVna 255
Cdd:cd05923 102 TAAVIAVdaqvmDAIFQSGVRVLALSDLVGLGEP------------------------------ESAGPLIEDPPREP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 256 EDPLFILYTSGSTGKPKGVL--HTTGGYLVyAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegV 333
Cdd:cd05923 150 EQPAFVFYTSGTTGLPKGAVipQRAAESRV-LFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYV----V 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 PNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNakcPIVDTW 413
Cdd:cd05923 225 VEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGATMPDAVLERVNQHLPG---EKVNIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 414 WQTETGGFMITPLPgatelKAGSATRPFFGVQPALVDNVGTPQEGAC---EGNLvIVDSWPGQARTlfGDHDRFEQTYFS 490
Cdd:cd05923 300 GTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEALAngeEGEL-IVAAAADAAFT--GYLNQPEATAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 491 TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEE 570
Cdd:cd05923 372 LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTL 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 727190822 571 PTPELYAEVRNwvrKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05923 452 SADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-623 |
6.27e-37 |
|
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: 148.47 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IfggfSPEAVAGRII----DSNAKLVITaDEGLRA---GRAVPLkKNVDDAlknpgvvsvanvvvfqrtgkpgywqegrd 234
Cdd:COG1020 556 L----DPAYPAERLAymleDAGARLVLT-QSALAArlpELGVPV-LALDAL----------------------------- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 235 lwwhELTQGvSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIywctadVGWVTGHS 314
Cdd:COG1020 601 ----ALAAE-PATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLS 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 -----YLLYGPLACGATTLMF--EGVPNypgVNRLSQVIDKHQVNILYTAPTAIRALMAEGdkaieGTRRDSLRIMGSVG 387
Cdd:COG1020 669 fdasvWEIFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVGG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 388 EPINPEAWEWYYNKIGNakCPIVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNVGTPQ-EGACeGNL 464
Cdd:COG1020 741 EALPPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYEVTPPDADGGSVPigRPIANTRVYVLDAHLQPVpVGVP-GEL 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 465 VIvdSWPGQARtlfGDHDRFEQT--YF----STFKG--MYFSGDGARRDEDG---YYwitGRVDDVLNVSGHR--LGtaE 531
Cdd:COG1020 818 YI--GGAGLAR---GYLNRPELTaeRFvadpFGFPGarLYRTGDLARWLPDGnleFL---GRADDQVKIRGFRieLG--E 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRnwvRKEIGPIATPDVLHWTDSLPKTRSGKIM 611
Cdd:COG1020 888 IEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAAVVLLLPLPLTGNGKLD 964
|
570
....*....|..
gi 727190822 612 RRILRKIAAGDT 623
Cdd:COG1020 965 RLALPAPAAAAA 976
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
1.33e-36 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 144.05 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 90 GDQTAIIWEgDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 170 AVAGRIIDSNAKLVITADEGLRAGRAvpLKKNVDDALKNpgvvsvanvVVFQRTGKPGywQEGRDLWWHELTQGVSADCP 249
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQ--IQQEDATPLRH---------ICLTRVALPA--DDGVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 250 PEEVNAEDPLFILYTSGSTGKPKGVLHTT-----GGYL-----------VYAAMTFKYVFDYHdgdiywCTAdvgwvtgh 313
Cdd:PRK08008 167 APPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYsawqcalrdddVYLTVMPAFHIDCQ------CTA-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 314 sylLYGPLACGATTLMFEgvpNYPGVNRLSQVIdKHQVNILYTAPTAIRALMAEgdKAIEGTRRDSLRIMgsvgepinpe 393
Cdd:PRK08008 233 ---AMAAFSAGATFVLLE---KYSARAFWGQVC-KYRATITECIPMMIRTLMVQ--PPSANDRQHCLREV---------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 394 aweWYYNKIGNA---------KCPIVDTWWQTETGGFMITPLPGAtELKAGSATRPFFGVQPALVDNVGTPQEGACEGNL 464
Cdd:PRK08008 294 ---MFYLNLSDQekdafeerfGVRLLTSYGMTETIVGIIGDRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 465 VIvDSWPGqaRTLF-GDHDRFEQTYfSTFK--GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:PRK08008 370 CI-KGVPG--KTIFkEYYLDPKATA-KVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPK 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 542 IAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08008 446 IQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
48-617 |
4.79e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.14 E-value: 4.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 48 WIKPYTKVKNTSFDPGhvsirwfeDGTLnlaANCLDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKL 127
Cdd:PRK05605 15 WLQSYAPWTPHDLDYG--------DTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 128 GVKKGDVVAIYMPMVPEAAVAMLACARIGAV---HSVIFggfSPEAVAGRIIDSNAKLVITAD------EGLRAG----- 193
Cdd:PRK05605 78 GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLRRTtplet 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 194 -------RAVPLKKNVddALKNPGVVSVANVVvfQRTGK-PGYwqegrdLWWHELT------QGVSADCPpeEVNAEDPL 259
Cdd:PRK05605 155 ivsvnmiAAMPLLQRL--ALRLPIPALRKARA--ALTGPaPGT------VPWETLVdaaiggDGSDVSHP--RPTPDDVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 260 FILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGD--------IYwctadvgwvtgHSY-----LLYGPLaCGAT 326
Cdd:PRK05605 223 LILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPervlaalpMF-----------HAYgltlcLTLAVS-IGGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 327 TLMFegvPNyPGVNRLSQVIDKHQVNILYTAPT---AIRALMAEGDKAIEGTRrdslrimgsvgepinpeawewyyNKIG 403
Cdd:PRK05605 291 LVLL---PA-PDIDLILDAMKKHPPTWLPGVPPlyeKIAEAAEERGVDLSGVR-----------------------NAFS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 404 NAKCPIVDT--WWQTETGGFMI--------TPL----PGATELKAGSATRPFFGVQPALVD--NVGTPQEGACEGNLVIv 467
Cdd:PRK05605 344 GAMALPVSTveLWEKLTGGLLVegygltetSPIivgnPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLV- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 dswpgQARTLF-GDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:PRK05605 423 -----RGPQVFkGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAA 497
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 547 VVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 498 VVGLPREDGSEEVVAAVVLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
8.73e-35 |
|
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: 137.23 E-value: 8.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnAEDPLFILYTSGS 267
Cdd:cd05935 82 E------------------------------------------------------------------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnypgvNR--LSQV 345
Cdd:cd05935 96 TGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW------DRetALEL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 346 IDKHQVNILYTAPTAIRALMAegDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITP 425
Cdd:cd05935 169 IEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTETMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 426 LPGAteLKAGSATRPFFGVQPALVD-NVGTPQEGACEGNLVIvdSWPgQARTLFGDHDRFEQTYFSTFKGMYF--SGDGA 502
Cdd:cd05935 244 PPLR--PKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVV--RGP-QIFKGYWNRPEETEESFIEIKGRRFfrTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGE--EPTPElyaEVR 580
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEE---DII 395
|
490 500 510
....*....|....*....|....*....|....*
gi 727190822 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 396 EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
107-617 |
1.40e-34 |
|
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: 135.94 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 107 KVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspeavagriidsnaklvita 186
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 deglragrAVPLKKNvddalknpgvvsvanvvvfqrtgkpgywqegrdLWWHELT-QGVSADcppeeVNAEDPLFILYTS 265
Cdd:cd05912 53 --------AVLLNTR---------------------------------LTPNELAfQLKDSD-----VKLDDIATIMYTS 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLvYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnypgVNRLS 343
Cdd:cd05912 87 GTTGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVdkFD-------AEQVL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 344 QVIDKHQVNILYTAPTAIRALMAEGDkaieGTRRDSLRIMGSVGEPINPEAWEwyynkignaKC-----PIVDTWWQTET 418
Cdd:cd05912 159 HLINSGKVTIISVVPTMLQRLLEILG----EGYPNNLRCILLGGGPAPKPLLE---------QCkekgiPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 419 GGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEgacEGNLVIvdSWPGQARTLFGDHDR----FEQTYFSTfkg 494
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYE---VGEILL--KGPNVTKGYLNRPDAteesFENGWFKT--- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 495 myfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITlnhGEEPTPE 574
Cdd:cd05912 298 ----GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---SERPISE 370
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 727190822 575 lyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 371 --EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
1.64e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 138.63 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 ADeglragRAVPLKKNVDDA--LKNPGVVSVANVVVFQRTGKPGYWQEGRD-------------LW---WHELTQGVSAD 247
Cdd:PRK06710 128 LD------LVFPRVTNVQSAtkIEHVIVTRIADFLPFPKNLLYPFVQKKQSnlvvkvsesetihLWnsvEKEVNTGVEVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 248 CPPEEvnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDiywctaDVGWVTGHSYLLYGPLACGATT 327
Cdd:PRK06710 202 CDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 328 LMfEG-----VPNYpGVNRLSQVIDKHQVNILYTAPTAIRALMaeGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKI 402
Cdd:PRK06710 272 IM-QGykmvlIPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 403 G---------NAKCPIVDT--WWQTETGGFMITPLPGA----TELKAGSATRPffgvqpalvdnvGTPQEGACEGNLVIV 467
Cdd:PRK06710 348 GgklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKGPQIMK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 DSWpgqartlfgdhDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:PRK06710 416 GYW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 548 VGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 485 IGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-620 |
1.81e-34 |
|
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: 137.97 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIwEGDdptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 ----H-------------------SVIFGGFSPEAVAGRIIDSNAKL--VITADEglrAGRAVPLkknvDDALKNPgvvs 213
Cdd:COG1021 105 alpaHrraeishfaeqseavayiiPDRHRGFDYRALARELQAEVPSLrhVLVVGD---AGEFTSL----DALLAAP---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 214 vanvvvfqrtgkpgywqegrdlwwheltqgvsADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTtggylvyaamtfkyvf 293
Cdd:COG1021 174 --------------------------------ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRT---------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 294 dyHDgDiYWCT----ADVGWVTGHS-YL---------------LYGPLACGATTLMfegVPNyPGVNRLSQVIDKHQVNI 353
Cdd:COG1021 206 --HD-D-YLYSvrasAEICGLDADTvYLaalpaahnfplsspgVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 354 LYTAPTAIRALMAegdkAIEGTRRD--SLRIMGSVGEPINPEAWEWYYNKIGnakCpivdtWWQ-----TEtGGFMITPL 426
Cdd:COG1021 278 TALVPPLALLWLD----AAERSRYDlsSLRVLQVGGAKLSPELARRVRPALG---C-----TLQqvfgmAE-GLVNYTRL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 427 PGATELKAGSATRPffgVQPA----LVDNVGTP-QEGAcEGNLVivdswpgqAR---TLFG-----DHDrfeQTYFsTFK 493
Cdd:COG1021 345 DDPEEVILTTQGRP---ISPDdevrIVDEDGNPvPPGE-VGELL--------TRgpyTIRGyyrapEHN---ARAF-TPD 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 494 GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNhGEEPTP 573
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTL 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 727190822 574 elyAEVRNWVRkEIGpIAT---PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:COG1021 488 ---AELRRFLR-ERG-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
87-615 |
4.47e-34 |
|
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: 135.92 E-value: 4.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 87 AERG-DQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfgg 165
Cdd:cd17655 7 AEKTpDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 166 fSPEAVAGRII----DSNAKLVITADeglragravPLKKNVDDAlknpgvvsvanVVVFQRTGKPGYWQEGRDLwwhelt 241
Cdd:cd17655 78 -DPDYPEERIQyileDSGADILLTQS---------HLQPPIAFI-----------GLIDLLDEDTIYHEESENL------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgvsadcpPEEVNAEDPLFILYTSGSTGKPKGVLHTTGG--YLVYAAmTFKYVFDYHDgdiywctaDVGWVTGHSYLL-- 317
Cdd:cd17655 131 --------EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWA-NKVIYQGEHL--------RVALFASISFDAsv 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 318 ---YGPLACGATTLMFEGVPNYPGVnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEgtrrdSLRIMGSVGEPINPE- 393
Cdd:cd17655 194 teiFASLLSGNTLYIVRKETVLDGQ-ALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-----SLKHLIVGGEALSTEl 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 394 AWEWYynKIGNAKCPIVDTWWQTETG-GFMITPLPGATELKAG-SATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWP 471
Cdd:cd17655 268 AKKII--ELFGTNPTITNAYGPTETTvDASIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQPVGVAGELYI--GGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 472 GQARTLFGDHD----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:cd17655 344 GVARGYLNRPEltaeKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 548 VGIPHNIKGQAIYAYITlnhGEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17655 424 IARKDEQGQNYLCAYIV---SEKELPV--AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-621 |
2.22e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.72 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 75 LNLAANCLDRhLAERGDQTAIIwegDDPTqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI---DGAT-GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 155 IGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT----AD--EGLRAGRAVPLKkNVDDALKNPgvvsvanvvvfqrtgkpgy 228
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIITqscyVDklKGLAEDDGVTVV-TIDDPPEGC------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 229 wqegrdLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFkyvfdyhDGD---IYWCTA 305
Cdd:PLN02246 158 ------LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQV-------DGEnpnLYFHSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 306 DVGWVT---GHSYLLYGPLACG-----ATTLM--FEgvpnypgVNRLSQVIDKHQVNILYTAPTAIRALMaegdKAIEGT 375
Cdd:PLN02246 225 DVILCVlpmFHIYSLNSVLLCGlrvgaAILIMpkFE-------IGALLELIQRHKVTIAPFVPPIVLAIA----KSPVVE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 376 RRD--SLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVDTWWQTETG-------GFMITPLPgateLKAGSATRPFFGVQP 446
Cdd:PLN02246 294 KYDlsSIRMVLSGAAPLGKELEDAFRAKLPNAV--LGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 447 ALVDnvgtPQEGACEG-NLvivdswPGQ-------------------ARTLfgDHDRFEQTyfstfkgmyfsGDGARRDE 506
Cdd:PLN02246 368 KIVD----PETGASLPrNQ------PGEicirgpqimkgylndpeatANTI--DKDGWLHT-----------GDIGYIDD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKE 586
Cdd:PLN02246 425 DDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQ 501
|
570 580 590
....*....|....*....|....*....|....*.
gi 727190822 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILR-KIAAG 621
Cdd:PLN02246 502 VVFYKRIHKVFFVDSIPKAPSGKILRKDLRaKLAAG 537
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
2.26e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.90 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 79 ANCLDRHLAERGDQTAIIWEGDDptqskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGGFSPEAVAGRIIDSNAKLVITADEglragrAVPLKKNVDDAlkNPGVVSVANVVVFQRTGKPGYwqegrdlwwH 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVTEAA------LAPVATAVRDI--VPLLSTVVVAGGSSDDSVLGY---------E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 239 ELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAAMTFKYVFDYHDG-DIYWCTADVGWVTGHSY 315
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 316 LLYGpLACGATTLMfegvpnYP----GVNRLSQVIDKHQVNILYTAPTAIRALMAEgdkaiEGTR-RD-SLRIMGSVGEP 389
Cdd:PRK07786 234 MLPG-LLLGAPTVI------YPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE-----QQARpRDlALRVLSWGAAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 390 INPEAWEWYYNKIGNAKcpIVDTWWQTEtggfmITP----LPGATEL-KAGSATRPFFGVQPALVDN------VGTPQEG 458
Cdd:PRK07786 302 ASDTLLRQMAATFPEAQ--ILAAFGQTE-----MSPvtcmLLGEDAIrKLGSVGKVIPTVAARVVDEnmndvpVGEVGEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 459 ACEGNLVIVDSWPGQARTLfgdhDRFEQTYFStfkgmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVS 538
Cdd:PRK07786 375 VYRAPTLMSGYWNNPEATA----EAFAGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLAS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 539 HPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK- 617
Cdd:PRK07786 444 HPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALT--LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELREr 521
|
570
....*....|....
gi 727190822 618 IAAGDTSNLGDTST 631
Cdd:PRK07786 522 YGACVNVERRSASA 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
109-622 |
1.85e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.08 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADe 188
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 glRAGRAVPLKKNVDD-ALKNPGVVSvanvvvfqrtgkPGYWQEGrdlwwheltqgvsadcPPEEVNAEDPLFILYTSGS 267
Cdd:PRK12316 617 --HLGRKLPLAAGVQVlDLDRPAAWL------------EGYSEEN----------------PGTELNPENLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGYLVY-AAMTFKYVFDYHDGDIYWCT--ADVGwvtghSYLLYGPLACGATTLMFEgvpnyPGVNR--- 341
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRlCWMQQAYGLGVGDTVLQKTPfsFDVS-----VWEFFWPLMSGARLVVAA-----PGDHRdpa 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 342 -LSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtRRDSLRIMGSVGEPINPEAWEWYYNKIGNakCPIVDTWWQTETGg 420
Cdd:PRK12316 737 kLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQ--AGLYNLYGPTEAA- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 421 fmiTPLPGATELKAGSAT----RPFFGVQPALVDNVGTPQEGACEGNLVIVDSwpGQARTLFG----DHDRFEQTYFSTF 492
Cdd:PRK12316 810 ---IDVTHWTCVEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAG 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 493 KGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYITLnhgEEPT 572
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL---ESEG 957
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 727190822 573 PELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 958 GDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
3.58e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 129.87 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 117 VCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEavagrIIDSNAKLVITadegLRAGRAV 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 197 PLKKNVDDALKnpgvvsvanvVVFQRTGKPGYWQEGRDLWwheltqGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVL- 275
Cdd:cd05922 74 LADAGAADRLR----------DALPASPDPGTVLDADGIR------AARASAPAHEVSHEDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 276 -HTTggyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFEGVPNYPGVNRLsqvIDKHQVNIL 354
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNDGVLDDAFWED---LREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 355 YTAPTaIRALMAEGDKAIEGTrrDSLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVDTWWQTETGGFMiTPLPGATEL-K 433
Cdd:cd05922 211 AGVPS-TYAMLTRLGFDPAKL--PSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEATRRM-TYLPPERILeK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 434 AGSATRPFFGVQPALVDNVGTPQ------EGACEGNLVIVDSWpgqartlfgdHDRFEQTYFSTFKGMYFSGDGARRDED 507
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYW----------NDPPYRRKEGRGGGVLHTGDLARRDED 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkGQAIYAYITLNHGEEPtpelyAEVRNWVRKEI 587
Cdd:cd05922 355 GFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP-----KDVLRSLAERL 428
|
490 500
....*....|....*....|....*....
gi 727190822 588 GPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 429 PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
5.24e-32 |
|
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: 129.70 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIweGDDPTqskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHsVIFGGFSPEA 170
Cdd:cd12114 2 DATAVI--CGDGT----LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY-VPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRII-DSNAKLVITADEGLRAGRAVPLKKNVDDALknpgvvsvanvvvfqrtgkpgywqegrdlwwheltQGVSADCP 249
Cdd:cd12114 75 RREAILaDAGARLVLTDGPDAQLDVAVFDVLILDLDA-----------------------------------LAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 250 PEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAAMTFKYVFDYHDGdiywctadvgwVTGHS--------YLLYGP 320
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVGPDDR-----------VLALSslsfdlsvYDIFGA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 321 LACGATtLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGdkAIEGTRRDSLR-IMGSvGEPINPEawewyy 399
Cdd:cd12114 189 LSAGAT-LVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL--EAAQALLPSLRlVLLS-GDWIPLD------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 400 nkignakcpIVDTWWQTETGGFMITpLPGATELKAGSAT----------------RPFFGVQPALVDNVGTPQEGACEGN 463
Cdd:cd12114 259 ---------LPARLRALAPDARLIS-LGGATEASIWSIYhpidevppdwrsipygRPLANQRYRVLDPRGRDCPDWVPGE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 464 LVIvdSWPGQARTLFGDHDRFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:cd12114 329 LWI--GGRGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 542 IAEAAVVGIPhNIKGQAIYAYITLnhGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 407 VARAVVVVLG-DPGGKRLAAFVVP--DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
106-615 |
8.49e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 128.74 E-value: 8.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 adeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevNAEDPLFILYTS 265
Cdd:cd17650 91 --------------------------------------------------------------------QPEDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTtggYLVYAAMTFKYVFDYHdgdIYWCTADVGWVTGHSY-LLYGPLAcgaTTLMFEG----VPNYPGVN 340
Cdd:cd17650 103 GTTGKPKGVMVE---HRNVAHAAHAWRREYE---LDSFPVRLLQMASFSFdVFAGDFA---RSLLNGGtlviCPDEVKLD 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 341 --RLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLR--IMGSVGEPINPEAWEwyYNKIGnAKCPIVDTWWQT 416
Cdd:cd17650 174 paALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRllIVGSDGCKAQDFKTL--AARFG-QGMRIINSYGVT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 417 E----TGGFMIT--PLPGATELKAGsatRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARTLFGDHD----RFEQ 486
Cdd:cd17650 249 EatidSTYYEEGrdPLGDSANVPIG---RPLPNTAMYVLDERLQPQPVGVAGELYI--GGAGVARGYLNRPEltaeRFVE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 487 TYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVgIPHNIKGQA-IYAYITL 565
Cdd:cd17650 324 NPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVVA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 727190822 566 NHgeepTPELyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 403 AA----TLNT-AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
91-616 |
2.11e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 128.47 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK06145 17 DRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITaDEGLRAGRAVPLKKNVDDAlknpgvvsvANVVVFQRTGKPGywqegrdlwwheltqgvsADCPP 250
Cdd:PRK06145 91 VAYILGDAGAKLLLV-DEEFDAIVALETPKIVIDA---------AAQADSRRLAQGG------------------LEIPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 EEVNAEDPLF-ILYTSGSTGKPKGVLHTTggylvyaamtfkyvfdyhdGDIYWCTAD----VGWVTGHSYLLYGPL-ACG 324
Cdd:PRK06145 143 QAAVAPTDLVrLMYTSGTTDRPKGVMHSY-------------------GNLHWKSIDhviaLGLTASERLLVVGPLyHVG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 ATTLMFEGVPNYPGVNRLSQ---------VIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLRIMGSVGEPINPEAW 395
Cdd:PRK06145 204 AFDLPGIAVLWVGGTLRIHRefdpeavlaAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLAWCIGGGEKTPESRI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 396 EWYYNKIGNAKcpIVDTWWQTETGGfMITPLPGATEL-KAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDswPGQA 474
Cdd:PRK06145 282 RDFTRVFTRAR--YIDAYGLTETCS-GDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG--PKVT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 475 RTLFGDHdrfEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNI 554
Cdd:PRK06145 357 KGYWKDP---EKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727190822 555 KGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06145 434 WGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-623 |
2.21e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 128.00 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 GLRAGRAVPLkkNVDDalknpgvvsvanvvvfqrtgkpgywqegrdlwwheLTQGVSADCPP--EEVNAEDPLFILYTSG 266
Cdd:PRK09088 103 AVAAGRTDVE--DLAA-----------------------------------FIASADALEPAdtPSIPPERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 267 STGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FE------------ 331
Cdd:PRK09088 146 TSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVsngFEpkrtlgrlgdpa 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 332 -GVPNYPGVNRLSQVIdKHQVNIlytAPTAIRALMAegdkaiegtrrdslriMGSVGEPINPEAWEWYYNkignAKCPIV 410
Cdd:PRK09088 225 lGITHYFCVPQMAQAF-RAQPGF---DAAALRHLTA----------------LFTGGAPHAAEDILGWLD----DGIPMV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 411 DTWWQTETGGFMITPL-PGATELKAGSATRPFFGVQPALVDN------VGTPQEGACEGNLVIVDSW---PGQARTLFGD 480
Cdd:PRK09088 281 DGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDqgndcpAGVPGELLLRGPNLSPGYWrrpQATARAFTGD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 481 hdrfeqtyfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:PRK09088 361 -------------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGY 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727190822 561 AYITLNHGeepTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK09088 428 LAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
2.32e-31 |
|
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: 127.98 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEgddptqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITADEglragRAVPLKKNVDDALKNPgvvsvanvvvfqrtgkpgywqegrDLWWHELTQGVSAdcpp 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----LKSKLSFNKSTILLED------------------------PSISQEDTSNIDY---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 eEVNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVyaAMTFKYVFDYHDGDIYW---CTADVGWVTGHSYLLYGplacGA 325
Cdd:cd17656 124 -INNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSG----GT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 326 TTLMFEGVPNypGVNRLSQVIDKHQVNILYTaPTAIRALMAEGDKAIEgTRRDSLRIMGSVGEP--INPEAWEWY----- 398
Cdd:cd17656 197 LYIIREETKR--DVEQLFDLVKRHNIEVVFL-PVAFLKFIFSEREFIN-RFPTCVKHIITAGEQlvITNEFKEMLhehnv 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 399 --YNKIGNAKCPIVDTwwqtetggFMITPLPGATELKagSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQART 476
Cdd:cd17656 273 hlHNHYGPSETHVVTT--------YTINPEAEIPELP--PIGKPISNTWIYILDQEQQLQPQGIVGELYI--SGASVARG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 477 LFGD----HDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd17656 341 YLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKAD 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727190822 553 NIKGQAIYAYITLNHgEEPTPELyaevRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17656 421 DKGEKYLCAYFVMEQ-ELNISQL----REYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
1.81e-30 |
|
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: 114.18 E-value: 1.81e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 531 EIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
106-549 |
2.00e-30 |
|
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: 124.63 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 ADeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnAEDPLFILYTS 265
Cdd:cd05907 84 ED-------------------------------------------------------------------PDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYAAMTFKYVFDYhDGDIYWCTADVGWVTGHSYLLYGPLACGAT------------------- 326
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERRAGLYVPLLAGARiyfassaetllddlsevrp 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 327 TLMFeGVPnypgvnrlsQVIDKHQVNILYTAPTAIRALMAegDKAIEGtrrdSLRIMGSVGEPINPEAWEWyYNKIGnak 406
Cdd:cd05907 176 TVFL-AVP---------RVWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHF-FRALG--- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 407 CPIVDTWWQTETGGFMITPLPGAteLKAGSATRPFFGVQPALVDNvgtpQEGACEGNLVivdswpgqartLFGDHDRFEQ 486
Cdd:cd05907 236 IPVYEGYGLTETSAVVTLNPPGD--NRIGTVGKPLPGVEVRIADD----GEILVRGPNV-----------MLGYYKNPEA 298
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 487 TYFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVL-NVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05907 299 TAEALDAdGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
82-620 |
2.44e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 126.04 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEgddpTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12583 24 FDATVARFPDREALVVR----HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADeGLRA--------GRAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGYwqegr 233
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTsdyhamlqELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGF----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 dLWWHELT---QGVSADCPPE---EVNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAAMTFKYvfdyHDG---- 298
Cdd:PRK12583 174 -LAWHELQargETVSREALAErqaSLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLTE----HDRlcvp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 299 -DIYWC----TADVGWVTGHSYLLY-----GPLAcgatTLmfegvpnypgvnrlsQVIDKHQVNILYTAPTAIRALMAEG 368
Cdd:PRK12583 249 vPLYHCfgmvLANLGCMTVGACLVYpneafDPLA----TL---------------QAVEEERCTALYGVPTMFIAELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 369 DKAiegtRRD--SLR--IMGsvGEPINPEAWEwyyNKIGNAKCP-IVDTWWQTETGGfmITPLPGAT---ELKAGSATRP 440
Cdd:PRK12583 310 QRG----NFDlsSLRtgIMA--GAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAAddlERRVETVGRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 441 FFGVQPALVDNVG-TPQEGA----C-EGNLVIVDSWPGQARTLFG-DHDrfeqtyfstfkGMYFSGDGARRDEDGYYWIT 513
Cdd:PRK12583 379 QPHLEVKVVDPDGaTVPRGEigelCtRGYSVMKGYWNNPEATAESiDED-----------GWMHTGDLATMDEQGYVRIV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 514 GRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATP 593
Cdd:PRK12583 448 GRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVP 524
|
570 580
....*....|....*....|....*..
gi 727190822 594 DVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12583 525 RYFRFVDEFPMTVTGKVQKFRMREISI 551
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
3.60e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 124.80 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 83 DRHLAERGDQTAIIWEGDDPTqskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGEV----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 FGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVP---------LKKNVDDALknpgvvsvanvvvfqrtgkPGYWQegr 233
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKLDVARALLkqcpgvrhrLVLDGDGEL-------------------EGFVG--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 dlwWHELTQGVSADCPPEEVNAEDplfILYTSGSTGKPKGVLH--------TTGGYLvyaaMTFKYVFDYHDGDIYWCTA 305
Cdd:PRK13391 138 ---YAEAVAGLPATPIADESLGTD---MLYSSGTTGRPKGIKRplpeqppdTPLPLT----AFLQRLWGFRSDMVYLSPA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 306 DVGwvtgHSyllyGPLACGATTLMFEG---VPNYPGVNRLSQVIDKHQVNILYTAPTA-IRALmaegdKAIEGTRR---- 377
Cdd:PRK13391 208 PLY----HS----APQRAVMLVIRLGGtviVMEHFDAEQYLALIEEYGVTHTQLVPTMfSRML-----KLPEEVRDkydl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 378 DSLRIMGSVGEPINPEAWE----WYynkignakCPIVDTWW-QTETGGFMITPLPGATElKAGSATRPFFGVqPALVDNV 452
Cdd:PRK13391 275 SSLEVAIHAAAPCPPQVKEqmidWW--------GPIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 453 GTPQEgacegnlvivdswPGQARTLFGDHDR-FEqtYF----------STFKGMYFSGDGARRDEDGYYWITGRVDDVLN 521
Cdd:PRK13391 345 GAELP-------------PGEPGTIWFEGGRpFE--YLndpaktaearHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMII 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 522 VSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDS 601
Cdd:PRK13391 410 SGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDE 489
|
570
....*....|....*
gi 727190822 602 LPKTRSGKIMRRILR 616
Cdd:PRK13391 490 LPRLPTGKLYKRLLR 504
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
4.08e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 125.60 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGLRAgRAVPLKKN--------VDDALKNPGVVSVANVVVFQRTGKPGYWQEGR 233
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQLD-KLLEVRDElpslrhivVLDPRGLRDDPRLLSLDELLALGREVADPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 DLWWheltqgvsadcppEEVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDiywctadvgwvtgh 313
Cdd:COG1022 174 EARR-------------AAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGD-------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 314 SYLLYGPLA-----CGATTLMFEGVPNY--PGVNRLSQVIDKHQVNILYTAP-------TAIRALMAEG--------DKA 371
Cdd:COG1022 226 RTLSFLPLAhvferTVSYYALAAGATVAfaESPDTLAEDLREVKPTFMLAVPrvwekvyAGIQAKAEEAgglkrklfRWA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 372 IE-GTRR----------------------------------DSLRIMGSVGEPINPEAWEWYYNkIGnakCPIVDTWWQT 416
Cdd:COG1022 306 LAvGRRYararlagkspslllrlkhaladklvfsklrealgGRLRFAVSGGAALGPELARFFRA-LG---IPVLEGYGLT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 417 ETGGFMITPLPGATelKAGSATRPFFGVQPALVDNvgtpqegacegNLVIVDSwPGqartLF-GDHDRFEQT-------- 487
Cdd:COG1022 382 ETSPVITVNRPGDN--RIGTVGPPLPGVEVKIAED-----------GEILVRG-PN----VMkGYYKNPEATaeafdadg 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 488 YFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGhrlGT----AEIESALVSHPKIAEAAVVG 549
Cdd:COG1022 444 WLHT-------GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-617 |
5.78e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 124.38 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 75 LNLAaNCLDRHLAERGDQTAIIWeGDdptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 155 IGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD---EGLRAGRAVPLKKNVDDALKNPGvvsvanvvvfqrtGKPGYwqe 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTHVVAIGGAR-------------AGLDY--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 232 gRDLwwheLTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaAMTFkyVFDYHDGDIYWCT--ADVGW 309
Cdd:PRK07470 144 -EAL----VARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG------QMAF--VITNHLADLMPGTteQDASL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 310 VTGhsyllygPLACGAttlmfegvpnypGVNRLSQV----------------------IDKHQVNILYTAPTaIRALMAE 367
Cdd:PRK07470 211 VVA-------PLSHGA------------GIHQLCQVargaatvllpserfdpaevwalVERHRVTNLFTVPT-ILKMLVE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 368 gDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAkcpIVDTWWQTETGGfMITPLPGA-------TELKAGSATRP 440
Cdd:PRK07470 271 -HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTG-NITVLPPAlhdaedgPDARIGTCGFE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 441 FFGVQPALVDNVGTPQEGACEGNLVIVdswpGQArTLFGDHDRFEQTYfSTFKGMYF-SGDGARRDEDGYYWITGRVDDV 519
Cdd:PRK07470 346 RTGMEVQIQDDEGRELPPGETGEICVI----GPA-VFAGYYNNPEANA-KAFRDGWFrTGDLGHLDARGFLYITGRASDM 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 520 LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWT 599
Cdd:PRK07470 420 YISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFW 496
|
570
....*....|....*...
gi 727190822 600 DSLPKTRSGKIMRRILRK 617
Cdd:PRK07470 497 DALPKSGYGKITKKMVRE 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
6.31e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 121.43 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 263 YTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATtLMFEGVPNYPG---V 339
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLAGPAGYRNpglF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 340 NRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGtrrdSLRIMGSVGEPINPEAWEWYYNKIGnakCPIVDTWWQTE-T 418
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQVPVNADIS----SLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEaT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 419 GGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTPQEgACEGNLVIVDSWPGqaRTLFGDHDRFEQTYFSTFKGMYF- 497
Cdd:cd05944 160 CLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLR-DCAPDEVGEICVAG--PGVFGGYLYTEGNKNAFVADGWLn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElya 577
Cdd:cd05944 237 TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE--- 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 727190822 578 EVRNWVRKEIGP-IATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05944 314 ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
2.22e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 122.69 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 90 GDQTAIIWeGDdptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GD-----RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 170 AVAGRIIDSNAKLVITADEglRAGRAVPLKKN---------VDDALKNPGvvsvanvvvfqRTGKPGYwqegRDLwwheL 240
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPRVAEVLPRlpklrtlvvVEDGSGNDL-----------LPGAVDY----EDA----L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 TQGvSADCPPEEVNAEDpLFILYTSGSTGKPKGVLHTTGG-YLV----YAAMTFKYVFDYHDGdiywcTADVGWVTGHSY 315
Cdd:PRK07798 150 AAG-SPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRQEDiFRVllggRDFATGEPIEDEEEL-----AKRAAAGPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 316 LLYGPLACGATTL-----MFEG--VPNYPGV----NRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMG 384
Cdd:PRK07798 223 FPAPPLMHGAGQWaafaaLFSGqtVVLLPDVrfdaDEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 385 SVGEPINPEAWEWYYNKIGNAKcpIVDTWWQTETGgFMITplpGATELKAGSATRPFFGVQP--ALVDNVGTPQEgaceg 462
Cdd:PRK07798 303 SGGALFSPSVKEALLELLPNVV--LTDSIGSSETG-FGGS---GTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVE----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 463 nlvivdswPGQ------ART------LFGDHDRFEQTYFsTFKGMYFS--GDGARRDEDGYYWITGRVDDVLNVSGHRLG 528
Cdd:PRK07798 372 --------PGSgeigwiARRghiplgYYKDPEKTAETFP-TIDGVRYAipGDRARVEADGTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 529 TAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAG 519
|
.
gi 727190822 609 K 609
Cdd:PRK07798 520 K 520
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
4.16e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 118.92 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAAMTFKyvfdyhDGDI-------YWCTADVGwvtghsyllyGPLAC 323
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT------EQDRlcipvplFHCFGSVL----------GVLAC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 324 ---GATTLMFEgvPNYPGVNRLsQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTrrDSLR--IMGsvGEPINPEAWEWY 398
Cdd:cd05917 66 lthGATMVFPS--PSFDPLAVL-EAIEKEKCTALHGVPTMFIAELEHPDFDKFDL--SSLRtgIMA--GAPCPPELMKRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 399 YNKIGNAKCPIVdtWWQTETGGFMITPLPGAT-ELKAGSATRPFFGVQPALVD-------NVGTPQEGACEGNLVIVDSW 470
Cdd:cd05917 139 IEVMNMKDVTIA--YGMTETSPVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDpeggivpPVGVPGELCIRGYSVMKGYW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 pgqartlfGDHDRFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:cd05917 217 --------NDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 551 PHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 287 PDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
84-623 |
9.41e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 121.30 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLA-ERGDQTAIIWEGDDptqskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK06178 40 RAWArERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 fggfSPEAVAGRII----DSNAKLVITAD------EGLRAGRAVP--LKKNVDDALknPGVVSVANVVVFQ--RTGKPGy 228
Cdd:PRK06178 114 ----SPLFREHELSyelnDAGAEVLLALDqlapvvEQVRAETSLRhvIVTSLADVL--PAEPTLPLPDSLRapRLAAAG- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 229 WQegrDLWWHELTQGVSADCPPEEVNAedPLFILYTSGSTGKPKGVLHTTgGYLVYAAMTFKYVFDYHDGDiywctaDVG 308
Cdd:PRK06178 187 AI---DLLPALRACTAPVPLPPPALDA--LAALNYTGGTTGMPKGCEHTQ-RDMVYTAAAAYAVAVVGGED------SVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 309 -------WVTGHSYLLYGPLACGATTLMF---------EGVPNYpGVNRLSQVIDKHqVNILYTAPTAIRALmaegdkai 372
Cdd:PRK06178 255 lsflpefWIAGENFGLLFPLFSGATLVLLarwdavafmAAVERY-RVTRTVMLVDNA-VELMDHPRFAEYDL-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 373 egtrrDSLRIMGSVG--EPINPEawewYYNKignakcpivdtwWQTETGGFMITPLPGATELK-AGSATRPF------FG 443
Cdd:PRK06178 325 -----SSLRQVRVVSfvKKLNPD----YRQR------------WRALTGSVLAEAAWGMTETHtCDTFTAGFqdddfdLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 444 VQPALvdnVGTPQEGA----CE---GNLVIVDSwPGQ--ART---LFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYW 511
Cdd:PRK06178 384 SQPVF---VGLPVPGTefkiCDfetGELLPLGA-EGEivVRTpslLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 512 ITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIA 591
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAVYK 536
|
570 580 590
....*....|....*....|....*....|..
gi 727190822 592 TPDVlHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK06178 537 VPEI-RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
1.26e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 120.62 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIwegDDptQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DN--HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVI-------TADEGLragrAVPLKKNVD--------DALKnPGVVSVANVVVFQRtGKPgywqegrdl 235
Cdd:PRK06087 113 LVWVLNKCQAKMFFaptlfkqTRPVDL----ILPLQNQLPqlqqivgvDKLA-PATSSLSLSQIIAD-YEP--------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 236 wwheltqgVSADCPpeeVNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSY 315
Cdd:PRK06087 178 --------LTTAIT---THGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 316 LLYGPLACGATTLMFEgvpNYPGVNRLSQvIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPInP--- 392
Cdd:PRK06087 246 GVTAPFLIGARSVLLD---IFTPDACLAL-LEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-Pkkv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 393 --EAWEwyynkignAKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDN------VGTPQEGACEGNL 464
Cdd:PRK06087 319 arECQQ--------RGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlpPGCEGEEASRGPN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 465 VIV---DSWPGQARTLfgDHDrfeqtyfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:PRK06087 391 VFMgylDEPELTARAL--DEE-----------GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPK 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 542 IAEAAVVGIPHNIKGQAIYAYITLNhGEEPTPELyAEVRNWV-RKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 458 IHDACVVAMPDERLGERSCAYVVLK-APHHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
84-618 |
1.50e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 120.42 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERG-DQTAIIwegDDPTQskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAI----YMPMVpeaaVAMLACARIGAV 158
Cdd:PRK07788 56 AHAARRApDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPlkknvddalknpgvvsvanvvvfqrTGKPGY--WQEGRDlw 236
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-------------------------PDLGRLraWGGNPD-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 237 whELTQGVSADCPPEEV---NAEDPL--------FILYTSGSTGKPKGVLHTT-------GGYLvyAAMTFKYvfdyhdG 298
Cdd:PRK07788 179 --DDEPSGSTDETLDDLiagSSTAPLpkppkpggIVILTSGTTGTPKGAPRPEpsplaplAGLL--SRVPFRA------G 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 299 DIYWCTADVGWVTGHSYLLYGpLACGATTLM---FEGVpnypgvnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGT 375
Cdd:PRK07788 249 ETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrFDPE-------ATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 376 RRDSLRIMGSVGEPINPEawewyynkIGNAKcpivdtwwqTETGGFMITPLPGATELKAGS-ATRPFFGVQPALVdnvGT 454
Cdd:PRK07788 321 DTSSLKIIFVSGSALSPE--------LATRA---------LEAFGPVLYNLYGSTEVAFATiATPEDLAEAPGTV---GR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 455 PQEGAcegNLVIVDS-----WPGQARTLF-GDHDRFEQtYFS-----TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK07788 381 PPKGV---TVKILDEngnevPRGVVGRIFvGNGFPFEG-YTDgrdkqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 524 GHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLP 603
Cdd:PRK07788 457 GENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELP 533
|
570
....*....|....*
gi 727190822 604 KTRSGKIMRRILRKI 618
Cdd:PRK07788 534 RNPTGKVLKRELREM 548
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
2.90e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 119.46 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 79 ANCLDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGGFSPEAVAGRIIDSNAKLVI----------------TADEGLRAGRAVPLKKNVDDALKNPGvvsvanvvvfqr 222
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaaVPPDALPPLRAIAVVDDAADATPAPA------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 223 tgkPGYWQEGRDLwwhELTQGVSADCPPEEVnaEDPLFILY-TSGSTGKPKGVLHTTGGYLVYAAMTFKyVFDYHDGDIY 301
Cdd:PRK06164 155 ---PGARVQLFAL---PDPAPPAAAGERAAD--PDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 302 WCTADVGWVTGHSYLLyGPLACGATTLM---FEGVpnypgvnRLSQVIDKHQVNILYTAPTAIRALMAEgdkaiEGTRRD 378
Cdd:PRK06164 226 LAALPFCGVFGFSTLL-GALAGGAPLVCepvFDAA-------RTARALRRHRVTHTFGNDEMLRRILDT-----AGERAD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 379 --SLRIMGSVG-EPINPEAWEWyynkignakcpivdtwwqTETGGFMITPLPGATELKA----GSATRPF--------FG 443
Cdd:PRK06164 293 fpSARLFGFASfAPALGELAAL------------------ARARGVPLTGLYGSSEVQAlvalQPATDPVsvriegggRP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 444 VQPALVDNVGTPQEGAC-----EGNLVIvdSWPGQARTLFGDHDRFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRVDD 518
Cdd:PRK06164 355 ASPEARVRARDPQDGALlpdgeSGEIEI--RAPSLMRGYLDNPDATARAL--TDDGYFRTGDLGYTRGDGQFVYQTRMGD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 519 VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHniKGQAI-YAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLH 597
Cdd:PRK06164 431 SLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR--DGKTVpVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQ 505
|
570 580
....*....|....*....|....*
gi 727190822 598 WTDSLPKTRSG---KIMRRILRKIA 619
Cdd:PRK06164 506 VVEAFPVTESAngaKIQKHRLREMA 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
3.49e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 115.51 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYV-FDyhDGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegvpn 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRSLLAGAELVL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 336 yPGVNRLSQViDKHQVNILYTA--PTAIRALMAEGdkaIEGTRRDSLRIMGSVGEPINPEAWEwyynKIGNAKCPIVDTW 413
Cdd:cd17630 72 -LERNQALAE-DLAPPGVTHVSlvPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 414 WQTETGGfMITPLPgATELKAGSATRPFFGVQPALVDN----VGTPQegacegnlVIVDSWPGQARTLFgdhdrFEQTYF 489
Cdd:cd17630 143 GMTETAS-QVATKR-PDGFGRGGVGVLLPGRELRIVEDgeiwVGGAS--------LAMGYLRGQLVPEF-----NEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 490 STfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGE 569
Cdd:cd17630 208 TT-------KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 727190822 570 EPtpelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 281 DP-----AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
108-617 |
1.17e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.88 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EGLR------AGRAVPLKKNVDdalknpgvvsvanvvvfqrtgkpgywqegrdlWWheltQGVSADCPPEEVNAEDPLFI 261
Cdd:PRK12467 618 HLLAqlpvpaGLRSLCLDEPAD--------------------------------LL----CGYSGHNPEVALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 262 LYTSGSTGKPKGVLHTTGGYLVYAAMTFKYvfdyhdgdiYWCTADVGWVTGHSY-------LLYGPLACGATTLMFEgvp 334
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLLP--- 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 335 nyPGVNR----LSQVIDKHQVNILYTAPTAIRALMAegDKAIEGTRRDSLRIMGsvGEPINPEAWEWYYNKIGNAKcpIV 410
Cdd:PRK12467 730 --PDCARdaeaFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GEALQVDLLARVRALGPGAR--LI 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 411 DTWWQTETG-GFMITPLPGATELKAGSAT-RPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARTLFG----DHDRF 484
Cdd:PRK12467 802 NHYGPTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYI--GGAGLARGYHRrpalTAERF 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 485 EQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPhNIKGQAIYAYI 563
Cdd:PRK12467 880 VPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYL 958
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 564 TLNHGEEPT--PELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 959 VPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
1.17e-27 |
|
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: 117.01 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEgddptqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVItADEGLragravplkkNVDDALKnpgvvsvanvvvfqrTGKPGY-WQEGRDLWwhel 240
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-VDREF----------EYEDLLA---------------EGDPDFeWIPPADEW---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 tqgvsadcppeevnaeDPLFILYTSGSTGKPKGVLHT-TGGYLvyAAMTFKYVFDYHDGDIYWCTADV----GWVtghsy 315
Cdd:cd12118 134 ----------------DPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC----- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 316 LLYGPLACGATTLMFEGVpNYPGVNRLsqvIDKHQVNILYTAPTAIRALMaegDKAIEGTRRDSLRIMGSVGEPINPEAW 395
Cdd:cd12118 191 FPWTVAAVGGTNVCLRKV-DAKAIYDL---IEKHKVTHFCGAPTVLNMLA---NAPPSDARPLPHRVHVMTAGAPPPAAV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 396 EWYYNKIGNAKC----------PIVDTWWQTETGGfmitpLPgaTELKAGSATR---PFFGVQPALVDNVGTPQ------ 456
Cdd:cd12118 264 LAKMEELGFDVThvygltetygPATVCAWKPEWDE-----LP--TEERARLKARqgvRYVGLEEVDVLDPETMKpvprdg 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 457 ----EGACEGNLVivdswpgqARTLFGDHdrfEQTYfSTFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:cd12118 337 ktigEIVFRGNIV--------MKGYLKNP---EATA-EAFRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDsLPKTRSGKIM 611
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQ 480
|
....*.
gi 727190822 612 RRILRK 617
Cdd:cd12118 481 KFVLRD 486
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
107-615 |
2.08e-27 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 115.43 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 107 KVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITa 186
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 deglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevNAEDPLFILYTSG 266
Cdd:cd17652 91 -------------------------------------------------------------------TPDNLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 267 STGKPKGVL--HTTGGYLVYAAMTFKYVfdyhdgdiywcTADVGWVTGHS-------YLLYGPLACGATTLMFEGVPNYP 337
Cdd:cd17652 104 STGRPKGVVvtHRGLANLAAAQIAAFDV-----------GPGSRVLQFASpsfdasvWELLMALLAGATLVLAPAEELLP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 338 GvNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtrrdsLRIMGSVGEPINPE-AWEW-----YYNKIGNAKCPIVD 411
Cdd:cd17652 173 G-EPLADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAElVDRWapgrrMINAYGPTETTVCA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 412 TWWQtetggfmitPLPGATELKAGsatRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARtlfGDHDRFEQTY--- 488
Cdd:cd17652 244 TMAG---------PLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYI--AGAGLAR---GYLNRPGLTAerf 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 489 ----FSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYI 563
Cdd:cd17652 307 vadpFGAPGSrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 727190822 564 TLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 387 VPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-619 |
3.23e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 115.65 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIwegddpTQSKKVTYKQLHHDVCQFANVLKKLGvKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK07638 16 NKIAIK------ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITADEglragravpLKKNVDDAlknpgvvsvanvvvfqrtgkpgywqEGRDLWWHELTQGVSADCP- 249
Cdd:PRK07638 89 LKERLAISNADMIVTERY---------KLNDLPDE-------------------------EGRVIEIDEWKRMIEKYLPt 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 250 --PEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLvyaamtfkYVFDYHDGDIYWCTADVGWVTG---HSYLLYGP---L 321
Cdd:PRK07638 135 yaPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHSLFLYGAistL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 322 ACGAT-TLMFEGVPNypgvnrlsQVIDK---HQVNILYTAPTAIRALMAEgdkaiEGTRRDSLRIMGSvGEPINPEAWEW 397
Cdd:PRK07638 207 YVGQTvHLMRKFIPN--------QVLDKletENISVMYTVPTMLESLYKE-----NRVIENKMKIISS-GAKWEAEAKEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 398 YYNKIGNAKcpIVDTWWQTETgGFMITPLPGATELKAGSATRPFFGVQPALVDNVGTpqegACEgnlvivdswPGQARTL 477
Cdd:PRK07638 273 IKNIFPYAK--LYEFYGASEL-SFVTALVDEESERRPNSVGRPFHNVQVRICNEAGE----EVQ---------KGEIGTV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 478 FGDHDRFEQTYFS--------TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:PRK07638 337 YVKSPQFFMGYIIggvlarelNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 550 IPHNIKGQAIYAYItlnHGEEPTPELyaevRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK07638 417 VPDSYWGEKPVAII---KGSATKQQL----KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
3.26e-27 |
|
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: 112.75 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNy 336
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 337 pgvnRLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMGSVGEPINPEAWEwyynKIGNAkcpivdTWW-- 414
Cdd:cd17637 79 ----EALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLRHVLGLDAPETIQRFE----ETTGA------TFWsl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 415 --QTETGGFmITPLPgATElKAGSATRPFFGVQPALVDN------VGTPQEGACEGNLVIVDSWPGQARTLFgdhdrfeq 486
Cdd:cd17637 143 ygQTETSGL-VTLSP-YRE-RPGSAGRPGPLVRVRIVDDndrpvpAGETGEIVVRGPLVFQGYWNLPELTAY-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 487 tyfsTFK-GMYFSGDGARRDEDGYYWITGRV--DDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYI 563
Cdd:cd17637 212 ----TFRnGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 727190822 564 TLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 288 VLKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-621 |
3.48e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.52 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 81 CLDRHLAERG----DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:PRK12316 4552 CVHQLVAERArmtpDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 157 AVHSVIFGGFSPEAVAGRIIDSNAKLVITADeglRAGRAVPLKKNVDdalknpgvvsvanVVVFQRTGKpgywqegrdlw 236
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQS---HLLQRLPIPDGLA-------------SLALDRDED----------- 4678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 237 WheltQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTfkyvfdyhdGDIYWCTADVGWVTGHSYL 316
Cdd:PRK12316 4679 W----EGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFS 4745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 317 -------LYGPLACGATTLMFEgvPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMaegdkaiEGTRRD----SLRIMGS 385
Cdd:PRK12316 4746 fdgshegLYHPLINGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLA-------EHAERDgeppSLRVYCF 4816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 386 VGEPINPEAW-EWY--------YNKIGNAKCPIVDTWWQTETGgfmitPLPGATELKAGsatRPFFGVQPALVDNVGTPQ 456
Cdd:PRK12316 4817 GGEAVAQASYdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIG---TPLGNRSGYVLDGQLNPL 4888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 457 EGACEGNLVIvdSWPGQARTLFGDHD----RFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK12316 4889 PVGVAGELYL--GGEGVARGYLERPAltaeRFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGE 4966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 532 IESALVSHPKIAEAAVVGIPHNIkGQAIYAYITLNHGE-EPTPELYAEVRNWVRKEIGPiATPDVL---HWT--DSLPKT 605
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPAlADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLT 5044
|
570
....*....|....*.
gi 727190822 606 RSGKIMRRILRKIAAG 621
Cdd:PRK12316 5045 PNGKLDRKALPQPDAS 5060
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
236-617 |
1.39e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 114.01 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 236 WWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAAMTFKYVFDYHDGDIYWCTAD--------V 307
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 GWVTGhsyllygpLACGATTLM---FEGVPNYPGVNRL----SQVIDKHQVNILYTAPtairalmAEGDkaiegtRRDSL 380
Cdd:PRK07867 211 GWAVA--------LAAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPE-------RPDD------ADNPL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 381 RIM-GSVGEPINPEAWEWYYNkignakCPIVDTWWQTEtGGFMITPLPGATElkaGSATRPFFGVQ-----------PAL 448
Cdd:PRK07867 270 RIVyGNEGAPGDIARFARRFG------CVVVDGFGSTE-GGVAITRTPDTPP---GALGPLPPGVAivdpdtgtecpPAE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 449 VDNVGTPQEGACEGNLVIVDSwPGQARTLFGDHDRFEQtyfSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLG 528
Cdd:PRK07867 340 DADGRLLNADEAIGELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 529 TAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNwVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATF 494
|
....*....
gi 727190822 609 KIMRRILRK 617
Cdd:PRK07867 495 KVLKRQLSA 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-620 |
1.64e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGL-RAGRAVPLKKNVDDalknpgvvsvanvvvfqrtgkpgywqegRDLWWhel 240
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLTQAHLLeQLPAPAGDTALTLD----------------------------RLDLN--- 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 tqGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVY-AAMTFKYVFDYHDGDIYWCTADVgwvTGHSYLLYG 319
Cdd:PRK12467 3224 --GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHlCWIAEAYELDANDRVLLFMSFSF---DGAQERFLW 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 320 PLACGATTLMFEGVPNYPgvNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiEGTrrdSLRIMGSVGEPINPEAWEWY- 398
Cdd:PRK12467 3299 TLICGGCLVVRDNDLWDP--EELWQAIHAHRISIACFPPAYLQQFAEDAGGA-DCA---SLDIYVFGGEAVPPAAFEQVk 3372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 399 --------YNKIGNAKCPIVDTWWQTETGGfmitpLPGATELKAGsatRPFFGVQPALVDNVGTPQEGACEGNLVIvdSW 470
Cdd:PRK12467 3373 rklkprglTNGYGPTEAVVTVTLWKCGGDA-----VCEAPYAPIG---RPVAGRSIYVLDGQLNPVPVGVAGELYI--GG 3442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 PGQARtlfGDH-------DRFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PRK12467 3443 VGLAR---GYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 543 AEAAVVGIPhNIKGQAIYAYITLNhgeEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12467 3520 REAVVLARD-GAGGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
89-618 |
1.75e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.42 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 89 RGDQTAIIwegddpTQSKKVTYKQLHHDVCQFANVLK-KLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:PRK06839 15 HPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 168 PEAVAGRIIDSNAKLVITADEglRAGRAVPLKKNVDDAlknpgvvsvanvvvfqrtgkPGYWQEGRDlwwhELTQGVSAD 247
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKT--FQNMALSMQKVSYVQ--------------------RVISITSLK----EIEDRKIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 248 CppEEVNAEDPLFILYTSGSTGKPKGVLhttggyLVYAAMTFKYVFDYHDGDIywcTADVGWVTGHSYLLYGPLACGATT 327
Cdd:PRK06839 143 F--VEKNESASFIICYTSGTTGKPKGAV------LTQENMFWNALNNTFAIDL---TMHDRSIVLLPLFHIGGIGLFAFP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 328 LMFEG----VPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLRimgsvgepinpeaweWYYNkiG 403
Cdd:PRK06839 212 TLFAGgviiVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVR---------------WFYN--G 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 404 NAKCPIV-------------DTWWQTETGG--FMITPLPGATelKAGSATRPFFGVQPALVDNVG--TPQEGACE----G 462
Cdd:PRK06839 273 GAPCPEElmrefidrgflfgQGFGMTETSPtvFMLSEEDARR--KVGSIGKPVLFCDYELIDENKnkVEVGEVGEllirG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 463 NLVIVDSWpgqartlfgdhDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PRK06839 351 PNVMKEYW-----------NRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDV 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 543 AEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK06839 420 YEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
91-616 |
2.16e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 113.70 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIwegDDptqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAvHSVIFG-GFSPE 169
Cdd:PRK13382 58 DRPGLI---DE---LGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 170 AVAGRIIDSNAKLVITADEglragravpLKKNVDDALKnpgvvsvanvvvfqrtGKPGY-----WQEGRDLWWHE-LTQG 243
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDEE---------FSATVDRALA----------------DCPQAtrivaWTDEDHDLTVEvLIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 244 VSADCPPEEVNAEDplFILYTSGSTGKPKGVLHTTGGylvyAAMTFKYVFDyhdgdiywctaDVGWVTGHSYLLYGPL-- 321
Cdd:PRK13382 186 HAGQRPEPTGRKGR--VILLTSGTTGTPKGARRSGPG----GIGTLKAILD-----------RTPWRAEEPTVIVAPMfh 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 322 ACGATTLMFEGVPNYPGVNRLS-------QVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEA 394
Cdd:PRK13382 249 AWGFSQLVLAASLACTIVTRRRfdpeatlDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 395 WEWYYNKIGNAkcpIVDTWWQTETGgfMITPlpgAT--ELKAGsatrpffgvqpalVDNVGTPQEGAcegNLVIVDSW-- 470
Cdd:PRK13382 329 VIAFMDQFGDV---IYNNYNATEAG--MIAT---ATpaDLRAA-------------PDTAGRPAEGT---EIRILDQDfr 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 ---PGQARTLFGDHDRFEQTYFS-----TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PRK13382 385 evpTGEVGTIFVRNDTQFDGYTSgstkdFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 543 AEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 465 AEAAVIGVDDEQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-622 |
1.03e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.90 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 aDEGLRagraVPLKKNVDDALKNPGVvsvanvvvfqrtgkpgywqegrdlwwheltQGVSADCPPEEVNAEDPLFILYTS 265
Cdd:PRK12316 3161 -QSHLR----LPLAQGVQVLDLDRGD------------------------------ENYAEANPAIRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYA-AMTFKYVFDYHDGDIYWCTADVgwvTGHSYLLYGPLACGATTLMfEGVPNYPGVNRLSQ 344
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLcWMQQAYGLGVGDRVLQFTTFSF---DVFVEELFWPLMSGARVVL-AGPEDWRDPALLVE 3281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 345 VIDKHQVNILYTAPTAIRALMAEGDKAiegtRRDSLRIMGSVGEPINPEAWEWYynkigNAKCPIVDTWWQTETGGFMIT 424
Cdd:PRK12316 3282 LINSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEATITVTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 425 PLPGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIvdSWPGQARTLFGDHD----RFEQTYFSTFKGMYFSGD 500
Cdd:PRK12316 3353 WQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYL--GGEGLARGYHNRPGltaeRFVPDPFVPGERLYRTGD 3430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 501 GARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYITLnhgEEPTPELYAEVR 580
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP---EDEAGDLREALK 3503
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 727190822 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 3504 AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-620 |
1.74e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 111.06 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIwegdDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADeGLRAGRAVPLKKNVDDALKN--PGVVSVANVVVFQRTGKPGYWQEGRDLWWHE 239
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD-GFKDSDYVAMLYELAPELATcePGQLQSARLPELRRVIFLGDEKHPGMLNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 240 LTQGVSADCPPE------EVNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAAMTFKY-------VFDYHdgdiy 301
Cdd:PRK08315 177 LLALGRAVDDAElaarqaTLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLTEedrlcipVPLYH----- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 302 wCtadVGWVTGHsyllygpLAC---GATTLMfegvPNyPGVNRLS--QVIDKHQVNILYTAPTAIRALMAEGDKAiegtR 376
Cdd:PRK08315 252 -C---FGMVLGN-------LACvthGATMVY----PG-EGFDPLAtlAAVEEERCTALYGVPTMFIAELDHPDFA----R 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 377 RD--SLR--IM-GSVgepinpeawewyynkignakCPI------VD---------TWWQTETGgfmitplPGAT------ 430
Cdd:PRK08315 312 FDlsSLRtgIMaGSP--------------------CPIevmkrvIDkmhmsevtiAYGMTETS-------PVSTqtrtdd 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 431 --ELKAGSATRPFFGVQPALVDN-------VGTPQEGACEGNLVIVDSWPGQART---LfgDHDRFeqtyfstfkgMYfS 498
Cdd:PRK08315 365 plEKRVTTVGRALPHLEVKIVDPetgetvpRGEQGELCTRGYSVMKGYWNDPEKTaeaI--DADGW----------MH-T 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 499 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaE 578
Cdd:PRK08315 432 GDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---D 508
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 727190822 579 VRNWVRkeiGPIA---TPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08315 509 VRDFCR---GKIAhykIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-615 |
4.07e-25 |
|
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: 109.34 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIwegDDPTQskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd05920 21 LARSAARHPDRIAVV---DGDRR---LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEglragravplkknvddalknpgvvsvanvvvfqrtgkpgywQEGRDlwWHELT 241
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDR-----------------------------------------HAGFD--HRALA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 QGVSADCPpeevnaeDPLFILYTSGSTGKPKGVLHTTGGYlVYAAMTFKYV--FDYHDgdIYWCTADVGwvtgHSYLLYG 319
Cdd:cd05920 132 RELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVcgLDQDT--VYLAVLPAA----HNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 320 P-----LACGATTLMfegVPNyPGVNRLSQVIDKHQVNILYTAPTAIRALMaegDKAIEGTRRD-SLRIMGSVGEPINPE 393
Cdd:cd05920 198 PgvlgtLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWL---DAAASRRADLsSLRLLQVGGARLSPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 394 AWEwyynKIGNAKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPffgVQP----ALVDNVGTPQEGACEGNLVivds 469
Cdd:cd05920 271 LAR----RVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEEGELL---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 470 wpgqAR---TLFG-----DHDrfeQTYFsTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:cd05920 340 ----TRgpyTIRGyyrapEHN---ARAF-TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 542 IAEAAVVGIPHNIKGQAIYAYITLNhgeePTPELYAEVRNWVRkEIGpIAT---PDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 412 VHDAAVVAMPDELLGERSCAFVVLR----DPPPSAAQLRRFLR-ERG-LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
106-616 |
1.55e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 107.79 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPeAVAGRII-DSNAKLVI 184
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA-PEADYIVgDSGARVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 T--ADEGLRAGRAVPLKKNVDDAlknpgvvsvanvvvfqrtgkpgywqeGRDLWWHELTQGVSADCPPEevnAEDPL--F 260
Cdd:PRK13390 102 AsaALDGLAAKVGADLPLRLSFG--------------------------GEIDGFGSFEAALAGAGPRL---TEQPCgaV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 261 ILYTSGSTGKPKGV--------LHTTGGYLVYAAMTFkyvFDYHDGDIYWCTADVGwvtgHSyllyGPL-------ACGA 325
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 326 TTLMfegVPNYPGVNRLSQvIDKHQVNILYTAPTAIRALMAEGDKAieGTRRD--SLRIMGSVGEPINPEAWEWYYNKIG 403
Cdd:PRK13390 222 TVVL---AKRFDAQATLGH-VERYRITVTQMVPTMFVRLLKLDADV--RTRYDvsSLRAVIHAAAPCPVDVKHAMIDWLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 404 nakcPIVDTWWQ-TETGGFMITPLPGATElKAGSATRPFFGVQPALVDnvgtpqegacEGNlvivDSWPGQARTLFGDHD 482
Cdd:PRK13390 296 ----PIVYEYYSsTEAHGMTFIDSPDWLA-HPGSVGRSVLGDLHICDD----------DGN----ELPAGRIGTVYFERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 483 RF--------EQTYFSTFKGMYF---SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK13390 357 RLpfrylndpEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 552 HNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-620 |
4.33e-24 |
|
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: 106.09 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERGDQTAI-IWEGDdptqskkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhSVI 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA-FVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 FGGFSPEAVAGRII-DSNAKLVITADeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwhelt 241
Cdd:cd05918 79 LDPSHPLQRLQEILqDTGAKVVLTSS------------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgvsadcppeevnAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAAMTFK----------------YVFDYHDGDIywc 303
Cdd:cd05918 105 -------------PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGralgltsesrvlqfasYTFDVSILEI--- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 304 tadvgwvtghsyllYGPLACGATTLmfegVP-NYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKaiegtrrdSLRI 382
Cdd:cd05918 166 --------------FTTLAAGGCLC----IPsEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPEDVP--------SLRT 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 383 MGSVGEPINPEawewyynkignakcpIVDTWWQ----------TETGGFMITPLPGATElKAGSATRPfFGVQPALVDN- 451
Cdd:cd05918 220 LVLGGEALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVPST-DPRNIGRP-LGATCWVVDPd 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 452 -------VGTPQEGACEGNLV----IVDswPGQARTLFGDHDRFEQTYFSTFKG-MYFSGDGARRDEDG--YYwiTGRVD 517
Cdd:cd05918 283 nhdrlvpIGAVGELLIEGPILargyLND--PEKTAAAFIEDPAWLKQEGSGRGRrLYRTGDLVRYNPDGslEY--VGRKD 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 518 DVLNVSGHRLGTAEIESALVSHP---KIAEAAVVGIPHNIKGQAIYAYITLNHGE-----------EPTPELY---AEVR 580
Cdd:cd05918 359 TQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQLVAFVVLDGSSsgsgdgdslflEPSDEFRalvAELR 438
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 727190822 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05918 439 SKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-617 |
5.00e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.51 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 87 AERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGF 166
Cdd:PRK12316 2014 ARAPEAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 167 SPEAVAGRIIDSNAKLVITaDEGLRAGRAVPlkknvddalknpgvvsvanvvvfqrTGKPGYWQEgRDLWWHELTQGVsa 246
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLT-QRHLLERLPLP-------------------------AGVARLPLD-RDAEWADYPDTA-- 2138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 247 dcPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-AMTFKYVFDYHDGDIYWCT-ADVGWVTGhsylLYGPLACG 324
Cdd:PRK12316 2139 --PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCqAAGERYELSPADCELQFMSfSFDGAHEQ----WFHPLLNG 2212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 ATTLMFEGVPNYPGvnRLSQVIDKHQVNILYTAPTAIRALMAEgdKAIEGtRRDSLRIMGSVGEPINPEAWEWYYNKIGN 404
Cdd:PRK12316 2213 ARVLIRDDELWDPE--QLYDEMERHGVTILDFPPVYLQQLAEH--AERDG-RPPAVRVYCFGGEAVPAASLRLAWEALRP 2287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 405 AKcpIVDTWWQTETggfMITPL---------PGATELKAGSAtrpfFGVQPALVDNVG---TPQEGAceGNLVIvdSWPG 472
Cdd:PRK12316 2288 VY--LFNGYGPTEA---VVTPLlwkcrpqdpCGAAYVPIGRA----LGNRRAYILDADlnlLAPGMA--GELYL--GGEG 2354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 473 QARTLFG----DHDRFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:PRK12316 2355 LARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 548 VGIpHNIKGQAIYAYITlnhGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 2435 VAQ-DGASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
243-616 |
5.53e-24 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 105.54 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 243 GVSADCPPEEVNAedPLFILYTSGSTGKPKGVLHTTGGYLVYAA--MTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGP 320
Cdd:cd05929 114 GGSPETPIEDEAA--GWKMLYSGGTTGRPKGIKRGLPGGPPDNDtlMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 321 LACGATTLMfegvPNYPGVNRLsQVIDKHQVNILYTAPTAIRALMAegdkaIEGTRRD-----SLRIMGSVGEPINPEA- 394
Cdd:cd05929 192 FMGGTLVLM----EKFDPEEFL-RLIERYRVTFAQFVPTMFVRLLK-----LPEAVRNaydlsSLKRVIHAAAPCPPWVk 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 395 -----------WEWYYNKIGNAKCPIVDTWWQTEtggfmitplpgatelkAGSATRPFFGVQpALVDNVGTPQEGACEGN 463
Cdd:cd05929 262 eqwidwggpiiWEYYGGTEGQGLTIINGEEWLTH----------------PGSVGRAVLGKV-HILDEDGNEVPPGEIGE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 464 LVIVDSWPgqartlFGDHDRFEQTYFSTFKGMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:cd05929 325 VYFANGPG------FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKV 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 543 AEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 399 LDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
6.67e-24 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 102.87 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYaamtfkyvFDYHDGDIYWCTADVGWVTG---HSYLLYGPLACGATTLMFEGV 333
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGAISALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 PNYpGVNRLSQVIDKHQVNILYTAPTAIRALmaegdkAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVDTW 413
Cdd:cd17633 73 RKF-NPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKAN--LIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 414 WQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDN---------VGTPQ--EGACEGNLVIVDSWpgqartlfgdhd 482
Cdd:cd17633 144 GTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNAdggeigkifVKSEMvfSGYVRGGFSNPDGW------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 483 rfeqtyFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAY 562
Cdd:cd17633 210 ------MSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 727190822 563 ITlnhGEEPTpelYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 277 YS---GDKLT---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-615 |
1.65e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.78 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 105 SKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVI 184
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 TADEGLRAgraVPLKKNVDDALKNPgvvsvanvvvfqrtgkPGYWQEGRDlwwheltqgvsaDCPPEEVNAEDPL-FILY 263
Cdd:PRK12467 1677 TQSHLQAR---LPLPDGLRSLVLDQ----------------EDDWLEGYS------------DSNPAVNLAPQNLaYVIY 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 264 TSGSTGKPKGVLHTTGGYL-VYAAMTFKYVFdyhdgdiywCTADVgWVTGHSYL-------LYGPLACGATTLMfegVPn 335
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVnRLCATQEAYQL---------SAADV-VLQFTSFAfdvsvweLFWPLINGARLVI---AP- 1791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 336 yPGVNR----LSQVIDKHQVNILYTAPTAIRALMaEGDKAIEGTRrdSLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVD 411
Cdd:PRK12467 1792 -PGAHRdpeqLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHPL--SLRRVVCGGEALEVEALRPWLERLPDTG--LFN 1865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 412 TWWQTETggfMITPLPGATELK--AGSATRPfFGVQPA-----LVDNVGTPQEGACEGNLVIvdSWPGQARtlfGDH--- 481
Cdd:PRK12467 1866 LYGPTET---AVDVTHWTCRRKdlEGRDSVP-IGQPIAnlstyILDASLNPVPIGVAGELYL--GGVGLAR---GYLnrp 1936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 482 ----DRFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVvgIPHN-IK 555
Cdd:PRK12467 1937 altaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgAN 2014
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 556 GQAIYAYIT-----LNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK12467 2015 GKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-625 |
1.85e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 104.92 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 48 WIKPYTKVKNTSFDPGHVSIrwfeDGTLNLAANCLDRHlaERGDQTAIIwegdDPTQSKKVTYKQLHHDVCQFANVL-KK 126
Cdd:PLN02574 17 WYSPETGIYSSKHPPVPLPS----DPNLDAVSFIFSHH--NHNGDTALI----DSSTGFSISYSELQPLVKSMAAGLyHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 127 LGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEglRAGRAVPLKKNVDDAL 206
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPE--NVEKLSPLGVPVIGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 207 KNpgvvsvanvvvfqrtgkpGYWQEGRDLW--WHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVY 284
Cdd:PLN02574 165 EN------------------YDFDSKRIEFpkFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 285 AAMTFKY---VFDYHDGD-IYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnypGVNRLSQVIDKHQVNILYTAPTA 360
Cdd:PLN02574 227 VELFVRFeasQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 361 IRALMAEGdKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIgnakcPIVDTwwqteTGGFmitplpGATElKAGSATRP 440
Cdd:PLN02574 303 LMALTKKA-KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDF-----IQGY------GMTE-STAVGTRG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 441 FFGVQPALVDNVG--TPQEGAcegnlVIVDsW-------PGQARTLFGDHDRFEQTYFSTFKGMYFS---------GDGA 502
Cdd:PLN02574 365 FNTEKLSKYSSVGllAPNMQA-----KVVD-WstgcllpPGNCGELWIQGPGVMKGYLNNPKATQSTidkdgwlrtGDIA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNW 582
Cdd:PLN02574 439 YFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINY 515
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 727190822 583 VRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PLN02574 516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
106-617 |
3.29e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 103.91 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhsviFGGFSPEAVAGRIID----SNAK 181
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEIKKqaeaAGAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 182 LVITADEGLRAGRAVPLKKNVDDALKNPGVVSvanvvvfqrtgkpgywqegrdlwWHELTQG---VSADCPPEEVNAEDP 258
Cdd:PLN02330 130 LIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVN-----------------------WKELLEAadrAGDTSDNEEILQTDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 259 LFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIywctADVGWVTghSYLLYGPLACGATTLMFEG---VPN 335
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIP--FFHIYGITGICCATLRNKGkvvVMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 336 YPGVNRLSQVIDKHQVNILYTAPTAIRALMAegDKAIE--GTRRDSLRIMGSVGEPINPEAWEWYYNKIGNAKcpIVDTW 413
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEefDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQ--VQEAY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 414 WQTETGgfMITPLPGATELKAGSATRPFFG-VQPALVDNVGTPQEGacegnLVIVDSWPGQ--ART---LFGDHDRFEQT 487
Cdd:PLN02330 337 GLTEHS--CITLTHGDPEKGHGIAKKNSVGfILPNLEVKFIDPDTG-----RSLPKNTPGElcVRSqcvMQGYYNNKEET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 488 YFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLN 566
Cdd:PLN02330 410 DRTIDEdGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 727190822 567 HGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 490 PKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
121-628 |
7.08e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.91 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 121 ANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI---FGGFSPEAVAGRiidSNAKLVITADEGLRAGRAVP 197
Cdd:PRK06155 60 AHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPIntaLRGPQLEHILRN---SGARLLVVEAALLAALEAAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 198 lkknvddalknPGvvsvanvvvfqRTGKPGYWQEGRDLWWHeLTQGVS--------ADCPPEEVNAEDPLFILYTSGSTG 269
Cdd:PRK06155 137 -----------PG-----------DLPLPAVWLLDAPASVS-VPAGWStaplppldAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 270 KPKGVLHTTGGYLVYAAMTFKyVFDYHDGDIYWCTADVGWVTGHSyLLYGPLACGATTLM---FEGVPNYPGVNRlsqvi 346
Cdd:PRK06155 194 PSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVLeprFSASGFWPAVRR----- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 347 dkHQVNILYTAPTAIRALMAEgdKAIEGTRRDSLRIMGSVGEPinPEAWEWYYNKIGnakCPIVDTWWQTETGGFMITPL 426
Cdd:PRK06155 267 --HGATVTYLLGAMVSILLSQ--PARESDRAHRVRVALGPGVP--AALHAAFRERFG---VDLLDGYGSTETNFVIAVTH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 427 PgatELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWPGQ-ARTLFGDHdrfEQTyFSTFKGMYF-SGDGARR 504
Cdd:PRK06155 338 G---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAfATGYFGMP---EKT-VEAWRNLWFhTGDRVVR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVR 584
Cdd:PRK06155 411 DADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV---ALVRHCE 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 727190822 585 KEIGPIATPDVLHWTDSLPKTRSGKIMRRILRkiAAGDTSNLGD 628
Cdd:PRK06155 488 PRLAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQGVTADTWD 529
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
117-616 |
7.71e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 102.47 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 117 VCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAK-LVITAD--EGLRAg 193
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARvLIAHADllHGLAS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 194 rAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGY--WQEgrdlwWheLTQGVSADCPPeevnAEDPLFILYTSGSTGKP 271
Cdd:PRK12406 100 -ALPAGVTVLSVPTPPEIAAAYRISPALLTPPAGAidWEG-----W--LAQQEPYDGPP----VPQPQSMIYTSGTTGHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 272 KGVLH---TTGGYLVYAAMTfkyvfdyhdGDIYwctadvGWVTGHSYLLYGPlacgattlMFEGVPNYPGVN-------- 340
Cdd:PRK12406 168 KGVRRaapTPEQAAAAEQMR---------ALIY------GLKPGIRALLTGP--------LYHSAPNAYGLRagrlggvl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 341 ---------RLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAwewyynkignaKCPIVD 411
Cdd:PRK12406 225 vlqprfdpeELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV-----------KRAMIE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 412 tWWqtetgGFMITPLPGATEL-------------KAGSATRPFFGVQPALVDNVGTPQEGACEGNlvIVDSWPGQArtLF 478
Cdd:PRK12406 294 -WW-----GPVIYEYYGSTESgavtfatsedalsHPGTVGKAAPGAELRFVDEDGRPLPQGEIGE--IYSRIAGNP--DF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 479 GDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQA 558
Cdd:PRK12406 364 TYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 559 IYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 444 LMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
107-617 |
8.37e-23 |
|
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: 102.51 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 107 KVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITA 186
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 DEGLR-AGRAVPLKKNVDDalkNPGVVSVANV-VVFQRTGKPGYWqegrdlwwheltqgvsadcPPEEVNAEDPLFILYT 264
Cdd:cd05915 104 PNLLPlVEAIRGELKTVQH---FVVMDEKAPEgYLAYEEALGEEA-------------------DPVRVPERAACGMAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGVLHT-TGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLlYGPLACGATTLMFEGVPNYpgvNRLS 343
Cdd:cd05915 162 TGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLDP---ASLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 344 QVIDKHQVNILYTAPTAIRaLMAEGDKAIEGTRRDSLRIMGSVGEPinPEAWeWYYNKIGNAK------CPIV-----DT 412
Cdd:cd05915 238 ELFDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVEvrqgygLTETspvvvQN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 413 WWQTEtggFMITPLPGATELKAGSATRPFFGVQPAL-VDNVGTPQEG------ACEGNLVIvdswpgqaRTLFGDHDRFE 485
Cdd:cd05915 314 FVKSH---LESLSEEEKLTLKAKTGLPIPLVRLRVAdEEGRPVPKDGkalgevQLKGPWIT--------GGYYGNEEATR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 486 QTYFStfKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITL 565
Cdd:cd05915 383 SALTP--DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 727190822 566 NHGEEPTPELYaevrNWVRKEIGPIAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 461 RGEKPTPEELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
9.90e-23 |
|
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: 100.03 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDyhdgdiyWCTADVGWVTGHSYLLYGpLACGATTLMFEGV-- 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 --PNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRrdSLRIMGSVGE-PINPEAWEWYYNKIGNakcpIV 410
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADVRFIEATGLTN----TA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 411 DTWWQTETGGFMITPLpGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSWpgqarTLFGDHDRFEQTYFS 490
Cdd:cd17635 147 QVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 491 TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNhgEE 570
Cdd:cd17635 221 LIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 727190822 571 PTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
249-616 |
2.25e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 100.83 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 249 PPEEVNAEDPLFILYTSGSTGKPKGVLhttggyLVYAAMTfkyvfdyhdGDI-------YWCTADV-----------GWV 310
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVV------LSRRAIA---------ADLdalaeawQWTADDVlvhglplfhvhGLV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 311 TGhsylLYGPLACGAT--------------------TLMFeGVPNYpgvnrLSQVIDkhqvnilytAPTAIRALmaegdk 370
Cdd:PRK07787 186 LG----VLGPLRIGNRfvhtgrptpeayaqalseggTLYF-GVPTV-----WSRIAA---------DPEAARAL------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 371 aiegtRRDSLRIMGSVGEPInPEawewyYNKIGNAKC-PIVDTWWQTETggFMITPLPGATELKAGSATRPFFGVQPALV 449
Cdd:PRK07787 241 -----RGARLLVSGSAALPV-PV-----FDRLAALTGhRPVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 450 DNVGT--PQEGACEGNLVIvdswpgQARTLF-GDHDRFEQTYFS-TFKGMYFSGDGARRDEDGYYWITGRVD-DVLNVSG 524
Cdd:PRK07787 308 DEDGGpvPHDGETVGELQV------RGPTLFdGYLNRPDATAAAfTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 525 HRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITlnHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPK 604
Cdd:PRK07787 382 YRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALPR 456
|
410
....*....|..
gi 727190822 605 TRSGKIMRRILR 616
Cdd:PRK07787 457 NAMGKVLKKQLL 468
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-621 |
2.74e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 101.24 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 76 NLAANCLDRHLAERGDQ-TAIIWEGDDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQpEAIALRRCDGTSA--LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 155 IGAVHSVIFGGFSPEAVA--GRIIDSNAKLVitaDEGLRAGravplkknvddALKNPGVVSVANVVVFQRTGKPGYWQEG 232
Cdd:PRK05857 89 LGAIAVMADGNLPIAAIErfCQITDPAAALV---APGSKMA-----------SSAVPEALHSIPVIAVDIAAVTRESEHS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 233 RDLwwheltqgvsaDCPPEEVN--AEDPLFILYTSGSTGKPKGVLhttggylvYAAMTFKYVFD-YHDGDIYWctadVGW 309
Cdd:PRK05857 155 LDA-----------ASLAGNADqgSEDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VTW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 310 VTGHSylLYGPLACG--------ATTLMFEGVPNYPGVNRLS--QVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDS 379
Cdd:PRK05857 212 VVGET--TYSPLPAThigglwwiLTCLMHGGLCVTGGENTTSllEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 380 LRIMGSVGEpinpEAWEWYYNKIGNAKCPIVDTWWQTETGGFMITpLPGATE----LKAGSATRPFFGVQPALVD----- 450
Cdd:PRK05857 288 LRLVGYGGS----RAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPTDDGsivkIEAGAVGRPYPGVDVYLAAtdgig 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 451 -NVGTPQEGACEGNLvivdsWPGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK05857 363 pTAPGAGPSASFGTL-----WIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAP 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 530 AEIESALVSHPKIAEAAVVGIPHN----IKGQAIYAYITLNhgEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKT 605
Cdd:PRK05857 438 DEVDRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRT 515
|
570
....*....|....*.
gi 727190822 606 RSGKIMRRILRKIAAG 621
Cdd:PRK05857 516 QSGKVMRASLAAAATA 531
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
3.02e-22 |
|
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: 99.94 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG------QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITadeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcpp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 eevNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAAMTFKYVFDYHDGDIYWCTADVGWvTGHSYLLYGPLACGATTL 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 329 MFEGVPNYpGVNRLSQVIDKHQVNILYTaPTAIralmAEGDKAIEGTrrdSLRIMGSVGEPINPEAWEWY--YNKIGNAK 406
Cdd:cd17645 175 VVPSERRL-DLDALNDYFNQEGITISFL-PTGA----AEQFMQLDNQ---SLRVLLTGGDKLKKIERKGYklVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 407 CPIVDTwwqtetgGFMITPLPGATelkagSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSwpGQARTLFGDHD---- 482
Cdd:cd17645 246 NTVVAT-------SFEIDKPYANI-----PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNRPEltae 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 483 RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAY 562
Cdd:cd17645 312 KFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 727190822 563 ITLNhgEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 392 VTAP--EEIPHE---ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
91-621 |
6.91e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 100.09 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWegddptQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PLN03102 29 NRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALKNP-----GVVSVANVVVFQRTGKPGYWQEGrdlwwhELTQGVS 245
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLpvifiHEIDFPKRPSSEELDYECLIQRG------EPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 246 ADCPPEEvNAEDPLFILYTSGSTGKPKGVLHT-TGGYLVyaamTFKYVFDYHDG--DIYWCTADV----GWVtghsyLLY 318
Cdd:PLN03102 177 ARMFRIQ-DEHDPISLNYTSGTTADPKGVVIShRGAYLS----TLSAIIGWEMGtcPVYLWTLPMfhcnGWT-----FTW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 319 GPLACGATTLMFEGVPnypgVNRLSQVIDKHQVNILYTAPTAIRALMaEGDKAIEGTRRDSLRIMGSVGEPinPEAWEWY 398
Cdd:PLN03102 247 GTAARGGTSVCMRHVT----APEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAALVKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 399 YNKIG----------NAKCPIVDTWWQTETGGFmitPLPGATELKAGSATRpFFGVQPALVDNVGT----PQEGACEGNL 464
Cdd:PLN03102 320 VQRLGfqvmhaygltEATGPVLFCEWQDEWNRL---PENQQMELKARQGVS-ILGLADVDVKNKETqesvPRDGKTMGEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 465 VIVDSwpgqarTLFGDHDRFEQTYFSTFK-GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PLN03102 396 VIKGS------SIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 544 EAAVVGIPHNIKGQAIYAYITLNHGEEPTPE----LYAEVRN---WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03102 470 ETAVVAMPHPTWGETPCAFVVLEKGETTKEDrvdkLVTRERDlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
....*
gi 727190822 617 KIAAG 621
Cdd:PLN03102 550 DIAKG 554
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
1.26e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.81 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 79 ANCLDRHLAERGDQTAIIWEGDdptqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVVTAD----RIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGGFSPEAVAGRIIDSNAKLVITADEG-----LRAGRAVPLKKNVDdalKNPGVVSVANVVVFQRTGKPgywqegr 233
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVVLIDADGphdraEPTTRWWPLTVNVG---GDSGPSGGTLSVHLDAATEP------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 dlwwhelTQGVSAdcpPEEVNAEDPLfILYTSGSTGKPKGVLHTTGGYlvyAAMTFKYVFDYHDGDIYWCTADVGWVTGH 313
Cdd:PRK05852 165 -------TPATST---PEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 314 syllyGPLACGATTLMFEGVPNYPGVNRLSQVI---DKHQVN-ILYTA-PTAIRALMAEGDKAIEGTRRDSLRIMGSVGE 388
Cdd:PRK05852 231 -----GLIAALLATLASGGAVLLPARGRFSAHTfwdDIKAVGaTWYTAvPTIHQILLERAATEPSGRKPAALRFIRSCSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 389 PINPEAWEWYYNKIGnakCPIVDTWWQTET---------GGFMITPLPGATELKAGSATrpffGVQPALVDNVGTPQEGA 459
Cdd:PRK05852 306 PLTAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 460 CEGNLVIvdSWPGQARTLFGDHdrfEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH 539
Cdd:PRK05852 379 AVGEVWL--RGTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASH 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727190822 540 PKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK05852 454 PNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
1.48e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 98.95 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 237 WHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-AMTFKYvfDYHDGDIYWCTADVGwvtgHS- 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 315 --YLLYGP-LACGATTLMfegVPNYPGVNRLSQViDKHQVNILYTAPTAIRALMAEGDKAIEGTRRdsLRImgSVGEPIN 391
Cdd:PRK13388 205 avMAGWAPaVASGAAVAL---PAKFSASGFLDDV-RRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 392 PEAWEWYYNKIGnakCPIVDTWWQTETGGfMITPLPGATElkaGSATRPFFGVQ-----------PALVDNVGT---PQE 457
Cdd:PRK13388 277 PRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPGTPP---GSIGRGAPGVAiynpetltecaVARFDAHGAllnADE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 458 GACEgnlvIVDSwpgQARTLF--------GDHDRFEQtyfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK13388 350 AIGE----LVNT---AGAGFFegyynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 530 AEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNwVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:PRK13388 416 APIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRIAADLPSTATNK 494
|
....*..
gi 727190822 610 IMRRILR 616
Cdd:PRK13388 495 VLKRELI 501
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
2.22e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 98.41 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEglragravplkknVDDALKNPGVVSVANVVVFQRTGKPGYWQEG-RDLwwHEL 240
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEE-------------LVEAFEEARADLARPPRLWVAGGDTLDDPEGyEDL--AAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 TQGVSADCPPE--EVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMtFKYVFDYHDGDIYWCTadvgwvtghsyL-L 317
Cdd:PRK08279 182 AAGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG-FGGLLRLTPDDVLYCC-----------LpL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 318 Y---GPLACGATTLMFEGvpnypgvnrlSQVIDKH--------QVnILYTApTAI-------RALMAEGDKAIEgtRRDS 379
Cdd:PRK08279 250 YhntGGTVAWSSVLAAGA----------TLALRRKfsasrfwdDV-RRYRA-TAFqyigelcRYLLNQPPKPTD--RDHR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 380 LRIMgsVGEPINPEAWEwyynkignakcpivdtWWQTETGGFMITPLPGATEL---------KAGSATR-PFFGVQP-AL 448
Cdd:PRK08279 316 LRLM--IGNGLRPDIWD----------------EFQQRFGIPRILEFYAASEGnvgfinvfnFDGTVGRvPLWLAHPyAI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 449 V----DNvGTPQEGAcEGNLVIVDswPGQARTLFGD---------------------HDRFEQ--TYFSTfkgmyfsGDG 501
Cdd:PRK08279 378 VkydvDT-GEPVRDA-DGRCIKVK--PGEVGLLIGRitdrgpfdgytdpeasekkilRDVFKKgdAWFNT-------GDL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 502 ARRDEDGYYWITGRVDDVL-----NVSghrlgTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYAYITLNHGEEPTP-E 574
Cdd:PRK08279 447 MRDDGFGHAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDLaA 521
|
....*.
gi 727190822 575 LYAEVR 580
Cdd:PRK08279 522 LAAHLY 527
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-617 |
3.92e-21 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 96.61 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 83 DRHLAERGDQTAIiwegDDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:cd17653 4 ERIAAAHPDAVAV----ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 FGGfSPEAVAGRIID-SNAKLVITADeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwhelt 241
Cdd:cd17653 78 DAK-LPSARIQAILRtSGATLLLTTD------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgvsadcppeevNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA---------------AMTFKYVFDYHDGDIYwctad 306
Cdd:cd17653 103 ------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsqpparldvgpgsrvAQVLSIAFDACIGEIF----- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 307 vgwvtghSYLLYGplacgaTTLMFEGVPNYpgvnrLSQVIDKhqVNILYTAPTAIRALmaegdkaiEGTRRDSLRIMGSV 386
Cdd:cd17653 166 -------STLCNG------GTLVLADPSDP-----FAHVART--VDALMSTPSILSTL--------SPQDFPNLKTIFLG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 387 GEPINP---EAWEW---YYNKIGNAKCPIVDTWWQTETGGFMI--TPLPGATE--LKAgsatrpffGVQPALVDNVGTpq 456
Cdd:cd17653 218 GEAVPPsllDRWSPgrrLYNAYGPTECTISSTMTELLPGQPVTigKPIPNSTCyiLDA--------DLQPVPEGVVGE-- 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 457 egacegnlvIVDSWPGQARTLFGDH----DRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:cd17653 288 ---------ICISGVQVARGYLGNPaltaSKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 533 ESALVSHPKIAEAAVVgIPHNikgQAIYAYItlnhgeepTPELYAE--VRNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17653 359 EEVVLQSQPEVTQAAA-IVVN---GRLVAFV--------TPETVDVdgLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
....*..
gi 727190822 611 MRRILRK 617
Cdd:cd17653 427 DRKALRE 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-621 |
1.29e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 233 RDLWWHELTQGVSADCPPEEVNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVfDYHDGDIYWCTADVGWVT 311
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTASQSFDI 3923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 312 GHSYLLYGPLACGATTLMFEGVPNYPGvNRLSQVIDKhQVNILYTAPTAIRALMAEGDKAIegtrrDSLRIMGSVGEPIN 391
Cdd:PRK05691 3924 SVWQFLAAPLFGARVEIVPNAIAHDPQ-GLLAHVQAQ-GITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMP 3996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 392 PE-AWEWY--YNKIG--NAKCPI----------VDTwwQTETGGFmitplpgateLKAGSATRP----FFGVQPALVdnv 452
Cdd:PRK05691 3997 PElARQWLqrYPQIGlvNAYGPAecsddvaffrVDL--ASTRGSY----------LPIGSPTDNnrlyLLDEALELV--- 4061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 453 gtPQeGACeGNLVIVDSwpGQARTLFGDHDRFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK05691 4062 --PL-GAV-GELCVAGT--GVGRGYVGDPLRTALAFVPHPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRI 4135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 528 GTAEIESALVSHPKIAEAAvVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRS 607
Cdd:PRK05691 4136 ELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNAN 4214
|
410
....*....|....
gi 727190822 608 GKIMRRILRKIAAG 621
Cdd:PRK05691 4215 GKLDRKALPALDIG 4228
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
107-617 |
1.30e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.97 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 107 KVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITa 186
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 187 DEGLragraVPLKKNVDDALKN-PGVVSVANVVVFQRTGKPGYwqegrdLWWHELTQGVSADCPPEEVNAEDPLFILYTS 265
Cdd:PRK06018 118 DLTF-----VPILEKIADKLPSvERYVVLTDAAHMPQTTLKNA------VAYEEWIAEADGDFAWKTFDENTAAGMCYTS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYAAMTfkyvfdyHDGDIYWCTA-DV-----------GWVTGHSyllyGPlACGATTLMfegv 333
Cdd:PRK06018 187 GTTGDPKGVLYSHRSNVLHALMA-------NNGDALGTSAaDTmlpvvplfhanSWGIAFS----AP-SMGTKLVM---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 pnyPGVN----RLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLRiMGSVGEPINPEAWEWYYNKIGnakCPI 409
Cdd:PRK06018 251 ---PGAKldgaSVYELLDTEKVTFTAGVPTVWLMLLQYMEK--EGLKLPHLK-MVVCGGSAMPRSMIKAFEDMG---VEV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 410 VDTWWQTETggfmiTPLPGATELKAGSAT--------------RPFFGVQPALVDNVGT--PQEGACEGNLVIvdSWPGQ 473
Cdd:PRK06018 322 RHAWGMTEM-----SPLGTLAALKPPFSKlpgdarldvlqkqgYPPFGVEMKITDDAGKelPWDGKTFGRLKV--RGPAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 474 ARTLF--GDHDRFEQTYFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK06018 395 AAAYYrvDGEILDDDGFFDT-------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 552 HNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 468 HPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
1.55e-20 |
|
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: 93.60 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDyHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 336 YPGV-----NRLS-----QVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNKIGNA 405
Cdd:cd05924 82 GGQTvvlpdDRFDpeevwRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 406 KcpIVDTWWQTETGGFMItplpgATELKAGSATRPFFGVQP--ALVDNVGTPQEGACEGnlvivdswPGQ-ART------ 476
Cdd:cd05924 162 T--LVDAFGSSETGFTGS-----GHSAGSGPETGPFTRANPdtVVLDDDGRVVPPGSGG--------VGWiARRghiplg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 477 LFGDHDRFEQTYFSTFKGMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIK 555
Cdd:cd05924 227 YYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 727190822 556 GQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 307 GQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
31-81 |
3.90e-20 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 84.06 E-value: 3.90e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 727190822 31 SVQDPEAFWGEHGKILDWIKPYTKVKNTSFDPGhvsIRWFEDGTLNLAANC 81
Cdd:pfam16177 8 SIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
76-616 |
4.22e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 94.71 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 76 NLAAnCLDRHLAERGdqtaiiWEgDDPT--QSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:PRK06060 5 NLAG-LLAEQASEAG------WY-DRPAfyAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 154 RIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADeglragravPLKKNvddalknpgvvsvanvvvFQrtgkPGYWQEGR 233
Cdd:PRK06060 77 ARGVMAFLANPELHRDDHALAARNTEPALVVTSD---------ALRDR------------------FQ----PSRVAEAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 234 DLWwHELTQGVSADCPPeeVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIYWCTADVGWVTGH 313
Cdd:PRK06060 126 ELM-SEAARVAPGGYEP--MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 314 SYLLYGPLACGATTLMfEGVPnyPGVNRLSQVIDKHQVNILYTAPTairaLMAEGDKAIEGTRRDSLRIMGSVGEPINPE 393
Cdd:PRK06060 203 GNSVWFPLATGGSAVI-NSAP--VTPEAAAILSARFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALELG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 394 AWEWYYNKIGNakCPIVDTWWQTETGGFMITPlpGATELKAGSATRPFFGVQPALVDNVGTPQEGACEGNL-----VIVD 468
Cdd:PRK06060 276 LAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLwvrgpAIAK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 469 SWPGQARTLFGDHDRFEqtyfstfkgmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:PRK06060 352 GYWNRPDSPVANEGWLD------------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVV 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 549 GIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 420 AVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
104-612 |
6.32e-20 |
|
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: 93.28 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 104 QSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLV 183
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 184 ITADEglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnaEDPLFILY 263
Cdd:cd05914 84 FVSDE-------------------------------------------------------------------DDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 264 TSGSTGKPKGVLHTTGGYLVYAAMTFKYVFdYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTL--------------M 329
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkipsakiialaF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 330 FEGVPNYpGVNRLSQVIDKHQVNI------------LYTAPTAIRALMAEGDKAIE--GTRrdsLRIMGSVGEPINPEAW 395
Cdd:cd05914 176 AQVTPTL-GVPVPLVIEKIFKMDIipkltlkkfkfkLAKKINNRKIRKLAFKKVHEafGGN---IKEFVIGGAKINPDVE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 396 EWYYnKIGnakCPIVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVDNVGTPQEGA--CEGNLVIVDSWPGQ 473
Cdd:cd05914 252 EFLR-TIG---FPYTIGYGMTETAPIISYSPPN--RIRLGSAGKVIDGVEVRIDSPDPATGEGEiiVRGPNVMKGYYKNP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 474 ARTlfgdhdrfeQTYFsTFKGMYFSGDGARRDEDGYYWITGRVDDV-LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd05914 326 EAT---------AEAF-DKDGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 553 NIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGpIATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 396 KLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
7.48e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.47 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 70 FEDGTLNLAANC--------LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 142 VPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT--------ADEGLRAGRAVPLKKNVDDALKNPGVVS 213
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVdtefaevaREALALLPGPKPLVIDVDDPEYPGGRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 214 VANV-VVFQRTGKPGY-WQEGRDLWwheltqgvsadcppeevnaeDPLFILYTSGSTGKPKGVL-HTTGGYLvyAAMTFK 290
Cdd:PRK08162 158 GALDyEAFLASGDPDFaWTLPADEW--------------------DAIALNYTSGTTGNPKGVVyHHRGAYL--NALSNI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 291 YVFDYHDGDIY-W------CTadvGWvtghsyllygplaCGATTLMFEGvpnypGVN---------RLSQVIDKHQVNIL 354
Cdd:PRK08162 216 LAWGMPKHPVYlWtlpmfhCN---GW-------------CFPWTVAARA-----GTNvclrkvdpkLIFDLIREHGVTHY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 355 YTAPTAIRALMAEGDKAIEGTRRdslRIMGSVGEPINPEAwewyynKIGnakcpivdtwwQTETGGFMITPLPGATEL-- 432
Cdd:PRK08162 275 CGAPIVLSALINAPAEWRAGIDH---PVHAMVAGAAPPAA------VIA-----------KMEEIGFDLTHVYGLTETyg 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 433 -------KAGSATRPFF---------GVQPALVD--NVGTPQ-------------EGACEGNLVIvdswpgqartlfgdh 481
Cdd:PRK08162 335 patvcawQPEWDALPLDeraqlkarqGVRYPLQEgvTVLDPDtmqpvpadgetigEIMFRGNIVM--------------- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 482 drfeQTYF-------STFKGMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:PRK08162 400 ----KGYLknpkateEAFAGGWFhTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 554 IKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 476 KWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
103-617 |
7.67e-20 |
|
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: 92.88 E-value: 7.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 103 TQSKKVTYKQLHHDVCQFANVLKK-LGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAK 181
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 182 LVItadeglragravplkknVDDalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnaEDPLFI 261
Cdd:cd05937 81 FVI-----------------VDP---------------------------------------------------DDPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 262 LYTSGSTGKPKGVLHTTGGYLVyAAMTFKYVFDYHDGD-IYWCTAdvgwvtghsylLY---GPLACGATTLMFEGV---- 333
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDrTYTCMP-----------LYhgtAAFLGACNCLMSGGTlals 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 334 PNYPGVNRLSQVIDKHQVNILYTAPTaIRALMAeGDKAIEgTRRDSLRIMgsVGEPINPEAWEWYYNKIGnakCPIVD-- 411
Cdd:cd05937 161 RKFSASQFWKDVRDSGATIIQYVGEL-CRYLLS-TPPSPY-DRDHKVRVA--WGNGLRPDIWERFRERFN---VPEIGef 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 412 --------TWWQTETGGFMItplpGATELKaGSATRPFFGVQPALV-------DNVGTPQEGACE-------GNLVI--- 466
Cdd:cd05937 233 yaategvfALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVkmdpetdDPIRDPKTGFCVrapvgepGEMLGrvp 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 ---VDSWPG--------QARTLfgdHDRFEqtyfstfKG-MYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:cd05937 308 fknREAFQGylhnedatESKLV---RDVFR-------KGdIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVA 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 534 SALVSHPKIAEAAVVGI--PHNiKGQAIYAYITL-NHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:cd05937 378 DVLGAHPDIAEANVYGVkvPGH-DGRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQ 456
|
....*..
gi 727190822 611 MRRILRK 617
Cdd:cd05937 457 QKGVLRD 463
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
93-620 |
1.64e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.63 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 93 TAIIWEGDDPTQS---KKVTYKQLHHDVCQFAN-VLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:PRK08751 33 TSVAKFADRPAYHsfgKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 169 EAVAGRIIDSNAKLVITADEGLRAGRAV----PLKK----NVDDALKNPGVVSVANVVVFQRTGKPGYWQEGRDLWWHEL 240
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNFGTTVQQViadtPVKQvittGLGDMLGFPKAALVNFVVKYVKKLVPEYRINGAIRFREAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 TQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGV-----------------LHTTGGYLVYAAMTFKYVFDYHdgdIYWC 303
Cdd:PRK08751 193 ALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAmlthrnlvanmqqahqwLAGTGKLEEGCEVVITALPLYH---IFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 304 TADvGWV----TGHSYLLYGP----------------LACGATTLmFEGVPNYPGVNRlsqvIDKHQVNILYTAPTAIRA 363
Cdd:PRK08751 270 TAN-GLVfmkiGGCNHLISNPrdmpgfvkelkktrftAFTGVNTL-FNGLLNTPGFDQ----IDFSSLKMTLGGGMAVQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 364 LMAEGDKAIEGTrrdslrimgsvgepinpeawewyynkignakcPIVDTWWQTETG-GFMITPLpgatELKA--GSATRP 440
Cdd:PRK08751 344 SVAERWKQVTGL--------------------------------TLVEAYGLTETSpAACINPL----TLKEynGSIGLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 441 FFGVQPALVDNVGTPQEGACEGNLVIvdswpGQARTLFGDHDRFEQT-YFSTFKGMYFSGDGARRDEDGYYWITGRVDDV 519
Cdd:PRK08751 388 IPSTDACIKDDAGTVLAIGEIGELCI-----KGPQVMKGYWKRPEETaKVMDADGWLHTGDIARMDEQGFVYIVDRKKDM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 520 LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITlnhgeEPTPELYAE-VRNWVRKEIGPIATPDVLHW 598
Cdd:PRK08751 463 ILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEF 537
|
570 580
....*....|....*....|..
gi 727190822 599 TDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08751 538 RKELPKTNVGKILRRELRDAAK 559
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-622 |
5.63e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.00 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 90 GDQTAIIWEGDDPTQSkkvTYKQLHHDVCQFANVLK-KLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQT---TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 169 EAVAgRIIDSNAKLVITADEGLrAGRAVPLKKNVD--DALKNPGVVSVANVVVFQRTGKPGYWQEgrdlwwhELTQGVSA 246
Cdd:PRK05620 101 DQIV-HIINHAEDEVIVADPRL-AEQLGEILKECPcvRAVVFIGPSDADSAAAHMPEGIKVYSYE-------ALLDGRST 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 247 DCPPEEVNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLVYAAMTFKY-VFDYHDgdIYWCTADVGWVTG 312
Cdd:PRK05620 172 VYDWPELDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESFLCcVPIYHV--LSWGVPLAAFMSG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 313 HSYLLYGPLACGATtlmfegvpnypgvnrLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLRIMGSVGEPINP 392
Cdd:PRK05620 250 TPLVFPGPDLSAPT---------------LAKIIATAMPRVAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGSAVPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 393 ---EAWEWYYNkignakCPIVDTWWQTETG--GFMITPLPGAtelkAGSATRPFFGVQ---PA-----LVD--------- 450
Cdd:PRK05620 313 iliKAWEERYG------VDVVHVWGMTETSpvGTVARPPSGV----SGEARWAYRVSQgrfPAsleyrIVNdgqvmestd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 451 -NVGTPQegaCEGNLVIVDSW------PGQARTLFGDHDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK05620 383 rNEGEIQ---VRGNWVTASYYhspteeGGGAASTFRGEDVEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 524 GHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLP 603
Cdd:PRK05620 460 GEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEID 539
|
570 580
....*....|....*....|
gi 727190822 604 KTRSGKIMRRILRK-IAAGD 622
Cdd:PRK05620 540 KTSVGKFDKKDLRQhLADGD 559
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
109-616 |
6.25e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.32 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADE 188
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 GLRAGRAVPLKKNV------DDAlknpgvvsvanvvvfqRTGKpgywqegrdlwWHELTQGVSADCPPEEVNAEDPLFIL 262
Cdd:PRK07514 110 NFAWLSKIAAAAGAphvetlDAD----------------GTGS-----------LLEAAAAAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 263 YTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGD-------IYwctadvgwvtgHSYLLY----GPLACG------- 324
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvatnVALLAGasmiflp 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 -------------ATTLMfeGVPNYpgvnrlsqvidkhqvnilYTaptaiRALMAEG-DKaiEGTRRDSLRIMGSVgePI 390
Cdd:PRK07514 231 kfdpdavlalmprATVMM--GVPTF------------------YT-----RLLQEPRlTR--EAAAHMRLFISGSA--PL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 391 NPEAWEWYYNKIGNAkcpIVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDnvgtPQEGA----------- 459
Cdd:PRK07514 282 LAETHREFQERTGHA---ILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTD----PETGAelppgeigmie 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 460 CEGNLVIVDSW--PGQARTLFgdhdrfeqtyfsTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:PRK07514 353 VKGPNVFKGYWrmPEKTAEEF------------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEID 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 538 SHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07514 421 ELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
103-619 |
6.69e-19 |
|
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: 90.08 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 103 TQSKKVTYKQLHHDVCQFANVLKKlGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKL 182
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 183 VITADEGLRAGRAVPLKKN--------VDDALKNPGvvsvanvvvfqrtgkpgywqegrdlWWHELTQGVSADCPPEE-- 252
Cdd:cd05909 82 VLTSKQFIEKLKLHHLFDVeydarivyLEDLRAKIS-------------------------KADKCKAFLAGKFPPKWll 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 253 -------VNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAMTfkyVFDYHDGDIywctadvgwVTG-----HSYLLY 318
Cdd:cd05909 137 rifgvapVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV---------VFGalpffHSFGLT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 319 G----PLACGATTLMFEGVPNYPGVNRLsqvIDKHQVNILYTAPTAIRALMaegdKAIEGTRRDSLRIMGSVGEPINPEA 394
Cdd:cd05909 205 GclwlPLLSGIKVVFHPNPLDYKKIPEL---IYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 395 WEWYYNKIGnakCPIVDTWWQTETGGF--MITPLPGAtelKAGSATRPFFGVQPALVDNVGTPQEGACEGNLVIVDSwPG 472
Cdd:cd05909 278 RQEFQEKFG---IRILEGYGTTECSPVisVNTPQSPN---KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PN 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 473 QARTLFGDHdrfEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH-PKIAEAAVVGIP 551
Cdd:cd05909 351 VMLGYLNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVP 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 552 HNIKGQAIYAYITlnhGEEPTPElyaEVRNWVRK-EIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 428 DGRKGEKIVLLTT---TTDTDPS---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-615 |
3.38e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 89.33 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK10252 464 VAQQAAKTPDAPALADARY------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEglRAGRAVplkknvddalknpgvvsvanvvvfqrtGKPGYWQEGRDLWWhelt 241
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD--QLPRFA---------------------------DVPDLTSLCYNAPL---- 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 242 qgVSADCPPEEVNA-EDPLFILYTSGSTGKPKGVL--HTTggyLVYAAMTFKYVFDYHDGDIYW----CTADVG-WVtgh 313
Cdd:PRK10252 585 --APQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMvgQTA---IVNRLLWMQNHYPLTADDVVLqktpCSFDVSvWE--- 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 314 sylLYGPLACGATTLMFEgvpnyPGVNR----LSQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEP 389
Cdd:PRK10252 657 ---FFWPFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEA 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 390 INPE---AWE-WYYNKIGNAKCPI---VD-TWWqtetggfmitPLPGATELKAGSAT----RPFFGVQPALVDNVGTPQE 457
Cdd:PRK10252 729 LPADlcrEWQqLTGAPLHNLYGPTeaaVDvSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILDARMRPVP 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 458 GACEGNLVIVdswpG-Q-ARTLFGDHD----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK10252 799 PGVAGDLYLT----GiQlAQGYLGRPDltasRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGE 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 532 IESALVSHPKIAEAAVV------GIPHNIKGQAIYAYITLNHGEeptPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKT 605
Cdd:PRK10252 875 IDRAMQALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGL---PLDTSALQAQLRERLPPHMVPVVLLQLDQLPLS 951
|
570
....*....|
gi 727190822 606 RSGKIMRRIL 615
Cdd:PRK10252 952 ANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
3.44e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVD-DALKnpgvvsvanvvvfqrtgkpgywqegRDLWwhel 240
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIAlDSLH-------------------------LDSW---- 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 tqgvSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAA-MTFKYVFDyhDGDIYWCTADVGWVTGhSYLLYG 319
Cdd:PRK05691 1262 ----PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQwMQATYALD--DSDVLMQKAPISFDVS-VWECFW 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 320 PLACGATtLMFEGVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKAiegtRRDSLRIMGSVGEPINPEAWE--- 396
Cdd:PRK05691 1335 PLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAELRNrvl 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 397 ------WYYNKIGNAKCPIVDTWWQTETGGFMITPLpgatelkagsaTRPFFGVQPALVDNVGTPQEGACEGNLVIvdSW 470
Cdd:PRK05691 1410 qrlpqvQLHNRYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCI--GG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 PGQARTLFG----DHDRF-EQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PRK05691 1477 AGLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA 1556
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 546 AVVgIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 1557 AVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
82-618 |
3.44e-18 |
|
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: 88.35 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHlAERGDQTAIIwegdDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17642 24 MKRY-ASVPGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLV----ITADEGLRAGRAVPLKKNVDDALKNPGVVSVANVVVFQRTGKPGYWQEgrdlww 237
Cdd:cd17642 99 TNDIYNERELDHSLNISKPTIVfcskKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNE------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 238 heltqgvsADCPPEEVNAEDPL-FILYTSGSTGKPKGVLHT--------------TGGYLVYAAMTFKYVFDYHDGdiYW 302
Cdd:cd17642 173 --------YDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFHHG--FG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 303 CTADVGWVTghsyllygplaCGATTLM---FEGvpnypgvNRLSQVIDKHQVNILYTAPTairaLMAEGDKA--IEGTRR 377
Cdd:cd17642 243 MFTTLGYLI-----------CGFRVVLmykFEE-------ELFLRSLQDYKVQSALLVPT----LFAFFAKStlVDKYDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 378 DSLRIMGSVGEPINPEAWEWYYNKIgnaKCPIV-DTWWQTE-TGGFMITPlpgATELKAGSATR--PFFG---VQPALVD 450
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRF---KLPGIrQGYGLTEtTSAILITP---EGDDKPGAVGKvvPFFYakvVDLDTGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 451 NVGTPQEGA-CEGNLVIVDSWPG--QARTLFGDHDrfeqtyfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:cd17642 375 TLGPNERGElCVKGPMIMKGYVNnpEATKALIDKD-----------GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 528 GTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIA-TPDVLHWTDSLPKTR 606
Cdd:cd17642 444 PPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKrLRGGVKFVDEVPKGL 520
|
570
....*....|..
gi 727190822 607 SGKIMRRILRKI 618
Cdd:cd17642 521 TGKIDRRKIREI 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
8.57e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 84.86 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 261 ILYTSGSTGKPKGVL--HTTGgYLVYAAmtfkyvfdyhdgdiyWCtaDVGWVT-GHSYLLYGPL------ACGATTLMFE 331
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPFfhtfgyKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 332 GVPNYP----GVNRLSQVIDKHQVNILYTAPTAIRALMAEGDKaiEGTRRDSLR--IMGSVGEPinpeawewyynkigna 405
Cdd:cd17638 67 GATVVPvavfDVDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRaaVTGAATVP---------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 406 kcPIVDTWWQTETGGFMITPLPGATELKAGSATRPffGVQPALVDN-VGTPQEG---ACEGNLVIVDSWPGQARTLFGDH 481
Cdd:cd17638 129 --VELVRRMRSELGFETVLTAYGLTEAGVATMCRP--GDDAETVATtCGRACPGfevRIADDGEVLVRGYNVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 482 DRFEQTYFStfKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYA 561
Cdd:cd17638 205 EATAEAIDA--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 727190822 562 YITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 283 FVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
9.62e-18 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 86.91 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAERGDQTAIIWEGDDPTQSKKVTYKQLHHDVCQFANVLKKLGvKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 164 GGFSPEA---VAGRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALknpgvvsvanvvvfqrtgkpgyWQEGRDLwwheL 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTP----------------------RLLVVDL----L 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 241 TQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKyVFDYHDGDIY--W--CTADVGWVTGhsyl 316
Cdd:cd05931 134 PDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 317 LYGPLACGAT-TLM----FegvpnypgVNR----LsQVIDKHQVNILYtAPT-----AIRALMAEGdkaIEGTRRDSLRI 382
Cdd:cd05931 209 LLTPLYSGGPsVLMspaaF--------LRRplrwL-RLISRYRATISA-APNfaydlCVRRVRDED---LEGLDLSSWRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 383 MGSVGEPINPEAWEWYYNKIGNAKCPivdtwWQT--------ETGGFMITPLPGAT--------ELKAGSATRPFFGVQP 446
Cdd:cd05931 276 ALNGAEPVRPATLRRFAEAFAPFGFR-----PEAfrpsyglaEATLFVSGGPPGTGpvvlrvdrDALAGRAVAVAADDPA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 447 A--LVdNVGTPQEGaCEgnLVIVDS--------------W---PGQARTLFGDHDRFEQTYF---STFKGMYF-SGD-GA 502
Cdd:cd05931 351 AreLV-SCGRPLPD-QE--VRIVDPetgrelpdgevgeiWvrgPSVASGYWGRPEATAETFGalaATDEGGWLrTGDlGF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 503 RRdeDGYYWITGRVDDVLNVSGHRLGTAEIE-SALVSHPKIAE--AAVVGIPHNIKGQ-AIYAYITLNHGEEPTPELYAE 578
Cdd:cd05931 427 LH--DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAA 504
|
570 580 590
....*....|....*....|....*....|....*....
gi 727190822 579 VRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 505 IRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRA 543
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
91-615 |
1.34e-17 |
|
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: 85.95 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd17644 15 DAVAVVFED------QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL----DPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 171 VAGRIidsnakLVITADEGLRAgravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwhELTQGvsadcpp 250
Cdd:cd17644 85 PQERL------TYILEDAQISV----------------------------------------------LLTQP------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 251 eevnaEDPLFILYTSGSTGKPKGVL--------HTTGGYLVYAAMTFKYV-------FDYHDGDIYwctadVGWVTGHSY 315
Cdd:cd17644 106 -----ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 316 LLygplacgATTLMFEGVPNYpgvnrlSQVIDKHQVNILYTAPTAIRALMAEGDKAIeGTRRDSLRIMGSVGEPINPEAW 395
Cdd:cd17644 176 VL-------RPEEMRSSLEDF------VQYIQQWQLTVLSLPPAYWHLLVLELLLST-IDLPSSLRLVIVGGEAVQPELV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 396 E-W---------YYNKIGNAKCPIVDTWwqtetggFMITPLPGATELKAgSATRPFFGVQPALVDN------VGTPqega 459
Cdd:cd17644 242 RqWqknvgnfiqLINVYGPTEATIAATV-------CRLTQLTERNITSV-PIGRPIANTQVYILDEnlqpvpVGVP---- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 460 ceGNLVIVDSwpGQARTLFGDHD----RFEQTYF--STFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:cd17644 310 --GELHIGGV--GLARGYLNRPEltaeKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd17644 386 AVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
..
gi 727190822 614 IL 615
Cdd:cd17644 463 AL 464
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-619 |
2.99e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.28 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEgddptqSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PLN02479 26 LERAAVVHPTRKSVVHG------SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVIT-------ADEGLR--AGRAV-----PLKKNVDDALKNPGVVSVANV------VVFQ 221
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVdqefftlAEEALKilAEKKKssfkpPLLIVIGDPTCDPKSLQYALGkgaieyEKFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 222 RTGKPGY-WQEGRDLWwheltqgvsadcppeevnaeDPLFILYTSGSTGKPKGV-LHTTGGYLvyAAMTFKYVFDYHDGD 299
Cdd:PLN02479 180 ETGDPEFaWKPPADEW--------------------QSIALGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMNEGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 300 IYWCTADVGWVTGHSYLLYGPLACGaTTLMFEGVPnypgVNRLSQVIDKHQVNILYTAPTAIRALmaegdkaiegtrrds 379
Cdd:PLN02479 238 VYLWTLPMFHCNGWCFTWTLAALCG-TNICLRQVT----AKAIYSAIANYGVTHFCAAPVVLNTI--------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 380 lrIMGSVGEPINPEAWEWYYNKIGNAKCPIVdtWWQTETGGFMITPLPGATELKAGS---ATRPFFGVQPA--------- 447
Cdd:PLN02479 298 --VNAPKSETILPLPRVVHVMTAGAAPPPSV--LFAMSEKGFRVTHTYGLSETYGPStvcAWKPEWDSLPPeeqarlnar 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 448 ------------LVD---NVGTPQEGACEGNLVIvdswpgQARTLFGDHDRFEQTYFSTFKGMYF-SGDGARRDEDGYYW 511
Cdd:PLN02479 374 qgvryiglegldVVDtktMKPVPADGKTMGEIVM------RGNMVMKGYLKNPKANEEAFANGWFhSGDLGVKHPDGYIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 512 ITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPE--LYAEVRNWVRKEIGP 589
Cdd:PLN02479 448 IKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPA 527
|
570 580 590
....*....|....*....|....*....|
gi 727190822 590 IATPDVLHWtDSLPKTRSGKIMRRILRKIA 619
Cdd:PLN02479 528 YWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-615 |
4.74e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.99 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 260 FILYTSGSTGKPKGVLHTTGGYlvyaAMTFKYV---FDYHDGD----IYWCTADVGwvtghSYLLYGPLACGA-TTLMFE 331
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEI----AMHCQAVierFGMRADDcelhFYSINFDAA-----SERLLVPLLCGArVVLRAQ 2407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 332 GvpnYPGVNRLSQVIDKHQVNILYTAPT----AIRALMAEGDkaiegtrRDSLRIMGSVGEPINPEAWEwyynKIGNAKC 407
Cdd:PRK05691 2408 G---QWGAEEICQLIREQQVSILGFTPSygsqLAQWLAGQGE-------QLPVRMCITGGEALTGEHLQ----RIRQAFA 2473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 408 P--IVDTWWQTETggfMITPL--PGATELKAGSATRPFFGVQPALV------DNVGTPQEGAceGNLVIvdswpGQARTL 477
Cdd:PRK05691 2474 PqlFFNAYGPTET---VVMPLacLAPEQLEEGAASVPIGRVVGARVayildaDLALVPQGAT--GELYV-----GGAGLA 2543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 478 FGDHDR-------FEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:PRK05691 2544 QGYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 550 IpHNIKGQAIYAYI---TLNHGEEPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 2624 L-DTPSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
480-617 |
3.33e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.47 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 480 DHDRF-EQTYFSTfkgmyfsgDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQA 558
Cdd:PRK07824 226 DPDPFaEPGWFRT--------DDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQR 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 559 IYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 298 VVAAVVGDGGPAPTLE---ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
247-615 |
8.80e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.43 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 247 DCPPEEVNAEDPLFILYTSGSTGKPKGVLHT--------------------TGGYLVYAAMTFKyvfdyhdgdiywctad 306
Cdd:PRK13383 165 ESGGRPAVAAPGRIVLLTSGTTGKPKGVPRApqlrsavgvwvtildrtrlrTGSRISVAMPMFH---------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 307 vGWVTGhsyLLYGPLACGATTLMFEgvpNYPGVNRLSQViDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSV 386
Cdd:PRK13383 229 -GLGLG---MLMLTIALGGTVLTHR---HFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 387 GEPINPEAWEWYYNKIGNAkcpIVDTWWQTETG-GFMITPlpgaTELKAGSAT--RPFFGVQPALVDNVGTPQEGACEGN 463
Cdd:PRK13383 301 GDRLDPTLGQRFMDTYGDI---LYNGYGSTEVGiGALATP----ADLRDAPETvgKPVAGCPVRILDRNNRPVGPRVTGR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 464 LVIVDSWPGQARTLFGDHdrfeqtyfSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK13383 374 IFVGGELAGTRYTDGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVA 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727190822 544 EAAVVGIPHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 446 DNAVIGVPDERFGHRLAAFVVLHPGSGVDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
498-616 |
1.15e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 80.48 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHgEEPTPElya 577
Cdd:PRK08974 436 TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEE--- 511
|
90 100 110
....*....|....*....|....*....|....*....
gi 727190822 578 EVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08974 512 ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
494-620 |
2.04e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.65 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 494 GMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPtp 573
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA-- 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 727190822 574 elyAEVRNWVRkEIGpIAT---PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK10946 487 ---VQLRRFLR-EQG-IAEfklPDRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
498-616 |
2.65e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPTPElya 577
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE--- 513
|
90 100 110
....*....|....*....|....*....|....*....
gi 727190822 578 EVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK05677 514 QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
109-549 |
2.82e-15 |
|
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: 79.05 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADe 188
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 glragravpLKKNVDDALKNPGVVSVANVVvfqrtgkpgYWQEGRDlwwHELTQGVSADCPPEE----VNAEDPLFILYT 264
Cdd:cd05932 87 ---------LDDWKAMAPGVPEGLISISLP---------PPSAANC---QYQWDDLIAQHPPLEerptRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 265 SGSTGKPKGVLHTTGGYlVYAAMTFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNYP------- 337
Cdd:cd05932 146 SGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVedvqrar 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 338 -----GVNRL-----SQVIDK---HQVNILYTAPTaIRALMaeGDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYNkIGn 404
Cdd:cd05932 225 ptlffSVPRLwtkfqQGVQDKipqQKLNLLLKIPV-VNSLV--KRKVLKGLGLDQCRLAGCGSAPVPPALLEWYRS-LG- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 405 akCPIVDTWWQTETGGFMITPLPGATelKAGSATRPFFGVQpalvDNVGTPQEgacegnlVIVDSwPGqarTLFGDHDRF 484
Cdd:cd05932 300 --LNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVE----VRISEDGE-------ILVRS-PA---LMMGYYKDP 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 485 EQTYFS-TFKGMYFSGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05932 361 EATAEAfTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
4.03e-15 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 78.52 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIWEGddptqsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07059 29 LEESFRQYADRPAFICMG------KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 162 IFGGFSPEAVAGRIIDSNAKLVITADEGLRAGRAVPLKKNVD--------DALknpGVVSVANVVVFQRTGK--PGYWQE 231
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKhvvvasmgDLL---GFKGHIVNFVVRRVKKmvPAWSLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 232 GRDLWWHELTQGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYL---------VYAAMTFKYVFD-------- 294
Cdd:PRK07059 180 GHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawLQPAFEKKPRPDqlnfvcal 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 295 --YHdgdIYWCTAdvgwvtghSYLLygPLACGATTLMfegVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAEGDkaI 372
Cdd:PRK07059 260 plYH---IFALTV--------CGLL--GMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--F 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 373 EGTRRDSLRI-----MgSVGEPInPEAWewyYNKIGnakCPIVDTWWQTETGGFMITPLPGATELkAGSATRPFFGVQPA 447
Cdd:PRK07059 322 DKLDFSKLIVangggM-AVQRPV-AERW---LEMTG---CPITEGYGLSETSPVATCNPVDATEF-SGTIGLPLPSTEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 448 LVDN------VGTPQEGACEGNLVIVDSWpgqartlfgdhDRFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRVDDVL 520
Cdd:PRK07059 393 IRDDdgndlpLGEPGEICIRGPQVMAGYW-----------NRPDETAKVMTADGFFrTGDVGVMDERGYTKIVDRKKDMI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 521 NVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITlnhgeEPTPELY-AEVRNWVRKEIGPIATPDVLHWT 599
Cdd:PRK07059 462 LVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-----KKDPALTeEDVKAFCKERLTNYKRPKFVEFR 536
|
570
....*....|....*..
gi 727190822 600 DSLPKTRSGKIMRRILR 616
Cdd:PRK07059 537 TELPKTNVGKILRRELR 553
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-549 |
3.75e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 75.54 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 ADEglragravplkKNVDDALK-NPGVVSVANVVVFQRTGKPGYwQEGRDLWWHEL-TQGVSADCP-PEEVNA------- 255
Cdd:cd17641 90 EDE-----------EQVDKLLEiADRIPSVRYVIYCDPRGMRKY-DDPRLISFEDVvALGRALDRRdPGLYERevaagkg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 256 EDPLFILYTSGSTGKPKGVLHTTGGYL----VYAAMTFKyvfdyHDGDIYWCTADVGWVTGHSYLLYGPLACG------- 324
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLghcaAYLAADPL-----GPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 325 -ATTLM---FEGVPNY----PGV--NRLSQV-------------IDKHQVNILYTA----------PTAIRALMAEGDKA 371
Cdd:cd17641 233 ePETMMedlREIGPTFvllpPRVweGIAADVrarmmdatpfkrfMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 372 IEGTRRDSL-----RIMGSVGEPINPEAWEwYYNKIGnakCPIVDTWWQTEtggfmitpLPGATELKAGSATRPffgvqp 446
Cdd:cd17641 313 LFRPLRDRLgfsrlRSAATGGAALGPDTFR-FFHAIG---VPLKQLYGQTE--------LAGAYTVHRDGDVDP------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 447 alvDNVGTPQEGAcegNLVIVDSWPGQART--LFGDHDRFEQTYFSTFK--GMYFSGDGARRDEDGYYWITGRVDDVLNV 522
Cdd:cd17641 375 ---DTVGVPFPGT---EVRIDEVGEILVRSpgVFVGYYKNPEATAEDFDedGWLHTGDAGYFKENGHLVVIDRAKDVGTT 448
|
490 500
....*....|....*....|....*...
gi 727190822 523 S-GHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17641 449 SdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
254-615 |
7.82e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.97 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 254 NAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLV----YAAMTF--KYVFDYHdgdIYWCTADVgwVTGHSYL 316
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGrdngDEAVLFfsNYVFDFF---VEQMTLAL--LNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 317 LYGPlacgattlmfEGVPNYPgvnRLSQVIDKHQVNILYTAPTAIralmaegdKAIEGTRRDSLRIMGSVGEPINPEAwe 396
Cdd:cd17648 167 VPPD----------EMRFDPD---RFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 397 wyYNKI-GNAKCPIVDTWWQTETGGF-MITPLPGATELKAgSATRPFFGV---------QPALVDNVGTPQEGACegnlv 465
Cdd:cd17648 224 --FEKLrSRFAGLIINAYGPTETTVTnHKRFFPGDQRFDK-SLGRPVRNTkcyvlndamKRVPVGAVGELYLGGD----- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 466 ivdswpGQARtlfGDH-------DRFEQTYFST--------FKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:cd17648 296 ------GVAR---GYLnrpeltaERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 531 EIESALVSHPKIAEAAVVGIPHNIKGQA-----IYAYITLNhgEEPTPElyAEVRNWVRKEIGPIATPDVLHWTDSLPKT 605
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPE--PGHVPE--SDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
410
....*....|
gi 727190822 606 RSGKIMRRIL 615
Cdd:cd17648 443 INGKLDVRAL 452
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
493-619 |
1.24e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 74.09 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 493 KGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPT 572
Cdd:PRK12492 440 EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSV 519
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 727190822 573 PELYAevrnWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12492 520 EELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
106-617 |
2.21e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 72.77 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 adeglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevnaeDPLFILYTS 265
Cdd:cd05940 82 -----------------------------------------------------------------------DAALYIYTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYAAMtFKYVFDYHDGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNYPGVNRLSQV 345
Cdd:cd05940 91 GTTGLPKAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRK---KFSASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 346 IdKHQVNILYTAPTAIRALMAEgdKAIEGTRRDSLRIMgsVGEPINPEAWEWYYNKIGNAKcpIVDTWWQTE--TGGFMI 423
Cdd:cd05940 167 R-KYQATIFQYIGELCRYLLNQ--PPKPTERKHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFINF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 424 TPLPGATElKAGSATRPFFGVQPALVD-NVGTP---QEGACE-------GNLV--IVDSWP------GQARTLFGDHDRF 484
Cdd:cd05940 240 FGKPGAIG-RNPSLLRKVAPLALVKYDlESGEPirdAEGRCIkvprgepGLLIsrINPLEPfdgytdPAATEKKILRDVF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 485 EQ--TYFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYA 561
Cdd:cd05940 319 KKgdAWFNT-------GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMA 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 562 YITLNHGEEPTPELYAevrNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 392 AIVLQPNEEFDLSALA---AHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-617 |
6.19e-13 |
|
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: 71.30 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 adeglragravplkkNVDDALKNpgvvsvanvvvfQRTGKPGywqegrdlwwheltqgvSADCppeeVNAEDPLFILYTS 265
Cdd:cd05939 82 ---------------NLLDPLLT------------QSSTEPP-----------------SQDD----VNFRDKLFYIYTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 266 GSTGKPKGVLHTTGGYLVYAAMTFkYVFDYHDGDIywctadvgwvtghsylLYGPLAcgattlMFEGVPNYPGV-----N 340
Cdd:cd05939 114 GTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDV----------------VYDCLP------LYHSAGGIMGVgqallH 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 341 RLSQVI-------------DKHQVNILYTAPTAIRALMAEgdKAIEGTRRDSLRIMgsVGEPINPEAWEWYYNKIGNAKc 407
Cdd:cd05939 171 GSTVVIrkkfsasnfwddcVKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQ- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 408 pivdtwwqtetggfmITPLPGATELKAGSATrpffgvqpalVDNvgtpQEGACEGN-----------LVIVDSW------ 470
Cdd:cd05939 246 ---------------IGEFYGATEGNSSLVN----------IDN----HVGACGFNsrilpsvypirLIKVDEDtgelir 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 ----------PGQARTLFGDHD------RFE----------QTYFSTFKG---MYFSGDGARRDEDGYYWITGRVDDVLN 521
Cdd:cd05939 297 dsdglcipcqPGEPGLLVGKIIqndplrRFDgyvnegatnkKIARDVFKKgdsAFLSGDVLVMDELGYLYFKDRTGDTFR 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 522 VSGHRLGTAEIESALVSHPKIAEAAVVG--IPHnIKGQAIYAYITLNHGEEPTPELYAEvrnwVRKEIGPIATPDVLHWT 599
Cdd:cd05939 377 WKGENVSTTEVEGILSNVLGLEDVVVYGveVPG-VEGRAGMAAIVDPERKVDLDRFSAV----LAKSLPPYARPQFIRLL 451
|
570
....*....|....*...
gi 727190822 600 DSLPKTRSGKIMRRILRK 617
Cdd:cd05939 452 PEVDKTGTFKLQKTDLQK 469
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
79-617 |
8.07e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 71.37 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 79 ANCLDRHLAERGDQTAIIwegddpTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PLN02860 10 CQCLTRLATLRGNAVVTI------SGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 159 HSVIFGGFSPEAVAGRIIDSNAKLVITaDEG-------LRAGRAVPLKKNVddALKNPGVVSVANVVVFQRTgkpgywqe 231
Cdd:PLN02860 84 VAPLNYRWSFEEAKSAMLLVRPVMLVT-DETcsswyeeLQNDRLPSLMWQV--FLESPSSSVFIFLNSFLTT-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 232 gRDLWWHELTqgvsadcpPEEVN----AEDPLFILYTSGSTGKPKGVL--HTTggyLVYAAMTFKYVFDYHDGDIYWCTA 305
Cdd:PLN02860 153 -EMLKQRALG--------TTELDyawaPDDAVLICFTSGTTGRPKGVTisHSA---LIVQSLAKIAIVGYGEDDVYLHTA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 306 DVGWVTGHSYLLygplacgaTTLMFEG----VPNYPGVNRLsQVIDKHQVNILYTAPTAIRALMAEGDKAIEGTRRDSLR 381
Cdd:PLN02860 221 PLCHIGGLSSAL--------AMLMVGAchvlLPKFDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 382 IM----GSVGEPINPEAWEWYynkiGNAKcpIVDTWWQTETGG---FMitPLPGATELKAGSATRPFFGVQPALVDnvgt 454
Cdd:PLN02860 292 KIlnggGSLSSRLLPDAKKLF----PNAK--LFSAYGMTEACSsltFM--TLHDPTLESPKQTLQTVNQTKSSSVH---- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 455 PQEGACEGN------LVI---VDSWPGQARTLfGDH-------DRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDD 518
Cdd:PLN02860 360 QPQGVCVGKpaphveLKIgldESSRVGRILTR-GPHvmlgywgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 519 VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHG------EEPTPE-----------LYAEVRN 581
Cdd:PLN02860 439 RIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnEKENAKknltlssetlrHHCREKN 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 727190822 582 WVRKEIGPIatpdVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02860 519 LSRFKIPKL----FVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
7.48e-12 |
|
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: 66.94 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTfkyvfdyhdgdiywctADVGWVTGHS-YLLYGPL------ACGATTLM 329
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVL----------------AVLQAIDEGTvFLNSGPLfhigtlMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 330 FEGVPNY-PGVN--RLSQVIDKHQVNILYTAPTAIRALMaegdKAIEGTRRD--SLRIMgsvgepinPEAWEWyynkigN 404
Cdd:cd17636 65 AGGTNVFvRRVDaeEVLELIEAERCTHAFLLPPTIDQIV----ELNADGLYDlsSLRSS--------PAAPEW------N 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 405 AKCPIVDTWW--------QTETGGFMITPLPGATElkAGSATRPFFGVQPALVDN------VGTPQEGACEGNLVIVDSW 470
Cdd:cd17636 127 DMATVDTSPWgrkpggygQTEVMGLATFAALGGGA--IGGAGRPSPLVQVRILDEdgrevpDGEVGEIVARGPTVMAGYW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 471 pgqartlfgdhDRFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:cd17636 205 -----------NRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 727190822 551 PHNIKGQAIYAYITLNHGEEPTPelyAEVRNWVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 274 PDPRWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
263-616 |
1.13e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 67.81 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 263 YTSGSTGKPKGVL--HTTGGYLVYAAMTfkyvfdyhdGDIYWCTA-DV-----------GWVTGHSYLLYGplacgaTTL 328
Cdd:PRK07008 183 YTSGTTGNPKGALysHRSTVLHAYGAAL---------PDAMGLSArDAvlpvvpmfhvnAWGLPYSAPLTG------AKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 329 MFEGvPNYPGVNrLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLR---IMGSVGEPINPEAWEWYYNkigna 405
Cdd:PRK07008 248 VLPG-PDLDGKS-LYELIEAERVTFSAGVPTVWLGLLNHMREA--GLRFSTLRrtvIGGSACPPAMIRTFEDEYG----- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 406 kCPIVDTWWQTEtggfmITPLPGATELKAGSATRP--------------FFGVQPALVDNVGT--PQEGACEGNLVIVDS 469
Cdd:PRK07008 319 -VEVIHAWGMTE-----MSPLGTLCKLKWKHSQLPldeqrkllekqgrvIYGVDMKIVGDDGRelPWDGKAFGDLQVRGP 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 470 WPGQaRTLFGDHDRFEQTYFSTfkgmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:PRK07008 393 WVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 550 IPHNIKGQAIYAYITLNHGEEPTPElyaEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 465 CAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-549 |
1.03e-10 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 64.30 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 106 KKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVhSVIFGGFSPEAVAGRII-DSNAKLVI 184
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-DVVRGSDSSVEELLYILnHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 185 tadeglragravplkknVDdalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeevNAEDPL-FILY 263
Cdd:cd17640 83 -----------------VE--------------------------------------------------NDSDDLaTIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 264 TSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIYWCTADVgWvtgHSY---LLYGPLACGATTLmfegvpnYPGVN 340
Cdd:cd17640 96 TSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 341 RLSQVIDKHQVNILYTAPTAIRALMAEGDKAIEG---TRRDSLRIMGSVGE---PIN-----PEAWEWYYNKIGnakCPI 409
Cdd:cd17640 164 TLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKsspIKQFLFLFFLSGGIfkfGISgggalPPHVDTFFEAIG---IEV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 410 VDTWWQTETGGFMITPLPGATelKAGSATRPFFGVQPALVDNvgtpqegacEGNLVIVdswPGQARTLFGDHDRFEQTYF 489
Cdd:cd17640 241 LNGYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDP---------EGNVVLP---PGEKGIVWVRGPQVMKGYY 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 490 S---------TFKGMYFSGDGARRDEDGYYWITGRVDD--VLNvSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17640 307 KnpeatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
108-559 |
1.39e-10 |
|
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: 64.16 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITad 187
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 eglragravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdlwwheltqgvsadcppeEVNAEDPLFILYTSGS 267
Cdd:cd17639 84 ----------------------------------------------------------------DGKPDDLACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 268 TGKPKGVLHTTGGylVYAAMtfkyvfdyhdgdiywcTADVGWVTGH-----SYLLYGPLA----------C---GAT--- 326
Cdd:cd17639 100 TGNPKGVMLTHGN--LVAGI----------------AGLGDRVPELlgpddRYLAYLPLAhifelaaenvClyrGGTigy 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 327 ----TL------------------MFEGVP------------NYPGVNRLSQVIDKH-------QVNILYTAP------- 358
Cdd:cd17639 162 gsprTLtdkskrgckgdltefkptLMVGVPaiwdtirkgvlaKLNPMGGLKRTLFWTayqsklkALKEGPGTPlldelvf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 359 TAIRALMaegdkaieGTRrdsLRIMGSVGEPINPEAWEWyynkIGNAKCPIVDTWWQTETGGFMITPLPGatELKAGSAT 438
Cdd:cd17639 242 KKVRAAL--------GGR---LRYMLSGGAPLSADTQEF----LNIVLCPVIQGYGLTETCAGGTVQDPG--DLETGRVG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 439 RPFFGVQPALVDnvgTPQEGA------CEGNLVIvdswPGQARTLfGDHDRFEQTYFSTFKGMYF-SGDGARRDEDGYYW 511
Cdd:cd17639 305 PPLPCCEIKLVD---WEEGGYstdkppPRGEILI----RGPNVFK-GYYKNPEKTKEAFDGDGWFhTGDIGEFHPDGTLK 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 727190822 512 ITGRVDD-VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17639 377 IIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAI 425
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
394-625 |
3.93e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 62.32 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 394 AWEWYYNKIGNAKCPIVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNVgtpqegacEGNLVIvdswpgQ 473
Cdd:PRK07445 242 AWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITI------Q 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 474 ARTLF-GDHDRFEQTYfstfkGMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:PRK07445 308 AQSLAlGYYPQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPD 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 553 NIKGQAIYAYITLNHGeEPTPElyaEVRNWVRKEIGPIATPDvlHW--TDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PRK07445 383 PHWGEVVTAIYVPKDP-SISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-618 |
5.29e-10 |
|
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: 62.30 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 87 AERGDQTAIIWEGDDPTQsKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACarigavhsvIFGGF 166
Cdd:cd05906 20 AERGPTKGITYIDADGSE-EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 167 SPEAVAGRIIDSNAKLVITADEGLRA--GRAVPLkknVDDALKNPgvvsvanvvvFQRTGKPGYWQEgrdlwWHELTQGV 244
Cdd:cd05906 90 VPAPLTVPPTYDEPNARLRKLRHIWQllGSPVVL---TDAELVAE----------FAGLETLSGLPG-----IRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 245 SADCPPEEV----NAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKyVFDYHDGDIY--WCTAD--VGWVTGHSYL 316
Cdd:cd05906 152 LLDTAADHDlpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLDhvGGLVELHLRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 317 LYgpLACG----ATTLMFEGVPnypgvnRLSQVIDKHQVNILYtAPTAIRALMAEGDKAIEGTRRD--SLRIMGSVGEPI 390
Cdd:cd05906 231 VY--LGCQqvhvPTEEILADPL------RWLDLIDRYRVTITW-APNFAFALLNDLLEEIEDGTWDlsSLRYLVNAGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 391 NPEAWEWYYNKIGNAKCP---IVDTWWQTETGGFMI----TPLPGAT-ELKAGSATRPFFGVQPALVDNVGTPQEGACEG 462
Cdd:cd05906 302 VAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCSGVIysrsFPTYDHSqALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 463 NLVIvdswpgQARTLFGDHDRFEQTYFSTFK--GMYFSGDGARRDeDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:cd05906 382 RLQV------RGPVVTKGYYNNPEANAEAFTedGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 541 KIAEAAVVGIPHNIKGQ-----AIYAYITLNHgEEPTPELYAEVRNWVRKEIG-------PIAtpdvlhwTDSLPKTRSG 608
Cdd:cd05906 455 GVEPSFTAAFAVRDPGAeteelAIFFVPEYDL-QDALSETLRAIRSVVSREVGvspayliPLP-------KEEIPKTSLG 526
|
570
....*....|
gi 727190822 609 KIMRRILRKI 618
Cdd:cd05906 527 KIQRSKLKAA 536
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-615 |
5.80e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGEEPtpely 576
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP----- 368
|
90 100 110
....*....|....*....|....*....|....*....
gi 727190822 577 AEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-551 |
7.05e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.84 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHL----AERGDQTAII----WEGDDPTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 156 GAVHSVIFGGFSPEAVAGRIIDSNAKLVITADEGLRA----GRAVP-LKKNVddalknpgvvsvanvvvfqrTGKPGYWQ 230
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlfGWGKPsVRRLV--------------------TVGGRLLW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 231 EGRDLwwHELTQGVS-ADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAmtfKYVFDYHDGDIYWCTADV 307
Cdd:PRK09274 150 GGTTL--ATLLRDGAaAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEIDLPTFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 308 gwvtghsYLLYGPlACGATTLMFEGVPNYPG-VN--RLSQVIDKHQVNILYTAPTAIRALMAEGDKAieGTRRDSLRIMG 384
Cdd:PRK09274 225 -------FALFGP-ALGMTSVIPDMDPTRPAtVDpaKLFAAIERYGVTNLFGSPALLERLGRYGEAN--GIKLPSLRRVI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 385 SVGEPINPEAWEwYYNKIGNAKCPIVDTWWQTETggfmitpLP----GATEL--KAGSATRPFFGVqpalvdNVGTPQEG 458
Cdd:PRK09274 295 SAGAPVPIAVIE-RFRAMLPPDAEILTPYGATEA-------LPissiESREIlfATRAATDNGAGI------CVGRPVDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 459 AcegNLVIV-------DSWPGQARTLFGD---------------HDRFEQTYFS--------TFKGMyfsGDGARRDEDG 508
Cdd:PRK09274 361 V---EVRIIaisdapiPEWDDALRLATGEigeivvagpmvtrsyYNRPEATRLAkipdgqgdVWHRM---GDLGYLDAQG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 727190822 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK09274 435 RLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
90-610 |
1.40e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 60.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 90 GDQTAIIwegDDPTQSKK-VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:cd17654 1 PDRPALI---IDQTTSDTtVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 169 EAVAGRIIDSNAKLVITADEGLRAGRA-VPLKKNVDdalknpgvvsvanvvvfqrtgkpgywqegrdlwwhELTQGVSAd 247
Cdd:cd17654 78 QRSLTVMKKCHVSYLLQNKELDNAPLSfTPEHRHFN-----------------------------------IRTDECLA- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 248 cppeevnaedplFILYTSGSTGKPKGVlHTTGGYLVYAAMTFKYVFDYHDGDIYWCTA----DVGWVTghsylLYGPLAC 323
Cdd:cd17654 122 ------------YVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLTSpltfDPSVVE-----IFLSLSS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 324 GATTLMfegVPNYPGV--NRLSQVIDK-HQVNILYTAPTAIRALMAEGDKAIEGTRRDSLRIMGSVGEPInP-----EAW 395
Cdd:cd17654 184 GATLLI---VPTSVKVlpSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPF-PslvilSSW 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 396 EWYYNKIgnakcPIVDTWWQTETGGFMIT--------PLPGATELkAGSATRpffgvqpaLVDNVGTPQEGacegnlviV 467
Cdd:cd17654 260 RGKGNRT-----RIFNIYGITEVSCWALAykvpeedsPVQLGSPL-LGTVIE--------VRDQNGSEGTG--------Q 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 468 DSWPGQARTLF--GDHDRFEQTyfstfkgMYFSGDGARRdEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIaEA 545
Cdd:cd17654 318 VFLGGLNRVCIldDEVTVPKGT-------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ES 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727190822 546 AVVGIPHNikgQAIYAYITlnhgeepTPELYAEVRNWVRKEIGPI-ATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17654 389 CAVTLSDQ---QRLIAFIV-------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPLTSHGKV 444
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
109-322 |
1.73e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.90 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITADE 188
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 glragravPLKKNVD-----DALKNPGVVSVANVVVFQRTGKPGYWQEGRDLWWHELTQGVSADcpPEEVNAEDPLFILY 263
Cdd:PLN02387 188 --------QLKKLIDissqlETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVD--PDLPSPNDIAVIMY 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 727190822 264 TSGSTGKPKGVLHTTGGYLVYAAMTFKYVFDYHDGDIywctadvgwvtghsYLLYGPLA 322
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-580 |
2.80e-09 |
|
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: 59.78 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 255 AEDPLFILYTSGSTGKPKGVLHTTGgylVYAAM--TFKYVFDYHDGDIYWCTADVgwvtghsYLLYGPlACGATTLMFEG 332
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHG---TFAAQidALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 333 VPNYPG-VN--RLSQVIDKHQVNILYTAPTAIRALMAEGdkAIEGTRRDSLRIMGSVGEPInPEAWEWYYNKIGNAKCPI 409
Cdd:cd05910 153 DPTRPArADpqKLVGAIRQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPV-PIALAARLRKMLSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 410 VDTWWQTET-------GGFMITPLPGATELKAGSAT-RPFFGVQPALVDNVGTP---QEGACEGNLV----IVDSWPGQA 474
Cdd:cd05910 230 LTPYGATEAlpvssigSRELLATTTAATSGGAGTCVgRPIPGVRVRIIEIDDEPiaeWDDTLELPRGeigeITVTGPTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 475 RTLfgdHDRFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05910 310 PTY---VNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
330 340 350
....*....|....*....|....*....|.
gi 727190822 550 IPHNIKGQAIYAYITLNHGEEPTPELYAEVR 580
Cdd:cd05910 387 VGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
91-615 |
4.12e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 59.52 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 91 DQTAIIWEGDdptqskKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIG------AVHSvifg 164
Cdd:PRK04813 17 DFPAYDYLGE------KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSS---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 165 gfSPEAVAgRIID-SNAKLVITADEglragravpLKKNVDDAlknpgvvsvanvvvfqRTGKPGywqegrdlwwhELTQG 243
Cdd:PRK04813 87 --PAERIE-MIIEvAKPSLIIATEE---------LPLEILGI----------------PVITLD-----------ELKDI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 244 VSADCPPEE---VNAEDPLFILYTSGSTGKPKGV--LHTTggyLVyaamTFkyvfdyhdgdIYWCTADVGWVTGHSYL-- 316
Cdd:PRK04813 128 FATGNPYDFdhaVKGDDNYYIIFTSGTTGKPKGVqiSHDN---LV----SF----------TNWMLEDFALPEGPQFLnq 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 317 -----------LYGPLACGAT-TLMFEGVPNYPGvnRLSQVIDKHQVNILYTAPTAIRalMAEGDKAIEGTRRDSLRIMG 384
Cdd:PRK04813 191 apysfdlsvmdLYPTLASGGTlVALPKDMTANFK--QLFETLPQLPINVWVSTPSFAD--MCLLDPSFNEEHLPNLTHFL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 385 SVGEPINPEAWEWYYNKIGNAKcpIVDTWWQTETGGFM----IT--------PLP-GATelKAGSATrpffgvqpALVDN 451
Cdd:PRK04813 267 FCGEELPHKTAKKLLERFPSAT--IYNTYGPTEATVAVtsieITdemldqykRLPiGYA--KPDSPL--------LIIDE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 452 VGTPQEGACEGNLVIVdswpGQARTL--FGDHDRFEQTYFsTFKGM--YFSGDGARRDeDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK04813 335 EGTKLPDGEQGEIVIS----GPSVSKgyLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 528 GTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYITLNHGE-EPTPELYAEVRNWVRKEIGPIATPDVLHWTDSLPKTR 606
Cdd:PRK04813 409 ELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDfEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTP 488
|
....*....
gi 727190822 607 SGKIMRRIL 615
Cdd:PRK04813 489 NGKIDRKAL 497
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
108-277 |
1.56e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 54.38 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLK-KLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAG-------RIIDSN 179
Cdd:cd17632 68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPilaetepRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 180 AKLVITADEGLRAGRAVPlKKNVDDALKNPGVVSVANVVVFQRTGKPGYWQEGRDLWWHELTQGVSADCPPEEVNAEDPL 259
Cdd:cd17632 148 AEHLDLAVEAVLEGGTPP-RLVVFDHRPEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLA 226
|
170
....*....|....*...
gi 727190822 260 FILYTSGSTGKPKGVLHT 277
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYT 244
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
109-277 |
4.03e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 53.28 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVaGRIID-SNAKLVITAD 187
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAV-DYIVDhAEIDFVFVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EGLR------AGRAVPLKKNVddALKNPGVVSVANVVVFQRtgKPGYWQEgrdlWWHELTQGVSADCPPEevnAEDPLFI 261
Cdd:PLN02430 157 KKIKellepdCKSAKRLKAIV--SFTSVTEEESDKASQIGV--KTYSWID----FLHMGKENPSETNPPK---PLDICTI 225
|
170
....*....|....*.
gi 727190822 262 LYTSGSTGKPKGVLHT 277
Cdd:PLN02430 226 MYTSGTSGDPKGVVLT 241
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
108-283 |
7.80e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.15 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 108 VTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNAKLVITAD 187
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 188 EGLRAGRAVplKKNVDDALKnpgvvSVANVVVFQRTGKPGYWQEGRDLW-WHELTQGVSADCPPEEVNAEDPLFILYTSG 266
Cdd:PLN02861 158 SKISSILSC--LPKCSSNLK-----TIVSFGDVSSEQKEEAEELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSG 230
|
170
....*....|....*..
gi 727190822 267 STGKPKGVLHTTGGYLV 283
Cdd:PLN02861 231 TTGEPKGVILTNRAIIA 247
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
109-277 |
2.47e-06 |
|
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: 50.68 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVK--KGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagRIIDSNAKL-VIT 185
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAI--EYILNHAEIsIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 186 ADEGLRagravplkknvddalknpgvvsvanvvvfqrtgkpgywqegrdLW-WHEL-TQGVSADCPPEEVNAEDPLFILY 263
Cdd:cd05927 85 CDAGVK-------------------------------------------VYsLEEFeKLGKKNKVPPPPPKPEDLATICY 121
|
170
....*....|....
gi 727190822 264 TSGSTGKPKGVLHT 277
Cdd:cd05927 122 TSGTTGNPKGVMLT 135
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
82-279 |
4.54e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 49.97 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 82 LDRHLAERGDQTAIIW---------EGDDPTQSKKV------------TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMP 140
Cdd:PTZ00216 75 LERICKERGDRRALAYrpvervekeVVKDADGKERTmevthfnetryiTYAELWERIVNFGRGLAELGLTKGSNVAIYEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 141 MVPEAAVAMLACARIGAVHSVIFGGFSPEAVA-------GRIIDSNAKLVITADEGLRAGRAVPLKKNVDDALknPgvvs 213
Cdd:PTZ00216 155 TRWEWLASIYGIWSQSMVAATVYANLGEDALAyalreteCKAIVCNGKNVPNLLRLMKSGGMPNTTIIYLDSL--P---- 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727190822 214 vanvvvfqrtgkPGYWQEGRDL--WWHELTQGVSA----DCPPEEvNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 229 ------------ASVDTEGCRLvaWTDVVAKGHSAgshhPLNIPE-NNDDLALIMYTSGTTGDPKGVMHTHG 287
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
253-621 |
4.71e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.92 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 253 VNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAAMtfkyVFDYHDGDIywctadvgwVTG-----HSY----LLYGP 320
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLP 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 321 LACGATTLMfegVPNYPGVNRLSQVIDKHQVNILYTAPTAIRALMAegDKAIEGTRRDSLRIMGSVGEPINPEAWEWYYN 400
Cdd:PRK08633 846 LLEGIKVVY---HPDPTDALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEE 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 401 KignakcpivdtwwqtetggFMITPLPG--ATEL----------------------KAGSATRPFFGVQPALVD-NVGTP 455
Cdd:PRK08633 921 K-------------------FGIRILEGygATETspvasvnlpdvlaadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEE 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 456 QEGACEGNLVIvdswpGQARTLFGDHDRFEQT----YFSTFKGMYFSGDGARRDEDGYYWITGRVDdvlnvsghRLgtAE 531
Cdd:PRK08633 982 LPPGEDGLILI-----GGPQVMKGYLGDPEKTaeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYS--------RF--AK 1046
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 532 IESALVSHPKIAEA------------AVVGIPHNIKGQAIYAYITlnHGEEPTPELYAEVRNwvrKEIGPIATPDVLHWT 599
Cdd:PRK08633 1047 IGGEMVPLGAVEEElakalggeevvfAVTAVPDEKKGEKLVVLHT--CGAEDVEELKRAIKE---SGLPNLWKPSRYFKV 1121
|
410 420
....*....|....*....|..
gi 727190822 600 DSLPKTRSGKIMRRILRKIAAG 621
Cdd:PRK08633 1122 EALPLLGSGKLDLKGLKELALA 1143
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
249-613 |
7.39e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 48.84 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 249 PPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGylVYA---AMTFKYVFDY-HDGDIYW--CTADVGWVTGhsylLYGPLA 322
Cdd:PRK07768 145 DPVETGEDDLALMQLTSGSTGSPKAVQITHGN--LYAnaeAMFVAAEFDVeTDVMVSWlpLFHDMGMVGF----LTVPMY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 323 CGA-----TTLMFEGVPnypgvnrLS--QVIDKHQVNILyTAPTAIRALMAEG-DKAIEGTRRD--SLRIMGSVGEPINP 392
Cdd:PRK07768 219 FGAelvkvTPMDFLRDP-------LLwaELISKYRGTMT-AAPNFAYALLARRlRRQAKPGAFDlsSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 393 EAWEwyynKIGNAKCP-------IVDTWWQTET---------GGFMITPLPGATELKA-GSATRPFFGVQPALVDnVGTP 455
Cdd:PRK07768 291 ADVE----DLLDAGARfglrpeaILPAYGMAEAtlavsfspcGAGLVVDEVDADLLAAlRRAVPATKGNTRRLAT-LGPP 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 456 QEGaCEGNLVIVDSWPGQART-----LFGDH--------DRFEQTyfSTFKGMYFSGDGARRDEDGYYWITGRVDDVLNV 522
Cdd:PRK07768 366 LPG-LEVRVVDEDGQVLPPRGvgvieLRGESvtpgyltmDGFIPA--QDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIM 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 523 SGHRLGTAEIESALVSHPKIAEAAVVGI----PHNIKGQAIYAYITLNHGEEPTPELYAEVRNWVRKEIGpiATPDVLHW 598
Cdd:PRK07768 443 AGRNIYPTDIERAAARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVV 520
|
410
....*....|....*..
gi 727190822 599 TD--SLPKTRSGKIMRR 613
Cdd:PRK07768 521 LGpgSIPKTPSGKLRRA 537
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
92-275 |
1.28e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.52 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 92 QTAIIWEGDDPTQSkkVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE-- 169
Cdd:TIGR03443 257 ETPSFLDPSSKTRS--FTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPArq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 170 ---------------AVAGRI-------IDSNAKLV-------ITADEGLRAGRavpLKKNVDDALKNpgvvsvANVVVF 220
Cdd:TIGR03443 335 tiylsvakpraliviEKAGTLdqlvrdyIDKELELRteipalaLQDDGSLVGGS---LEGGETDVLAP------YQALKD 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 221 QRTGKPgywqegrdlwwheltqgVSADCPPEevnaedplfILYTSGSTGKPKGVL 275
Cdd:TIGR03443 406 TPTGVV-----------------VGPDSNPT---------LSFTSGSEGIPKGVL 434
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
109-275 |
7.09e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 46.17 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 109 TYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagRIIDSNAKLVITADE 188
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAV--EFIISHSEVSIVFVE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 189 GLRAGRAVPLKKNVDDALKNP---GVVSVANVVVFQRTGKPGY-WQEgrdlwWHELTQGVSADCPPEEvnAEDPLFILYT 264
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVvsfGGVSREQKEEAETFGLVIYaWDE-----FLKLGEGKQYDLPIKK--KSDICTIMYT 231
|
170
....*....|.
gi 727190822 265 SGSTGKPKGVL 275
Cdd:PLN02614 232 SGTTGDPKGVM 242
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
100-336 |
1.16e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.26 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 100 DDPtQSKKVTYKQLhhdvCQFANVL-KKL--GVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfgGFSpeAVAGRII 176
Cdd:PRK06814 652 EDP-VNGPLTYRKL----LTGAFVLgRKLkkNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANIL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 177 DS----NAKLVITADEGLRAGRAVPLKKNVDdalknpgvvsvanvvvfqrtgkpgywQEGRDLWWHELTQGVS------- 245
Cdd:PRK06814 723 SAckaaQVKTVLTSRAFIEKARLGPLIEALE--------------------------FGIRIIYLEDVRAQIGladkikg 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 246 ------ADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTFKYVfDYHDGDIYWCTADVgwvtGHSYLLYG 319
Cdd:PRK06814 777 llagrfPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPV----FHSFGLTG 851
|
250
....*....|....*..
gi 727190822 320 placGATTLMFEGVPNY 336
Cdd:PRK06814 852 ----GLVLPLLSGVKVF 864
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
103-169 |
1.28e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 41.73 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727190822 103 TQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17647 16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPA 82
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
467-607 |
2.41e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 41.24 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 467 VDSWPGQARTLFGDHDrfeqTYFSTfkGMYFsgdgaRRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:PRK07868 820 IDPTASVKRGVFAPAD----TWIST--EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAV 888
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727190822 547 VVGIPHNIKGQAIYAyITLNHGEEPTPelyAEVRNWVRkEIGPIATPDVLHWTDSLPKTRS 607
Cdd:PRK07868 889 TYGVEVGGRQLAVAA-VTLRPGAAITA---ADLTEALA-SLPVGLGPDIVHVVPEIPLSAT 944
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
84-289 |
3.45e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 40.24 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 84 RHLAE-RGDQTAIIwegddpTQSKKVTYKQLHHDVCQFANVLKKLGVKKGDVVAIYMPMVPEAAVAMLACARIGAvhsvi 162
Cdd:PRK09029 10 RHWAQvRPQAIALR------LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 163 fggfspeavagriidsnaklvitadeglragRAVPLkknvddalkNPGVVSVANVVVFQRTGKPGYWQEGRDLWWHELT- 241
Cdd:PRK09029 79 -------------------------------RVLPL---------NPQLPQPLLEELLPSLTLDFALVLEGENTFSALTs 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 727190822 242 --QGVSADCPPEEVNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAA-----MTF 289
Cdd:PRK09029 119 lhLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEgvlslMPF 173
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
254-393 |
6.51e-03 |
|
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: 39.39 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 254 NAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAAMTFKYVFDYHDGDIY--W--CTADVGWVTGHsyllYGPLACGAT--- 326
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNqyl 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727190822 327 --TLMFEGVPnypgVNRLSQvIDKHQVNILYTAPTAIRALMAE-GDKAIEGTRRDSLRIMGSVGEPINPE 393
Cdd:cd05908 179 mpTRLFIRRP----ILWLKK-ASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| |
