|
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: 1345.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 6 KHAIPANIADRCLINPEQYEAKYQQSINEPDTFWGEQGKILDWITPYkkvkNTSFAPGNVSIKWYEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 86 LQENGDRTAIIWEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 166 FSPEAVAGRIIDSSSRLVITADEGVRAGRGIPLKKNVDDALKNPNvnSVEHVVVLKRTGGKVDWHEGRDLWWSDVIEKSS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 326 TTLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 406 KCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 486 QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 566 NHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTsNLGDTSTLADPGVVEKLLEEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
gi 501084078 646 QAIA 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 ... |
18-644 |
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: 1200.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 18 LINPEQYEAKYQQSINEPDTFWGEQGK-ILDWITPYKKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQENGDRTAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 97 WEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 177 DSSSRLVITADEGVRAGRGIPLKKNVDDALKNPNVnSVEHVVVLKRTGGKVD-WHEGRDLWWSDVIEKSSADHQPEEMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPV-SVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 WPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 416 TETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGN-LVITDSWPGQARTLFGDHERFEQTYFSTFKN 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 575 LYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEE 644
Cdd:TIGR02188 557 LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
22-634 |
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: 1185.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 22 EQYEAKYQQSINEPDTFWGEQGKILDWITPYKKVKNTSFapGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK--GPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 102 ATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 182 LVITADEGVRAGRGIPLKKNVDDALKNpnVNSVEHVVVLKRTGGKVDWHEGRDLWWSDVIEKSSADHQPEEMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 342 MAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGF 421
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 422 MITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDG 501
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRN 581
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdTSNLGDTSTLAD 634
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
24-611 |
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: 1056.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 24 YEAKYQQSINEPDTFWGEQGKILDWITPYKKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDAT 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 104 QSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ITADEGVRAGRGIPLKKNVDDALkNPNVNSVEHVVVLKRTGGKVDWHEGRDLWWSDVIEKSSADHQPEEMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 264 TSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMA 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 344 QVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGFMI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 424 TPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 501084078 584 RKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 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: 944.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 68 KWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDATqSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGEDGE-ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 148 AMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRGIPLKKNVDDALKNpnVNSVEHVVVLKRTGGKV 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEE--LPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 228 DWHEgrDLWWSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 308 GWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 388 EPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPGaTELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 468 DSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 548 VGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 501084078 628 DTSTLADPGVVEKLLE 643
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 832.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 20 NPEQYEAKYQQSINEPDTFWGEQGKILDWITPYKKVK----NTSFAPGNVSIKWYEDGTLNLAANCLDRHLQE-NGDRTA 94
Cdd:PLN02654 28 SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEvcseNLDVRKGPISIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 95 IIWEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGR 174
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 175 IIDSSSRLVITADEGVRAGRGIPLKKNVDDALKNPNVNSV--------EHVVVLKRTGGKvdWHEGRDLWWSDVIEKSSA 246
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVsvgicltyENQLAMKREDTK--WQEGRDVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 247 DHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 TLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEK 406
Cdd:PLN02654 346 VLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 407 CPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQ 486
Cdd:PLN02654 426 CPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYET 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 487 TYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLN 566
Cdd:PLN02654 506 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 567 HGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLE 643
Cdd:PLN02654 586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-638 |
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: 651.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 24 YEAKYQQSINEPDTFWGEQGKILDWITPYKKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQE-NGDRTAIIWEGDDA 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPP---FTRWFVGGRLNTCYNALDRHVEAgRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 103 TQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 183 VITADEGVRAGRGIPLKKNVDDALKNPNVNSvEHVVVLKRTGGKVD-WHEGRDLWWSDVIeKSSADHQPEEMNAEDPLFI 261
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSGHKP-HHVLVLNRPQVPADlTKPGRDLDWSELL-AKAEPVDCVPVAATDPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVP-NWPTPA 340
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 341 RMAQVVDKHQVTILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTET 418
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 419 GGFMITPLPGATEL--KAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSW-PGQARTLFGDHERFEQTYFSTFKNM 495
Cdd:cd05967 393 GWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPE- 574
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEe 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501084078 575 LYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADPGVV 638
Cdd:cd05967 553 LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVL 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-649 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 611.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 22 EQYEAKYQQSINEPDTFWGEQGKILDWITPYKKVKNTS---FApgnvsiKWYEDGTLNLAANCLDRHLQENGDRTAIIWE 98
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSnppFA------RWFVGGRTNLCHNAVDRHLAKRPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 99 GDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDS 178
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 179 SSRLVITADEGVRAGRGIPLKKNVDDALKNPNvNSVEHVVVLKRTGGKVDWHEGRDLWWSDVIEKSSADHQPEE-MNAED 257
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQ-HKPRHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARVPVEwLESNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWP 337
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 338 TPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekcPVVDTWWQTE 417
Cdd:PRK10524 315 DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 418 TGGFMITPLPG--ATELKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVITDSW-PGQARTLFGDHERFEQTYFSTF- 492
Cdd:PRK10524 392 TGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG---- 568
Cdd:PRK10524 472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsla 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 569 -EDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG-DTsnlGDTSTLADPGVVEKLleeKQ 646
Cdd:PRK10524 552 dREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI---RQ 625
|
...
gi 501084078 647 AIA 649
Cdd:PRK10524 626 ALE 628
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-635 |
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: 552.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 22 EQYEAKYQQSINEPDTFWGEQGKILD--WITPYKKVKNTSfaPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEG 99
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 100 DDATqSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSS 179
Cdd:cd05968 85 EDGT-SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 180 SRLVITADEGVRAGRGIPLKKNVDDALKNpnVNSVEHVVVLKRTGGKVDWHEGRDLWWSDviEKSSADHQPEEMNAEDPL 259
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACAQ--CPTVEKVVVVRHLGNDFTPAKGRDLSYDE--EKETAGDGAERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDD-IYWCTaDVGWVTGhSYLLYGPLACGATTLMFEGVPNWPT 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 339 PARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTET 418
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 419 GGFMITPLPgATELKAGSATRPFFGVQPALVDNEGHPQEGaTEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFS 498
Cdd:cd05968 398 SGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 499 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTE 578
Cdd:cd05968 476 GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEE 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 579 VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADP 635
Cdd:cd05968 556 LMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-628 |
5.58e-176 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 512.52 E-value: 5.58e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 69 WYEDGTLNLAANCLDRHLQEN-GDRTAIIWEGDDATQSkhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGrKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 148 AMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRagrgiplKKNVDDalknpnVNSVEHVVVlkrTGGKV 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD------LPSLKHVLL---VGEDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 228 DWHEG-RDLWwsDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPDDIYWCTAD 306
Cdd:PRK04319 178 EEGPGtLDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTAD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 307 VGWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSV 386
Cdd:PRK04319 255 PGWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 387 GEPINPEAWEWYWKKIGNekcPVVDTWWQTETGGFMITPLPgATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVI 466
Cdd:PRK04319 332 GEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 467 TDSWPGQARTLFGDHERFEQtYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:PRK04319 408 KKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 547 VVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK----IAAGD 622
Cdd:PRK04319 485 VIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgLPEGD 564
|
....*.
gi 501084078 623 TSNLGD 628
Cdd:PRK04319 565 LSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
109-619 |
4.02e-147 |
|
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: 434.24 E-value: 4.02e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 189 gvragrgiplkknvddalknpnvnsvehvvvLKrtggkvdwhegrdlwwsdviekssadhqpEEMNAEDPLFILYTSGST 268
Cdd:cd05969 82 -------------------------------LY-----------------------------ERTDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 269 GKPKGVLHTTGGYLVYAATTfKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMAQVVDK 348
Cdd:cd05969 102 GTPKGVLHVHDAMIFYYFTG-KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 349 HQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPG 428
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 429 aTELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEqtyfSTFKN-MYFSGDGARRDED 507
Cdd:cd05969 255 -MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYK----NSFIDgWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEI 587
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
gi 501084078 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05969 410 GAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
109-617 |
4.21e-123 |
|
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: 372.05 E-value: 4.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITade 188
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 189 gvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemNAEDPLFILYTSGST 268
Cdd:cd05972 79 -----------------------------------------------------------------DAEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 269 GKPKGVLHTTGgYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwpTPARMAQVVDK 348
Cdd:cd05972 94 GLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLER 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 349 HQVTILYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEWyWKKIGNEkcPVVDTWWQTETGgFMITPLPG 428
Cdd:cd05972 171 YGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEW-WRAATGL--PIRDGYGQTETG-LTVGNFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 429 aTELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDG 508
Cdd:cd05972 244 -MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDY---YLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 509 YYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIG 588
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 501084078 589 PLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
4.22e-115 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 350.84 E-value: 4.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAiiWEGDDatqSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvragrgiPLKKNVDDALKNPNVnsVEHVVVLKRTggkvDWHEGRDLWWSDVI 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEV--VKLVLVLDRD----PVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EkSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTFKYV----FDYHPDDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 142 A-DVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 318 YGPLACGATTLMFEGVPNwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 398 YWKKIGnekCPVVDTWWQTETGGFMITPLPGATEL-KAGSATRPFFGVQPALVD-NEGHPQEGATEGNLVItdSWPGQAR 475
Cdd:pfam00501 297 FRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 501084078 476 TLFGDHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 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 |
2.01e-108 |
|
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: 334.86 E-value: 2.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITAdegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdvi 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssadhqpeemnaedplFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMfegVPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:COG0318 165 LAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 402 IGnekCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTLFGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 482 ERFEQTyfstFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRDgWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 561 AYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:COG0318 390 AFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-611 |
1.02e-101 |
|
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: 313.45 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGWVtGHSYLLYGPLACGATTLMFEGvpnw 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 337 PTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 417 ETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQartlfGDHERFEQTYFSTFKNMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK-----GYWNNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPEly 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 501084078 577 tEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
3.91e-89 |
|
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: 284.41 E-value: 3.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsDVIEKSSADhqpeemnaEDPLFILYTSGS 267
Cdd:cd05973 79 ---------------------------------------------------DAANRHKLD--------SDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLVYAATtFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARmaqVVD 347
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWR---VIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 348 KHQVTILYTAPTAIRALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLP 427
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 428 GATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVI-TDSWPgqaRTLFGDHERFEQTYFStfKNMYFSGDGARRDE 506
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSP---LMWFRGYQLPDTPAID--GGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKE 586
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
gi 501084078 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
24-639 |
3.53e-88 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 288.23 E-value: 3.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 24 YEAKYQQSINEPDTFWGEqgkILDWI-----TPYKKVKNTSFAPGNvsiKWYEDGTLNLAANCLdRHlqENGDRTAIIWE 98
Cdd:PRK03584 36 YAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLAGRRMPGA---RWFPGARLNYAENLL-RH--RRDDRPAIIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 99 GDDATQSKhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDS 178
Cdd:PRK03584 107 GEDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 179 SSRLVITADeGVRAGrGiplkKNVDDALKNPNV----NSVEHVVVLKRTGGKVDW-HEGRDLWWSDVIEKSSADH-QPEE 252
Cdd:PRK03584 186 EPKVLIAVD-GYRYG-G----KAFDRRAKVAELraalPSLEHVVVVPYLGPAAAAaALPGALLWEDFLAPAEAAElEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 253 MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDD-IYWCTAdVGW------VTGhsyllygpLACGA 325
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 326 TTLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNe 405
Cdd:PRK03584 331 TLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 406 kcpvvDTWWQTETGG------FMI-TPL----PGatELKAgsatrPFFGVQPALVDNEGHPQEGATeGNLVITDSWPGQA 474
Cdd:PRK03584 410 -----DVWLASISGGtdicscFVGgNPLlpvyRG--EIQC-----RGLGMAVEAWDEDGRPVVGEV-GELVCTKPFPSMP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 475 RTLFGD--HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:PRK03584 477 LGFWNDpdGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEW 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 553 NIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM----RRILRKIAAGDTSNLGd 628
Cdd:PRK03584 557 PDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAVNRD- 635
|
650
....*....|.
gi 501084078 629 tsTLADPGVVE 639
Cdd:PRK03584 636 --ALANPEALD 644
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
24-639 |
1.36e-87 |
|
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: 286.09 E-value: 1.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 24 YEAKYQQSINEPDTFWGEqgkILDWI-----TPYKKV-KNTSFAPGNvsiKWYEDGTLNLAANCLDRHlqENGDRTAIIW 97
Cdd:cd05943 19 YAALHRWSVDDPGAFWAA---VWDFSgvrgsKPYDVVvVSGRIMPGA---RWFPGARLNYAENLLRHA--DADDPAAIYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 98 EGDDATQskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIID 177
Cdd:cd05943 91 AEDGERT--EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 178 SSSRLVITADEGVRAGRGIPLKKNVDDALKnpNVNSVEHVVVLKRTG--GKVDW-HEGRDLWWSDVI-EKSSADHQPEEM 253
Cdd:cd05943 169 IEPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVaaGQPDLsKIAKALTLEDFLaTGAAGELEFEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 254 NAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSylLYGPLACGATTLMFEGV 333
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 334 PNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekcpvvDTW 413
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 414 WQTETGG------FMIT-PL----PGatELKAgsatrPFFGVQPALVDNEGHPQEGATeGNLVITDSWPGQARTLFGDHE 482
Cdd:cd05943 399 LASISGGtdiiscFVGGnPLlpvyRG--EIQC-----RGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPSMPVGFWNDPD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 483 --RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:cd05943 471 gsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVI 550
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 561 AYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdtSNLGDTSTLADPGVVE 639
Cdd:cd05943 551 LFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPESLD 627
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-616 |
3.07e-82 |
|
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: 269.36 E-value: 3.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 64 NVSIKWYEdgTLNLAANCLDRHLQENGDRTAIIWeGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVP 143
Cdd:cd05970 7 NFSINVPE--NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 144 EAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGvragrGIPlkKNVDDALknPNVNSVEhvvVLKRT 223
Cdd:cd05970 84 EFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-----NIP--EEIEKAA--PECPSKP---KLVWV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 224 GGKVdwhegRDLW--WSDVIEKSSADHQPEEMNA----EDPLFILYTSGSTGKPKGVLHTTG---GYLVyaatTFKYVFD 294
Cdd:cd05970 152 GDPV-----PEGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 295 YHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGvpNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGdkaIEG 374
Cdd:cd05970 223 VREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED---LSR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 375 TDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGgFMITPLPGaTELKAGSATRPFFGVQPALVDNEGH 454
Cdd:cd05970 298 YDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 455 PQEGATEGNLVITDSwPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:cd05970 373 SCEAGEEGEIVIRTS-KGKPVGLFGGYYKDAEKTAEVWHDgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05970 452 SALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRV 531
|
...
gi 501084078 614 ILR 616
Cdd:cd05970 532 EIR 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-616 |
1.06e-80 |
|
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: 264.23 E-value: 1.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 78 AANCLDRHLQEN-GDRTAIIwegDDAtqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEGrGDKTAFI---DDA---GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 157 AVHSVIFGGFSPEAVAGRIIDSSSRLVITADEgvragrgipLKKNVDDALKNpnvnSVEHVVVLKRTGGKVDwhEGRDLW 236
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTK----SEHTLVVLIVSGGAGP--EAGALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 237 WSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYL 316
Cdd:cd05959 144 LAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 317 LYGPLACGATTLMFegvPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 397 WYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT-DSwpgqar 475
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRgPS------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 476 TLFGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNI 554
Cdd:cd05959 368 SATMYWNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 555 KGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
18-617 |
1.28e-77 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 260.06 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 18 LINPEQYEAKYQQSINEPDTFWGEQG-KILDWITPYKKVkntsFAPGNVSIKWYEDGTLNLAANCLDRHLQ--ENGDRTA 94
Cdd:PTZ00237 4 LSDPFDYENDSNYANSNPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVKnpLKRDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 95 IIWEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGR 174
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 175 IIDSSSRLVITADEGVRAGRGIPLKKNVDDALK----NPNvnsveHVVVLKRTggkvDWHEGRD-------------LWW 237
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIElstfKPS-----NVITLFRN----DITSESDlkkietiptipntLSW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 238 SDVIEKSSADHQ-------PEEMNaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWV 310
Cdd:PTZ00237 231 YDEIKKIKENNQspfyeyvPVESS--HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 311 TGHSYlLYGPLACGATTLMFEG--VPNWPTPARMAQVVDKHQVTILYTAPTAIRALM---AEGDKAIEGTDRSSLRILGS 385
Cdd:PTZ00237 309 SFHGF-LYGSLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIktdPEATIIRSKYDLSNLKEIWC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 386 VGEPINPEAWEWYWKKIgneKCPVVDTWWQTETGgfmITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGN 463
Cdd:PTZ00237 388 GGEVIEESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCYGHINIPYNAtgVPSIFIKPSILSEDGKELNVNEIGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 464 LVITDSW-PGQARTLFGDHERFEQTyFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PTZ00237 462 VAFKLPMpPSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEDPSP----ELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 541 LECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-616 |
3.95e-74 |
|
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: 245.03 E-value: 3.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 105 SKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 185 TaDEgvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 265 SGSTGKPKGVLHTTGgYLVYAATTFKYVFDYHP--DDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwpTPARM 342
Cdd:cd05971 97 SGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF--DPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 343 AQVVDKHQVTILYTAPTAIRaLMAEGDKAIEGTDRSsLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTEtGGFM 422
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVE---VNEFYGQTE-CNLV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 423 ITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFknmYFSGDGA 502
Cdd:cd05971 248 IGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDW---LLTGDLG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNW 582
Cdd:cd05971 325 RKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQEL 404
|
490 500 510
....*....|....*....|....*....|....
gi 501084078 583 VRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 405 VKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
92-616 |
3.70e-72 |
|
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: 239.67 E-value: 3.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 92 RTAIIwegdDATQSkhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV 171
Cdd:cd05919 1 KTAFY----AADRS--VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 172 AGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpe 251
Cdd:cd05919 75 AYIARDCEARLVVT------------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 252 emNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADV--GWVTGHSylLYGPLACGATTLM 329
Cdd:cd05919 89 --SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 330 FegvPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEwYWKKIGNekCPV 409
Cdd:cd05919 165 N---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFG--GPI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 410 VDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFGDHERFEQTYF 489
Cdd:cd05919 237 LDGIGATEVGHIFLSNRPGAWRL--GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 490 STFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE 569
Cdd:cd05919 313 GGW---YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 501084078 570 DPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 390 APQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
6.54e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 241.24 E-value: 6.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 72 DGTLNLAaNCLDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 152 CARIGAV-HSV-IFggFSPEAVAGRIIDSSSRLVITADEGVragrgiPLKKNVDDALKnpnvnSVEHVVVL---KRTGGK 226
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQLP-----TVRTVIVEgdgPAAPLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 227 VDWHEgrdlwWSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyaattfKYVFDYHPD 298
Cdd:PRK06187 143 PEVGE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVvlshrnlfLHSLAV---------CAWLKLSRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 299 DIYWCTADV----GWVTGhsyllYGPLACGATTLM---FEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALMAEgdKA 371
Cdd:PRK06187 209 DVYLVIVPMfhvhAWGLP-----YLALMAGAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQMLLKA--PR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 372 IEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFM-ITPLP---GATELKAGSATRPFFGVQPA 447
Cdd:PRK06187 275 AYFVDFSSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPEdqlPGQWTKRRSAGRPLPGVEAR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 448 LVDNEGH--PQEGATEGNLVITDSWPGQArtLFGDHERFEqtyfSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK06187 352 IVDDDGDelPPDGGEVGEIIVRGPWLMQG--YWNRPEATA----ETIDGgWLHTGDVGYIDEDGYLYITDRIKDVIISGG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 525 HRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPK 604
Cdd:PRK06187 426 ENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPR 502
|
570
....*....|....*....
gi 501084078 605 TRSGKIMRRILR-KIAAGD 622
Cdd:PRK06187 503 TSVGKILKRVLReQYAEGK 521
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
9.93e-70 |
|
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: 233.27 E-value: 9.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVItadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdvi 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssadhqpeemnaEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMFEGvpnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPInPEAWEWYWKK 401
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 402 IGnekCPVVDTWWQTETGGfMITPL-PGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARtlfGD 480
Cdd:cd17631 236 RG---VKFVQGYGMTETSP-GVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA---GY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 481 HERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17631 307 WNRPEATA-AAFRDGWFhTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 560 YAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 386 VAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-616 |
6.16e-69 |
|
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: 232.07 E-value: 6.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 159 HSVIFGgfsPEAVAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrDLWWS 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIV------------------------------------------------AVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 DVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFK--YVFDYHPDDIYWCTADVGwvtgHSY- 315
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN-LVANALQIKawLEDLLEGDDVVLAALPLF----HVFg 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 ----LLYgPLACGATTLMfegVPNwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPIN 391
Cdd:cd05936 183 ltvaLLL-PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLCISGGAPLP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 392 PEAWEWYWKKIGnekCPVVDTWWQTETG-GFMITPLPGATelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITdsw 470
Cdd:cd05936 256 VEVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR--- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 471 pGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05936 328 -GPQVMK-GYWNRPEETA-EAFVDGWLrTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 550 IPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 405 VPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-617 |
9.13e-69 |
|
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: 233.51 E-value: 9.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 76 NLAANCLDR--HLQENGDRT---AIIWEGDDATQSKHiSYRELHRDVCRFANTLLEL-GIKKGDVVAIYMPMVPEAAVAM 149
Cdd:cd05928 6 NFASDVLDQwaDKEKAGKRPpnpALWWVNGKGDEVKW-SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 150 LACARIGAVhsVIFGGFSPEA--VAGRIIDSSSRLVITADEgvragrgipLKKNVDD-ALKNPNVNSVEHVVvlkrtggk 226
Cdd:cd05928 85 VACIRTGLV--FIPGTIQLTAkdILYRLQASKAKCIVTSDE---------LAPEVDSvASECPSLKTKLLVS-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 227 vdwHEGRDLWWS--DVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCT 304
Cdd:cd05928 146 ---EKSRDGWLNfkELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 305 ADVGWVTGHSYLLYGPLACGATTLMFEgVPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEgtdRSSLRILG 384
Cdd:cd05928 223 SDTGWIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYK---FPSLQHCV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 385 SVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNL 464
Cdd:cd05928 298 TGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 465 VITDSwPGQARTLFGDHERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:cd05928 373 GIRVK-PIRPFGLFSGYVDNPEKTAATIRgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 544 EAAVVGIPHNIKGQAIYAYVTLN---HGEDPSpELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 452 ESAVVSSPDPIRGEVVKAFVVLApqfLSHDPE-QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-616 |
1.60e-63 |
|
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: 216.39 E-value: 1.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 107 HISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITa 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 187 degvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 267 STGKPKGVLhTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMAQVV 346
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 347 DKHQVTILYTAPTAIRALMAEGDKAiegTDRSS-LRILGsvGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITP 425
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSP---DDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 LPGATelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITdSWPGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARR 504
Cdd:cd05934 239 RDEPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR-GLRGWGFFK-GYYNMPEATA-EAMRNGWFhTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVR 584
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCE 390
|
490 500 510
....*....|....*....|....*....|..
gi 501084078 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 391 GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
103-617 |
1.03e-62 |
|
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: 216.02 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 103 TQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRL 182
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 183 VITADEGVRagrgiplkknvdDALKNPNVNSVEHVVVLKRTGGKVDWHEGRDLwwSDVIEKSSADHQPEEMNAEDPLFIL 262
Cdd:cd05926 90 VLTPKGELG------------PASRAASKLGLAILELALDVGVLIRAPSAESL--SNLLADKKNAKSEGVPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtp 339
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFSASTFWP-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 340 armaQVVDkHQVTiLYTA-PTAIRAL--MAEGDKAIEgtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQT 416
Cdd:cd05926 233 ----DVRD-YNAT-WYTAvPTIHQILlnRPEPNPESP---PPKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 417 ETGGFMIT-PLPGATElKAGSATRPFfGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFGDHErfeQTYFSTFKNM 495
Cdd:cd05926 301 EAAHQMTSnPLPPGPR-KPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNPE---ANAEAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 496 YF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPE 574
Cdd:cd05926 374 WFrTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 501084078 575 lytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 454 ---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-624 |
9.15e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 214.41 E-value: 9.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFGDRSWT------YAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEgvragrgipLKKNVDDALKNPNVNSVEHVVVLKRTGgkvdwHEGRDLWWSDVIEKSSADHQP 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGRE-----APGGWLDFADWAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 EEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaATTFKYV-----FDYHPDDI-------YWCTAdvgwvtGHSYLly 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVscivaGDMSADDIplhalplYHCAQ------LDVFL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 319 GP-LACGATTLMFEGvpnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGTDRSSLRiLGSVGEPINPEAwew 397
Cdd:PRK08316 232 GPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR-KGYYGASIMPVE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 398 YWKKIgNEKCPVVDTW---WQTEtggfmITPL-----PGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVitds 469
Cdd:PRK08316 302 VLKEL-RERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 wpgqART------LFGDHERFEQtyfsTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PRK08316 372 ----HRSpqlmlgYWDDPEKTAE----AFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK08316 444 AEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
..
gi 501084078 623 TS 624
Cdd:PRK08316 521 FT 522
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-611 |
6.63e-61 |
|
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: 210.92 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 101 DATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 181 RLVITADEGVragrgiplkKNVDDALKNpnVNSVEHVVVLkrtGGKVDWHEGRDLWWSDViEKSSADHQPEEMN--AEDP 258
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAKE--LGPKDKIIVL---DDKPDGVLSIEDLLSPT-LGEEDEDLPPPLKdgKDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 259 LFILYTSGSTGKPKGVLHTTGGYL--VYAATTFKYVfDYHPDDIYWCTADVGWVTGHSYLLYGPLaCGATTLMFegvpNW 336
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNLIanLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM----PK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 337 PTPARMAQVVDKHQVTILYTAPtAIRALMAEgDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQT 416
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVP-PIAAALAK-SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPN--ATIKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 417 ETGGfMITPLPGaTELKAGSATRPFFGVQPALVDNEGHPQEGATE-GNLVItdsWPGQArtLFGDHERFEQTYFSTFKNM 495
Cdd:cd05911 299 ETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEpGEICV---RGPQV--MKGYYNNPEATKETFDEDG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 496 YF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPE 574
Cdd:cd05911 372 WLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEK 451
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 501084078 575 lytEVRNWVRKEIgplatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 452 ---EVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
6.01e-60 |
|
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: 208.92 E-value: 6.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 73 GTLNLAANCLDRHLQE-NGDRTAIIwegDDATQskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI---DDISS---LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 152 CARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEgvragrgipLKKNVDDALKNpnVNSVEHVVVLKRT-GGKVDWH 230
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA---------LLPVIKAALGK--SPHLEHRVVVGRPeAGEVQLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 231 EgrdlwwsdviekSSADHQPEEMNA----EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTAD 306
Cdd:TIGR02262 144 E------------LLATESEQFKPAatqaDDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 307 VGWVTGHSYLLYGPLACGATTLMFegvPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRssLRILGSV 386
Cdd:TIGR02262 212 LFFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVR--LRLCTSA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 387 GEPInPEAWEWYWK-KIGNEkcpVVDTWWQTETGGFMITPLPGAteLKAGSATRPFFGVQPALVDNEGHPQEGATEGNLV 465
Cdd:TIGR02262 287 GEAL-PAEVGQRWQaRFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 466 ItdSWPGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:TIGR02262 361 I--SGPSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEA 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501084078 546 AVVGIP---HNIKGQaiyAYVTLNHGEDpspELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 436 AVVGVAdedGLIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-617 |
8.93e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.60 E-value: 8.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvragrGIPLKKNVDDALknpnvNSVEHVVVLkrTGGKVDWHEGRDLWWSDVI 241
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGL------FLGVDYSATTRL-----PALEHVVIC--ETEEDDPHTEKMKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPDDIYWCTA--------DVGWVTgh 313
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANpffhvfgyKAGVNA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 314 syllygPLACGATTLMfegVPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEgtDRSSLRILGSVGEPINPE 393
Cdd:PRK07656 229 ------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE--DLSSLRLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 394 AWEWYWKKIGnekCPVVDTWWQ-TETGGFM-ITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswP 471
Cdd:PRK07656 297 LLERFESELG---VDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG--P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 472 GQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK07656 372 NVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 552 HNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
109-616 |
1.20e-59 |
|
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: 206.17 E-value: 1.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVaGRIIDSSSRLVITAD 187
Cdd:cd05958 12 TYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL-AYILDKARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 EGVRAgrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnAEDPLFILYTSGS 267
Cdd:cd05958 91 HALTA--------------------------------------------------------------SDDICILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMAQVVD 347
Cdd:cd05958 109 TGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 348 KHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLP 427
Cdd:cd05958 185 RYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISARP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 428 GatELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFgdhERFEQTYFSTFKNmyFSGDGARRDED 507
Cdd:cd05958 260 G--DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCRYLA---DKRQRTYVQGGWN--ITGDTYSRDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEI 587
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHI 410
|
490 500
....*....|....*....|....*....
gi 501084078 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 411 APYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
2.10e-59 |
|
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: 205.84 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRII----DSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssa 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 247 dhqpeemNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTA----DVGWVTghsylLYGPLA 322
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE-----IFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTLMfegVPN--WPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEwYWK 400
Cdd:cd05930 158 AGATLVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVR-RWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 KIGNeKCPVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVITDswPGQARTL 477
Cdd:cd05930 230 ELLP-GARLVNLYGPTEATVDATYYRVPPDDEEDGRVPigRPIPNTRVYVLDENLRPVpPGVP-GELYIGG--AGLARGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FGDHE----RFEQTYFSTFKNMYFSGDGARRDEDG--YYwiTGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:cd05930 306 LNRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARE 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 552 HNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 384 DGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
22-617 |
3.24e-57 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 206.08 E-value: 3.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 22 EQYEAKYQQSINEPDTFWG----EQGkiLDWITPYKKVKNTSFA--PGNvsiKWYEDGTLNLAANCLDRHLQENGDRTAI 95
Cdd:PLN03052 120 SSFSEFQRFSVENPEVYWSivldELS--LVFSVPPRCILDTSDEsnPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 96 IW--EGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAG 173
Cdd:PLN03052 195 IWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIAT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 174 RIIDSSSRLVITADEGVRAGRGIPLKKNVDDAlKNPNvnsvehVVVLKRTGGKVDWH-EGRDLWWSDVIEKSSADHQPEE 252
Cdd:PLN03052 275 RLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA-KAPK------AIVLPADGKSVRVKlREGDMSWDDFLARANGLRRPDE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 253 -----MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPDDIY-WCTaDVGWVTGHsYLLYGPLACGAT 326
Cdd:PLN03052 348 ykaveQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGAT 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 TLMFEGVPNWPTPARMAQvvdKHQVTILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEk 406
Cdd:PLN03052 425 LALYNGSPLGRGFAKFVQ---DAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK- 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 407 cPVVDTWWQTETGG-FMITPLPGATELKAGSAtrPFFGVQPALVDNEGH--PQEGATEGNLVITDSWPGQARTLF-GDHe 482
Cdd:PLN03052 499 -PIIEYCGGTELGGgFVTGSLLQPQAFAAFST--PAMGCKLFILDDSGNpyPDDAPCTGELALFPLMFGASSTLLnADH- 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 483 rfEQTYfstFKNM-YFSGDGARRDED-------GYYWITGRVDDVLNVSGHRLGTAEIESAL-VSHPKIAEAAVVGIPHN 553
Cdd:PLN03052 575 --YKVY---FKGMpVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPP 649
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 554 IKGQ---AIYAYVTLNHGEDPSPELYTEVRN-WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 650 GGGPeqlVIAAVLKDPPGSNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-624 |
1.10e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 201.05 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITAdegvRAGRGIPLKKNVDdALKnPNVNSVEHVVVLkrtGGKVD-----------WH 230
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVP----KTFRGFDHAAMAR-RLR-PELPALRHVVVV---GGDGAdsfeallitpaWE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 231 EGRDLwwsdviEKSSADHQPeemNAEDPLFILYTSGSTGKPKGVLHTT----GGYLVYAATtfkyvFDYHPDDIYWCTAD 306
Cdd:PRK13295 181 QEPDA------PAILARLRP---GPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMASP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 307 VGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMAQVVDKHQVTilYT-APTAIRALMAEGDKAiEGTDRSSLRILGS 385
Cdd:PRK13295 247 MAHQTGFMYGLMMPVMLGATAVLQD---IW-DPARAAELIRTEGVT--FTmASTPFLTDLTRAVKE-SGRPVSSLRTFLC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 386 VGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLV 465
Cdd:PRK13295 320 AGAPIPGALVERARAALGAK---IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 466 ITdswpgqARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PRK13295 397 VR------GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 546 AVVGIPHNIKGQAIYAYVTLNHGEdpSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTS 624
Cdd:PRK13295 471 AIVAYPDERLGERACAFVVPRPGQ--SLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
9.49e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 197.49 E-value: 9.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIW--EGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 160 SvIFGGFSPEAVAGRIIDSSSRLVITAdeGVRAGRGIPLKknVDDALKN-PNVNSVEHVVVLKRTGGKVDW--------H 230
Cdd:PRK07529 111 P-INPLLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQK--VAEVLAAlPELRTVVEVDLARYLPGPKRLavplirrkA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 231 EGRDLWWSDVIEKSSADH--QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVG 308
Cdd:PRK07529 186 HARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 WVTGHSYLLYGPLACGATTLmfegvpnWPTPA---------RMAQVVDKHQVTILYTAPTAIRALMaegDKAIEGTDRSS 379
Cdd:PRK07529 265 HVNALLVTGLAPLARGAHVV-------LATPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 380 LRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTE-TGGFMITPLPGatELKAGSATRPFFG--VQPALVDNEGH-P 455
Cdd:PRK07529 335 LRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGRyL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 456 QEGATE--GNLVItdSWPGQART-LFGDHER---FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK07529 410 RDCAVDevGVLCI--AGPNVFSGyLEAAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 530 AEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIG-PLATPDVLHWTDSLPKTRSG 608
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVG 557
|
570
....*....|..
gi 501084078 609 KIMRRILRKIAA 620
Cdd:PRK07529 558 KIFKPALRRDAI 569
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
2.25e-54 |
|
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: 192.14 E-value: 2.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 eemNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTfkYVFDYHPDDIywctadvgWVTGHSYL-------LYGPLA 322
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTLMfegVPNWP--TPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLR--ILGsvGEPINPEAWEWY 398
Cdd:cd17643 158 HGGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 399 WKKIGNEKCPVVDTWWQTETGGFM-ITPLpGATELKAGSAT---RPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQA 474
Cdd:cd17643 231 AGRFGLDRPQLVNMYGITETTVHVtFRPL-DAADLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 475 RTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17643 308 RGYLGrpelTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 550 IPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 388 REDEPGDTRLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
6.75e-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: 190.47 E-value: 6.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsVIfggfspeavagriidSSSRLVITAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV--VI---------------PATTLLTPDD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 EGVRAGRGIPLKKNVDDAlknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeeMNAEDPLFILYTSGS 267
Cdd:cd05974 64 LRDRVDRGGAVYAAVDEN-----------------------------------------------THADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLVYAATTFkYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFegvpNWP--TPARMAQV 345
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 346 VDKHQVTILYTAPTAIRALMAEGDKAIegtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGfMITP 425
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTA-LVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 LPGATeLKAGSATRPFFGVQPALVDNEGHPqegATEGN--LVITDSWP-GQARTLFGDHERfeqTYFSTFKNMYFSGDGA 502
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGAP---ATEGEvaLDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNW 582
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 501084078 583 VRKEIGPLATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
109-617 |
3.77e-52 |
|
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: 186.05 E-value: 3.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFggfspeavagriidsssrlvitade 188
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPIL------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 189 gvragrgiplkknvddalknPNVNSVEHVVVLKRTGGKVDwhegrdlwwsdVIEKSSADHQPEEMNAeDPLFILYTSGST 268
Cdd:cd05903 58 --------------------PFFREHELAFILRRAKAKVF-----------VVPERFRQFDPAAMPD-AVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMAQVVDK 348
Cdd:cd05903 106 GEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IW-DPDKALALMRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 349 HQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVvdtWWQTETGGFMITPLPG 428
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGAVTSITPA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 429 ATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDED 507
Cdd:cd05903 256 PEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS------RGPSVFLGYLDRPDLTADAAPEGWFrTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEdpSPELYTEVRNWVRKEI 587
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGA--LLTFDELVAYLDRQGV 407
|
490 500 510
....*....|....*....|....*....|
gi 501084078 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 408 AKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
4.16e-51 |
|
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: 184.75 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 87 QENGDRTAIIwegdDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 167 SPEAVAGRIIDSSSRLVITADEGVragrgiplKKNVDDALKnpnvnsvehVVVLKRTggkvdwHEGRDLWWSDVIEKSSA 246
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELA--------EKLASLALP---------VVLLDSA------EFDSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 247 DHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFD--YHPDDIYWCTADVGWVTGHSYLLYGPLACG 324
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 325 ATTL---MFEgvpnwptPARMAQVVDKHQVTILYTAPTAIRAlMAEGDKAiEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:cd05904 228 ATVVvmpRFD-------LEELLAAIERYKVTHLPVVPPIVLA-LVKSPIV-DKYDLSSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 402 IGNekCPVVDTWWQTE-TGGFMITPLPGATELKAGSATRPFFGVQPALVD-NEGHPQEGATEGNLVITDswPGQARTLFG 479
Cdd:cd05904 299 FPN--VDLGQGYGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG--PSIMKGYLN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 480 DHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd05904 375 NPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 560 YAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 453 MAFVVRKPGSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
5.04e-51 |
|
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: 184.76 E-value: 5.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDATQskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGEVH--RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEGVragrgiPLKKNVDDALKNpnvnsVEHVVVLKRTGGKVDWHEGRDLWWSDVI 241
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFL------PLLEAIAPRLPT-----VEHVVVMTDDAAMPEPAGVGVLAYEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyAATTFKYVfdyHPDDIY-----------W 302
Cdd:cd12119 149 AAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHAMAA----LLTDGLGL---SESDVVlpvvpmfhvnaW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 303 CTADVGWVTGHSYLLYGPlacgattlmfegvpnWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRI 382
Cdd:cd12119 222 GLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 383 LGSVGEPINPEAWEWyWKKIGnekCPVVDTWWQTETG--GFMITPLPGATELKAG-------SATRPFFGVQPALVDNEG 453
Cdd:cd12119 285 VVIGGSAVPRSLIEA-FEERG---VRVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 454 H--PQEGATEGNLVITDSWpgQARTLFGDHER----FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:cd12119 361 RelPWDGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLRT-------GDVATIDEDGYLTITDRSKDVIKSGGEWI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 528 GTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:cd12119 432 SSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTST 508
|
570
....*....|
gi 501084078 608 GKIMRRILRK 617
Cdd:cd12119 509 GKIDKKALRE 518
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-620 |
3.64e-48 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 177.26 E-value: 3.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIwEGDdatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 159 ------HSVI--FGGFSpEAVAgriidsssrlVITAD-----------EGVRAGrgiplkknvddalknpnVNSVEHVVV 219
Cdd:COG1021 105 alpahrRAEIshFAEQS-EAVA----------YIIPDrhrgfdyralaRELQAE-----------------VPSLRHVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 220 LKRTGGKVDWhegrdlwwSDVIEKSSADHQPEeMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPDD 299
Cdd:COG1021 157 VGDAGEFTSL--------DALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 300 IYWCTADVGwvtgHSYllygPLAC---------GATTLMfegVPNwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDK 370
Cdd:COG1021 227 VYLAALPAA----HNF----PLSSpgvlgvlyaGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWLDAAER 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 371 aiEGTDRSSLRILGSVGEPINPEAWewywKKIGnekcPVVDTWWQ-----TEtGGFMITPLPGATELKAGSATRPffgVQ 445
Cdd:COG1021 295 --SRYDLSSLRVLQVGGAKLSPELA----RRVR----PALGCTLQqvfgmAE-GLVNYTRLDDPEEVILTTQGRP---IS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 446 PA----LVDNEGHPQEGATEGNLV------IT---DSwPGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWI 512
Cdd:COG1021 361 PDdevrIVDEDGNPVPPGEVGELLtrgpytIRgyyRA-PEHNARAF-TPDGF-----------YRTGDLVRRTPDGYLVV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 513 TGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhGEDPSPElytEVRNWVRkEIGpLAT 592
Cdd:COG1021 428 EGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLA---ELRRFLR-ERG-LAA 501
|
570 580 590
....*....|....*....|....*....|.
gi 501084078 593 ---PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:COG1021 502 fklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
91-615 |
4.20e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 177.46 E-value: 4.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08314 25 DKTAIVFYG------RAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEgvRAGRGIPLKKNVddalknpnvnSVEHVVV------LKRTGGKV--DW----------HE 231
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSE--LAPKVAPAVGNL----------RLRHVIVaqysdyLPAEPEIAvpAWlraepplqalAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 232 GRDLWWSDVIEkssADHQPEEMNA--EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGW 309
Cdd:PRK08314 167 GGVVAWKEALA---AGLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 310 VTGHSYLLYGPLACGATTLMfegVPNWPTPArMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEP 389
Cdd:PRK08314 243 VTGMVHSMNAPIYAGATVVL---MPRWDREA-AARLIERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 390 InPEA-WEWYWKKIGnekCPVVDTWWQTETGGFMITPLPGATELK-AGSatrPFFGVQPALVDneghPQEGAT-----EG 462
Cdd:PRK08314 317 M-PEAvAERLKELTG---LDYVEGYGLTETMAQTHSNPPDRPKLQcLGI---PTFGVDARVID----PETLEElppgeVG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 463 NLVItdSWPGQARTLFGDHERFEQTyFSTF--KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK08314 386 EIVV--HGPQVFKGYWNRPEATAEA-FIEIdgKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 541 KIAEAAVVGIPHNIKGQAIYAYVTLN--HGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08314 463 AIQEACVIATPDPRRGETVKAVVVLRpeARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
1.02e-46 |
|
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: 172.07 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVIT-ADEGVRAGRGIPLKKNVDDALKNPnvnsvehvvvlkrtggkvdwhegrdlwwsdv 240
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTtADLAARLPAGGDVALLGDEALAAP------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 241 iekSSADHQPEEMNAeDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGW-VTGhsYLLYG 319
Cdd:cd17646 127 ---PATPPLVPPRPD-NLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 320 PLACGATTLMFEgvPNWPT-PARMAQVVDKHQVTILYTAPTAIRALMAEGDkaieGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:cd17646 200 PLVAGARLVVAR--PGGHRdPAYLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 399 WKKIG----NEKCP---VVD-TWWQTeTGGFMITPLP-GatelkagsatRPFFGVQPALVDNEGHPQEGATEGNLVITDs 469
Cdd:cd17646 274 LALPGaelhNLYGPteaAIDvTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGELYLGG- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 wPGQARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd17646 342 -VQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHA 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 546 AVVGIPHNIKGQAIYAYVTL-NHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17646 421 VVVARAAPAGAARLVGYVVPaAGAAGPDTA---ALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-617 |
2.02e-46 |
|
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: 171.89 E-value: 2.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 104 QSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ITADEGVRAgrgiplkknVDDALknPNVNSVEHVV-VLKRTGGKVDWHEGRDLWWSDVIEKSSADhQPEEMNAEDPLFIL 262
Cdd:TIGR03098 102 VTSSERLDL---------LHPAL--PGCHDLRTLIiVGDPAHASEGHPGEEPASWPKLLALGDAD-PPHPVIDSDMAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 263 YTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegvpNWPTPA 340
Cdd:TIGR03098 170 YTSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH-----DYLLPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 341 RMAQVVDKHQVTILYTAPtAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTEtgG 420
Cdd:TIGR03098 242 DVLKALEKHGITGLAAVP-PLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMYGLTE--A 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 421 FMITPL-PGATELKAGSATR--PFFGVQPALVDNE----GHPQEGATEGNLVITDSWPGQARTlfgdHERFE-----QTY 488
Cdd:TIGR03098 315 FRSTYLpPEEVDRRPDSIGKaiPNAEVLVLREDGSecapGEEGELVHRGALVAMGYWNDPEKT----AERFRplppfPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 489 FSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:TIGR03098 391 LHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501084078 569 EDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 471 EELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-616 |
2.90e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 171.71 E-value: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 73 GTLNLAAncLDRHlqenGDRTAIIWegDDATqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLAC 152
Cdd:PRK06188 15 GHLLVSA--LKRY----PDRPALVL--GDTR----LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 153 ARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVItADEGVRAGRGIPLKKNVDdalknpnvnSVEHVVVLKRTGGkvdwheG 232
Cdd:PRK06188 83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVPD------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 233 RDLWwsdvIEKSSADHQPEEMNAE--DPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfkyvfdyhpddiyWCTADVGWV 310
Cdd:PRK06188 147 VDLL----AAAAKFGPAPLVAAALppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 311 TGHSYLLYGPL--ACGAT---TLM----------FEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGT 375
Cdd:PRK06188 208 ADPRFLMCTPLshAGGAFflpTLLrggtvivlakFD-------PAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 376 DRSSLRILGSVGEPINP----EAWEwywkKIGnekcPV-VDTWWQTETGGFmITPLP-----GATELKAGSATRPFFGVQ 445
Cdd:PRK06188 279 DLSSLETVYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 446 PALVDNEGHPQEGATEGNLVItdSWPGQARtlfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK06188 350 VALLDEDGREVAQGEVGEICV--RGPLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 525 HRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPK 604
Cdd:PRK06188 424 FNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPL 500
|
570
....*....|..
gi 501084078 605 TRSGKIMRRILR 616
Cdd:PRK06188 501 TALGKPDKKALR 512
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-616 |
4.90e-46 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 170.22 E-value: 4.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHLQENGDRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 164 GGFSPEAVAGRIIDSSSRLVITADE-----GVRAGRGIPlkknvDDALKNPNVNSVEHVVvlkrtggkvdwhegrdlwws 238
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlagelAVELVAVTL-----LDQPGAAAGADAEPDP-------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 dviekssadhqpeEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyVFDYHPDDIYWCTADVGW-VTGHSy 315
Cdd:cd17651 132 -------------ALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQAR---ASSLGPGARTLQFAGLGFdVSVQE- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 lLYGPLACGATtLMFEGvPNW-PTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEP--INP 392
Cdd:cd17651 195 -IFSTLCAGAT-LVLPP-EEVrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNLVItdSW 470
Cdd:cd17651 270 DLREFCAGLPGLR---LHNHYGPTETHVVTALSLPGDPAAWPAPPPigRPIDNTRVYVLDAALRPVPPGVPGELYI--GG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 471 PGQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:cd17651 345 AGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAV 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 547 VVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17651 425 VLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
5.07e-46 |
|
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: 169.47 E-value: 5.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17649 2 DAVALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwHEGRDLWWsdviekssadhqp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQLAY------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 eemnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGWVTGHSYLlYGPLACGATTLMf 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 331 EGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGtDRSSLRILGSVGEPINPEAWeWYWKKIGnekCPVV 410
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELL-RRWLKAP---VRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 411 DTWWQTETggfMITPL--PGATELKAGSAT----RPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARtlfGDHERF 484
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASmpigRPLGGRSAYILDADLNPVPVGVTGELYIGG--EGLAR---GYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 485 EQT--------YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkG 556
Cdd:cd17649 313 ELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 557 QAIYAYVTLNhGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 392 KQLVAYVVLR-AAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
7.30e-46 |
|
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: 167.83 E-value: 7.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLEL-GIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGfSPEAVAGRII-DSSSRLVITA 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-YPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 187 DEGVRAGRGIPLkknvddalknpnvnsvEHVVVlkrtggkvdwhegRDLWWSDVIEKSSADHQPEEMNAEDPLFILYTSG 266
Cdd:TIGR01733 80 SALASRLAGLVL----------------PVILL-------------DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 267 STGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTA----DVgwvtghSYL-LYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFAslsfDA------SVEeIFGALLAGATLVVPPEDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 342 MAQVVDKHQVTILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTE-TGG 420
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTEtTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 421 FMITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVItdSWPGQARTLFGD----HERF-EQTYF-ST 491
Cdd:TIGR01733 277 STATLVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVpVGVV-GELYI--GGPGVARGYLNRpeltAERFvPDPFAgGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 492 FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:TIGR01733 354 GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
88-615 |
5.39e-45 |
|
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: 167.38 E-value: 5.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 88 ENGDRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfS 167
Cdd:cd12117 9 RTPDAVAVVYGDRSLT------YAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL----D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 168 PEAVAGRIidsssRLVItADEGVRagrgiplkknvddalknpnvnsvehvVVLKRTGGKVDWHEGRDLWWSDVIEKSSAD 247
Cdd:cd12117 79 PELPAERL-----AFML-ADAGAK--------------------------VLLTDRSLAGRAGGLEVAVVIDEALDAGPA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 248 HQPEEMN-AEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVfDYHPDDIYWCTADVGWvTGHSYLLYGPLACGAT 326
Cdd:cd12117 127 GNPAVPVsPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT-NYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGAR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 -TLMFEGVPnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEPINPEawewyWKKIGNE 405
Cdd:cd12117 204 lVLAPKGTL--LDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPP-----HVRRVLA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 406 KCP---VVDTWWQTETGGF----MITPL-PGATELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTL 477
Cdd:cd12117 272 ACPglrLVNGYGPTENTTFttshVVTELdEVAGSIPIG---RPIANTRVYVLDEDGRPVPPGVPGELYV--GGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:cd12117 347 LNRpaltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 554 IKGQAIYAYVTLNHGEDPspelyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 427 GGDKRLVAYVVAEGALDA-----AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
5.38e-43 |
|
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: 160.95 E-value: 5.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHLQENGDRTAIIwegddaTQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 164 GGFSPEAVAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviek 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 244 ssadhqpeemNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATTFKyvfdyhPDDIywctADVGWVTG-----HSY 315
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFS------AEEL----AGVLASTSicfdlSVF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 LLYGPLACGATTLMFEGVPNWPT-PARMaqvvdkhQVTILYTAPTAIRALMAEGDKAiegtdrSSLRILGSVGEPINPEA 394
Cdd:cd12115 163 ELFGPLATGGKVVLADNVLALPDlPAAA-------EVTLINTVPSAAAELLRHDALP------ASVRVVNLAGEPLPRDL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 WEWYWKKIGNEKcpVVDTWWQTETGGF-MITPLPGATElKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQ 473
Cdd:cd12115 230 VQRLYARLQVER--VVNLYGPSEDTTYsTVAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYI--GGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 474 ARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd12115 305 ARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 550 IPHNIKGQAIYAYVTLnhgEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 385 IGDAAGERRLVAYIVA---EPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
92-616 |
6.48e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 161.61 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 92 RTAIIWEGDdatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV 171
Cdd:PRK08276 1 PAVIMAPSG-----EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 172 AGRIIDSSSRLVITADEGVRAGRGIPlkknvdDALKNpnvnsveHVVVLKRTGGKVDWHEGRDLWwsdviekssADHQPE 251
Cdd:PRK08276 76 AYIVDDSGAKVLIVSAALADTAAELA------AELPA-------GVPLLLVVAGPVPGFRSYEEA---------LAAQPD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 252 EMNAEDPL--FILYTSGSTGKPKGVLHTTGGYLVYAA---TTFKYVFDYH--PDDIYWCTADvgwvtghsylLY--GPLA 322
Cdd:PRK08276 134 TPIADETAgaDMLYSSGTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYggPDSVYLSPAP----------LYhtAPLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTLMFEGV----PNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA---- 394
Cdd:PRK08276 204 FGMSALALGGTvvvmEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVkram 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 WEWyWKKIGNEkcpvvdTWWQTETGGF-MITPLPGATelKAGSATRPFFGVQpALVDNEGHPQEGATEGNlvITDSWPGQ 473
Cdd:PRK08276 283 IDW-WGPIIHE------YYASSEGGGVtVITSEDWLA--HPGSVGKAVLGEV-RILDEDGNELPPGEIGT--VYFEMDGY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 474 ARTLFGDHERFEQTY----FSTFknmyfsGDGARRDEDGYYWITGRVDDVLnVSGhrlGT----AEIESALVSHPKIAEA 545
Cdd:PRK08276 351 PFEYHNDPEKTAAARnphgWVTV------GDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 546 AVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 421 AVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-649 |
1.42e-42 |
|
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: 165.80 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IfggfSPEAVAGRII----DSSSRLVITADEgvragrgiplkknVDDALKNPNVNSVEhvvvlkrtggkVDwhegrdlww 237
Cdd:COG1020 556 L----DPAYPAERLAymleDAGARLVLTQSA-------------LAARLPELGVPVLA-----------LD--------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 238 SDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIywctadVGWVTGHS--- 314
Cdd:COG1020 599 ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfda 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 315 --YLLYGPLACGATTLMF--EGVPNwptPARMAQVVDKHQVTILYTAPTAIRALMAEGdkaieGTDRSSLRILGSVGEPI 390
Cdd:COG1020 672 svWEIFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVGGEAL 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 391 NPEAWEWYWKKIGNekCPVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVIt 467
Cdd:COG1020 744 PPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYEVTPPDADGGSVPigRPIANTRVYVLDAHLQPVpVGVP-GELYI- 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 468 dSWPGQARtlfGDHERFEQT--YF--STFKN----MYFSGDGARRDEDG---YywiTGRVDDVLNVSGHR--LGtaEIES 534
Cdd:COG1020 820 -GGAGLAR---GYLNRPELTaeRFvaDPFGFpgarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRieLG--EIEA 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 535 ALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRnwvRKEIGPLATPDVLHWTDSLPKTRSGKimrrI 614
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAAVVLLLPLPLTGNGK----L 963
|
570 580 590
....*....|....*....|....*....|....*
gi 501084078 615 LRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIA 649
Cdd:COG1020 964 DRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLL 998
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
1.86e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 160.62 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 90 GDRTAIIWEgDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEGvragrgIPLKKnvddALKNPNVNSVEHVVVLKRTGGKVDwhegrdlwwsDVIEKSSA-DH 248
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQF------YPMYR----QIQQEDATPLRHICLTRVALPADD----------GVSSFTQLkAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 249 QPEEMN------AEDPLFILYTSGSTGKPKGVLHTT-----GGYLVYAATTFKYvfdyhpDDIYW-----------CTAd 306
Cdd:PRK08008 160 QPATLCyapplsTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYSAWQCALRD------DDVYLtvmpafhidcqCTA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 307 vgwvtghsylLYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTD--RSSLRILg 384
Cdd:PRK08008 233 ----------AMAAFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclREVMFYL- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 385 svgePINPEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGAtELKAGSATRPFFGVQPALVDNEGHPQEGATEGNL 464
Cdd:PRK08008 298 ----NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 465 VITDSwPGqaRTLFgdherfeQTYF----STFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK08008 370 CIKGV-PG--KTIF-------KEYYldpkATAKVLeadgwLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 536 LVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08008 440 IATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
.
gi 501084078 616 R 616
Cdd:PRK08008 517 K 517
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
8.10e-42 |
|
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: 157.45 E-value: 8.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwegddaTQSKHISYRELHRDVCRFANTLLELG-IKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd05941 1 DRIAIV------DDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVItadegvragrgiplkknvDDALknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhq 249
Cdd:cd05941 75 ELEYVITDSEPSLVL------------------DPAL------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 peemnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpddIYWCTADV-----------GWVTGhsylLY 318
Cdd:cd05941 94 -----------ILYTSGTTGRPKGVVLTHANLAANVRALVDA--------WRWTEDDVllhvlplhhvhGLVNA----LL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 319 GPLACGATTLMfegVPNwPTPARMAQVVDKHQVTILYTAPT-------AIRALMAEGDKAIEGTDRSsLRILGSVGEPIN 391
Cdd:cd05941 151 CPLFAGASVEF---LPK-FDPKEVAISRLMPSITVFMGVPTiytrllqYYEAHFTDPQFARAAAAER-LRLMVSGSAALP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 392 PEAWEwYWKKIGNEkcPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVDNE-GHPQEGATEGNL------ 464
Cdd:cd05941 226 VPTLE-EWEAITGH--TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIqvrgps 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 465 VITDSWPGQARTlfgdHERF-EQTYFSTfknmyfsGDGARRDEDGYYWITGRV-DDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:cd05941 301 VFKEYWNKPEAT----KEEFtDDGWFKT-------GDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGV 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEDP-SPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05941 370 SECAVIGVPDPDWGERVVAVVVLRAGAAAlSLE---ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
8.87e-42 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 158.44 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 139 MPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRGIPLKKNVDDAlkNPNVnsvehVV 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA--APAK-----AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 219 VLKRTGGKVDWH-EGRDLWWSDVIEKSSADH-------QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 291 YVfDYHPDDIYWCTADVGWVTGhSYLLYGPLACGATTLMFEGVpnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDK 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA---PLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 371 AIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcPVVDTWWQTETGGFMI--TPL-PGAtelkAGSATRPFFGVQPA 447
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLqPQA----PGAFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 448 LVDNEG--HPQEGATEGNLVITDSWPGQA-RTLFGDHerfEQTYFSTFKnMYFS--------GDGARRDEDGYYWITGRV 516
Cdd:PLN03051 304 LLNDNGvpYPDDQPCVGEVALAPPMLGASdRLLNADH---DKVYYKGMP-MYGSkgmplrrhGDIMKRTPGGYFCVQGRA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 517 DDVLNVSGHRLGTAEIESALVSHPK-IAEAAVVGIPHNIKGQAIYAYVTLN------HGEDPSPELYTEVRNWVRKEIGP 589
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGPELLVIFLVLgeekkgFDQARPEALQKKFQEAIQTNLNP 459
|
490 500
....*....|....*....|....*..
gi 501084078 590 LATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 460 LFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
1.91e-41 |
|
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: 156.64 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 86 LQENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 166 FSPEAVAgRIIDSSSRLVITADEGvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekss 245
Cdd:cd05945 75 SPAERIR-EILDAAKPALLIADGD-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 adhqpeemnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGW---VTGhsylLYGPLA 322
Cdd:cd05945 98 -----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFdlsVMD----LYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTlmfegvpnWPTP-------ARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGEPI-NPEA 394
Cdd:cd05945 162 SGATL--------VPVPrdatadpKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLpHKTA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 WEWywkKIGNEKCPVVDTWWQTET----GGFMITPLP--GATELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVITD 468
Cdd:cd05945 232 RAL---QQRFPDARIYNTYGPTEAtvavTYIEVTPEVldGYDRLPIG---YAKPGAKLVILDEDGRPVPPGEKGELVISG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 swPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:cd05945 306 --PSVSKGYLNNPEKTAAAFFPDEGQrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 548 VGIPHNIKGQAIYAYVTLNHGEDPSPElyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 384 VPKYKGEKVTELIAFVVPKPGAEAGLT--KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-615 |
6.16e-41 |
|
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: 156.13 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwegdDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITAD-----EGVRAGRGIPLKKNVDDALKNPNVNSvehvvvlkrtggkvdwhegrdlwwsdvieKSS 245
Cdd:cd05923 92 LAELIERGEMTAAVIAVdaqvmDAIFQSGVRVLALSDLVGLGEPESAG-----------------------------PLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEemnAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATTFKYVFDYH-------PddIYWctadvgwVTGHSY 315
Cdd:cd05923 143 EDPPRE---PEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHnvvlglmP--LYH-------VIGFFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 LLYGPLACGATTLmfegVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAW 395
Cdd:cd05923 211 VLVAALALDGTYV----VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 396 EWYWKKIGNEKcpvVDTWWQTETGGFMITPLPgatelKAGSATRPFFGVQPALVDNEGHPQEGAT---EGNLVITDS--- 469
Cdd:cd05923 285 ERVNQHLPGEK---VNIYGTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEALAngeEGELIVAAAada 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 -WPGQARtlfgdheRFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd05923 357 aFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 549 GIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNwvrKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05923 430 GVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
4.10e-40 |
|
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: 152.25 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHsvifggfspeavagriidsssrlvitad 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVV---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgIPLkknvddalkNPNVNSVEHVVVLKRTGGKVdwhegrdlwwsdVIEKSSADhqpeemnaeDPLFILYTSGS 267
Cdd:cd05935 54 --------VPI---------NPMLKERELEYILNDSGAKV------------AVVGSELD---------DLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYlvyAATTFKYVFDYH--PDDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegVPNWPTPArMAQV 345
Cdd:cd05935 96 TGLPKGCMHTHFSA---AANALQSAVWTGltPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL---MARWDRET-ALEL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 346 VDKHQVTILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITP 425
Cdd:cd05935 169 IEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 LPGAteLKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVItdSWPGQARTLFGDHERFEQTYFSTFKNMYF-SGDGAR 503
Cdd:cd05935 244 PPLR--PKLQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIEIKGRRFFrTGDLGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE--DPSPElytEVRN 581
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEE---DIIE 396
|
490 500 510
....*....|....*....|....*....|....
gi 501084078 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 397 WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-615 |
2.65e-39 |
|
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: 150.90 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 90 GDRTAIiwEGDDATqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd12116 1 PDATAV--RDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITadegvragrgiplkknvDDALKNPnvnsvehvvvLKRTGGKVDWHEGRDlwwsdvieKSSADHQ 249
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDALPDR----------LPAGLPVLLLALAAA--------AAAPAAP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 PEEMNAEDPLFILYTSGSTGKPKGV----------LHTTGGYL-------VYAATTfkYVFDYhpddiywctadvgwvtg 312
Cdd:cd12116 120 RTPVSPDDLAYVIYTSGSTGRPKGVvvshrnlvnfLHSMRERLglgpgdrLLAVTT--YAFDI----------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 313 hSYL-LYGPLACGATTLMFEGVPNwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGdkaieGTDRSSLRIL-GsvGEPI 390
Cdd:cd12116 181 -SLLeLLLPLLAGARVVIAPRETQ-RDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAGLTALcG--GEAL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 391 NPEawewywkkIGNEKCPVVDTWWQ----TETggfmiTPLPGATELKAGSAT----RPFFGVQPALVDNEGHPQEGATEG 462
Cdd:cd12116 252 PPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPipigRPLANTQVYVLDAALRPVPPGVPG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 463 NLVITDswPGQARTLFGD----HERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:cd12116 319 ELYIGG--DGVAQGYLGRpaltAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALA 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 538 SHPKIAEAAVVGIPHNIKGQaIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12116 397 AHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
3.44e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.85 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 79 ANCLDRHLQENGDRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNTTT------WRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 159 HSVIFGGFSPEAVAGRIIDSSSRLVITadEGVRAgrgiPLKKNVDDAlknpnVNSVEHVVVLkrtGGKVDwheGRDLWWS 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALA----PVATAVRDI-----VPLLSTVVVA---GGSSD---DSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 DVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAATTFKYVFDYH-PDDIYWCTADVGWVTGHSY 315
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 LLYGpLACGATTLMFegvpnwPT----PARMAQVVDKHQVTILYTAPTAIRALMAegDKAIEGTDRsSLRILGSVGEPIN 391
Cdd:PRK07786 234 MLPG-LLLGAPTVIY------PLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDL-ALRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 392 PEAWEWYwkkigNEKCP---VVDTWWQTEtggfmITP----LPGATEL-KAGSATRPFFGVQPALVDNE------GHPQE 457
Cdd:PRK07786 304 DTLLRQM-----AATFPeaqILAAFGQTE-----MSPvtcmLLGEDAIrKLGSVGKVIPTVAARVVDENmndvpvGEVGE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 458 GATEGNLVITDSWPGQARTLfgdhERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:PRK07786 374 IVYRAPTLMSGYWNNPEATA----EAFAGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 538 SHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDpSPELyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07786 443 SHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDA-ALTL-EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
570
....*....|....*
gi 501084078 618 -IAAGDTSNLGDTST 631
Cdd:PRK07786 521 rYGACVNVERRSASA 535
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-617 |
7.94e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 150.58 E-value: 7.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 75 LNLAaNCLDRHLQENGDRTAIIWeGDdatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 155 IGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD---EGVRAGRGIPLkknvddalknpnvnSVEHVVVLKRTGGKVDWHE 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASP--------------DLTHVVAIGGARAGLDYEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 232 GrdlwwsdVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaatTFKYVFDYHPDDIYWCT--ADVGW 309
Cdd:PRK07470 146 L-------VARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG--------QMAFVITNHLADLMPGTteQDASL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 310 VT-------GHSYLLygPLACGATTLMFEGVPNwpTPARMAQVVDKHQVTILYTAPTaIRALMAEgDKAIEGTDRSSLRI 382
Cdd:PRK07470 211 VVaplshgaGIHQLC--QVARGAATVLLPSERF--DPAEVWALVERHRVTNLFTVPT-ILKMLVE-HPAVDRYDHSSLRY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 383 LGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGfMITPLPGA-------TELKAGSATRPFFGVQPALVDNEGHP 455
Cdd:PRK07470 285 VIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTG-NITVLPPAlhdaedgPDARIGTCGFERTGMEVQIQDDEGRE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 456 -QEGATEGNLVItdswpGQArtLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK07470 361 lPPGETGEICVI-----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK07470 434 EKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
....
gi 501084078 614 ILRK 617
Cdd:PRK07470 511 MVRE 514
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
87-618 |
2.99e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 146.23 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 87 QENGDRTAIIwegDDATQskhISYRELHRDVCRFANTLLELGIKKGDVVAI----YMPMVpeaaVAMLACARIGAVHSVI 162
Cdd:PRK07788 60 RRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 163 FGGFSPEAVAGRIIDSSSRLVITADEGVRAGRGIPlkknvddalknPNVNSVeHVVVLKRTGGKVDWHEGRDLwwSDVIE 242
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRL-RAWGGNPDDDEPSGSTDETL--DDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 243 KSSADHQPEemnAEDP-LFILYTSGSTGKPKGVLHTTggylVYAATTFKYVFDYHP---DDIYWCTADVGWVTGHSYLLY 318
Cdd:PRK07788 196 GSSTAPLPK---PPKPgGIVILTSGTTGTPKGAPRPE----PSPLAPLAGLLSRVPfraGETTLLPAPMFHATGWAHLTL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 319 GpLACGATTLM---FEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAW 395
Cdd:PRK07788 269 A-MALGSTVVLrrrFD-------PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 396 EWYWKKIGnekcPVV-DTWWQTETGGFMI-TPlpgaTELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNLVITDSWP 471
Cdd:PRK07788 341 TRALEAFG----PVLyNLYGSTEVAFATIaTP----EDLAEAPGTvgRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 472 GQARTLFGDHERFeqtyfstfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK07788 413 FEGYTDGRDKQII--------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 552 HNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK07788 485 DEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
3.66e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 146.05 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwegDDatQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DN--HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVI--TADEGVR-AGRGIPLKKNVDdalknpnvnSVEHVVVLKRTGGKVDwhegrDLWWSDVIEKSSAD 247
Cdd:PRK06087 113 LVWVLNKCQAKMFFapTLFKQTRpVDLILPLQNQLP---------QLQQIVGVDKLAPATS-----SLSLSQIIADYEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 248 HQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATT 327
Cdd:PRK06087 179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 328 LMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPInP-----EAWEWYWKki 402
Cdd:PRK06087 258 VLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PkkvarECQQRGIK-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 403 gnekcpVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNE------GHPQEGATEGnlvitdswPGQART 476
Cdd:PRK06087 329 ------LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEArktlppGCEGEEASRG--------PNVFMG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 477 LFGDHERfeqtyfsTFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP 551
Cdd:PRK06087 395 YLDEPEL-------TARALdeegwYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 552 HNIKGQAIYAYVTLNhGEDPSPELyTEVRNWV-RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 468 DERLGERSCAYVVLK-APHHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
4.88e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 144.72 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEGVRagrgiplkknvddalknpnvnsvEHVVVLKRTggkvdwhegrdlwWSDVIEKSSADHQP 250
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA-----------------------KLIPGISVK-------------FAELMNGPKEEAEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 -EEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLL----YG-PLacg 324
Cdd:PRK03640 135 qEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMrsviYGmRV--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 325 atTLM--FEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaiEGTDRSSLR--ILGsvGEPINPEAWEwywk 400
Cdd:PRK03640 211 --VLVekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLG---EGTYPSSFRcmLLG--GGPAPKPLLE---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 kIGNEK-CPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNeGHPQEGATEGNLVItdswpgQARTLFG 479
Cdd:PRK03640 273 -QCKEKgIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV------KGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 480 DHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQA 558
Cdd:PRK03640 345 GYLNREDATRETFQDGWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 559 IYAYVTlnHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 425 PVAFVV--KSGEVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
82-620 |
1.09e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 144.92 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEgddaTQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12583 24 FDATVARFPDREALVVR----HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADeGVRA-------GRGIP-LKKNVDDALKNPNVNSVEHVVVL--KRTGGKVDWHE 231
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTsdyhamlQELLPgLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 232 --GRdlwwSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTF----KYVFdyhPDDI 300
Cdd:PRK12583 179 lqAR----GETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---PVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 301 YWC----TADVGWVTGHSYLLY-----GPLAcgatTLmfegvpnwptparmaQVVDKHQVTILYTAPTAIRALMAEGDKA 371
Cdd:PRK12583 252 YHCfgmvLANLGCMTVGACLVYpneafDPLA----TL---------------QAVEEERCTALYGVPTMFIAELDHPQRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 372 ieGTDRSSLRILGSVGEPINPEAWEwywKKIGNEKCP-VVDTWWQTETGGfmITPLPGAT---ELKAGSATRPFFGVQPA 447
Cdd:PRK12583 313 --NFDLSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAAddlERRVETVGRTQPHLEVK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 448 LVDNEGH--PQ----EGATEGNLVITDSWpgqartlfGDHERfeqTYFSTFKN--MYfSGDGARRDEDGYYWITGRVDDV 519
Cdd:PRK12583 386 VVDPDGAtvPRgeigELCTRGYSVMKGYW--------NNPEA---TAESIDEDgwMH-TGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 520 LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWT 599
Cdd:PRK12583 454 IIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFV 530
|
570 580
....*....|....*....|.
gi 501084078 600 DSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12583 531 DEFPMTVTGKVQKFRMREISI 551
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
91-615 |
2.82e-36 |
|
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: 142.47 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd17655 12 DHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRII----DSSSRLVITADegvragrgiPLKKNVDDAlknpnvnsvEHVVVLKrtggkvdwhegrdlwwSDVIEKSSA 246
Cdd:cd17655 82 PEERIQyileDSGADILLTQS---------HLQPPIAFI---------GLIDLLD----------------EDTIYHEES 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 247 DHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGG--YLVYAATTfKYVFDYHpddiywctADVGWVTGHSYLL-----YG 319
Cdd:cd17655 128 ENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWANK-VIYQGEH--------LRVALFASISFDAsvteiFA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 320 PLACGATTLMFEGVPNWPTPARMaQVVDKHQVTILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWEwYW 399
Cdd:cd17655 199 SLLSGNTLYIVRKETVLDGQALT-QYIRQNRITIIDLTPAHLKLLDAADD-----SEGLSLKHLIVGGEALSTELAK-KI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 400 KKIGNEKCPVVDTWWQTETG-GFMITPLPGATELKAG-SATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTL 477
Cdd:cd17655 272 IELFGTNPTITNAYGPTETTvDASIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQPVGVAGELYI--GGEGVARGY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:cd17655 350 LNrpelTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 554 IKGQAIYAYVTLNHGEDPSpelytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17655 430 QGQNYLCAYIVSEKELPVA-----QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
4.49e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 142.72 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 90 GDRTAIIWeGDDAtqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEgvRAGRgiplkknVDDALknPNVNSVEHVVVLKRTGGKVDWHEGRDlwWSDVIEKSSADHQ 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPR-------VAEVL--PRLPKLRTLVVVEDGSGNDLLPGAVD--YEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 PEEMNAEDpLFILYTSGSTGKPKGVLHTT--------GGYLVYAATTfkyvfdyhPDDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEP--------IEDEEELAKRAAAGPGMRRFPAPPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTL-----MFEG----VPNWPT--PARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPI 390
Cdd:PRK07798 229 MHGAGQWaafaaLFSGqtvvLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 391 NPEAWEWYWKKIGNekCPVVDTWWQTETGgFMITplpGATELKAGSATRPFFGVQP--ALVDNEGHPQEGATEGNLVItd 468
Cdd:PRK07798 309 SPSVKEALLELLPN--VVLTDSIGSSETG-FGGS---GTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVEPGSGEIGWI-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 swpgqART------LFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:PRK07798 381 -----ARRghiplgYYKDPEKTAETFPTIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPD 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 542 IAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK07798 456 VADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
1.11e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 140.27 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 117 VCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP---EAVAGRIIDSSSRLVITADEGVRag 193
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPtlkESVLRYLVADAGGRIVLADAGAA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 194 rgiplkknvdDALKNPNVNSVEHVVVLkrtggkvdwheGRDLWWSDviEKSSADHQPEEmnaEDPLFILYTSGSTGKPKG 273
Cdd:cd05922 81 ----------DRLRDALPASPDPGTVL-----------DADGIRAA--RASAPAHEVSH---EDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 274 VL--HTTggyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGpLACGATTLMFE-GVPnwptPARMAQVVDKHQ 350
Cdd:cd05922 135 VRlsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNdGVL----DDAFWEDLREHG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 351 VTILYTAPTaIRALMAEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYwkkigNEKCP---VVDTWWQTETGGFMiTPLP 427
Cdd:cd05922 207 ATGLAGVPS-TYAMLTRLGFDPAKL--PSLRYLTQAGGRLPQETIARL-----RELLPgaqVYVMYGQTEATRRM-TYLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 428 GATEL-KAGSATRPFFGVQPALVDNEGHPQ------EGATEGNLVITDSWPGQArtlfgdherfEQTYFSTFKNMYFSGD 500
Cdd:cd05922 278 PERILeKPGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYWNDPP----------YRRKEGRGGGVLHTGD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 501 GARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIkGQAIYAYVTLNHGEDPSPelyteVR 580
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-----VL 421
|
490 500 510
....*....|....*....|....*....|....*.
gi 501084078 581 NWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 422 RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
2.08e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 141.39 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDATQSkhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEGVragrgipLKKnVDDALKnpNVNSVEHVVVLKRTGGKVDwheGRDLWWSDVI 241
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRD--ELPSLRHIVVLDPRGLRDD---PRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEMNA-------EDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIY-----WCtadvgW 309
Cdd:COG1022 162 ALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 310 VTGHSyLLYGPLACGATTLMFEGVPNwpTPARMAQVvdkhQVTILYTAP-------TAIRALMAEG--------DKAIE- 373
Cdd:COG1022 236 VFERT-VSYYALAAGATVAFAESPDT--LAEDLREV----KPTFMLAVPrvwekvyAGIQAKAEEAgglkrklfRWALAv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 374 GTDRSSLRILG----------------------------------SVGEPINPEAWEWYWkKIGnekCPVVDTWWQTETG 419
Cdd:COG1022 309 GRRYARARLAGkspslllrlkhaladklvfsklrealggrlrfavSGGAALGPELARFFR-ALG---IPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 420 GFMITPLPGATelKAGSATRPFFGVQpalV----DNE----------G-HPQEGATegnlvitdswpgqARTLFGDHerf 484
Cdd:COG1022 385 PVITVNRPGDN--RIGTVGPPLPGVE---VkiaeDGEilvrgpnvmkGyYKNPEAT-------------AEAFDADG--- 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 485 eqtYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGhrlGT----AEIESALVSHPKIAEAAVVG 549
Cdd:COG1022 444 ---WLHT-------GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
2.50e-35 |
|
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: 139.71 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwegddaTQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHsVIFGGFSPEA 170
Cdd:cd12114 2 DATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY-VPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRII-DSSSRLVITADEgvragrgiplkknvdDALKNPNVNsvehvvvlkrtggkvdwhegRDLWWSDVIEKSSADHQ 249
Cdd:cd12114 75 RREAILaDAGARLVLTDGP---------------DAQLDVAVF--------------------DVLILDLDALAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 PEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTFKYVFDyhPDDIYWCTADVGW---VtghsYLLYGPLACGA 325
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSSLSFdlsV----YDIFGALSAGA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 326 TtLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGdkAIEGTDRSSLR-ILGSvGEPINPEawewywkkign 404
Cdd:cd12114 194 T-LVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL--EAAQALLPSLRlVLLS-GDWIPLD----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 405 ekcpVVDTWWQTETGGFMITpLPGATELKAGSAT----------------RPFFGVQPALVDNEGHPQEGATEGNLVItd 468
Cdd:cd12114 259 ----LPARLRALAPDARLIS-LGGATEASIWSIYhpidevppdwrsipygRPLANQRYRVLDPRGRDCPDWVPGELWI-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 SWPGQARTLFGDHERFEQTYFS--TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:cd12114 332 GGRGVALGYLGDPELTAARFVThpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 547 VVGIPhNIKGQAIYAYVTLnhGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 412 VVVLG-DPGGKRLAAFVVP--DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
70-617 |
3.20e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.52 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 70 YEDGTLnlaANCLDRHLQENGDRTAIIWEGddATQSkhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAM 149
Cdd:PRK05605 29 YGDTTL---VDLYDNAVARFGDRPALDFFG--ATTT----YAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 150 LACARIGAV---HSVIFggfSPEAVAGRIIDSSSRLVITADegvragrgiplkKNVDDALKNPNVNSVEHVV-------- 218
Cdd:PRK05605 100 YAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWD------------KVAPTVERLRRTTPLETIVsvnmiaam 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 219 -VLKRTGGKV---DWHEGRD---------LWWSDVI------EKSSADHqpEEMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PRK05605 165 pLLQRLALRLpipALRKARAaltgpapgtVPWETLVdaaiggDGSDVSH--PRPTPDDVALILYTSGTTGKPKGAQLTHR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 280 GYLVYAATTfkyvfdyhpddiywctadVGWVTG---------------HSY-----LLYGPLaCGATTLMFegvpnwPTP 339
Cdd:PRK05605 243 NLFANAAQG------------------KAWVPGlgdgpervlaalpmfHAYgltlcLTLAVS-IGGELVLL------PAP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 340 aRMAQVVD---KHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEawewywkkignekcpVVDTWwQT 416
Cdd:PRK05605 298 -DIDLILDamkKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMALPVS---------------TVELW-EK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 417 ETGGFMI--------TPL----PGATELKAGSATRPFFGVQPALVD--NEGHPQEGATEGNLVItdswpgQARTLF-GDH 481
Cdd:PRK05605 359 LTGGLLVegygltetSPIivgnPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLV------RGPQVFkGYW 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 482 ERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYA 561
Cdd:PRK05605 433 NRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVA 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 562 YVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 513 AVVLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-623 |
3.25e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 139.56 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 189 GVRAGRGIPLKknvddalknpnvnsvehvvvLKRTGGKVDWHEGRDlwwsdvieKSSADhqpeemnAEDPLFILYTSGST 268
Cdd:PRK09088 103 AVAAGRTDVED--------------------LAAFIASADALEPAD--------TPSIP-------PERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVvdK 348
Cdd:PRK09088 148 GQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDP--A 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 349 HQVTILYTAPTAIRALMAEgdkaiEGTDRSSLRILGSV---GEPiNPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITP 425
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQ-----PGFDAAALRHLTALftgGAP-HAAEDILGWLDDG---IPMVDGFGMSEAGTVFGMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 L-PGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT--DSWPGQARTLFGDHERF-EQTYFSTfknmyfsGDG 501
Cdd:PRK09088 296 VdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAFtGDGWFRT-------GDI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRN 581
Cdd:PRK09088 369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE---RIRS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 501084078 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR-KIAAGDT 623
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRdALAAGRK 488
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
6.26e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 139.06 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 83 DRHLQENGDRTAIIWEGDDATqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGEV----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 163 FGGFSPEAVAGRIIDSSSRLVITAdegvRAGRGIplkknVDDALKN-PNVnsvEHVVVLKRTGGKVDWHEgrdlwWSDVI 241
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITS----AAKLDV-----ARALLKQcPGV---RHRLVLDGDGELEGFVG-----YAEAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEMNAEDplfILYTSGSTGKPKGVLH--------TTGGYLVYaattFKYVFDYHPDDIYWCTADVGwvtgH 313
Cdd:PRK13391 143 AGLPATPIADESLGTD---MLYSSGTTGRPKGIKRplpeqppdTPLPLTAF----LQRLWGFRSDMVYLSPAPLY----H 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 314 SyllyGPLAC-------GATTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSV 386
Cdd:PRK13391 212 S----APQRAvmlvirlGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 387 GEPINPEAWE----WyWKkignekcPVVDTWW-QTETGGFMITPLPGATElKAGSATRPFFGVqPALVDNEGHPQEgate 461
Cdd:PRK13391 284 AAPCPPQVKEqmidW-WG-------PIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDDGAELP---- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 462 gnlvitdswPGQARTLFGDHER-FEqtYF----------STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK13391 350 ---------PGEPGTIWFEGGRpFE--YLndpaktaearHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQ 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 531 EIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK13391 419 EAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
....*.
gi 501084078 611 MRRILR 616
Cdd:PRK13391 499 YKRLLR 504
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
88-621 |
7.09e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.40 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 88 ENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:PRK12316 4563 MTPDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 168 PEAVAGRIIDSSSRLVITADegvRAGRGIPLKKNVddalknpnvnsveHVVVLKRTGgkvDWhEGRdlwwsdviekssAD 247
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQS---HLLQRLPIPDGL-------------ASLALDRDE---DW-EGF------------PA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 248 HQPE-EMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpddiYWCTADVGWVTGHSYL-------LYG 319
Cdd:PRK12316 4685 HDPAvRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER---------YELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 320 PLACGATTLMFEgvPNWPTPARMAQVVDKHQVTILYTAPTAIRALmAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYW 399
Cdd:PRK12316 4756 PLINGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAW 4830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 400 KKIGNEKcpVVDTWWQTETggfMITPL---------PGATELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVITDSw 470
Cdd:PRK12316 4831 RALKPVY--LFNGYGPTET---TVTVLlwkardgdaCGAAYMPIG---TPLGNRSGYVLDGQLNPLPVGVAGELYLGGE- 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 471 pGQARTLFG----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PRK12316 4902 -GVARGYLErpalTAERFVPDPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 546 AVVGIPHNIkGQAIYAYVTLNHGE-DPSPELYTEVRNWVRKEIGPlATPDVL---HWT--DSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12316 4981 VVIAQEGAV-GKQLVGYVVPQDPAlADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLTPNGKLDRKALPQPD 5058
|
..
gi 501084078 620 AG 621
Cdd:PRK12316 5059 AS 5060
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
8.75e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.40 E-value: 8.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 ADegvragRGIPLKKNVDDALKnpnvnsVEHVVVL-------------------KRTG--GKVDWHEGRDLWWSDVIEKS 244
Cdd:PRK06710 128 LD------LVFPRVTNVQSATK------IEHVIVTriadflpfpknllypfvqkKQSNlvVKVSESETIHLWNSVEKEVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 245 SADHQPeeMNAEDPLFIL-YTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyhpddiywCTADVGWVTG--HSYLLYGPL 321
Cdd:PRK06710 196 TGVEVP--CDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYN--------CKEGEEVVLGvlPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMfEGVPNWPTPA---RMA-QVVDKHQVTILYTAPTAIRALMaeGDKAIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:PRK06710 266 AVMNLSIM-QGYKMVLIPKfdmKMVfEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 398 YWKKIG---------NEKCPVVDT--WWQTETGGFMITPLPGA----TELKAGSATRPffgvqpalvdneGHPQEGATEG 462
Cdd:PRK06710 343 FETVTGgklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 463 NLVITDSWpgqartlfgdhERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKI 542
Cdd:PRK06710 411 PQIMKGYW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 480 QEVVTIGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
1.02e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 135.30 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA-- 340
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV-------LAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 341 -------RMAQVVDKHQVTILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTW 413
Cdd:cd05944 81 rnpglfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 414 WQTE-TGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQE---GATEGNLVItdswpgQARTLFGDHERFEQTYF 489
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRdcaPDEVGEICV------AGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 490 STFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:cd05944 228 AFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 569 EDPSPElytEVRNWVRKEIGP-LATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05944 308 AVVEEE---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-622 |
5.57e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 5.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvRAGRGIPLKKNVDdalknpnvnsvehVVVLKRTGGKVDWHegrdlwwsdviekssADHQPE-EMNAEDPLFILYTSG 266
Cdd:PRK12316 617 ---HLGRKLPLAAGVQ-------------VLDLDRPAAWLEGY---------------SEENPGtELNPENLAYVIYTSG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 267 STGKPKGVLHTTGG---YLVYAATtfKYVFDYHpDDIYWCT---ADVGwvtghSYLLYGPLACGATtLMFEGVPNWPTPA 340
Cdd:PRK12316 666 STGKPKGAGNRHRAlsnRLCWMQQ--AYGLGVG-DTVLQKTpfsFDVS-----VWEFFWPLMSGAR-LVVAAPGDHRDPA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 341 RMAQVVDKHQVTILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTETGg 420
Cdd:PRK12316 737 KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQ--AGLYNLYGPTEAA- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 421 fmiTPLPGATELKAGSAT----RPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERFEQTYFSTF 492
Cdd:PRK12316 810 ---IDVTHWTCVEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAG 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEDPS 572
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL---ESEG 957
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501084078 573 PELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 958 GDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
108-615 |
2.81e-33 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 132.98 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITad 187
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhQPEemnaeDPLFILYTSGS 267
Cdd:cd17650 91 -------------------------------------------------------------QPE-----DLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTtggYLVYAATTFKYVFDYHPDDIywcTADVGWVTGHSY-LLYGPLAcgaTTLMFEG----VPN--WPTPA 340
Cdd:cd17650 105 TGKPKGVMVE---HRNVAHAAHAWRREYELDSF---PVRLLQMASFSFdVFAGDFA---RSLLNGGtlviCPDevKLDPA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 341 RMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRIL--GSVGEPINPEAWEWywKKIGnEKCPVVDTWWQTE- 417
Cdd:cd17650 176 ALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKAQDFKTLA--ARFG-QGMRIINSYGVTEa 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 418 ---TGGFMIT--PLPGATELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFGD----HERFEQTY 488
Cdd:cd17650 251 tidSTYYEEGrdPLGDSANVPIG---RPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpeltAERFVENP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 489 FSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVgIPHNIKGQA-IYAYVTLNH 567
Cdd:cd17650 326 FAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVVAAA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 501084078 568 GEDpspelYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 405 TLN-----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-617 |
3.27e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.40 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITaDEGVRAGRGIPlkknvddalknpnvnsvEHVVVLKRTggkvdwhegRDLWWSDvieksSADHQP 250
Cdd:PRK12316 2092 LAYMLEDSGAALLLT-QRHLLERLPLP-----------------AGVARLPLD---------RDAEWAD-----YPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 EEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGWVTGHSYLLYgPLACGATTLM 329
Cdd:PRK12316 2140 AVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFH-PLLNGARVLI 2217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 330 FEGvPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEgdKAIEGtDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcpV 409
Cdd:PRK12316 2218 RDD-ELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEH--AERDG-RPPAVRVYCFGGEAVPAASLRLAWEALRPVY--L 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 410 VDTWWQTETggfMITPL---------PGATELKAGSAtrpfFGVQPALVDNEGH---PQEGAteGNLVITDSwpGQARTL 477
Cdd:PRK12316 2291 FNGYGPTEA---VVTPLlwkcrpqdpCGAAYVPIGRA----LGNRRAYILDADLnllAPGMA--GELYLGGE--GLARGY 2359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FG----DHERFEQTYFS-TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIpH 552
Cdd:PRK12316 2360 LNrpglTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-D 2438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501084078 553 NIKGQAIYAYVTlnhGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 2439 GASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
3.76e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 134.10 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 79 ANCLDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 159 HSVIFGGFSPEAVAGRIIDSSSRLVITADegvrAGRGIPLKKNVDDALKNpNVNSVEHVVVLKRTGGKVDWHEGRDlWWS 238
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPD-ALPPLRAIAVVDDAADATPAPAPGA-RVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 DVIEKSSADHQ--PEEMNAEDPLFILY-TSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDDIYWCTADVGWVTGHSY 315
Cdd:PRK06164 161 LFALPDPAPPAaaGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 LLyGPLACGATTLM---FEGvpnwptpARMAQVVDKHQVTILYTAPTAIRALMAEGDkaiEGTDRSSLRILGSVG-EPIN 391
Cdd:PRK06164 240 LL-GALAGGAPLVCepvFDA-------ARTARALRRHRVTHTFGNDEMLRRILDTAG---ERADFPSARLFGFASfAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 392 PEAWEWywkkignekcpvvdtwwqTETGGFMITPLPGATELKAgsatrpFFGVQPA-------------LVDNEGH---- 454
Cdd:PRK06164 309 GELAAL------------------ARARGVPLTGLYGSSEVQA------LVALQPAtdpvsvriegggrPASPEARvrar 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 455 -PQEGA-----TEGNLVItdSWPGQARTLFGDHERFEQTYFStfkNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK06164 365 dPQDGAllpdgESGEIEI--RAPSLMRGYLDNPDATARALTD---DGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 528 GTAEIESALVSHPKIAEAAVVGIPHniKGQAI-YAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK06164 440 NPAEIEHALEALPGVAAAQVVGATR--DGKTVpVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTE 514
|
570
....*....|....*.
gi 501084078 607 SG---KIMRRILRKIA 619
Cdd:PRK06164 515 SAngaKIQKHRLREMA 530
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-615 |
5.53e-33 |
|
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: 131.99 E-value: 5.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17652 2 DAPAVVFGDE------TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqp 250
Cdd:cd17652 76 IAYMLADARPALLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 eemNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTFkyvFDYHPDDIYWCTADVGWVTGHSYLLyGPLACGATTL 328
Cdd:cd17652 91 ---TPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSFDASVWELL-MALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 329 MFEGVPNWPTPArMAQVVDKHQVTILYTAPTAIRALMAEGDKAiegtdrssLRILGSVGEPINPEawewywkkignekcp 408
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAE--------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 409 VVDTWWQ----------TET--GGFMITPLPGATELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARt 476
Cdd:cd17652 220 LVDRWAPgrrminaygpTETtvCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYI--AGAGLAR- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 477 lfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd17652 294 --GYLnrpgltaERFVADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 549 GIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 372 VRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-617 |
6.18e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.44 E-value: 6.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 83 DRHLQENGDRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK12467 519 EAQARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 163 FGGFSPEAVAGRIIDSSSRLVITADEGVRagrgiplKKNVDDALKnpnvnsvehVVVLKRTGgkvDWHEGRdlwwsdvie 242
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLA-------QLPVPAGLR---------SLCLDEPA---DLLCGY--------- 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 243 kssADHQPEEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDDIYWCTADVGWVTGHsYLLYGPL 321
Cdd:PRK12467 645 ---SGHNPEVALDPDNLaYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGAL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMFEGVPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIegtDRSSLRILgsVGEPINPEAWEWYWKK 401
Cdd:PRK12467 720 ASGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL---PRPQRALV--CGGEALQVDLLARVRA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 402 IGNEkCPVVDTWWQTETG-GFMITPLPGATELKAGSAT-RPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG 479
Cdd:PRK12467 794 LGPG-ARLINHYGPTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHR 870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 480 ----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPhNI 554
Cdd:PRK12467 871 rpalTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP-GD 949
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501084078 555 KGQAIYAYVTLNHGEDPS--PELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 950 AGLQLVAYLVPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-623 |
1.92e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 132.47 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 87 QENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggf 166
Cdd:PRK06178 44 RERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 167 SPEAVAGRII----DSSSRLVITADegvragRGIPLKKNVDDALknpnvnSVEHVVVLKRTG-----------GKVDWHE 231
Cdd:PRK06178 114 SPLFREHELSyelnDAGAEVLLALD------QLAPVVEQVRAET------SLRHVIVTSLADvlpaeptlplpDSLRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 232 GRDLWWSDVIEKSSADHQP---EEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVG 308
Cdd:PRK06178 182 LAAAGAIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 WVTGHSYLLYGPLACGATTLMfegVPNWPTPARMAqVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVG- 387
Cdd:PRK06178 262 WIAGENFGLLFPLFSGATLVL---LARWDAVAFMA-AVERYRVTRTVMLVDNAVELMDHPRFA--EYDLSSLRQVRVVSf 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 388 -EPINPEawewYWKKignekcpvvdtwWQTETGGFMITPLPGATE------LKAGSAT-------RPFF------GVQPA 447
Cdd:PRK06178 336 vKKLNPD----YRQR------------WRALTGSVLAEAAWGMTEthtcdtFTAGFQDddfdllsQPVFvglpvpGTEFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 448 LVDNE-GHPQEGATEGNLVItdswpgqaRT---LFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK06178 400 ICDFEtGELLPLGAEGEIVV--------RTpslLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 524 GHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVlHWTDSLP 603
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYKVPEI-RIVDALP 547
|
570 580
....*....|....*....|
gi 501084078 604 KTRSGKIMRRILRKIAAGDT 623
Cdd:PRK06178 548 MTATGKVRKQDLQALAEELK 567
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
108-617 |
2.09e-32 |
|
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: 129.77 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLvitad 187
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnaEDPLFILYTSGS 267
Cdd:cd05912 77 --------------------------------------------------------------------DDIATIMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnwptPARMAQV 345
Cdd:cd05912 89 TGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVdkFD-------AEQVLHL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 346 VDKHQVTILYTAPTAIRALMAEGDkaieGTDRSSLR--ILGsvGEPINPEAWEwywkkigneKC-----PVVDTWWQTET 418
Cdd:cd05912 161 INSGKVTIISVVPTMLQRLLEILG----EGYPNNLRciLLG--GGPAPKPLLE---------QCkekgiPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 419 GGFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEgatEGNLV-----ITDSWPGQARTlfgDHERFEQTYFSTfk 493
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYE---VGEILlkgpnVTKGYLNRPDA---TEESFENGWFKT-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 494 nmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgEDPSP 573
Cdd:cd05912 298 -----GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISE 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 501084078 574 ElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 371 E---ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-621 |
3.31e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 131.26 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 75 LNLAANCLDRhLQENGDRTAIIwegDDATQSKHiSYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI---DGATGRVY-TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 155 IGAVHSVIFGGFSPEAVAGRIIDSSSRLVITadegvragrgipLKKNVDdalKNPNVNSVEHVVVLkrtggKVDWHEGRD 234
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIIT------------QSCYVD---KLKGLAEDDGVTVV-----TIDDPPEGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 235 LWWSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfKYV------FDYHPDDIYWCTADVg 308
Cdd:PLN02246 158 LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPM- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 wvtGHSYLLYGPLACG-----ATTLM--FEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALmAEGDkAIEGTDRSSLR 381
Cdd:PLN02246 234 ---FHIYSLNSVLLCGlrvgaAILIMpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AKSP-VVEKYDLSSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 382 ILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTETG-------GFMITPLPgateLKAGSATRPFFGVQPALVDnegh 454
Cdd:PLN02246 302 MVLSGAAPLGKELEDAFRAKLPNAV--LGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAELKIVD---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 455 PQEGATEG-NLvitdswPGQ-------------------ARTLfgDHERFEQTyfstfknmyfsGDGARRDEDGYYWITG 514
Cdd:PLN02246 372 PETGASLPrNQ------PGEicirgpqimkgylndpeatANTI--DKDGWLHT-----------GDIGYIDDDDELFIVD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 515 RVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPD 594
Cdd:PLN02246 433 RLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIH 509
|
570 580
....*....|....*....|....*...
gi 501084078 595 VLHWTDSLPKTRSGKIMRRILR-KIAAG 621
Cdd:PLN02246 510 KVFFVDSIPKAPSGKILRKDLRaKLAAG 537
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-615 |
1.01e-31 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 128.98 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIwegDDATQskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd05920 21 LARSAARHPDRIAVV---DGDRR---LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwHEGrdlwwsdvi 241
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDR-----------------------------------------HAG--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssADHQP--EEMNAE--DPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPDDIYWCTADVGwvtgHSYLL 317
Cdd:cd05920 125 ----FDHRAlaRELAESipEVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 318 YGP-----LACGATTLMfegVPNwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINP 392
Cdd:cd05920 196 ACPgvlgtLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEWYWKKIGnekcPVVDTWWQTETGGFMITPLPGATELKAGSATRPffgVQP----ALVDNEGHPQEGATEGNLVITD 468
Cdd:cd05920 270 ALARRVPPVLG----CTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEEGELLTRG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 swPGQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd05920 343 --PYTIRGYYRAPEHNARAF--TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 549 GIPHNIKGQAIYAYVTLNhgeDPSPELyTEVRNWVRkEIGpLAT---PDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 419 AMPDELLGERSCAFVVLR---DPPPSA-AQLRRFLR-ERG-LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
91-618 |
1.53e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.82 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwegddaTQSKHISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEGVRAgrgiplkknvddALKNPNVNSVEHVVvlkrtggkvdwhegrdlWWSDVieKSSADHQ 249
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNM------------ALSMQKVSYVQRVI-----------------SITSL--KEIEDRK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 P---EEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PRK06839 140 IdnfVEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 TLmfegVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPInPEAWEWYWKKIGnek 406
Cdd:PRK06839 219 II----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVRWFYNGGAPC-PEELMREFIDRG--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 407 CPVVDTWWQTETGG--FMITPLPGATelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERF 484
Cdd:PRK06839 289 FLFGQGFGMTETSPtvFMLSEEDARR--KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI------RGPNVMKEYWNR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 485 EQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYV 563
Cdd:PRK06839 361 PDATEETIQDGWLcTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 501084078 564 TLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK06839 441 VKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-616 |
1.71e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 128.59 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 85 HLQENGDRTAIIWegddATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK13390 6 HAQIAPDRPAVIV----AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 165 GFSPeAVAGRII-DSSSRLVIT--ADEGVRAGRGIPLKKNVDdalknpnvnsvehvvvlkrTGGKVDWHEGrdlwwsdvI 241
Cdd:PRK13390 82 HLTA-PEADYIVgDSGARVLVAsaALDGLAAKVGADLPLRLS-------------------FGGEIDGFGS--------F 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEmnAEDPL--FILYTSGSTGKPKGV--------LHTTGGYLVYAATTFkyvFDYHPDDIYWCTADVGwvt 311
Cdd:PRK13390 134 EAALAGAGPRL--TEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 312 gHSyllyGPL-------ACGATTLM---FEGvpnwptpARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLR 381
Cdd:PRK13390 206 -HA----APLrwcsmvhALGGTVVLakrFDA-------QATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 382 ILGSVGEP------------INPEAWEWYWkkignekcpvvdtwwQTETGGFMITPLPGATElKAGSATRPFFGVQpALV 449
Cdd:PRK13390 274 AVIHAAAPcpvdvkhamidwLGPIVYEYYS---------------STEAHGMTFIDSPDWLA-HPGSVGRSVLGDL-HIC 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 450 DNEGHPQEGATEGNLVIT-DSWPgqartlFGDHERFEQTYFSTFKNMYF---SGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK13390 337 DDDGNELPAGRIGTVYFErDRLP------FRYLNDPEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISGGV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 526 RLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKT 605
Cdd:PRK13390 411 NIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRT 490
|
570
....*....|.
gi 501084078 606 RSGKIMRRILR 616
Cdd:PRK13390 491 PTGKLVKGLLR 501
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-616 |
3.73e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 127.69 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 85 HLQENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 165 GFSPEAVAGRIIDSSSRLVITaDEGVRAGRGIPLKKNVDDALKNPNVNsvehvvvlkrtggkvdwhegrdlwwsdVIEKS 244
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLV-DEEFDAIVALETPKIVIDAAAQADSR---------------------------RLAQG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 245 SADHQPEEMNAEDPLF-ILYTSGSTGKPKGVLHTTGgylvyaattfkyvfdyhpdDIYWCTAD----VGWVTGHSYLLYG 319
Cdd:PRK06145 137 GLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLVVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 320 PL----AC---GATTLMFEG---VPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRilgsvgep 389
Cdd:PRK06145 198 PLyhvgAFdlpGIAVLWVGGtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLA-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 390 inpeawewyWKKIGNEKCP---------------VVDTWWQTETGGfMITPLPGATEL-KAGSATRPFFGVQPALVDNEG 453
Cdd:PRK06145 268 ---------WCIGGGEKTPesrirdftrvftrarYIDAYGLTETCS-GDTLMEAGREIeKIGSTGRALAHVEIRIADGAG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 454 HPQEGATEGNLVITDswPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK06145 338 RWLPPNMKGEICMRG--PKVTKGYWKDPEKTAEAFYGDW---FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK06145 413 RVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKR 489
|
...
gi 501084078 614 ILR 616
Cdd:PRK06145 490 VLR 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-549 |
5.92e-31 |
|
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: 126.17 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnAEDPLFILYTSGS 267
Cdd:cd05907 86 -------------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYhPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPT------PAR 341
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDdlsevrPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 342 MAQV---VDKHQVTILYTAPTAIRALMAegDKAIEGtdrsSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQTET 418
Cdd:cd05907 178 FLAVprvWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHFF-RALG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 419 GGFMITPLPGAteLKAGSATRPFFGVQPALVDNeghpQEGATEGNLVITdswpgqartlfGDHERFEQTYFSTFKNMYF- 497
Cdd:cd05907 248 SAVVTLNPPGD--NRIGTVGKPLPGVEVRIADD----GEILVRGPNVML-----------GYYKNPEATAEALDADGWLh 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 498 SGDGARRDEDGYYWITGRVDDVL-NVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05907 311 TGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
1.83e-30 |
|
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: 122.38 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvp 334
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 335 nwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEwywkkignEKCPVvdTWW 414
Cdd:cd17637 77 ----PAEALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLRHVLGLDAPETIQRFE--------ETTGA--TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 415 ----QTETGGFmITPLPgATElKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFS 490
Cdd:cd17637 141 slygQTETSGL-VTLSP-YRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV------RGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 491 TFKN-MYFSGDGARRDEDGYYWITGRV--DDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:cd17637 212 TFRNgWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 501084078 568 GEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 292 GATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-620 |
3.93e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 125.31 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIwegdDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADegvrAGRG----------IP-LKKNVDDALKNPNVNSVEHVVVL--KRTGGKVD 228
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD----GFKDsdyvamlyelAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 229 WhegrdlwwSDVIEKSSADHQPE------EMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhP 297
Cdd:PRK08315 174 F--------DELLALGRAVDDAElaarqaTLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 298 DD-------IYWCtadVGWVTGHsyllygpLAC---GATT-LMFEGVpnwpTPARMAQVVDKHQVTILYTAPTairalM- 365
Cdd:PRK08315 240 EDrlcipvpLYHC---FGMVLGN-------LACvthGATMvYPGEGF----DPLATLAAVEEERCTALYGVPT-----Mf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 366 -AE-GDKAIEGTDRSSLR--IL-GSVgepinpeawewywkkignekCP------VVD---------TWWQTETGgfmitp 425
Cdd:PRK08315 301 iAElDHPDFARFDLSSLRtgIMaGSP--------------------CPievmkrVIDkmhmsevtiAYGMTETS------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 lPGAT--------ELKAGSATRPFFGVQPALVDNE-------GHPQEGATEGNLVITDSWPGQART---LfgDHERFeqt 487
Cdd:PRK08315 355 -PVSTqtrtddplEKRVTTVGRALPHLEVKIVDPEtgetvprGEQGELCTRGYSVMKGYWNDPEKTaeaI--DADGW--- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 488 yfstfknMYfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK08315 429 -------MH-TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 568 GEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08315 501 GATLTEE---DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
5.32e-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: 112.64 E-value: 5.32e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 531 EIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-628 |
6.38e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 124.49 E-value: 6.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK06155 27 LARQAERYPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 I---FGGFSPEAVAGRiidSSSRLVITADEGVRAGRGIPlkknvddalknPNVNSVEHVVVLkrtGGKVDWHEGRDLwws 238
Cdd:PRK06155 101 IntaLRGPQLEHILRN---SGARLLVVEAALLAALEAAD-----------PGDLPLPAVWLL---DAPASVSVPAGW--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 DVIEKSSADHQ--PEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDDIYWCTADVGWVTGHSyL 316
Cdd:PRK06155 161 STAPLPPLDAPapAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-A 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 317 LYGPLACGATTLM---FEGVPNWPTPARmaqvvdkHQVTILYTAPTAIRALMA----EGDKAiegtdrSSLRILGSVGEP 389
Cdd:PRK06155 239 FFQALLAGATYVLeprFSASGFWPAVRR-------HGATVTYLLGAMVSILLSqparESDRA------HRVRVALGPGVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 390 inPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPgatELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDS 469
Cdd:PRK06155 306 --AALHAAFRERFG---VDLLDGYGSTETNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 WPGQ-ARTLFGDHERFEQTYfstfKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAV 547
Cdd:PRK06155 378 EPFAfATGYFGMPEKTVEAW----RNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 548 VGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRkiAAGDTSNLG 627
Cdd:PRK06155 454 FPVPSELGEDEVMAAVVLRDGTALEPV---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQGVTADTW 528
|
.
gi 501084078 628 D 628
Cdd:PRK06155 529 D 529
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-620 |
7.69e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.81 E-value: 7.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITadegvragrgiplKKNVDDALKNPnvnSVEHVVVLKRtggkvdwhegrDLWWSDvi 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLEQLPAP---AGDTALTLDR-----------LDLNGY-- 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssADHQPE-EMNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLVYAATT----FKYVFDYHPDDIYWcta 305
Cdd:PRK12467 3226 ----SENNPStRVMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGAQERFLW--- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 306 dvgwvtghsyllygPLACGATtLMFEGVPNWpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDkaieGTDRSSLRILGS 385
Cdd:PRK12467 3299 --------------TLICGGC-LVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVF 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 386 VGEPINPEAWEWYWKKI---------GNEKCPVVDTWWQTETGGfmitpLPGATELKAGsatRPFFGVQPALVDNEGHPQ 456
Cdd:PRK12467 3359 GGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA-----VCEAPYAPIG---RPVAGRSIYVLDGQLNPV 3430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 457 EGATEGNLVITDSwpGQARtlfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLG 528
Cdd:PRK12467 3431 PVGVAGELYIGGV--GLAR---GYHqrpsltaERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 529 TAEIESALVSHPKIAEAAVVGIPhNIKGQAIYAYVTLNhgeDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
570
....*....|..
gi 501084078 609 KIMRRILRKIAA 620
Cdd:PRK12467 3582 KVDRKALPDPDA 3593
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-622 |
9.52e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.61 E-value: 9.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 ADEgvragrgiplkknvddaLKNPNVNSVEHVVVLKRTggkvdwhegrdlwwsdviEKSSADHQPEEMNAEDPLFILYTS 265
Cdd:PRK12316 3161 QSH-----------------LRLPLAQGVQVLDLDRGD------------------ENYAEANPAIRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 266 GSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDDIYWCTADVGWvTGHSYLLYGPLACGATTLMfEGVPNWPTPARMAQV 345
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWMQQ-AYGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGARVVL-AGPEDWRDPALLVEL 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 346 VDKHQVTILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYwkkigNEKCPVVDTWWQTETGGFMITP 425
Cdd:PRK12316 3283 INSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 426 LPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERFEQTYFSTFKNMYFSGDG 501
Cdd:PRK12316 3354 QCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNrpglTAERFVPDPFVPGERLYRTGDL 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEDPSPELYTEVRN 581
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP---EDEAGDLREALKA 3504
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 501084078 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 3505 HLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
105-616 |
2.63e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 122.11 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 105 SKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSR-LV 183
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARvLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ITAD--EGVRAGrgIPLKKNVDDALKNPNVNSVEHVVVLKRT--GGKVDWHEgrdlwWSDVIEKSSADHQPEEMNaedpl 259
Cdd:PRK12406 89 AHADllHGLASA--LPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG-----WLAQQEPYDGPPVPQPQS----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 260 fILYTSGSTGKPKGVLHT--TGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpn 335
Cdd:PRK12406 157 -MIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQprFD---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 wptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA----WEWyWKKIGNEkcpvvd 411
Cdd:PRK12406 232 ---PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEW-WGPVIYE------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 TWWQTETGgfMITplpGATELKA----GSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpgqARTLFGDHERFEQT 487
Cdd:PRK12406 302 YYGSTESG--AVT---FATSEDAlshpGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA----GNPDFTYHNKPEKR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 488 YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK12406 373 AEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 501084078 568 GEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 453 GATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-615 |
4.17e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.50 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 105 SKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 185 TadegvragrgiplKKNVDDALknPNVNSVEhVVVLKRTGgkvDWHEGRDlwwsdviekssaDHQPEEMNAEDPL-FILY 263
Cdd:PRK12467 1677 T-------------QSHLQARL--PLPDGLR-SLVLDQED---DWLEGYS------------DSNPAVNLAPQNLaYVIY 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 264 TSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIywctadvgWVTGHSYL-------LYGPLACGATTLMfegVPNW 336
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGA-LVNRLCATQEAYQLSAADV--------VLQFTSFAfdvsvweLFWPLINGARLVI---APPG 1793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 337 P--TPARMAQVVDKHQVTILYTAPTAIRALMaEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWW 414
Cdd:PRK12467 1794 AhrDPEQLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 415 QTETggfMITPLPGATELK--AGSATRPfFGVQPA-----LVDNEGHPQEGATEGNLVITDSwpGQARtlfGDH------ 481
Cdd:PRK12467 1869 PTET---AVDVTHWTCRRKdlEGRDSVP-IGQPIAnlstyILDASLNPVPIGVAGELYLGGV--GLAR---GYLnrpalt 1939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 482 -ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVvgIPHN-IKGQA 558
Cdd:PRK12467 1940 aERFVADPFGTVgSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgANGKQ 2017
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 559 IYAYVT-----LNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK12467 2018 LVAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
7.11e-29 |
|
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: 120.66 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFENQKLT------YRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEgvragrgiplkknvddaLKNPNVNSVEHVVVlkrtggkvDWhegrdlwwsDVIEKSSADHQP 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----------------LKSKLSFNKSTILL--------ED---------PSISQEDTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 EEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVyaATTFKYVFDYHPDDIYW---CTADVGWVTGHSYLLYGP---LA 322
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSGGtlyII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTLMFEgvpnwptpaRMAQVVDKHQVTILYTaPTAIRALMAEGDKAIEGTDRSSLRILgSVGEP--INPEAWEWYWK 400
Cdd:cd17656 201 REETKRDVE---------QLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFPTCVKHII-TAGEQlvITNEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 KigneKCPVVDTWWQTET---GGFMITPLPGATELKAgsATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTL 477
Cdd:cd17656 270 H----NVHLHNHYGPSEThvvTTYTINPEAEIPELPP--IGKPISNTWIYILDQEQQLQPQGIVGELYI--SGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHN 553
Cdd:cd17656 342 LNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 554 IKGQAIYAYVTlnhgedPSPELYT-EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17656 422 KGEKYLCAYFV------MEQELNIsQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
91-617 |
1.73e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 120.17 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDV-VAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07867 18 DDRGLYFED------SFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEGvragrgIPLKKNVDDALKNPNVNSVEHVVVLkrtggkvDWHEGrdlwwsdviekssADHQ 249
Cdd:PRK07867 92 ALARDIAHADCQLVLTESAH------AELLDGLDPGVRVINVDSPAWADEL-------AAHRD-------------AEPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 PEEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPDDIYWCTAD--------VGWVTGhsyllygpL 321
Cdd:PRK07867 146 FRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA--------L 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLM---FEGVPNWPTPARM----AQVVDKHQVTILYTAPtairalmaegdkaiEGTDRS-SLRIL-GSVGEPINP 392
Cdd:PRK07867 217 AAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPE--------------RPDDADnPLRIVyGNEGAPGDI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEwywKKIGnekCPVVDTWWQTEtGGFMITPLPGATElkaGSATRPFFGVQ-----------PALVDNEGHPQEGATE 461
Cdd:PRK07867 283 ARFA---RRFG---CVVVDGFGSTE-GGVAITRTPDTPP---GALGPLPPGVAivdpdtgtecpPAEDADGRLLNADEAI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 462 GNLVITDSwPGQARTLFGDHERFEQtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPK 541
Cdd:PRK07867 353 GELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPD 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 542 IAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07867 429 ATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
87-616 |
1.88e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 119.86 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 87 QENGDRTAIIwegDDATQskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAvHSVIFG-G 165
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 166 FSPEAVAGRIIDSSSRLVITADEGvragrgIPLkknVDDALKN-PNVNSVehvvvlkrtggkVDWHEGRDLWWSDVIEKS 244
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDEEF------SAT---VDRALADcPQATRI------------VAWTDEDHDLTVEVLIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 245 SADHQPEEMNAEDPLfILYTSGSTGKPKGVLHT-TGGYLvyaatTFKYVFDYHPddiywctadvgWVTGHSYLLYGPL-- 321
Cdd:PRK13382 186 HAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP-----------WRAEEPTVIVAPMfh 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMFEGVPNWP-------TPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:PRK13382 249 AWGFSQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 WEWYWKKIGnekcPVV-DTWWQTETGgfMITPlpgAT--ELKAG--SATRPFFGVQPALVDNEGHPQEGATEGNLVITDS 469
Cdd:PRK13382 329 VIAFMDQFG----DVIyNNYNATEAG--MIAT---ATpaDLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 wpgqarTLF-----GDHERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:PRK13382 400 ------TQFdgytsGSTKDFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 545 AAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 467 AAVIGVDDEQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
91-621 |
4.04e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 119.35 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWegddatQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PLN03102 29 NRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEGVRAGRGIPLKKNVDDALKNPNVNSVEHVVVLKRTGGKvdwhegrDLWWSDVIEK-----SS 245
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSE-------ELDYECLIQRgeptpSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEEMNAEDPLFILYTSGSTGKPKGVLHT-TGGYLVYAATTFKYVFDYHPddIYWCTADV----GWVtghsyLLYGP 320
Cdd:PLN03102 176 VARMFRIQDEHDPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMfhcnGWT-----FTWGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 321 LACGATTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALMaEGDKAIEGTDRSSLRILGSVGEPinPEAwewYWK 400
Cdd:PLN03102 249 AARGGTSVCMRHV----TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAA---LVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 KIGNEKCPVVDTWWQTETGGFMI----------TPLPGATELKAGSATRpFFGVQPALVDN----EGHPQEGATEGNLVI 466
Cdd:PLN03102 319 KVQRLGFQVMHAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGVS-ILGLADVDVKNketqESVPRDGKTMGEIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 467 TDSwpgqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PLN03102 398 KGS------SIMKGYLKNPKATSEAFKHGWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 546 AVVGIPHNIKGQAIYAYVTLNHGE----DPSPELYTEVRN---WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PLN03102 472 AVVAMPHPTWGETPCAFVVLEKGEttkeDRVDKLVTRERDlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
...
gi 501084078 619 AAG 621
Cdd:PLN03102 552 AKG 554
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
261-616 |
4.05e-28 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 118.25 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 261 ILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHP--DDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnw 336
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMekFD----- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 337 ptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINP---EAWEWYWKkignekcPVVDTW 413
Cdd:cd05929 205 --PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIDWGG-------PIIWEY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 414 WQ-TETGGFmiTPLPGATELK-AGSATRPFFGVQpALVDNEGHPQEGATEGNLVITDSWPgqartlFGDHERFEQTYFST 491
Cdd:cd05929 276 YGgTEGQGL--TIINGEEWLThPGSVGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 492 FKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGED 570
Cdd:cd05929 347 NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAD 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 501084078 571 PSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 427 AGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
84-619 |
4.47e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 118.34 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHLQENGDRTAIIwegddaTQSKHISYRELHRDVCRFANTLLELGiKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:PRK07638 9 KHASLQPNKIAIK------ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 164 GGFSPEAVAGRIIDSSSRLVITadegvragrgiplkknvDDALKNPnVNSVEHVVVlkrtggkvDWHEgrdlwWSDVIEK 243
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVT-----------------ERYKLND-LPDEEGRVI--------EIDE-----WKRMIEK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 244 SSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvyaattfkYVFDYHPDDIYWCTADVGWVTG---HSYLLYGP 320
Cdd:PRK07638 131 YLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHSLFLYGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 321 ---LACGAT-TLMFEGVPNwptparmaQVVDK---HQVTILYTAPTAIRALMAEgdkaiEGTDRSSLRILGSVGEpinpe 393
Cdd:PRK07638 203 istLYVGQTvHLMRKFIPN--------QVLDKletENISVMYTVPTMLESLYKE-----NRVIENKMKIISSGAK----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 394 awewyWKKIGNEKcpVVDTW--------WQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGhpqegategnlv 465
Cdd:PRK07638 265 -----WEAEAKEK--IKNIFpyaklyefYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAG------------ 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 466 iTDSWPGQARTLFGDHERFeqtyFSTFKNMYFS------------GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK07638 326 -EEVQKGEIGTVYVKSPQF----FMGYIIGGVLarelnadgwmtvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVtlnHGEDPSPELytevRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK07638 401 SVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQL----KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
....*.
gi 501084078 614 ILRKIA 619
Cdd:PRK07638 474 EAKSWI 479
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
87-617 |
6.46e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 118.54 E-value: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 87 QENGDRTAIIwegdDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsviFGGF 166
Cdd:PLN02330 39 ELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 167 SPEAVAGRIID----SSSRLVITADE--GVRAGRGIPlkknvddalknpnvnsvehVVVLKRT--GGKVDWHEgrdlwWS 238
Cdd:PLN02330 111 NPTALESEIKKqaeaAGAKLIVTNDTnyGKVKGLGLP-------------------VIVLGEEkiEGAVNWKE-----LL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 239 DVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfkyVFDYHPDDIYWCTAdVGWVTghSYLLY 318
Cdd:PLN02330 167 EAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS---LFSVGPEMIGQVVT-LGLIP--FFHIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 319 GPLACGATTLMFEG---VPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAegDKAIEGTDRSSLRI--LGSVGEPINPE 393
Cdd:PLN02330 241 GITGICCATLRNKGkvvVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 394 AWEWYWKKIGNEKcpVVDTWWQTETGgfMITPLPGATELKAGSATRPFFG-VQPALVDNEGHPQEGATegnlvITDSWPG 472
Cdd:PLN02330 319 LLTAFEAKFPGVQ--VQEAYGLTEHS--CITLTHGDPEKGHGIAKKNSVGfILPNLEVKFIDPDTGRS-----LPKNTPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 473 Q--ART---LFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAA 546
Cdd:PLN02330 390 ElcVRSqcvMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 547 VVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 470 VVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
246-616 |
6.72e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 117.40 E-value: 6.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYlvyAATtfkyvFDYHPDDIYWCTADV-----------GWVTGhs 314
Cdd:PRK07787 118 SWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI---AAD-----LDALAEAWQWTADDVlvhglplfhvhGLVLG-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 315 ylLYGPLACGATtLMFEGVPnwpTPARMAQVVDKHQvTILYTAPTAIRALMAEGDKAiegtdR--SSLRILGSVGEPINP 392
Cdd:PRK07787 188 --VLGPLRIGNR-FVHTGRP---TPEAYAQALSEGG-TLYFGVPTVWSRIAADPEAA-----RalRGARLLVSGSAALPV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEWYWKKIGNEkcpVVDTWWQTETggFMITPLPGATELKAGSATRPFFGVQPALVDNEGH--PQEGATEGNLVItdsw 470
Cdd:PRK07787 256 PVFDRLAALTGHR---PVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGGpvPHDGETVGELQV---- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 471 pgQARTLF-GDHERFEQT--------YFSTfknmyfsGDGARRDEDGYYWITGRVD-DVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK07787 327 --RGPTLFdGYLNRPDATaaaftadgWFRT-------GDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHP 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 541 KIAEAAVVGIPHNIKGQAIYAYVTlnHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07787 398 GVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
8.62e-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: 114.35 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYV-FDyhPDDIYWCTADVGWVTGHSYLLYGpLACGATTLMFEgvPN 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 WPTPARMAQVVDKHqvtiLYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEwywkKIGNEKCPVVDTWWQ 415
Cdd:cd17630 76 QALAEDLAPPGVTH----VSLVPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 416 TETGGfMITPLPgATELKAGSATRPFFGVQPALVDNEghpqEGATEGNLVITDSWPGQARTLFgdherFEQTYFSTfknm 495
Cdd:cd17630 145 TETAS-QVATKR-PDGFGRGGVGVLLPGRELRIVEDG----EIWVGGASLAMGYLRGQLVPEF-----NEDGWFTT---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 496 yfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSpel 575
Cdd:cd17630 210 ---KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA--- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 501084078 576 ytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 284 --ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
1.21e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 114.68 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhPDDI-------YWCTADVGwvtghsyllyGPLAC 323
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT------EQDRlcipvplFHCFGSVL----------GVLAC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 324 ---GATTLMFEgvpnwPT--PARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIegTDRSSLR--ILGsvGEPINPEAWE 396
Cdd:cd05917 66 lthGATMVFPS-----PSfdPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDK--FDLSSLRtgIMA--GAPCPPELMK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 397 WYWKKIGNEKCPVVdtWWQTETGGFMITPLPGAT-ELKAGSATRPFFGVQPALVDNEGHPQ-------EGATEGNLVITD 468
Cdd:cd05917 137 RVIEVMNMKDVTIA--YGMTETSPVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpgELCIRGYSVMKG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 SWpgqartlfGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVV 548
Cdd:cd05917 215 YW--------NDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVV 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 549 GIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 285 GVPDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
3.32e-27 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 116.39 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITaDE 188
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 189 GVragrgIPLKKNVDDALKnpnvnSVEHVVV-----------LKRTGGKVDWHEGR--DLWWSDVIEKSSADhqpeemna 255
Cdd:PRK06018 120 TF-----VPILEKIADKLP-----SVERYVVltdaahmpqttLKNAVAYEEWIAEAdgDFAWKTFDENTAAG-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 256 edplfILYTSGSTGKPKGVLHTTGGYLVYAATTFkyvfdyHPDDIYWCTADV-----------GWVTGHSyllyGPlACG 324
Cdd:PRK06018 182 -----MCYTSGTTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADTmlpvvplfhanSWGIAFS----AP-SMG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 325 ATTLMfegvpnwPTP----ARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiegtDRSSLRILGSV--GEPINPEAWEWY 398
Cdd:PRK06018 246 TKLVM-------PGAkldgASVYELLDTEKVTFTAGVPTVWLMLLQYMEK-----EGLKLPHLKMVvcGGSAMPRSMIKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 399 WKKIGNEkcpVVDTWWQTETggfmiTPLPGATELKAGSAT--------------RPFFGVQPALVDNEGH--PQEGATEG 462
Cdd:PRK06018 314 FEDMGVE---VRHAWGMTEM-----SPLGTLAALKPPFSKlpgdarldvlqkqgYPPFGVEMKITDDAGKelPWDGKTFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 463 NLVItdSWPGQARTLF--GDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK06018 386 RLKV--RGPAVAAAYYrvDGEILDDDGFFDT-------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHP 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 457 KVAEAAVIGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
1.40e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 113.55 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYGDRRYT------WRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVItadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkVDwhegRDLWWSDVI 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF------------------------------------------VD----REFEYEDLL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSADHQPEEMNAE-DPLFILYTSGSTGKPKGVLHT-TGGYLvyAATTFKYVFDYHPDDIYWCTADV----GWVtghsy 315
Cdd:cd12118 118 AEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC----- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 LLYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAw 395
Cdd:cd12118 191 FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVHVMTAGAPPPAA- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 396 ewYWKKIGNEKCPVVDTWWQTETGGFMIT--------PLPgaTELKAGSATR---PFFGVQPALV-DNEGH---PQEGAT 460
Cdd:cd12118 263 --VLAKMEELGFDVTHVYGLTETYGPATVcawkpewdELP--TEERARLKARqgvRYVGLEEVDVlDPETMkpvPRDGKT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 461 ------EGNLVitdswpgqARTLFGDHERFEQTyfstFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:cd12118 339 igeivfRGNIV--------MKGYLKNPEATAEA----FRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVE 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDsLPKTRSGKIMRR 613
Cdd:cd12118 407 GVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKF 482
|
....
gi 501084078 614 ILRK 617
Cdd:cd12118 483 VLRD 486
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-619 |
6.41e-26 |
|
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: 111.65 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFAnTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd05909 8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 EGVRAGrgiplkknvdDALKNPNVNSVEHVVVLKRTGGKVDWHEG---------RDLWWsdVIEKSSADHQPEemnaeDP 258
Cdd:cd05909 87 QFIEKL----------KLHHLFDVEYDARIVYLEDLRAKISKADKckaflagkfPPKWL--LRIFGVAPVQPD-----DP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 259 LFILYTSGSTGKPKGVLHTTGGYL--VYAATTfkyVFDYHPDDIywctadvgwVTG-----HSYLLYG----PLACGATT 327
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV---------VFGalpffHSFGLTGclwlPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 328 LMFegvPNwPTPAR-MAQVVDKHQVTILYTAPTAIRALMaegdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIG--- 403
Cdd:cd05909 218 VFH---PN-PLDYKkIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGiri 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 404 ------NEKCPVVDtwwqtetggfMITPLPGAtelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwPGQARTL 477
Cdd:cd05909 290 legygtTECSPVIS----------VNTPQSPN---KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FGDHerfEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSH-PKIAEAAVVGIPHNIKG 556
Cdd:cd05909 356 LNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501084078 557 QAIYAYVTlnhGEDPSPElytEVRNWVRK-EIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 433 EKIVLLTT---TTDTDPS---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-615 |
1.45e-25 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 112.83 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDdatqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK10252 464 VAQQAAKTPDAPALADARY------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvRAGR--GIPlkknvDDALKNPNVnsvehvvvlkrtggkvdwhegrdlWWSD 239
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD--QLPRfaDVP-----DLTSLCYNA------------------------PLAP 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 240 viekssADHQPEEMNA-EDPLFILYTSGSTGKPKGVL--HTTggyLV---------YAATTFKYVFDYHPddiywCTADV 307
Cdd:PRK10252 587 ------QGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMvgQTA---IVnrllwmqnhYPLTADDVVLQKTP-----CSFDV 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 308 G-WVtghsylLYGPLACGATTLMFEgvpnwPT----PARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRI 382
Cdd:PRK10252 653 SvWE------FFWPFIAGAKLVMAE-----PEahrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQ 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 383 LGSVGEPINPE---AWE-WYWKKIGNEKCPV---VD-TWWqtetggfmitPLPGATELKAGSAT----RPFFGVQPALVD 450
Cdd:PRK10252 722 VFCSGEALPADlcrEWQqLTGAPLHNLYGPTeaaVDvSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILD 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 451 NEGHPQEGATEGNLVITdswpG-Q-ARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK10252 792 ARMRPVPPGVAGDLYLT----GiQlAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRG 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 525 HRLGTAEIESALVSHPKIAEAAVV------GIPHNIKGQAIYAYVTLNHGEDPSPELyteVRNWVRKEIGPLATPDVLHW 598
Cdd:PRK10252 868 QRIELGEIDRAMQALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQ 944
|
570
....*....|....*..
gi 501084078 599 TDSLPKTRSGKIMRRIL 615
Cdd:PRK10252 945 LDQLPLSANGKLDRKAL 961
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
1.74e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 110.75 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 79 ANCLDRHLQENGDRTAIIWegddATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 159 HSVIFGGFSPEAVAGRIIDSSSRLVITADEGV-----RAGRGIPLKKNVDDalknpnvnsvehvvVLKRTGGKVDWHEGr 233
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVVLIDADGPhdraePTTRWWPLTVNVGG--------------DSGPSGGTLSVHLD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 234 dlwwsDVIEKSSADHQPEEMNAEDPLfILYTSGSTGKPKGVLHTTGGYlvyAATTFKYVFDYHPDDIYWCTADVGWVTGH 313
Cdd:PRK05852 160 -----AATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 314 SYL--LYGPLACGATTLMfegvpnwPTPARMAQVV---DKHQV-TILYTA-PTAIRALMAEGDKAIEGTDRSSLRILGSV 386
Cdd:PRK05852 231 GLIaaLLATLASGGAVLL-------PARGRFSAHTfwdDIKAVgATWYTAvPTIHQILLERAATEPSGRKPAALRFIRSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 387 GEPINPEAWEWYWKKIGnekCPVVDTWWQTET---------GGFMITPLPGATELKAGSATrpffGVQPALVDNEGHPQE 457
Cdd:PRK05852 304 SAPLTAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 458 GATEGNLVItdSWPGQARTLFGDHE----RFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK05852 377 AGAVGEVWL--RGTTVVRGYLGDPTitaaNFTDGWLRT-------GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 534 SALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK05852 448 GVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
3.08e-25 |
|
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: 106.72 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYaattfkyvFDYHPDDIYWCTADVGWVTG---HSYLLYGPL--------ACGA 325
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGAIsalylggtFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 326 TTLmfegvpnwpTPARMAQVVDKHQVTILYTAPTAIRALmaegdkAIEGTDRSSLRILGSVGEPINPEAWewywKKIGNE 405
Cdd:cd17633 73 RKF---------NPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFESTK----KKLKNI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 406 --KCPVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQ-----------EGATEGNLVITDSWpg 472
Cdd:cd17633 134 fpKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIgkifvksemvfSGYVRGGFSNPDGW-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 473 qartlfgdherfeqtyFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd17633 210 ----------------MSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 553 NIKGQ---AIYAYVTLNhgedpspelYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 267 ARFGEiavALYSGDKLT---------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
4.58e-25 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 109.64 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHLQENGDRTAIIWEGDDATQSKHISYRELHRDVCRFANTLLELGiKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 164 GGFSPEA---VAGRIIDSSSRLVITaDEGVRAGrgiplkknvddalknpnvnsvehvvvLKRTGGKVDWHEGRDLWWSDV 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLT-TAAALAA--------------------------VRAFAASRPAAGTPRLLVVDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 241 IEKSSADH-QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDDIY--W--CTADVGWVTGhsy 315
Cdd:cd05931 133 LPDTSAADwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 316 lLYGPLACGATTLMFEgvpnwPT-----PARMAQVVDKHQVTILYtAPT-----AIRALMAEGdkaIEGTDRSSLRILGS 385
Cdd:cd05931 209 -LLTPLYSGGPSVLMS-----PAaflrrPLRWLRLISRYRATISA-APNfaydlCVRRVRDED---LEGLDLSSWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 386 VGEPINPEAWEWYWKK--------------------------IGNEKCPVVDTW--WQTETGGFMITPL-PGATELKagS 436
Cdd:cd05931 279 GAEPVRPATLRRFAEAfapfgfrpeafrpsyglaeatlfvsgGPPGTGPVVLRVdrDALAGRAVAVAADdPAARELV--S 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 437 ATRPFFGVQPALVDNEGH-PQEGATEGNLVITDS------W--PGQARTLFG--DHERfEQTYFSTfknmyfsGD-GARR 504
Cdd:cd05931 357 CGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPsvasgyWgrPEATAETFGalAATD-EGGWLRT-------GDlGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 505 deDGYYWITGRVDDVLNVSGHRLGTAEIE-SALVSHPKIAE--AAVVGIPHNIKGQ-AIYAYVTLNHGEDPSPELYTEVR 580
Cdd:cd05931 429 --DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIR 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 501084078 581 NWVRKEIGpLATPDV-LHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 507 AAVAREHG-VAPADVvLVRPGSIPRTSSGKIQRRACRA 543
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-618 |
4.94e-25 |
|
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: 109.54 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 90 GDRTAIIwegdDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17642 31 PGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITADEGvragrgipLKKNVDDALKNPnvnSVEHVVVLKrtgGKVDWHEGRDLW----WSDVIEKSS 245
Cdd:cd17642 107 ELDHSLNISKPTIVFCSKKG--------LQKVLNVQKKLK---IIKTIIILD---SKEDYKGYQCLYtfitQNLPPGFNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYL-LYGPLAC 323
Cdd:cd17642 173 YDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFtTLGYLIC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 324 GATTLM---FEgvpnwptPARMAQVVDKHQVTILYTAPTairaLMAEGDKA--IEGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:cd17642 253 GFRVVLmykFE-------EELFLRSLQDYKVQSALLVPT----LFAFFAKStlVDKYDLSNLHEIASGGAPLSKEVGEAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 399 WKKIgneKCPVV-DTWWQTE-TGGFMITPlpgATELKAGSATR--PFFGVQpaLVDNEGHPQEGATE-GNLVITDswPGQ 473
Cdd:cd17642 322 AKRF---KLPGIrQGYGLTEtTSAILITP---EGDDKPGAVGKvvPFFYAK--VVDLDTGKTLGPNErGELCVKG--PMI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 474 ARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPH 552
Cdd:cd17642 392 MKGYVNNPE---ATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501084078 553 NIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLA-TPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:cd17642 469 EDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
6.77e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 109.27 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 70 YEDGTLNLAANC--------LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 142 VPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGV--------RAGRGIPLKKNVDDAL--KNPNV 211
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAevarealaLLPGPKPLVIDVDDPEypGGRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 212 NSVEHVVVLKRTGGKVDWHEGRDLWwsdviekssadhqpeemnaeDPLFILYTSGSTGKPKGVL-HTTGGYLVYAATTFK 290
Cdd:PRK08162 158 GALDYEAFLASGDPDFAWTLPADEW--------------------DAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 291 YVFDYHPddIY-W------CTadvGWvtghsyllygplaCGATTLMFEGVPN----WPTPARMAQVVDKHQVTILYTAPT 359
Cdd:PRK08162 218 WGMPKHP--VYlWtlpmfhCN---GW-------------CFPWTVAARAGTNvclrKVDPKLIFDLIREHGVTHYCGAPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 360 AIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAwewywkkignekcpVVDtwwQTETGGFMITPLPGATEL------- 432
Cdd:PRK08162 280 VLSALINAPAEWRAGIDH---PVHAMVAGAAPPAA--------------VIA---KMEEIGFDLTHVYGLTETygpatvc 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 433 --KAGSATRPFfGVQPALVDNEG---HPQEGAT----------------------EGNLVITDSWPGQARTlfgdHERFE 485
Cdd:PRK08162 340 awQPEWDALPL-DERAQLKARQGvryPLQEGVTvldpdtmqpvpadgetigeimfRGNIVMKGYLKNPKAT----EEAFA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 486 QTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTL 565
Cdd:PRK08162 415 GGWFHT-------GDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVEL 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 501084078 566 NHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 488 KDGASATEE---EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
1.13e-24 |
|
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: 105.93 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 WPT----------PARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNe 405
Cdd:cd05924 82 GGQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 406 kCPVVDTWWQTETGGFMItplpgATELKAGSATRPFFGVQP--ALVDNEGHPQEGATEGnlvitdswPGQ-ART------ 476
Cdd:cd05924 161 -ITLVDAFGSSETGFTGS-----GHSAGSGPETGPFTRANPdtVVLDDDGRVVPPGSGG--------VGWiARRghiplg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 477 LFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIK 555
Cdd:cd05924 227 YYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501084078 556 GQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 307 GQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
1.15e-24 |
|
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: 105.81 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyhpddiyWCTADVGWVTGHSYLLYGpLACGATTLMFEGV-- 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 334 --PNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGE-PINPEAWEWYWKKIGNekcpVV 410
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADVRFIEATGLTN----TA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 411 DTWWQTETGGFMITPLpGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWpgqarTLFGDHERFEQTYFS 490
Cdd:cd17635 147 QVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 491 TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGED 570
Cdd:cd17635 221 LIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 501084078 571 PSpeLYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 301 EN--AIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-621 |
1.25e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 108.17 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 76 NLAANCLDRHLQENGDR-TAIIWEGDDATQSkhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQpEAIALRRCDGTSA--LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 155 IGAVHSVIFGGFSPEAVA--GRIIDSSSrlVITADEGvragrgiplkkNVDDALKNPNVNSVEHVVVLKRTGGKVDWHEG 232
Cdd:PRK05857 89 LGAIAVMADGNLPIAAIErfCQITDPAA--ALVAPGS-----------KMASSAVPEALHSIPVIAVDIAAVTRESEHSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 233 rdlwwsdviEKSSADHQPEeMNAEDPLFILYTSGSTGKPKGVLhttggylvYAATTFKYVFD-YHPDDIYWctadVGWVT 311
Cdd:PRK05857 156 ---------DAASLAGNAD-QGSEDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VTWVV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 312 GHSylLYGPLACG--------ATTLMFEG--VPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLR 381
Cdd:PRK05857 214 GET--TYSPLPAThigglwwiLTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 382 ILGSVGEpinpEAWEWYWKKIGNEKCPVVDTWWQTETGGFMITpLPGATE----LKAGSATRPFFGVQPALVD-NEGHPQ 456
Cdd:PRK05857 290 LVGYGGS----RAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPTDDGsivkIEAGAVGRPYPGVDVYLAAtDGIGPT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 457 -----EGATEGNLVITDswPGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK05857 365 apgagPSASFGTLWIKS--PANMLGYWNNPERTAEVLIDGWVN---TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 532 IESALVSHPKIAEAAVVGIPHN----IKGQAIYAYVTLNhgEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK05857 440 VDRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQS 517
|
570
....*....|....
gi 501084078 608 GKIMRRILRKIAAG 621
Cdd:PRK05857 518 GKVMRASLAAAATA 531
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-620 |
4.26e-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: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHLQENGDRTAI-IWEGDdatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhSVI 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA-FVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 163 FGGFSPEAVAGRII-DSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdvi 241
Cdd:cd05918 79 LDPSHPLQRLQEILqDTGAKVVLT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssadHQPEemnaeDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPD-----------DIywCTADVg 308
Cdd:cd05918 103 ------SSPS-----DAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSEsrvlqfasytfDV--SILEI- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 wvtghsyllYGPLACGATTLmfegVP-NWPTPARMAQVVDKHQVTILYTAPTAIRALMAEgdkaiegtDRSSLRILGSVG 387
Cdd:cd05918 166 ---------FTTLAAGGCLC----IPsEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 388 EPINPEawewywkkignekcpVVDTWWQ----------TETGGFMITPLPGATElKAGSATRPFfGVQPALVDNEGHPQ- 456
Cdd:cd05918 225 EALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVPST-DPRNIGRPL-GATCWVVDPDNHDRl 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 457 --EGATeGNLVItdSWPGQARtlfGDHERFEQTYFSTFKN--------------MYFSGDGARRDEDG--YYwiTGRVDD 518
Cdd:cd05918 288 vpIGAV-GELLI--EGPILAR---GYLNDPEKTAAAFIEDpawlkqegsgrgrrLYRTGDLVRYNPDGslEY--VGRKDT 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 519 VLNVSGHRLGTAEIESALVSHPKIAEAAVVGI--PHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLAT---- 592
Cdd:cd05918 360 QVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAelrs 439
|
570 580 590
....*....|....*....|....*....|....*....
gi 501084078 593 -----------PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05918 440 klrqrlpsymvPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-617 |
1.31e-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: 104.82 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 115 RDVC-RFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVR-A 192
Cdd:cd05915 31 YQRArRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPlV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 193 GRGIPLKKNVDDalkNPNVNSvehvvvlkrtggKVDWHEgrdlwwsDVIEKSSADHQP-EEMNAEDPLFILYTSGSTGKP 271
Cdd:cd05915 111 EAIRGELKTVQH---FVVMDE------------KAPEGY-------LAYEEALGEEADpVRVPERAACGMAYTTGTTGLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 272 KGVLHT-TGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLlYGPLACGATTLMFEGVPNwptPARMAQVVDKHQ 350
Cdd:cd05915 169 KGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLD---PASLVELFDGEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 351 VTILYTAPTAIRaLMAEGDKAIEGTDRSSLRILGSVGEPinPEAWeWYWKKIGNEK------CPVV-----DTWWQTEtg 419
Cdd:cd05915 245 VTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVEvrqgygLTETspvvvQNFVKSH-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 420 gFMITPLPGATELKAGSATRPFFGVQPAL-VDNEGHPQEGAT------EGNLVITDswpgqartLFGDHERFEQTYFStf 492
Cdd:cd05915 319 -LESLSEEEKLTLKAKTGLPIPLVRLRVAdEEGRPVPKDGKAlgevqlKGPWITGG--------YYGNEEATRSALTP-- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPS 572
Cdd:cd05915 388 DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 501084078 573 PELYtevrNWVRKEIGPLAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 468 EELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-625 |
1.71e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 104.92 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 48 WITPYKKVKNTSFAPgnvsIKWYEDGTLNLAANCLDRHlQENGDrTAIIwegdDATQSKHISYRELHRDVCRFANTLLE- 126
Cdd:PLN02574 17 WYSPETGIYSSKHPP----VPLPSDPNLDAVSFIFSHH-NHNGD-TALI----DSSTGFSISYSELQPLVKSMAAGLYHv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 127 LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITADEGVraGRGIPLKKNVDDAL 206
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPVIGVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 207 KNPNVNSVEHvvvlkrtggkvdwhEGRDLWWsdvIEKSSADHQPEE-MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA 285
Cdd:PLN02574 165 ENYDFDSKRI--------------EFPKFYE---LIKEDFDFVPKPvIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 286 ATTFKY---VFDYH-PDDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAI 361
Cdd:PLN02574 228 ELFVRFeasQYEYPgSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 362 RALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIgnekcPVVDTwwqteTGGFmitplpGATElKAGSATRPF 441
Cdd:PLN02574 304 MALTKKA-KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDF-----IQGY------GMTE-STAVGTRGF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 442 F---------------GVQPALVDNE-GHPQEGATEGNLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARR 504
Cdd:PLN02574 366 NteklskyssvgllapNMQAKVVDWStGCLLPPGNCGELWIQG--PGVMKGYLNNPK---ATQSTIDKDGWLrTGDIAYF 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVR 584
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVA 517
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 501084078 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PLN02574 518 KQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
1.81e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.96 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvragrgipLKKNVDDALKNPNVnsveHVVVLKRTGGKVDWHEGrdlwWSDVI 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEE---------LVEAFEEARADLAR----PPRLWVAGGDTLDDPEG----YEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 EKSSA--DHQPEE---MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAtTFKYVFDYHPDDIYWCT--------ADVG 308
Cdd:PRK08279 180 AAAAGapTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCClplyhntgGTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 WVTGhsyllygpLACGATTLM---FEGVPNWPTparmaqvVDKHQVTILYtaptAI----RALMAEGDKAiegTDRS-SL 380
Cdd:PRK08279 259 WSSV--------LAAGATLALrrkFSASRFWDD-------VRRYRATAFQ----YIgelcRYLLNQPPKP---TDRDhRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 381 RILgsVGEPINPEAWEwywkkignekcpvvdtWWQTETGGFMITPLPGATEL---------KAGSATR-PFFGVQP-ALV 449
Cdd:PRK08279 317 RLM--IGNGLRPDIWD----------------EFQQRFGIPRILEFYAASEGnvgfinvfnFDGTVGRvPLWLAHPyAIV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 450 -----------DNEGHPQEGATE--GNLV--ITDSWP--GQA----------RTLF--GDherfeqTYFSTfknmyfsGD 500
Cdd:PRK08279 379 kydvdtgepvrDADGRCIKVKPGevGLLIgrITDRGPfdGYTdpeasekkilRDVFkkGD------AWFNT-------GD 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 501 GARRDEDGYYWITGRVDDVL-----NVSghrlgTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYAYVTLNHGEDPSP- 573
Cdd:PRK08279 446 LMRDDGFGHAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDLa 520
|
....*..
gi 501084078 574 ELYTEVR 580
Cdd:PRK08279 521 ALAAHLY 527
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
82-620 |
1.97e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 104.69 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQenGDRTAIIwEGDdatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsV 161
Cdd:PRK10946 31 LTRHAA--SDAIAVI-CGE-----RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPE-----AVAGRIidsSSRLVItadegvrAGRGIPLKKNVD--DALKNpNVNSVEHVVVLKRTGGkvdwhegRD 234
Cdd:PRK10946 101 VNALFSHQrselnAYASQI---EPALLI-------ADRQHALFSDDDflNTLVA-EHSSLRVVLLLNDDGE-------HS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 235 LwwSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPDDIYWCTADvgwvTGHS 314
Cdd:PRK10946 163 L--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSVRRSVEICGFTPQTRYLCALP----AAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 315 YLLYGPLA-----CGATTLMfegVPNwPTPARMAQVVDKHQVTILYTAPTA----IRALMAEGDKAiegtDRSSLRILgS 385
Cdd:PRK10946 236 YPMSSPGAlgvflAGGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAvslwLQAIAEGGSRA----QLASLKLL-Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 386 VGEPINPEAWEwywKKIGNE-KCPVVDTWWQTEtGGFMITPLPGATELKAGSATRPffgVQPA----LVDNEGHPQEGAT 460
Cdd:PRK10946 307 VGGARLSETLA---RRIPAElGCQLQQVFGMAE-GLVNYTRLDDSDERIFTTQGRP---MSPDdevwVADADGNPLPQGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 461 EGNLVITDSW--------PGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK10946 380 VGRLMTRGPYtfrgyyksPQHNASAF-DANGF-----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 533 ESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgedpSPELYTEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK10946 448 ENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK-----EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....*....
gi 501084078 612 RRILRKIAA 620
Cdd:PRK10946 523 KKQLRQWLA 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
249-615 |
2.55e-23 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 103.67 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 249 QPEEMnaedpLFILYTSGSTGKPKGVL--------HTTGGYLVYAATTFKYV-------FDYHPDDIYwctadVGWVTGH 313
Cdd:cd17644 104 QPENL-----AYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 314 SYLLygplacgATTLMFegvpnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKA-IEGTDRSSLRILGsvGEPINP 392
Cdd:cd17644 174 TLVL-------RPEEMR------SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStIDLPSSLRLVIVG--GEAVQP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEwYWKKIGNEKCPVVDTWWQTE-TGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNLVITDS 469
Cdd:cd17644 239 ELVR-QWQKNVGNFIQLINVYGPTEaTIAATVCRLTQLTERNITSVPigRPIANTQVYILDENLQPVPVGVPGELHIGGV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 470 wpGQARTLFG----DHERFEQTYF--STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:cd17644 318 --GLARGYLNrpelTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVK 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 544 EAAVVGIPHNIKGQAIYAYVTLNHGEDPSPelyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17644 396 TAVVIVREDQPGNKRLVAYIVPHYEESPST---VELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
2.13e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.32 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITadEGVRAGRgiplkknvddalknpnVNSVEHVVVLKRTGGKVDwhegrdlwwsdvi 241
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLT--QSHLLER----------------LPQAEGVSAIALDSLHLD------------- 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekSSADHQPE-EMNAEDPLFILYTSGSTGKPKGVLHTTGGY---LVYAATTfkYVFDyhPDDIYWCTADVGWVTGhSYLL 317
Cdd:PRK05691 1260 --SWPSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQAT--YALD--DSDVLMQKAPISFDVS-VWEC 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 318 YGPLACGATtLMFEGVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEW 397
Cdd:PRK05691 1333 FWPLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAELRNR 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 398 YWKKI---------GNEKCPVVDTWWQTETGGFMITPLpgatelkagsaTRPFFGVQPALVDNEGHPQEGATEGNLVITD 468
Cdd:PRK05691 1408 VLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 SwpGQARTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK05691 1477 A--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVA 1554
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 544 EAAVVgIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 1555 QAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
2.26e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 101.26 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 237 WSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-ATTFKYvfDYHPDDIYWCTADVGwvtgHS- 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 315 --YLLYGP-LACGATTLMfegvPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRssLRIlgSVGEPIN 391
Cdd:PRK13388 205 avMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 392 PEAWEWYWKKIGnekCPVVDTWWQTETGGfMITPLPGATElkaGSATRPFFGVQ-----------PALVDNEGHPQEGAT 460
Cdd:PRK13388 277 PRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPGTPP---GSIGRGAPGVAiynpetltecaVARFDAHGALLNADE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 461 E-GNLVITdswpgQARTLF--------GDHERFEQtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK13388 350 AiGELVNT-----AGAGFFegyynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAP 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK13388 418 IERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRIAADLPSTATNKVL 496
|
....*
gi 501084078 612 RRILR 616
Cdd:PRK13388 497 KRELI 501
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
91-616 |
5.20e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDDATqskHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK07514 15 DRDAPFIETPDGL---RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEGVRAGRGIPLKKNVddalknpnvnsvEHVVVL--KRTGGkvdwhegrdlwWSDVIEKSSADH 248
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAGA------------PHVETLdaDGTGS-----------LLEAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 249 QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPDD-------IYwctadvgwvtgHSYLLY--- 318
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDY-WRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 319 -GPLACGATtlMFegvpnWPTPARMAQVVDK-HQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVgePINPE--- 393
Cdd:PRK07514 217 nVALLAGAS--MI-----FLPKFDPDAVLALmPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSA--PLLAEthr 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 394 AWEwywKKIGNekcPVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNE-GHPQEGATEGNL------VI 466
Cdd:PRK07514 288 EFQ---ERTGH---AILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPEtGAELPPGEIGMIevkgpnVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 467 TDSW--PGQARTLFGdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:PRK07514 360 KGYWrmPEKTAEEFR-----ADGFFIT-------GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501084078 545 AAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAALDEA---AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
108-616 |
8.25e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 100.11 E-value: 8.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragrgiPLKknvdDALKNPNVNsvehvvvlkrtggkvdwhEGRDLWwSDVIEKSSADHQPeeMNAEDPLFILYTSGS 267
Cdd:PRK06060 111 ---------ALR----DRFQPSRVA------------------EAAELM-SEAARVAPGGYEP--MGGDALAYATYTSGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegVPNWPTPARMAQVVD 347
Cdd:PRK06060 157 TGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV----INSAPVTPEAAAILS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 348 -KHQVTILYTAPTairaLMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTETGGFMITPl 426
Cdd:PRK06060 233 aRFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 427 pGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNL-----VITDSWPGQARTLFGDHERFEqtyfstfknmyfSGDG 501
Cdd:PRK06060 306 -RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLwvrgpAIAKGYWNRPDSPVANEGWLD------------TRDR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRN 581
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHR 452
|
490 500 510
....*....|....*....|....*....|....*
gi 501084078 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 453 GLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
2.11e-21 |
|
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: 97.63 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWEGDDATqskhisYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRGQSLT------YKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 251 eemNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPDDIYWCTADVGWvTGHSYLLYGPLACGATTL 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 329 MFEGVPNWPTpARMAQVVDKHQVTILYTAPTAIRALMAegdkaiegTDRSSLRILGSVGEPInpeawewywKKIGNEKCP 408
Cdd:cd17645 175 VVPSERRLDL-DALNDYFNQEGITISFLPTGAAEQFMQ--------LDNQSLRVLLTGGDKL---------KKIERKGYK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 409 VVDTWWQTETGgFMITPLPGATELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERF 484
Cdd:cd17645 237 LVNNYGPTENT-VVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNrpelTAEKF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 485 EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVT 564
Cdd:cd17645 314 IVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 501084078 565 LNHGEDPSpelytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 394 APEEIPHE-----ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-636 |
2.43e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 98.32 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 90 GDRTAIIWEGDDATQskhISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 169 EAVAgRIIDSSSRLVITADEgVRAGRGIPLKKNVDdalknpnvnSVEHVVVLKR----TGGKVDWHEGRDLWWSDVIEKS 244
Cdd:PRK05620 101 DQIV-HIINHAEDEVIVADP-RLAEQLGEILKECP---------CVRAVVFIGPsdadSAAAHMPEGIKVYSYEALLDGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 245 SADHQPEEMNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLVYAATTFKY-VFDYHPddIYWCTADVGWV 310
Cdd:PRK05620 170 STVYDWPELDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESFLCcVPIYHV--LSWGVPLAAFM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 311 TGhsyllygplacgaTTLMFEGVPnwPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPI 390
Cdd:PRK05620 248 SG-------------TPLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGSAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 391 NP---EAWEwywKKIGNEkcpVVDTWWQTETG--GFMITPLPGAtelkAGSATRPFFGVQ---PA----LVDNEGHPQEG 458
Cdd:PRK05620 311 PPiliKAWE---ERYGVD---VVHVWGMTETSpvGTVARPPSGV----SGEARWAYRVSQgrfPAsleyRIVNDGQVMES 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 459 A--------TEGNLVI-------TDSWPGQARTLFGDHERFEQTYFsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK05620 381 TdrnegeiqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRF-TADGWLRTGDVGSVTRDGFLTIHDRARDVIRSG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 524 GHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK05620 460 GEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEID 539
|
570 580 590
....*....|....*....|....*....|....
gi 501084078 604 KTRSGKIMRRILRK-IAAGDTsnlgDTSTLADPG 636
Cdd:PRK05620 540 KTSVGKFDKKDLRQhLADGDF----EIIKLKGPG 569
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-621 |
2.51e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.86 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 233 RDLWWSDVIEKSSADHQPEEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPDDIYWCTADVGWVT 311
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTASQSFDI 3923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 312 GHSYLLYGPLAcGATTlmfEGVPNW----PTpARMAQVVDKhQVTILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVG 387
Cdd:PRK05691 3924 SVWQFLAAPLF-GARV---EIVPNAiahdPQ-GLLAHVQAQ-GITVLESVPSLIQGMLAEDRQALDG-----LRWMLPTG 3992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 388 EPINPE-AWEWY--WKKIGnekcpVVDTWWQTETG---GFMITPLPG--ATELKAGSATRP----FFGVQPALVdneghP 455
Cdd:PRK05691 3993 EAMPPElARQWLqrYPQIG-----LVNAYGPAECSddvAFFRVDLAStrGSYLPIGSPTDNnrlyLLDEALELV-----P 4062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 456 QeGATeGNLVITDSwpGQARTLFGDHERFEQTYF-----STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK05691 4063 L-GAV-GELCVAGT--GVGRGYVGDPLRTALAFVphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELG 4138
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 531 EIESALVSHPKIAEAAvVGIPHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK05691 4139 EIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
410
....*....|.
gi 501084078 611 MRRILRKIAAG 621
Cdd:PRK05691 4218 DRKALPALDIG 4228
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
9.68e-21 |
|
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: 85.60 E-value: 9.68e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 501084078 24 YEAKYQQSINEPDTFWGEQGKILDWITPYKKVKNTSFAPGnvsIKWYEDGTLNLAANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
2.01e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.47 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGddatqsKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07059 29 LEESFRQYADRPAFICMG------KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVITADEgvragrgipLKKNVDDALKNpnvNSVEHVVV------LKRTGGKVD------- 228
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVLEN---------FATTVQQVLAK---TAVKHVVVasmgdlLGFKGHIVNfvvrrvk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 229 -----WHEGRDLWWSDVI-EKSSADHQPEEMNAEDPLFILYTSGSTGKPKG--VLHT--------TGGYLVYAATTFKyv 292
Cdd:PRK07059 171 kmvpaWSLPGHVRFNDALaEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGatLLHRnivanvlqMEAWLQPAFEKKP-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 293 fdyHPDDIYWCTA----DVGWVTGHSYLlygPLACGATTLMfegVPNWPTPARMAQVVDKHQVTILYTAPTAIRALMAEG 368
Cdd:PRK07059 249 ---RPDQLNFVCAlplyHIFALTVCGLL---GMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 369 DkaIEGTDRSSLRI-LG---SVGEPInpeAWEWYwKKIGnekCPVVDTWWQTETGGFMITPLPGATELkAGSATRPFFGV 444
Cdd:PRK07059 320 D--FDKLDFSKLIVaNGggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSPVATCNPVDATEF-SGTIGLPLPST 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 445 QPALVDNEGH------PQEGATEGNLVITDSWpgqartlfgdhERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVD 517
Cdd:PRK07059 390 EVSIRDDDGNdlplgePGEICIRGPQVMAGYW-----------NRPDETAKVMTADGFFrTGDVGVMDERGYTKIVDRKK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 518 DVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTlnhGEDPSpelYTE--VRNWVRKEIGPLATPDV 595
Cdd:PRK07059 459 DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV---KKDPA---LTEedVKAFCKERLTNYKRPKF 532
|
570 580
....*....|....*....|.
gi 501084078 596 LHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07059 533 VEFRTELPKTNVGKILRRELR 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-620 |
2.28e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.33 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVI 184
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 185 TAD------EGVRAGrgIPLKKNVDD-----------ALKNPNVNSVEHVVVLKRTGGKVDWHEGRDLwwsdvieKSSAD 247
Cdd:PRK08751 129 VIDnfgttvQQVIAD--TPVKQVITTglgdmlgfpkaALVNFVVKYVKKLVPEYRINGAIRFREALAL-------GRKHS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 248 HQPEEMNAEDPLFILYTSGSTGKPKGVLHTtggylvyaattfkyvfdyHPDDIYWCTADVGWVTGHSYL----------- 316
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLT------------------HRNLVANMQQAHQWLAGTGKLeegcevvital 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 317 -LYGPLACGATTLMFEGVPNW----PTPARMAQVVDKHQVTiLYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEP 389
Cdd:PRK08751 262 pLYHIFALTANGLVFMKIGGCnhliSNPRDMPGFVKELKKT-RFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 390 INPEAWEwYWKKIGNekCPVVDTWWQTETG-GFMITPLpgatELKA--GSATRPFFGVQPALVDNEGHPQEGATEGNLVI 466
Cdd:PRK08751 341 VQRSVAE-RWKQVTG--LTLVEAYGLTETSpAACINPL----TLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 467 TDSwpgqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:PRK08751 414 KGP-----QVMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEV 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 546 AVVGIPHNIKGQAIYAYVTlnhgeDPSPELYTE-VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08751 489 AAVGVPDEKSGEIVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
3.64e-19 |
|
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: 89.10 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 261 ILYTSGSTGKPKGVL--HTTGgYLVYAAttfkyvfdyhpddiyWCtaDVGWVT-GHSYLLYGP-----------LAC--- 323
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPffhtfgykagiVACllt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 324 GATTL---MFEgvpnwptPARMAQVVDKHQVTILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:cd17638 67 GATVVpvaVFD-------VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 KIGNEKcpVVDTWWQTETG-GFMITPLPGATELkAGSATRPFFGVQPALVDneghpqegatEGNLVITDswPGQARTLFG 479
Cdd:cd17638 138 ELGFET--VLTAYGLTEAGvATMCRPGDDAETV-ATTCGRACPGFEVRIAD----------DGEVLVRG--YNVMQGYLD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 480 DHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17638 203 DPEATAEAIDA--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 501084078 560 YAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 281 KAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-617 |
4.40e-19 |
|
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: 90.06 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 83 DRHLQENGDRTAIiwegDDATQSkhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:cd17653 4 ERIAAAHPDAVAV----ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 163 FGGfSPEAVAGRIIDSS-SRLVITADegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdvi 241
Cdd:cd17653 78 DAK-LPSARIQAILRTSgATLLLTTD------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 242 ekssadhqpeemNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATT---------------FKYVFDYhpddiywCTAD 306
Cdd:cd17653 103 ------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDA-------CIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 307 VgwvtghsyllYGPLACGATTLMFEGVPNWPTPARmaqvvdkhQVTILYTAPTAIRALmaegdkaiEGTDRSSLRILGSV 386
Cdd:cd17653 164 I----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL--------SPQDFPNLKTIFLG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 387 GEPINPeawewywkkignekcPVVDTWWQ----------TETggfmiTPLPGATELKAGSAT---RPFFGVQPALVDNEG 453
Cdd:cd17653 218 GEAVPP---------------SLLDRWSPgrrlynaygpTEC-----TISSTMTELLPGQPVtigKPIPNSTCYILDADL 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 454 HPQEGATEGNLVItdSWPGQARTLFGDHE----RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:cd17653 278 QPVPEGVVGEICI--SGVQVARGYLGNPAltasKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINL 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 530 AEIESALVSHPKIAEAAVVgIPHNikgQAIYAYVTlnhgedPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd17653 356 EEIEEVVLQSQPEVTQAAA-IVVN---GRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 501084078 610 IMRRILRK 617
Cdd:cd17653 426 VDRKALRE 433
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-549 |
6.76e-19 |
|
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: 90.56 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 EgvragrgiplkKNVDDALK-NPNVNSVEHVVVLKRTGGKvDWHEGRDLWWSDVIEKSSADHQPE---------EMNAED 257
Cdd:cd17641 92 E-----------EQVDKLLEiADRIPSVRYVIYCDPRGMR-KYDDPRLISFEDVVALGRALDRRDpglyerevaAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvFDY-HPDDIYWCTADVGWVTGHSYLLYGPLACG--------ATTL 328
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPlGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 329 M-----------------FEGVPNwPTPARMA------QVVDKHQVTILYTA----------PTAIRALMAEGDKAIEGT 375
Cdd:cd17641 238 MedlreigptfvllpprvWEGIAA-DVRARMMdatpfkRFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 376 DR-----SSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQpALVD 450
Cdd:cd17641 317 LRdrlgfSRLRSAATGGAALGPDTFRFF-HAIG---VPLKQLYGQTELAGAYTVHRDG--DVDPDTVGVPFPGTE-VRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 451 NEGHpqegategnlvITDSWPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLG 528
Cdd:cd17641 390 EVGE-----------ILVRSPG---VFVGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFS 455
|
490 500
....*....|....*....|.
gi 501084078 529 TAEIESALVSHPKIAEAAVVG 549
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLG 476
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
103-617 |
8.47e-19 |
|
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: 89.80 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 103 TQSKHISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSR 181
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 182 LVItadegvragrgiplkknVDDalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnaEDPLFI 261
Cdd:cd05937 81 FVI-----------------VDP---------------------------------------------------DDPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIYWCTAdVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPt 338
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMP-LYHGTAAFLGACNCLMSGGTLALsrkFSASQFWK- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 339 parmaQVVDKHQVTILYTAPTaIRALMAegdKAIEGTDRSSlRILGSVGEPINPEAWEWYWKKIGnekCPVVD------- 411
Cdd:cd05937 171 -----DVRDSGATIIQYVGEL-CRYLLS---TPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFN---VPEIGefyaate 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 ---TWWQTETGGFMItplpGATELKaGSATRPFFGVQPALV--DNEG-----HPQEGATEGNLVITdswPGQA--RTLFG 479
Cdd:cd05937 238 gvfALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVkmDPETddpirDPKTGFCVRAPVGE---PGEMlgRVPFK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 480 DHERFeQTYFSTFK--------------NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd05937 310 NREAF-QGYLHNEDatesklvrdvfrkgDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAE 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 545 AAVVGI--PHNiKGQAIYAYVTL-NHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05937 389 ANVYGVkvPGH-DGRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
108-619 |
3.94e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 88.34 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLE-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSR-LV-- 183
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARaLVyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ---------ITADEG------VRAGRGIPLKKNvddALKNPNVNSVEHVV----VLKRTGGKVDWHEGRDLwwsdvieks 244
Cdd:PRK12492 130 nmfgklvqeVLPDTGieylieAKMGDLLPAAKG---WLVNTVVDKVKKMVpayhLPQAVPFKQALRQGRGL--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 245 saDHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDD--------------------IYWCT 304
Cdd:PRK12492 198 --SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN-LVANMLQVRACLSQLGPDgqplmkegqevmiaplplyhIYAFT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 305 ADVG--WVTG-HSYLLYGPLACGAttlmfegvpnwptparMAQVVDKHQVTILYTAPTAIRALMAEGDkaIEGTDRSSLR 381
Cdd:PRK12492 275 ANCMcmMVSGnHNVLITNPRDIPG----------------FIKELGKWRFSALLGLNTLFVALMDHPG--FKDLDFSALK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 382 ILGSVGEPINPEAWEwYWKKIGNekCPVVDTWWQTETGGFMITPlPGATELKAGSATRPFFGVQPALVDNEGHPQEGATE 461
Cdd:PRK12492 337 LTNSGGTALVKATAE-RWEQLTG--CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDGNELPLGER 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 462 GNLVITDSwpgqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHP 540
Cdd:PRK12492 413 GELCIKGP-----QVMKGYWQQPEATAEALDAEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 541 KIAEAAVVGIPHNIKGQAIYAYVTlnhGEDPSPELyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVV---ARDPGLSV-EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-580 |
4.56e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.03 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 84 RHL----QENGDRTAII----WEGDDATQSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 156 GAVHSVIFGGFSPEAVAGRIIDSSSRLVItadegvragrGIPlKKNVDDALKNPNVNSVEHVVVlkrTGGKVDWhEGRDL 235
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFI----------GIP-KAHLARRLFGWGKPSVRRLVT---VGGRLLW-GGTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 236 wwsDVIEKSSADHQPE--EMNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAttfKYVFDYHPDDIYWCTADVgwvt 311
Cdd:PRK09274 155 ---ATLLRDGAAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEIDLPTFPL---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 312 ghsYLLYGPlACGATTLmfegVPNW-PT------PARMAQVVDKHQVTILYTAPTAIRALMAEGdkaiEGTDRS--SLRI 382
Cdd:PRK09274 225 ---FALFGP-ALGMTSV----IPDMdPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYG----EANGIKlpSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 383 LGSVGEPINPEAWEWYwKKIGNEKCPVVDTWWQTETggfmitpLP----GATEL--KAGSATRPFFGVqpaLVdneGHPQ 456
Cdd:PRK09274 293 VISAGAPVPIAVIERF-RAMLPPDAEILTPYGATEA-------LPissiESREIlfATRAATDNGAGI---CV---GRPV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 457 EGATEGNLVITD----SWpGQARTLF----------GDHerFEQTYF----STFKN------------MyfsGDGARRDE 506
Cdd:PRK09274 359 DGVEVRIIAISDapipEW-DDALRLAtgeigeivvaGPM--VTRSYYnrpeATRLAkipdgqgdvwhrM---GDLGYLDA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501084078 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPhnIKGQAIYAY-VTLNHGEDPSPE-LYTEVR 580
Cdd:PRK09274 433 QGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLcVELEPGVACSKSaLYQELR 506
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
91-615 |
4.66e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 87.74 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIweGDDATqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK13383 50 GRTAII--DDDGA----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 171 VAGRIIDSSSRLVITADEGVRAGRGiplkknVDDALKnpnvnsvehvvvlkrtggkvdwhegrdlwwsdVIEKSSA---D 247
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAERIAG------ADDAVA--------------------------------VIDPATAgaeE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 248 HQPEEMNAEDPLFILYTSGSTGKPKGVLHT--------------------TGGYLVYAATTFKyvfdyhpddiywctadv 307
Cdd:PRK13383 166 SGGRPAVAAPGRIVLLTSGTTGKPKGVPRApqlrsavgvwvtildrtrlrTGSRISVAMPMFH----------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 308 GWVTGhsyLLYGPLACGATTLMFEgvpNWPTPARMAQVvDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK13383 229 GLGLG---MLMLTIALGGTVLTHR---HFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 388 EPINPEAWEWYWKKIGNekcPVVDTWWQTETG-GFMITPlpgaTELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNL 464
Cdd:PRK13383 302 DRLDPTLGQRFMDTYGD---ILYNGYGSTEVGiGALATP----ADLRDAPETvgKPVAGCPVRILDRNNRPVGPRVTGRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 465 VITDSWPGQARTLFGDHerfeqtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:PRK13383 375 FVGGELAGTRYTDGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVAD 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 545 AAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 447 NAVIGVPDERFGHRLAAFVVLHPGSGVDAA---QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-615 |
1.44e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.53 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDD----IYWCTADVGwvtghSYLLYGPLACGATtLMFEGVPN 335
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLLVPLLCGAR-VVLRAQGQ 2409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 WPTpARMAQVVDKHQVTILYTAPT----AIRALMAEGDkaiegtdRSSLRILGSVGEPINPEawewYWKKIGNEKCPVV- 410
Cdd:PRK05691 2410 WGA-EEICQLIREQQVSILGFTPSygsqLAQWLAGQGE-------QLPVRMCITGGEALTGE----HLQRIRQAFAPQLf 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 411 -DTWWQTETggfMITPL--PGATELKAGSATRPFFGVQPALV------DNEGHPQeGATeGNLVITDSwpGQARtlfGDH 481
Cdd:PRK05691 2478 fNAYGPTET---VVMPLacLAPEQLEEGAASVPIGRVVGARVayildaDLALVPQ-GAT-GELYVGGA--GLAQ---GYH 2547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 482 -------ERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIpHN 553
Cdd:PRK05691 2548 drpgltaERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DT 2626
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501084078 554 IKGQAIYAYV---TLNHGEDPSPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 2627 PSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
88-618 |
2.51e-17 |
|
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: 85.41 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 88 ENGDRTAIIWEGDDATQSKhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACarigavhsvIFGGFS 167
Cdd:cd05906 21 ERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 168 PeavagriidsssrlvitadegvragrgIPLKKNVDDALKNPNVNSVEHV-------VVLKRTGG--------KVDWHEG 232
Cdd:cd05906 91 P---------------------------APLTVPPTYDEPNARLRKLRHIwqllgspVVLTDAELvaefagleTLSGLPG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 233 RDLWWSDVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPDDIY--WCTAD--VG 308
Cdd:cd05906 144 IRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLDhvGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 309 WVTGHSYLLYgpLACG----ATTLMFEGVPNWptparmAQVVDKHQVTILYtAPTAIRALMAEGDKAIEGT--DRSSLRI 382
Cdd:cd05906 223 LVELHLRAVY--LGCQqvhvPTEEILADPLRW------LDLIDRYRVTITW-APNFAFALLNDLLEEIEDGtwDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 383 LGSVGEPINPEAWEWYWKKIgnEKCPVVDT-----WWQTETGGFMI----TPLPGAT-ELKAGSATRPFFGVQPALVDNE 452
Cdd:cd05906 294 LVNAGEAVVAKTIRRLLRLL--EPYGLPPDairpaFGMTETCSGVIysrsFPTYDHSqALEFVSLGRPIPGVSMRIVDDE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 453 GHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFSTFKN--MYFSGDGARRDeDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:cd05906 372 GQLLPEGEVGRLQV------RGPVVTKGYYNNPEANAEAFTEdgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 531 EIESALVSHPKIAEAAVVGIPHNIKGQ-----AIYAYVTLNHgEDPSPELYTEVRNWVRKEIG-------PLAtpdvlhw 598
Cdd:cd05906 445 EIEAAVEEVPGVEPSFTAAFAVRDPGAeteelAIFFVPEYDL-QDALSETLRAIRSVVSREVGvspayliPLP------- 516
|
570 580
....*....|....*....|
gi 501084078 599 TDSLPKTRSGKIMRRILRKI 618
Cdd:cd05906 517 KEEIPKTSLGKIQRSKLKAA 536
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
82-616 |
3.69e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.11 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDATqskhisYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHS 160
Cdd:PRK08974 29 FEQAVARYADQPAFINMGEVMT------FRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 161 VIFGGFSPEAVAGRIIDSSSRLVITADEGVRAGRGIPLKKNVD--------DALKNPNVNSVEHVV-VLKRTGGKVDW-- 229
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKhviltrmgDQLSTAKGTLVNFVVkYIKRLVPKYHLpd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 230 --------HEGRDLWWSdviekssadhQPEeMNAEDPLFILYTSGSTGKPKGVLHTTGGYLV---YAATTFKYVFD---- 294
Cdd:PRK08974 183 aisfrsalHKGRRMQYV----------KPE-LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleQAKAAYGPLLHpgke 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 295 --------YHpddIYWCTADVgwvtghsyLLYgpLACGATTLMFEGVPNWPTparMAQVVDKHQVTILYTAPTAIRALMa 366
Cdd:PRK08974 252 lvvtalplYH---IFALTVNC--------LLF--IELGGQNLLITNPRDIPG---FVKELKKYPFTAITGVNTLFNALL- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 367 eGDKAIEGTDRSSLRILGSVGEPINPEAWEwYWKKIgnEKCPVVDTWWQTETGGfMITPLPGATELKAGSATRPFFGVQP 446
Cdd:PRK08974 315 -NNEEFQELDFSSLKLSVGGGMAVQQAVAE-RWVKL--TGQYLLEGYGLTECSP-LVSVNPYDLDYYSGSIGLPVPSTEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 447 ALVDNEGHPQEGATEGNLvitdsWPGQARTLFGDHERFEQTYfSTFKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK08974 390 KLVDDDGNEVPPGEPGEL-----WVKGPQVMLGYWQRPEATD-EVIKDGWLAtGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 526 RLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgeDPSpelYT--EVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK08974 464 NVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK---DPS---LTeeELITHCRRHLTGYKVPKLVEFRDELP 537
|
570
....*....|...
gi 501084078 604 KTRSGKIMRRILR 616
Cdd:PRK08974 538 KSNVGKILRRELR 550
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
104-612 |
8.20e-16 |
|
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: 80.56 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 104 QSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLV 183
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ITADEgvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnaEDPLFILY 263
Cdd:cd05914 84 FVSDE-------------------------------------------------------------------DDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 264 TSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTL--------------M 329
Cdd:cd05914 97 TSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkipsakiialaF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 330 FEGVPNWPTPaRMAQVVDKHQVTI------------LYTAPTAIRALMAEGDKAIEGTDrSSLRILGSVGEPINPEAwEW 397
Cdd:cd05914 176 AQVTPTLGVP-VPLVIEKIFKMDIipkltlkkfkfkLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGAKINPDV-EE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 398 YWKKIGnekCPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVDneghPQEGATEGNLVITDSwpgqaRTL 477
Cdd:cd05914 253 FLRTIG---FPYTIGYGMTETAPIISYSPPN--RIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGP-----NVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 478 FGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDV-LNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIK 555
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFhTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 556 GQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGpLATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 399 ALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
376-616 |
1.21e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 80.19 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 376 DRSSLRILGSVGEPINPEAWEwYWKKIGNekCPVVDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGH- 454
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAE-RWKEVTG--CAICEGYGMTETSPVVSVNPSQAIQV--GTIGIPVPSTLCKVIDDDGNe 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 455 -----PQEGATEGNLVITDSWPGQARTlfgDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK05677 399 lplgeVGELCVKGPQVMKGYWQRPEAT---DEILDSDGWLKT-------GDIALIQEDGYMRIVDRKKDMILVSGFNVYP 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 530 AEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK05677 469 NELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
....*..
gi 501084078 610 IMRRILR 616
Cdd:PRK05677 546 ILRRELR 552
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
507-617 |
1.28e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 78.93 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGedPSPELyTEVRNWVRKE 586
Cdd:PRK07824 246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGG--PAPTL-EALRAHVART 322
|
90 100 110
....*....|....*....|....*....|.
gi 501084078 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 323 LDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
237-549 |
5.13e-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: 78.28 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 237 WSDVIekssADHQPEE----MNAEDPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPDDIYWCTADVGWVTG 312
Cdd:cd05932 118 WDDLI----AQHPPLEerptRFPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 313 HSYLLYGPLACGATTLMFEGVPNWPTPARMAQ-----------------VVDK---HQVTILYTAPTaIRALMaeGDKAI 372
Cdd:cd05932 193 RVFVEGGSLYGGVLVAFAESLDTFVEDVQRARptlffsvprlwtkfqqgVQDKipqQKLNLLLKIPV-VNSLV--KRKVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 373 EGTDRSSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQTETGGFMITPLPGATelKAGSATRPFFGVQPALVDne 452
Cdd:cd05932 270 KGLGLDQCRLAGCGSAPVPPALLEWY-RSLG---LNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRISE-- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 453 ghpqegatEGNLVITDswPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTA 530
Cdd:cd05932 342 --------DGEILVRS--PA---LMMGYYKDPEATAEAFTADGFLrTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPA 408
|
330
....*....|....*....
gi 501084078 531 EIESALVSHPKIAEAAVVG 549
Cdd:cd05932 409 PIENKLAEHDRVEMVCVIG 427
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-619 |
6.69e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.96 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEgddatqSKHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PLN02479 26 LERAAVVHPTRKSVVHG------SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 162 IFGGFSPEAVAGRIIDSSSRLVIT-------ADEGVR--AGRGI-----PL----------KKNVDDALKNpnvNSVEHV 217
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVdqefftlAEEALKilAEKKKssfkpPLlivigdptcdPKSLQYALGK---GAIEYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 218 VVLKRTGGKVDWHEGRDLWWSdviekssadhqpeemnaedpLFILYTSGSTGKPKGV-LHTTGGYLvyAATTFKYVFDYH 296
Cdd:PLN02479 177 KFLETGDPEFAWKPPADEWQS--------------------IALGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 297 PDDIYWCTADVGWVTGHSYLLYGPLACGaTTLMFEGVpnwpTPARMAQVVDKHQVTILYTAPTAIRALmaegdkaiegtd 376
Cdd:PLN02479 235 EGAVYLWTLPMFHCNGWCFTWTLAALCG-TNICLRQV----TAKAIYSAIANYGVTHFCAAPVVLNTI------------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 377 rsslrILGSVGEPINPEAWEWYWKKIGNEKCPVVdtWWQTETGGFMITPLPGATELKAGS---ATRPFFGVQPALVDNEG 453
Cdd:PLN02479 298 -----VNAPKSETILPLPRVVHVMTAGAAPPPSV--LFAMSEKGFRVTHTYGLSETYGPStvcAWKPEWDSLPPEEQARL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 454 H------------------------PQEGATEGNLVITDS--WPGQARTLFGDHERFEQTYFStfknmyfSGDGARRDED 507
Cdd:PLN02479 371 NarqgvryiglegldvvdtktmkpvPADGKTMGEIVMRGNmvMKGYLKNPKANEEAFANGWFH-------SGDLGVKHPD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSPE--LYTEVRNWVRK 585
Cdd:PLN02479 444 GYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRE 523
|
570 580 590
....*....|....*....|....*....|....
gi 501084078 586 EIGPLATPDVLHWtDSLPKTRSGKIMRRILRKIA 619
Cdd:PLN02479 524 RLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
1.93e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.03 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAattfkyvfdyhpddiyWCTADVGWVTGHS-YLLYGPL------ACGATTLM 329
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQA----------------LVLAVLQAIDEGTvFLNSGPLfhigtlMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 330 FEG----VPNWpTPARMAQVVDKHQVTILY-TAPT--AIRALMAEGdkaieGTDRSSLRILgsvgepinPEAWEWywkki 402
Cdd:cd17636 65 AGGtnvfVRRV-DAEEVLELIEAERCTHAFlLPPTidQIVELNADG-----LYDLSSLRSS--------PAAPEW----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 403 gNEKCPVVDTWW--------QTETGGFMITPLPGATElkAGSATRPFFGVQPALVDNEGH--PQ----EGATEGNLVITD 468
Cdd:cd17636 126 -NDMATVDTSPWgrkpggygQTEVMGLATFAALGGGA--IGGAGRPSPLVQVRILDEDGRevPDgevgEIVARGPTVMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 469 SW--PG--QARTLFGDHErfeqtyfstfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE 544
Cdd:cd17636 203 YWnrPEvnARRTRGGWHH---------------TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVAD 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501084078 545 AAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 268 AAVIGVPDPRWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
109-616 |
2.79e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.90 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 109 SYRELHRDVCRFANTLLELGIKKGDVVAI-----YMPMVpeaavAMLACARIGAVHSVIFGGFSPEAVAgRIIDSSSRLV 183
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTlawngYRHLE-----AYYGVSGSGAVCHTINPRLFPEQIA-YIVNHAEDRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 184 ITADEGVragrgIPLKKNVDDALKNpnvnsVEHVVVL----KRTGGKVDWhegrdLWWSDVIEKSSADHQPEEMNAEDPL 259
Cdd:PRK07008 115 VLFDLTF-----LPLVDALAPQCPN-----VKGWVAMtdaaHLPAGSTPL-----LCYETLVGAQDGDYDWPRFDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 260 FILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyvfdyhPDDIYWCTADV-----------GWVTGHSYLLYGplacgaT 326
Cdd:PRK07008 180 SLCYTSGTTGNPKGALysHRSTVLHAYGAAL--------PDAMGLSARDAvlpvvpmfhvnAWGLPYSAPLTG------A 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 TLMFegvpnwPTPA----RMAQVVDKHQVTILYTAPTAIRALMAEGDKAieGTDRSSLR---ILGSVGEPINPEAWEwyw 399
Cdd:PRK07008 246 KLVL------PGPDldgkSLYELIEAERVTFSAGVPTVWLGLLNHMREA--GLRFSTLRrtvIGGSACPPAMIRTFE--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 400 KKIGNEkcpVVDTWWQTEtggfmITPLPGATELKAGSATRP--------------FFGVQPALVDNEGH--PQEGATEGN 463
Cdd:PRK07008 315 DEYGVE---VIHAWGMTE-----MSPLGTLCKLKWKHSQLPldeqrkllekqgrvIYGVDMKIVGDDGRelPWDGKAFGD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 464 LVITDSWPGQaRTLFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIA 543
Cdd:PRK07008 387 LQVRGPWVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVA 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501084078 544 EAAVVGIPHNIKGQAIYAYVTLNHGEDPSPElytEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 459 EAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
260-610 |
2.55e-13 |
|
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: 72.50 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 260 FILYTSGSTGKPKGVlHTTGGYLVYAATTFKYVFDYHPDDIYWCTA----DVGWVTghsylLYGPLACGATTLMfegVPN 335
Cdd:cd17654 122 YVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLTSpltfDPSVVE-----IFLSLSSGATLLI---VPT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 336 W--PTPARMAQVVDK-HQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNeKCPVVDT 412
Cdd:cd17654 193 SvkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGN-RTRIFNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 413 WWQTETGGFMIT--------PLPGATELkAGSATRpffgvqpaLVDNEGHPQEGategnlviTDSWPGQARTLFGDHErf 484
Cdd:cd17654 272 YGITEVSCWALAykvpeedsPVQLGSPL-LGTVIE--------VRDQNGSEGTG--------QVFLGGLNRVCILDDE-- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 485 EQTYFSTfknMYFSGDGARRdEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIaEAAVVGIPHNikgQAIYAYVT 564
Cdd:cd17654 333 VTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIV 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 501084078 565 lnhgedpSPELYTEVRNWVRKEIGPL-ATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17654 405 -------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPLTSHGKV 444
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
91-615 |
8.48e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 70.89 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIWeGDdatqsKHISYRELHRDVCRFANTLLELG-IKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17648 2 DRVAVVY-GD-----KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 170 AVAGRIIDSSSRLVITadegvragrgiplkknvddalknpnvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhq 249
Cdd:cd17648 76 RIQFILEDTGARVVIT---------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 250 peemNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLV----YAATTF--KYVFDYHPDDIywCTAdvgWVTG 312
Cdd:cd17648 92 ----NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGrdngDEAVLFfsNYVFDFFVEQM--TLA---LLNG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 313 HSYLLYGPlacgattlmfEGVPnwpTPARMAQVVDKHQVTILYTAPTAIralmaegdKAIEGTDRSSLRILGSVGEPINP 392
Cdd:cd17648 163 QKLVVPPD----------EMRF---DPDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 393 EAWEwywKKIGNEKCPVVDTWWQTETGGF-MITPLPGATELKAgSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwp 471
Cdd:cd17648 222 PVFE---KLRSRFAGLIINAYGPTETTVTnHKRFFPGDQRFDK-SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGD-- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 472 GQARtlfGDH-------ERFEQTYFST--------FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd17648 296 GVAR---GYLnrpeltaERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAAL 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 537 VSHPKIAEAAVVGIPHNIKGQA-----IYAYVTLNHGEDPSpelyTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17648 373 ASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPE----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
....
gi 501084078 612 RRIL 615
Cdd:cd17648 449 VRAL 452
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-617 |
9.35e-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: 70.92 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 adegvragrgiplkknvddalknpnvnsvEHVVVLKRTggkvdwhegrdlwwsdvieksSADHQP--EEMNAEDPLFILY 263
Cdd:cd05939 82 -----------------------------NLLDPLLTQ---------------------SSTEPPsqDDVNFRDKLFYIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 264 TSGSTGKPKGVLHTTGGYLVYAATTFkYVFDYHPDDI-YWC-----TAdvGWVTGHSYLLYGplacGATTLM---FEGVP 334
Cdd:cd05939 112 TSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVvYDClplyhSA--GGIMGVGQALLH----GSTVVIrkkFSASN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 335 NWPTparmaqvVDKHQVTILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEK-------- 406
Cdd:cd05939 185 FWDD-------CVKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQigefygat 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 407 ---CPVVDTWWQTETGGFM------ITPL------PGATELKAGS-----ATRP-----FFGV---QPALVDNEGHPQEG 458
Cdd:cd05939 254 egnSSLVNIDNHVGACGFNsrilpsVYPIrlikvdEDTGELIRDSdglciPCQPgepglLVGKiiqNDPLRRFDGYVNEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 459 ATEGNLvitdswpgqARTLF--GDherfeqtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd05939 334 ATNKKI---------ARDVFkkGD-------------SAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 537 VSHPKIAEAAVVG--IPHnIKGQAIYAYVTlnhgeDPSPELYTEVRNWV-RKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05939 392 SNVLGLEDVVVYGveVPG-VEGRAGMAAIV-----DPERKVDLDRFSAVlAKSLPPYARPQFIRLLPEVDKTGTFKLQKT 465
|
....
gi 501084078 614 ILRK 617
Cdd:cd05939 466 DLQK 469
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
111-617 |
1.34e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 70.60 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 111 RELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITaDEGV 190
Cdd:PLN02860 36 HEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-DETC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 191 R-------AGRGIPLKKNV----DDALKNPNVNSVEHV-VVLKRTGGKVDWhegrDLWWSdviekssadhqpeemnAEDP 258
Cdd:PLN02860 115 SswyeelqNDRLPSLMWQVflesPSSSVFIFLNSFLTTeMLKQRALGTTEL----DYAWA----------------PDDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 259 LFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPDDIYWCTADVGWVTGHSYLLygplacgaTTLMFEG----VP 334
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQSLAKIAIV-GYGEDDVYLHTAPLCHIGGLSSAL--------AMLMVGAchvlLP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 335 NWPTPARMaQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLR-IL---GSVGEPINPEAWEWYWK-KIGN----- 404
Cdd:PLN02860 246 KFDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRkILnggGSLSSRLLPDAKKLFPNaKLFSaygmt 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 405 EKC------PVVDTWWQT--ETGGFMITPLPGATELKAGSATrpffGVQPALVDNEGHPQEGATEGNL------VITDSW 470
Cdd:PLN02860 325 EACssltfmTLHDPTLESpkQTLQTVNQTKSSSVHQPQGVCV----GKPAPHVELKIGLDESSRVGRIltrgphVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 471 pgqARTLFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI 550
Cdd:PLN02860 401 ---GQNSETASVLSNDGWLDT-------GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 551 PHNIKGQAIYAYVTLNHG---EDPSPELY--------TEVRNWVR-KEIGPLATPD-VLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02860 471 PDSRLTEMVVACVRLRDGwiwSDNEKENAkknltlssETLRHHCReKNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-279 |
3.86e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 69.23 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 69 WYEDGTL--NLAANCldrhlQENGDRTAI---------------------IWEGDDATQSKHISYRELHRDVCRFANTLL 125
Cdd:PTZ00216 65 WYYGPNFlqRLERIC-----KERGDRRALayrpvervekevvkdadgkerTMEVTHFNETRYITYAELWERIVNFGRGLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 126 ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAdegvragrgiplKKNVDDA 205
Cdd:PTZ00216 140 ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN------------GKNVPNL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 206 LKNPNVNSVEHVVV--LKRTGGKVDWHEGRDLWWSDVIEK--SSADHQPEEM--NAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 208 LRLMKSGGMPNTTIiyLDSLPASVDTEGCRLVAWTDVVAKghSAGSHHPLNIpeNNDDLALIMYTSGTTGDPKGVMHTHG 287
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
108-617 |
7.54e-12 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 67.76 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfspeavagriidsSSRLvitad 187
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI----------------NYNL----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 egvragRGIPLKKNVddalknpNVNSVEHVVVlkrtggkvdwhegrdlwwsdviekssadhqpeemnaeDPLFILYTSGS 267
Cdd:cd05940 63 ------RGESLAHCL-------NVSSAKHLVV-------------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPTparmaq 344
Cdd:cd05940 93 TGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDD------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 345 vVDKHQVTILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTE--TGGFM 422
Cdd:cd05940 166 -IRKYQATIFQYIGELCRYLLNQ--PPKPTERKHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 423 ITPLPGATElKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVITDSWPGQARTLFGDHERF----------EQTYFST 491
Cdd:cd05940 239 FFGKPGAIG-RNPSLLRKVAPLALVKYDLEsGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFdgytdpaateKKILRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 492 FK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIP-HNIKGQAIYAYVTLNH 567
Cdd:cd05940 318 FKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMAAIVLQP 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501084078 568 GEdpsPELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 398 NE---EFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
106-559 |
7.91e-12 |
|
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: 68.01 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVIT 185
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 adegvragrgiplkknvddalkNPNvnsvehvvvlkrtggkvdwhegrdlwwsdviekssadhqpeemnAEDPLFILYTS 265
Cdd:cd17639 84 ----------------------DGK--------------------------------------------PDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 266 GSTGKPKGVLHTTGGyLVYAATTF-KYVFDY-HPDDiywctadvgwvtghSYLLYGPLA----------C---GAT---- 326
Cdd:cd17639 98 GSTGNPKGVMLTHGN-LVAGIAGLgDRVPELlGPDD--------------RYLAYLPLAhifelaaenvClyrGGTigyg 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 327 ---TL------------------MFEGVPN-WPT--PARMAQVVDK--HQVTILYTAPTAIRALMAEG------DKAIEG 374
Cdd:cd17639 163 sprTLtdkskrgckgdltefkptLMVGVPAiWDTirKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGpgtpllDELVFK 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 375 TDRSS----LRILGSVGEPINPEAWEWywkkIGNEKCPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVD 450
Cdd:cd17639 243 KVRAAlggrLRYMLSGGAPLSADTQEF----LNIVLCPVIQGYGLTETCAGGTVQDPG--DLETGRVGPPLPCCEIKLVD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 451 NEghpqegatEGNLvITDSWPGQARTLFG---------------DHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGR 515
Cdd:cd17639 317 WE--------EGGY-STDKPPPRGEILIRgpnvfkgyyknpektKEAFDGDGWFHT-------GDIGEFHPDGTLKIIDR 380
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 501084078 516 VDD-VLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17639 381 KKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAI 425
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-580 |
8.72e-12 |
|
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: 67.87 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 255 AEDPLFILYTSGSTGKPKGVLHTTGgylvyaatTFKYVFDYHPDDIYWCTADVGWVTGHSYLLYGPlACGATTLMFEGVP 334
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHG--------TFAAQIDALRQLYGIRPGEVDLATFPLFALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 335 NWP---TPARMAQVVDKHQVTILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYwKKIGNEKCPVVD 411
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARL-RKMLSDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 TWWQTET-------GGFMITPLPGATELKAGSAT-RPFFGVQPALV--DNEGHPQEGATE-------GNLVITDswPGQA 474
Cdd:cd05910 232 PYGATEAlpvssigSRELLATTTAATSGGAGTCVgRPIPGVRVRIIeiDDEPIAEWDDTLelprgeiGEITVTG--PTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 475 RTLfgdHERFEQTYFSTFKN-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd05910 310 PTY---VNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
330 340 350
....*....|....*....|....*....|.
gi 501084078 550 IPHNIKGQAIYAYVTLNHGEDPSPELYTEVR 580
Cdd:cd05910 387 VGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-625 |
2.50e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.17 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 TWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNeghpqegaTEGNLVItdswpgQARTLF-GdherfeqtYFS 490
Cdd:PRK07445 260 TYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPAN--------QTGNITI------QAQSLAlG--------YYP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 491 TFKNMY---FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK07445 318 QILDSQgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 568 GeDPSPElytEVRNWVRKEIGPLATPDvlHW--TDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PRK07445 398 P-SISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-322 |
3.94e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 66.29 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITAD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 188 EgvragrgiPLKKNVDDALKnpnVNSVEHVVVLKRTGGKVDWHEGRDLWW-----SDVIEKSSADHQPEEM-NAEDPLFI 261
Cdd:PLN02387 187 K--------QLKKLIDISSQ---LETVKRVIYMDDEGVDSDSSLSGSSNWtvssfSEVEKLGKENPVDPDLpSPNDIAVI 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDIywctadvgwvtghsYLLYGPLA 322
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-615 |
1.56e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.52 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPSpely 576
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPV---- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 501084078 577 tEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-549 |
2.02e-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: 63.53 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 106 KHISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVifggfspeavagRIIDSSsrlvit 185
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV------------RGSDSS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 adegvragrgiplkknVDDALKnpNVNSVEHVVVlkrtggkvdwhegrdlwwsdVIEKSSadhqpeemnaEDPLFILYTS 265
Cdd:cd17640 66 ----------------VEELLY--ILNHSESVAL--------------------VVENDS----------DDLATIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 266 GSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIYWCTADVgWvtgHSY---LLYGPLACGATTLmfegvpnWPTPARM 342
Cdd:cd17640 98 GTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 343 AQVVDKHQVTILYTAPTAIRALMAEGDKAIEGTDRSSLRILG---SVGE---PIN-----PEAWEWYWKKIGnekCPVVD 411
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 TWWQTETGGFMITPLPGATelKAGSATRPFFGVQPALVDneghpqegaTEGNLVITdswPGQARTLF--GDHerFEQTYF 489
Cdd:cd17640 243 GYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVD---------PEGNVVLP---PGEKGIVWvrGPQ--VMKGYY 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 490 ----STFKNM----YF-SGDGARRDEDGYYWITGRVDD--VLNvSGHRLGTAEIESALVSHPKIAEAAVVG 549
Cdd:cd17640 307 knpeATSKVLdsdgWFnTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
107-613 |
5.44e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 62.32 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 107 HISYRELHRDVCRFANTLLELGIKKGDVVAIY--MP--MVPEAAVAMLACARIGAVHSvifggfsPEAvagriidsSSRL 182
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPveIAPTAQGLWMRGASLTMLHQ-------PTP--------RTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 183 VITADEGVRAGRGIPLKKNVddaLKNPNVNSVEhvvVLKRTGGKVdwHEGRDLWWSDVIEkssadhqPEEMNAEDPLFIL 262
Cdd:PRK07768 94 AVWAEDTLRVIGMIGAKAVV---VGEPFLAAAP---VLEEKGIRV--LTVADLLAADPID-------PVETGEDDLALMQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 263 YTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPDD---IYW--CTADVGWVTGhsylLYGPLACGATTLMFEGVPNWP 337
Cdd:PRK07768 159 LTSGSTGSPKAVQITHGNLYANAEAMFVAA-EFDVETdvmVSWlpLFHDMGMVGF----LTVPMYFGAELVKVTPMDFLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 338 TPARMAQVVDKHQVTILyTAPTAIRALMAE--GDKAIEGT-DRSSLRILGSVGEPINPEAWEWYW---KKIGNEKCPVVD 411
Cdd:PRK07768 234 DPLLWAELISKYRGTMT-AAPNFAYALLARrlRRQAKPGAfDLSSLRFALNGAEPIDPADVEDLLdagARFGLRPEAILP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 412 TWWQTET---------GGFMITPLPGATELKA--------GSATRPFF-------GVQPALVDNEGHPQ----------- 456
Cdd:PRK07768 313 AYGMAEAtlavsfspcGAGLVVDEVDADLLAAlrravpatKGNTRRLAtlgpplpGLEVRVVDEDGQVLpprgvgvielr 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 457 -EGATEGNLVITDSWPGQArtlfgdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK07768 393 gESVTPGYLTMDGFIPAQD----------ADGWLDT-------GDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 536 LVSHPKIAEAAVVGI----PHNIKGQAIYAYVTLNHGEDPSPELYTEVRNWVRKEIGplATPDVLHWTD--SLPKTRSGK 609
Cdd:PRK07768 456 AARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTPSGK 533
|
....
gi 501084078 610 IMRR 613
Cdd:PRK07768 534 LRRA 537
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
254-621 |
6.92e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 254 NAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATtfkyVFDYHPDDIywctadvgwVTG-----HSY----LLYGPL 321
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMfegVPNwPTPARM-AQVVDKHQVTILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:PRK08633 847 LEGIKVVY---HPD-PTDALGiAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEE 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 401 KIG---------NEKCPVV----------DTWWQTETggfmitplpgatelKAGSATRPFFGVQPALVD-NEGHPQEGAT 460
Cdd:PRK08633 921 KFGirilegygaTETSPVAsvnlpdvlaaDFKRQTGS--------------KEGSVGMPLPGVAVRIVDpETFEELPPGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 461 EGNLVITDS-----WPGQA-RTLFGDHERFEQTYfstfknmYFSGDGARRDEDGYYWITGRVDdvlnvsghRLgtAEIES 534
Cdd:PRK08633 987 DGLILIGGPqvmkgYLGDPeKTAEVIKDIDGIGW-------YVTGDKGHLDEDGFLTITDRYS--------RF--AKIGG 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 535 ALVSHPKIAEA------------AVVGIPHNIKGQAIYAYVTlnHGEDPSPELYTEVRNwvrKEIGPLATPDVLHWTDSL 602
Cdd:PRK08633 1050 EMVPLGAVEEElakalggeevvfAVTAVPDEKKGEKLVVLHT--CGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEAL 1124
|
410
....*....|....*....
gi 501084078 603 PKTRSGKIMRRILRKIAAG 621
Cdd:PRK08633 1125 PLLGSGKLDLKGLKELALA 1143
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-615 |
2.40e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.29 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 82 LDRHLQENGDRTAIIWEGDDatqskhISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIG----- 156
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEK------LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 157 -AVHSvifggfSPEAVAgRIIDSS-SRLVITADEgvragrgIPLkknvdDALKNPnVNSVEHVVVLKRTGGKVDwhegrd 234
Cdd:PRK04813 82 vDVSS------PAERIE-MIIEVAkPSLIIATEE-------LPL-----EILGIP-VITLDELKDIFATGNPYD------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 235 lwwsdviekssADHQpeeMNAEDPLFILYTSGSTGKPKGV--LHTTggyLVyaatTFkyvfdyhpddIYWCTADVGWVTG 312
Cdd:PRK04813 136 -----------FDHA---VKGDDNYYIIFTSGTTGKPKGVqiSHDN---LV----SF----------TNWMLEDFALPEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 313 HSYL-------------LYGPLACGATTLMfegVPNWPT--PARMAQVVDKHQVTILYTAPTAIRalMAEGDKAIEGTDR 377
Cdd:PRK04813 185 PQFLnqapysfdlsvmdLYPTLASGGTLVA---LPKDMTanFKQLFETLPQLPINVWVSTPSFAD--MCLLDPSFNEEHL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 378 SSLRILGSVGEPI-NPEAwewywKKIgNEKCP---VVDTWWQTETGGFM----IT--------PLP-GATelKAGSATrp 440
Cdd:PRK04813 260 PNLTHFLFCGEELpHKTA-----KKL-LERFPsatIYNTYGPTEATVAVtsieITdemldqykRLPiGYA--KPDSPL-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 441 ffgvqpALVDNEGHPQEGATEGNLVITdswpGQARTL--FGDHERFEQTYFsTFKNM--YFSGDGARRDeDGYYWITGRV 516
Cdd:PRK04813 330 ------LIIDEEGTKLPDGEQGEIVIS----GPSVSKgyLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE-DGLLFYQGRI 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 517 DDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE-DPSPELYTEVRNWVRKEIGPLATPDV 595
Cdd:PRK04813 398 DFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDfEREFELTKAIKKELKERLMEYMIPRK 477
|
570 580
....*....|....*....|
gi 501084078 596 LHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK04813 478 FIYRDSLPLTPNGKIDRKAL 497
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-322 |
8.87e-09 |
|
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: 58.38 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLLELGIK--KGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAgRIIDSSSRLVIT 185
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIE-YILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 186 ADEGVRagrgiplkknvddalknpnvnsvehvVVLkrtggkvdwhegrdlwWSDVIEKSSADHQPEEMNAEDPLF-ILYT 264
Cdd:cd05927 85 CDAGVK--------------------------VYS----------------LEEFEKLGKKNKVPPPPPKPEDLAtICYT 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501084078 265 SGSTGKPKGVLHTTGGYLVYAATTFKYVFDYH---PDDIYWctadvgwvtghSYLlygPLA 322
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDVYI-----------SYL---PLA 169
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
79-621 |
4.77e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 79 ANCLDRHLQENGDRTAIIWEGDDATQSKHISYRELHRDVCRFANTLLELGiKKGDVVAIYMPMVPEAAVAMLAC--ARIG 156
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGClyAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 157 AVHSvifggFSPEAV--------AGRIIDSSSRLVITaDEGVRAgrgiPLKKNvdDALKNPNVNSVEHVvvlkrtggkvd 228
Cdd:PRK05691 91 AVPA-----YPPESArrhhqerlLSIIADAEPRLLLT-VADLRD----SLLQM--EELAAANAPELLCV----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 229 whegrdlwwsDVIEKSSADH-QPEEMNAEDPLFILYTSGSTGKPKGVlHTTGGYLVYAATTFKYVF--DYHPDDIYwcta 305
Cdd:PRK05691 148 ----------DTLDPALAEAwQEPALQPDDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFgiDLNPDDVI---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 306 dVGWVT-GHSYLLYGPLACGattlMFEGVPN--------WPTPARMAQVVDKHQVTILYTAPTAIRaLMAE--GDKAIEG 374
Cdd:PRK05691 213 -VSWLPlYHDMGLIGGLLQP----IFSGVPCvlmspayfLERPLRWLEAISEYGGTISGGPDFAYR-LCSErvSESALER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 375 TDRSSLRILGSVGEPINPEAWEWYWKKI---GNEKCPVVDTWWQTETGGFMITPLPG----ATEL--KAGSATRPFFGVQ 445
Cdd:PRK05691 287 LDLSRWRVAYSGSEPIRQDSLERFAEKFaacGFDPDSFFASYGLAEATLFVSGGRRGqgipALELdaEALARNRAEPGTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 446 PALV----DNEGH------PQEGATEGNLVITDSW---PGQARTLFGDHERFEQTYFSTFKNMYF-SGD-GARRdeDGYY 510
Cdd:PRK05691 367 SVLMscgrSQPGHavlivdPQSLEVLGDNRVGEIWasgPSIAHGYWRNPEASAKTFVEHDGRTWLrTGDlGFLR--DGEL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 511 WITGRVDDVLNVSGHRLGTAEIESAL---VSHPKIAEAAVVGIPHN-IKGQAIYAYVTLNHGEDPSPE-LYTEVRNWVRK 585
Cdd:PRK05691 445 FVTGRLKDMLIVRGHNLYPQDIEKTVereVEVVRKGRVAAFAVNHQgEEGIGIAAEISRSVQKILPPQaLIKSIRQAVAE 524
|
570 580 590
....*....|....*....|....*....|....*..
gi 501084078 586 EIGPLATPDVLHWTDSLPKTRSGKIMRRILR-KIAAG 621
Cdd:PRK05691 525 ACQEAPSVVLLLNPGALPKTSSGKLQRSACRlRLADG 561
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
108-277 |
1.04e-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: 55.15 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTL-LELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGrIIDSSSRLVITA 186
Cdd:cd17632 68 ITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAP-ILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 187 DegvragrgiplKKNVDDALKN-PNVNSVEHVVVLkrtGGK--VDWHE-------------GRDLWWSDVIEKSSADHQP 250
Cdd:cd17632 147 S-----------AEHLDLAVEAvLEGGTPPRLVVF---DHRpeVDAHRaalesarerlaavGIPVTTLTLIAVRGRDLPP 212
|
170 180 190
....*....|....*....|....*....|..
gi 501084078 251 EEMNAE----DPL-FILYTSGSTGKPKGVLHT 277
Cdd:cd17632 213 APLFRPepddDPLaLLIYTSGSTGTPKGAMYT 244
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
91-610 |
1.79e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 54.06 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAIIwEGDDATQSKH--ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:cd17647 3 ERTCVV-ETPSLNSSKTrsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 169 EavagriidsssRLVITAdeGVRAGRGIplkknvddalknpnvnsvehvVVLKRTGGKVdwhegrdlwwsdvieksSADH 248
Cdd:cd17647 82 A-----------RQNIYL--GVAKPRGL---------------------IVIRAAGVVV-----------------GPDS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 249 QPEemnaedplfILYTSGSTGKPKGVL---HTTGGYLVYAATTFKYVfdyhPDDIYWCTADVgwvtGHSYL---LYGPLA 322
Cdd:cd17647 111 NPT---------LSFTSGSEGIPKGVLgrhFSLAYYFPWMAKRFNLS----ENDKFTMLSGI----AHDPIqrdMFTPLF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 323 CGATTLmfegVP---NWPTPARMAQVVDKHQVTILYTAPTAIRALMAEGDKAIEG-----------TDRSSLRILGSVge 388
Cdd:cd17647 174 LGAQLL----VPtqdDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKlhhaffvgdilTKRDCLRLQTLA-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 389 pinpeawewywkkignEKCPVVDTWWQTETGGFMitplpGATELKAGSATRPFF----GVQPA---------LVDNEGHP 455
Cdd:cd17647 248 ----------------ENVRIVNMYGTTETQRAV-----SYFEVPSRSSDPTFLknlkDVMPAgrgmlnvqlLVVNRNDR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 456 QE---------------GATEGNL---------------VITDSWPGQARTLfgdHERFEQTYFSTFKNMYFSGDGARRD 505
Cdd:cd17647 307 TQicgigevgeiyvragGLAEGYRglpelnkekfvnnwfVEPDHWNYLDKDN---NEPWRQFWLGPRDRLYRTGDLGRYL 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 506 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAE----------------AAVVGIPHNIKGQAIY-AYVTLNHG 568
Cdd:cd17647 384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrrdkdeeptlvSYIVPRFDKPDDESFAqEDVPKEVS 463
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 501084078 569 EDPS-------PELYTEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17647 464 TDPIvkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-277 |
4.31e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.96 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 54 KVKNTSFAPGNVSIKWYEDGTLNLAAN------------CLDRHLQENGDRTAIIwEGDDATQSKHISYRELHRDVCRFA 121
Cdd:PRK08180 5 RYRPVAFAPPAVEVERRADGTIYLRSAeplgdyprrltdRLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 122 NTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPeAVAGRIIDsSSRL----------VITADEGVR 191
Cdd:PRK08180 84 QALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP-AYSLVSQD-FGKLrhvlelltpgLVFADDGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 192 AGRGIplkknvdDALKnpnvnsVEHVVVLKRTGGKVDwheGRDLWWSDVIEKSSADHQPEEMNAEDPLFI---LYTSGST 268
Cdd:PRK08180 158 FARAL-------AAVV------PADVEVVAVRGAVPG---RAATPFAALLATPPTAAVDAAHAAVGPDTIakfLFTSGST 221
|
....*....
gi 501084078 269 GKPKGVLHT 277
Cdd:PRK08180 222 GLPKAVINT 230
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
124-620 |
5.74e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 124 LLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfgGFSpeAVAGRIIDSSS----RLVITADEGVRAGRGIPLK 199
Cdd:PRK06814 674 KLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSACKaaqvKTVLTSRAFIEKARLGPLI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 200 KNVDDALKnpnvnsVEHVVVLKRTGGKVDWHEGrdlwwsdVIEKSSADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PRK06814 750 EALEFGIR------IIYLEDVRAQIGLADKIKG-------LLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHR 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 280 GYLVYAATTFKYVfDYHPDDIYWCTADVgwvtGHSYLLYGplacGATTLMFEGVPN--WPTPAR---MAQVVDKHQVTIL 354
Cdd:PRK06814 817 NLLANRAQVAARI-DFSPEDKVFNALPV----FHSFGLTG----GLVLPLLSGVKVflYPSPLHyriIPELIYDTNATIL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 355 YTAPTAIR--ALMAegdkaiEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGF--MITPLpgat 430
Cdd:PRK06814 888 FGTDTFLNgyARYA------HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIR---ILEGYGVTETAPViaLNTPM---- 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 431 ELKAGSATRPFFGVQPALVDNEGHPQEG--------------ATEGNLVI---TDSWpgqartlfgdherfeqtyfstfk 493
Cdd:PRK06814 955 HNKAGTVGRLLPGIEYRLEPVPGIDEGGrlfvrgpnvmlgylRAENPGVLeppADGW----------------------- 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 494 nmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGIPHNIKGQAIyayVTLNHGEDPSP 573
Cdd:PRK06814 1012 --YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI---ILLTTASDATR 1086
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 501084078 574 ELYTevrNWVRKE-IGPLATPDVLHWTDSLPKTRSGKI----MRRILRKIAA 620
Cdd:PRK06814 1087 AAFL---AHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAA 1135
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
108-612 |
2.51e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 50.37 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 108 ISYRELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSSSRLVITA 186
Cdd:cd05938 6 YTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 187 DEgvragrgipLKKNVDD---ALKNPNVnsveHVVVLKRTggkvDWHEG-RDLwwSDVIEKSSADHQPEEMNAE----DP 258
Cdd:cd05938 86 PE---------LQEAVEEvlpALRADGV----SVWYLSHT----SNTEGvISL--LDKVDAASDEPVPASLRAHvtikSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 259 LFILYTSGSTGKPKGVLHTTggYLVYAATTFKYVFDYHPDDIYWCTADVGWVTGhsyLLYGPLAC---GATTLM---FEG 332
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISH--LRVLQCSGFLSLCGVTADDVIYITLPLYHSSG---FLLGIGGCielGATCVLkpkFSA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 333 VPNWPtparmaqvvD--KHQVT-ILYTAPTaIRALMAEGDKAIEGTDRSSLrilgSVGEPINPEAWEWYWKKIGNEKcpV 409
Cdd:cd05938 222 SQFWD---------DcrKHNVTvIQYIGEL-LRYLCNQPQSPNDRDHKVRL----AIGNGLRADVWREFLRRFGPIR--I 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 410 VDTWWQTE-TGGFM-ITPLPGATelkaGSATR------PF----FGVQPA--LVDNEGH--PQEGATEGNLV--ITDSWP 471
Cdd:cd05938 286 REFYGSTEgNIGFFnYTGKIGAV----GRVSYlykllfPFelikFDVEKEepVRDAQGFciPVAKGEPGLLVakITQQSP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 472 --GQArtlfGDHERFEQTYF-STFK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEA 545
Cdd:cd05938 362 flGYA----GDKEQTEKKLLrDVFKkgDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501084078 546 AVVGIP-HNIKGQAIYAYVTLNHGEDPSPE-LYTEVRNWvrkeIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05938 438 NVYGVTvPGHEGRIGMAAVKLKPGHEFDGKkLYQHVREY----LPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
91-275 |
4.70e-06 |
|
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: 50.06 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 91 DRTAII-WEGDDATQSKH--ISYRELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:TIGR03443 251 DRTCVVeTPSFLDPSSKTrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 168 PE------AVAgriidSSSRLVITADEGvragrgiPLKKNVDDALKNpNVNSVEHVVVLKR------TGGKVDWHEGrdl 235
Cdd:TIGR03443 331 PArqtiylSVA-----KPRALIVIEKAG-------TLDQLVRDYIDK-ELELRTEIPALALqddgslVGGSLEGGET--- 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501084078 236 wwsDVIekssadhQPEEMNAEDPLFIL----------YTSGSTGKPKGVL 275
Cdd:TIGR03443 395 ---DVL-------APYQALKDTPTGVVvgpdsnptlsFTSGSEGIPKGVL 434
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
246-617 |
1.51e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 47.87 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 246 ADHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPDDIY--W--CTADVGWVTGHsyllYGPL 321
Cdd:cd05908 96 TEEEVLCELADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 322 ACGATTLMFegvpnwPT------PARMAQVVDKHQVTILYTAPTAIRALMAE-GDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:cd05908 171 IAGMNQYLM------PTrlfirrPILWLKKASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYEL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 WEWYWKKIG----NEKCpvvdtwwqtetggfmITPLPGATELKAGS----ATRPFF-----------GVQPALVDNEGhp 455
Cdd:cd05908 245 CHEFLDHMSkyglKRNA---------------ILPVYGLAEASVGAslpkAQSPFKtitlgrrhvthGEPEPEVDKKD-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 456 QEGAT-----------------EGNLVITDSWPGQARtLFGdhERFEQTYFSTFK--NMYFSGDGARRDED------GYY 510
Cdd:cd05908 308 SECLTfvevgkpidetdiricdEDNKILPDGYIGHIQ-IRG--KNVTPGYYNNPEatAKVFTDDGWLKTGDlgfirnGRL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 511 WITGRVDDVLNVSGHRLGTAEIESALVSHPKIAEAAVVGI---PHNIKGQAIYAYVTLNHGEDPSPELYTEVRN------ 581
Cdd:cd05908 385 VITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACgvnNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKhlnkrg 464
|
410 420 430
....*....|....*....|....*....|....*..
gi 501084078 582 -WVRKEIGPLATpdvlhwtdsLPKTRSGKIMRRILRK 617
Cdd:cd05908 465 gWQINEVLPIRR---------IPKTTSGKVKRYELAQ 492
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
247-617 |
1.11e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 41.67 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 247 DHQPEEMNA---EDPLFILYTSGSTGKPKGVLHTTGGYLVYaATTFKYVF---DYHPDDIYWCTADVGWVTGHSYLLYGP 320
Cdd:COG1541 71 DNYPFGLFAvplEEIVRIHASSGTTGKPTVVGYTRKDLDRW-AELFARSLraaGVRPGDRVQNAFGYGLFTGGLGLHYGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 321 LACGATTlmfegVPNWP-TPARMAQVVDKHQVTILYTAPTAIRALmaeGDKAIE-GTD--RSSLR--ILGsvGEPInPEA 394
Cdd:COG1541 150 ERLGATV-----IPAGGgNTERQLRLMQDFGPTVLVGTPSYLLYL---AEVAEEeGIDprDLSLKkgIFG--GEPW-SEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 395 W-EWYWKKIGnekCPVVDTWWQTETGgfmitplPG-ATELKAgsatrpffgvQPALVDNEGH-------PQEGAT----- 460
Cdd:COG1541 219 MrKEIEERWG---IKAYDIYGLTEVG-------PGvAYECEA----------QDGLHIWEDHflveiidPETGEPvpege 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 461 EGNLVITdswpgqarTLF-----------GDHERFEQTYFST-FKNMYFSGdgarrdedgyywITGRVDDVLNVSGHRLG 528
Cdd:COG1541 279 EGELVVT--------TLTkeampliryrtGDLTRLLPEPCPCgRTHPRIGR------------ILGRADDMLIIRGVNVF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 529 TAEIESALVSHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEDPsPELYTEVRNWVRKEIGplATPDV-LHWTDSLPktRS 607
Cdd:COG1541 339 PSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASL-EALAEAIAAALKAVLG--LRAEVeLVEPGSLP--RS 413
|
410
....*....|
gi 501084078 608 GKIMRRILRK 617
Cdd:COG1541 414 EGKAKRVIDR 423
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
532-645 |
2.25e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 40.90 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501084078 532 IESALVSHPKIAEAAVVGIPHNIKGQAIYAYVtlnhgEDPSPELYTEVRNWVRKEIGPLAtPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....*
gi 501084078 612 RRILRKIAAGDTSNLGDTSTL-ADPGVVEKLLEEK 645
Cdd:PRK09188 319 DDILRLIAMNQIDELDDLLREpEIRGLVEAIAAHR 353
|
|
| |
