|
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: 1342.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 6 VYPVKENIKSTTHADNDTYLAMYQQSVSDPEGFWGEHGKIVDWIKPFtqvkNTSFDPGHIDIRWFEDGTLNVSANCIDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 86 LAERGDEVAIIWEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 166 FSPEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEALTNPEvkNIEKVVVFKRTGGDVAWHEHRDVWWHDAIANVS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 ADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 326 KTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 406 QSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDHDRFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 486 QTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 566 NDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDTgNLGDTSTLADPSVVDKLIAEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
gi 515671996 646 AELA 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: 1159.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 18 HADNDTYLAMYQQSVSDPEGFWGEHGK-IVDWIKPFTQVKNTSFDPghiDIRWFEDGTLNVSANCIDRHLAERGDEVAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 97 WEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 177 DSNSKVVITADEGVRGGRAVPLKKNVDEALTNPEVKnIEKVVVFKRTGGDVA-WHEHRDVWWHDAIANVSADCPPEEMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS-VEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 YPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQSPIVDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGN-LVILDSWPGQMRTVHGDHDRFEQTYFSTFKG 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 495 MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 575 LHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDTGNLGDTSTLADPSVVDKLIAE 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: 1147.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 22 DTYLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVKNTSFDPghIDIRWFEDGTLNVSANCIDRHLAERGDEVAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSKGP--PFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 102 PADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSK 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 182 VVITADEGVRGGRAVPLKKNVDEALTnpEVKNIEKVVVFKRTGGDVAWHEHRDVWWHDAIANVSADCPPEEMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALE--KCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 262 LYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPNTSR 341
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 342 MSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQSPIVDTWWQTETGGI 421
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 422 LIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDHDRFEQTYFSTFKGMYFTSDG 501
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 502 ARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKN 581
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 515671996 582 WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDTgNLGDTSTLAD 634
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| 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: 911.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 68 RWFEDGTLNVSANCIDRHLAERGDEVAIIWEGDDpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGED-GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 148 AMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEALtnPEVKNIEKVVVFKRTGGDV 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAL--EELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 228 AWHEhrDVWWHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 308 GWITGHTYLVYGPLANGAKTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 388 EPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPLPGaTDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIL 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 468 DSWPGQMRTVHGDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAI 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 548 VGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDtgNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 515671996 628 DTSTLADPSVVDKLIA 643
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| 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: 882.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 24 YLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVKNTSFDPGHIDIRWFEDGTLNVSANCIDRHLAERGDEVAIIWEGDDPA 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 104 DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 ITADEGVRGGRAVPLKKNVDEALtNPEVKNIEKVVVFKRTGGDVAWHEHRDVWWHDAIANVSADCPPEEMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPNTSRMS 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 344 EVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQSPIVDTWWQTETGGILI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 424 APLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDHDRFEQTYFSTFKGMYFTSDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 504 RDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 515671996 584 RKEIGPIATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 819.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 2 SEAH--VYPVKENIKSTTHADNDTYLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVK----NTSFDPGHIDIRWFEDGTL 75
Cdd:PLN02654 8 SEENdlVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEvcseNLDVRKGPISIEWFKGGKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 76 NVSANCIDRHL-AERGDEVAIIWEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTR 154
Cdd:PLN02654 88 NICYNCLDRNVeAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 155 IGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEALTNPEVKNI--------EKVVVFKRTggD 226
Cdd:PLN02654 168 IGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVsvgicltyENQLAMKRE--D 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 227 VAWHEHRDVWWHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTAD 306
Cdd:PLN02654 246 TKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTAD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 307 VGWITGHTYLVYGPLANGAKTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSV 386
Cdd:PLN02654 326 CGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 387 GEPINPEAWEWYYKTIGNEQSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVI 466
Cdd:PLN02654 406 GEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 467 LDSWPGQMRTVHGDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:PLN02654 486 KKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 547 IVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDTGNL 626
Cdd:PLN02654 566 VVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDEL 645
|
650
....*....|....*..
gi 515671996 627 GDTSTLADPSVVDKLIA 643
Cdd:PLN02654 646 GDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-641 |
0e+00 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 629.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 24 YLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVKNTSFDPGHidiRWFEDGTLNVSANCIDRH-LAERGDEVAIIWEGDDP 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFT---RWFVGGRLNTCYNALDRHvEAGRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 103 ADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKV 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 183 VITADEGVRGGRAVPLKKNVDEALTNPEVKNiEKVVVFKRtgGDV---AWHEHRDVWWHDAIANV-SADCPPeeMNAEDP 258
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSGHKP-HHVLVLNR--PQVpadLTKPGRDLDWSELLAKAePVDCVP--VAATDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 259 LFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVP-NYP 337
Cdd:cd05967 233 LYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 338 NTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRD--SLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQ 415
Cdd:cd05967 313 DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDlsSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPLPGATDL--KPGSATRPFFGVQPALVDNMGNIIEGATDGNLVI-LDSWPGQMRTVHGDHDRFEQTYFSTF 492
Cdd:cd05967 390 TETGWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIkLPLPPGCLLTLWKNDERFKKLYLSKF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 493 KGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPT 572
Cdd:cd05967 470 PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKIT 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 573 AE-LHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDtgNLGDTSTLADPSVVDKL 641
Cdd:cd05967 550 AEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-641 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 598.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 22 DTYLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVKNTSFDPGhidIRWFEDGTLNVSANCIDRHLAERGDEVAIIWEGDD 101
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPF---ARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 102 PADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSK 181
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 182 VVITADEGVRGGRAVPLKKNVDEALTNPEVKNiEKVVVFKRTGGDVAWHEHRDVWWHDAIANV-SADCPPEEMNAEDPLF 260
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIALAQHKP-RHVLLVDRGLAPMARVAGRDVDYATLRAQHlGARVPVEWLESNEPSY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 261 ILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPNTS 340
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 341 RMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGG 420
Cdd:PRK10524 318 IWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVIDNYWQTETGW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 421 ILIAPLPGATDL--KPGSATRPFFGVQPALVD-NMGNIIEGATDGNLVILDSW-PGQMRTVHGDHDRFEQTYFSTFKGM- 495
Cdd:PRK10524 395 PILAIARGVEDRptRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFGRQv 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 496 YFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDG-----EF 570
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsladRE 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 571 PTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATG-DTGNLgdtSTLADPSVVDKL 641
Cdd:PRK10524 555 ARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDPGDL---TTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-635 |
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: 535.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 24 YLAMYQQSVSDPEGFWGEHGKIVD--WIKPFTQVKNTSfdpGHIDI-RWFEDGTLNVSANCIDRHLAERGDEVAIIWEGD 100
Cdd:cd05968 9 LEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS---GGKPWaAWFVGGRMNIVEQLLDKWLADTRTRPALRWEGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 101 DPADdKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNS 180
Cdd:cd05968 86 DGTS-RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 181 KVVITADEGVRGGRAVPLKKNVDEALTN-PEVkniEKVVVFKRTGGDVAWHEHRDVWWHDAIAnvSADCPPEEMNAEDPL 259
Cdd:cd05968 165 KALITADGFTRRGREVNLKEEADKACAQcPTV---EKVVVVRHLGNDFTPAKGRDLSYDEEKE--TAGDGAERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 260 FILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGET-FWCTaDVGWITGhTYLVYGPLANGAKTILFEGVPNYPN 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLlTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 339 TSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQSPIVDTWWQTE- 417
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEi 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 418 TGGIL----IAPLpgatdlKPGSATRPFFGVQPALVDNMGNIIEGaTDGNLVILDSWPGQMRTVHGDHDRFEQTYFSTFK 493
Cdd:cd05968 398 SGGILgnvlIKPI------KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 494 GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTA 573
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 574 ELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDtgNLGDTSTLADP 635
Cdd:cd05968 551 ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-634 |
3.43e-162 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 477.08 E-value: 3.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 69 WFEDGTLNVSANCIDRHLA-ERGDEVAIIWEGDDPADDktLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADgGRKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 148 AMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRggravplKKNVDEAltnPEVKNIekVVVfkrtgGDV 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL---PSLKHV--LLV-----GED 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 228 AWHEHRDVWWHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHttggylVYAAM-----TFKYVFDYQEGETFW 302
Cdd:PRK04319 177 VEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH------VHNAMlqhyqTGKYVLDLHEDDVYW 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 303 CTADVGWITGHTYLVYGPLANGAKTILFEGvpnypntsRMS-----EVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSR 377
Cdd:PRK04319 251 CTADPGWVTGTSYGIFAPWLNGATNVIDGG--------RFSperwyRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 378 DSLRVMGSVGEPINPEAWEWYYKTIGNeqsPIVDTWWQTETGGILIAPLPgATDLKPGSATRPFFGVQPALVDNMGNIIE 457
Cdd:PRK04319 323 SSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 GATDGNLVILDSWPGQMRTVHGDHDRFEQtYFStfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:PRK04319 399 PNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 538 AFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK04319 476 EHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
570
....*....|....*....
gi 515671996 618 IATGdtgnL--GDTSTLAD 634
Cdd:PRK04319 556 WELG----LpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
108-619 |
2.48e-137 |
|
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: 408.81 E-value: 2.48e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITad 187
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 egvrggravplkknvdealtNPEVKniekvvvfkrtggdvawhehrdvwwhdaianvsadcppEEMNAEDPLFILYTSGS 267
Cdd:cd05969 79 --------------------TEELY--------------------------------------ERTDPEDPTLLHYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGGYLVYAaMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGvpnYPNTSRMSEVVD 347
Cdd:cd05969 101 TGTPKGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 348 KHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPLP 427
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 428 GaTDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDHDRFEQtYFSTfkGMYFTSDGARRDED 507
Cdd:cd05969 254 C-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 508 GYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEI 587
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
gi 515671996 588 GPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05969 410 GAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
108-617 |
2.64e-112 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 343.94 E-value: 2.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITad 187
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 egvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemNAEDPLFILYTSGS 267
Cdd:cd05972 79 ------------------------------------------------------------------DAEDPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGgYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPntSRMSEVVD 347
Cdd:cd05972 93 TGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDA--ERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 348 KHQVNILYTAPTAIRALMAKGneaVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGgILIAPLP 427
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 428 GaTDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDHDRFEqtyfSTFKG-MYFTSDGARRDE 506
Cdd:cd05972 243 D-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTE----ASIRGdYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 507 DGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKE 586
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKV 397
|
490 500 510
....*....|....*....|....*....|.
gi 515671996 587 IGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 398 LAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
3.67e-102 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 317.33 E-value: 3.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIiwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITADEgvrggravPLKKNVDEALTNPEVknIEKVVVFKRTGGDVAWHEHrdvwwHDAI 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEV--VKLVLVLDRDPVLKEEPLP-----EEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 ANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTgGYLVYAAMTFKYV----FDYQEGETFWCTADVGWITGHTYLV 317
Cdd:pfam00501 141 PADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 YGPLANGAKTILFEGVPNyPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdSLRVMGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 398 YYKTIGNeqsPIVDTWWQTETGGILIAPLPGATDL-KPGSATRPFFGVQPALVD-NMGNIIEGATDGNLVIldSWPGQMR 475
Cdd:pfam00501 297 FRELFGG---ALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 515671996 476 TVHGDHDRFEQTYFStfKGMYFTSDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:pfam00501 372 GYLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-625 |
2.38e-90 |
|
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: 287.86 E-value: 2.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITAdegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdai 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 anvsadcppeemnaedplFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 ANGAKTILFEGVpnypNTSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKT 401
Cdd:COG0318 165 LAGATLVLLPRF----DPERVLELIERERVTVLFGVPTMLARLLR--HPEFARYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IGneqSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 482 DRFEQTyfstFK-GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 561 AYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDTGN 625
Cdd:COG0318 390 AFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-611 |
7.41e-87 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 274.93 E-value: 7.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYvFDYQEGETFWCTADVGWItGHTYLVYGPLANGAKTILFEGvpny 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 337 PNTSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLK--APESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 417 ETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTvhgdhDRFEQTYFSTFKGMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYW-----NNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElh 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 515671996 577 kEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
22-639 |
5.82e-86 |
|
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: 281.47 E-value: 5.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 22 DTYLAMYQQSVSDPEGFWGEhgkIVDWIK-PFTQVKNTSFDPGHI--DIRWFEDGTLNVsANCIDRHlAERGDEVAIIWE 98
Cdd:cd05943 17 ADYAALHRWSVDDPGAFWAA---VWDFSGvRGSKPYDVVVVSGRImpGARWFPGARLNY-AENLLRH-ADADDPAAIYAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 99 GDDPADDktLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDS 178
Cdd:cd05943 92 EDGERTE--VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 179 NSKVVITADEGVRGGRAVPLKKNVDEALTnpEVKNIEKVVVFKRTGGDV---AWHEHRDVWWHDAIANvSADCPP--EEM 253
Cdd:cd05943 170 EPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVAAGqpdLSKIAKALTLEDFLAT-GAAGELefEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHtYLVYGpLANGAKTILFEGV 333
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWN-WLVSG-LAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 334 PNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNeqspivDTW 413
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 414 WQTETGGI-LIAPLPGATDLKP---GSATRPFFGVQPALVDNMGNIIEGATdGNLVILDSWPGQMRTVHGDHD--RFEQT 487
Cdd:cd05943 399 LASISGGTdIISCFVGGNPLLPvyrGEIQCRGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPSMPVGFWNDPDgsRYRAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 488 YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLND 567
Cdd:cd05943 478 YFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 568 GEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGDtgNLGDTSTLADPSVVD 639
Cdd:cd05943 558 GVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGR--PVKNAGALANPESLD 627
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
2.26e-83 |
|
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: 269.00 E-value: 2.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 egvrggravplkknvdealtnpEVKNIEKVvvfkrtggdvawhehrdvwwhdaianvsadcppeemnAEDPLFILYTSGS 267
Cdd:cd05973 79 ----------------------DAANRHKL-------------------------------------DSDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGGYLVYAAMtFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPNTSRmseVVD 347
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWR---VIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 348 KHQVNILYTAPTAIRALMAKGNEaVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPLP 427
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 428 GATDLKPGSATRPFFGVQPALVDNMGNiiegatdgnlvilDSWPGQMRTVHGDHDRFEQTYF--------STFKGMYF-T 498
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGD-------------ELGPGEPGRLAIDIANSPLMWFrgyqlpdtPAIDGGYYlT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 499 SDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKE 578
Cdd:cd05973 319 GDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE 398
|
490 500 510
....*....|....*....|....*....|....*....
gi 515671996 579 VKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 399 LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
11-649 |
1.04e-81 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 270.90 E-value: 1.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 11 ENIKSTTHADNDTYLAMYQQSVSDPEGFWGEhgkIVDWI-----KPFTQVKNtsfDPGHIDIRWFEDGTLNVSANcIDRH 85
Cdd:PRK03584 23 RWLAARRGLSFDDYAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLA---GRRMPGARWFPGARLNYAEN-LLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 86 laERGDEVAIIWEGDDpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGG 165
Cdd:PRK03584 96 --RRDDRPAIIFRGED-GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 166 FSPEALSGRIIDSNSKVVITADeGVR-GGRAVPLKKNVDEALtnPEVKNIEKVVVFKRTG-GDVAWHEHRDVWWHDAIAN 243
Cdd:PRK03584 173 FGVQGVLDRFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELR--AALPSLEHVVVVPYLGpAAAAAALPGALLWEDFLAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 244 VSADCP-PEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGET-FWCTAdVGWITGHtYLVYGpL 321
Cdd:PRK03584 250 AEAAELeFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRfFWYTT-CGWMMWN-WLVSG-L 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 ANGAKTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKT 401
Cdd:PRK03584 327 LVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEH 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IGNeqspivDTWWQTETGG-------ILIAP-LPgatdLKPGSATRPFFGVQPALVDNMGNIIEGATdGNLVILDSWPGQ 473
Cdd:PRK03584 407 VKA------DVWLASISGGtdicscfVGGNPlLP----VYRGEIQCRGLGMAVEAWDEDGRPVVGEV-GELVCTKPFPSM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 474 MRTVHGDHD--RFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIP 551
Cdd:PRK03584 476 PLGFWNDPDgsRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 552 HDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIM----RRILRKIATGDTGNLG 627
Cdd:PRK03584 556 WPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAVNRD 635
|
650 660
....*....|....*....|..
gi 515671996 628 dtsTLADPSVVDkLIAEKAELA 649
Cdd:PRK03584 636 ---ALANPEALD-WFADLAELR 653
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
74-616 |
4.16e-74 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 247.79 E-value: 4.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 74 TLNVSANCIDRHLAERGDEVAIIWeGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACT 153
Cdd:cd05970 15 NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 154 RIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVrggravpLKKNVDEALtnPEVKNIEKVVvfkRTGGDVawhehR 233
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAA--PECPSKPKLV---WVGDPV-----P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 234 DVW--WHDAIANVSADCPPEEMNA----EDPLFILYTSGSTGKPKGVMHTTG---GYLVyaamTFKYVFDYQEGETFWCT 304
Cdd:cd05970 157 EGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQNVREGGLHLTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 305 ADVGWITGHTYLVYGPLANGAKTILFEGVPNYPntSRMSEVVDKHQVNILYTAPTAIRALMakgNEAVEGTSRDSLRVMG 384
Cdd:cd05970 233 ADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDP--KALLEKLSKYGVTTFCAPPTIYRFLI---REDLSRYDLSSLRYCT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPEAWEWYYKTIGNEqspIVDTWWQTETGgILIAPLPGaTDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNL 464
Cdd:cd05970 308 TAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 465 VI--LDSWP-GQMRTVHGDHDRFEQTYFStfkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDK 541
Cdd:cd05970 383 VIrtSKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 542 IAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05970 460 VLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
79-616 |
7.73e-72 |
|
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: 240.73 E-value: 7.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAE-RGDEVAIIwegdDPADdkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGA 157
Cdd:cd05959 6 ATLVDLNLNEgRGDKTAFI----DDAG--SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 158 VHTVVFGGFSPEALSGRIIDSNSKVVITADEgvrggravpLKKNVDEALTNPEvkniEKVVVFKRTGGdvAWHEHRDVWW 237
Cdd:cd05959 80 VPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTKSE----HTLVVLIVSGG--AGPEAGALLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 238 HDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTF-KYVFDYQEGETFWCTADVGWITGHTYL 316
Cdd:cd05959 145 AELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 VYGPLANGAKTILFegvPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 WYYKTIGNEqspIVDTWWQTETGGILIAPLPGAtdLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVildswpgqmrt 476
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELY----------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 477 VHGDH------DRFEQTYfSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVG 549
Cdd:cd05959 363 VRGPSsatmywNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515671996 550 IPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 442 VEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
106-616 |
7.94e-67 |
|
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: 225.39 E-value: 7.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 adegvrggravplkknvDEAltnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnaEDPLFILYTS 265
Cdd:cd05971 85 -----------------DGS--------------------------------------------------DDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 266 GSTGKPKGVMHTTG---GYLVYAAMTFKyvFDYQEGETFWCTADVGWItghtylvyGPLANGAKTILFEGVPNYPNTS-- 340
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFN--LFPRDGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPVLAHRMtk 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 341 ----RMSEVVDKHQVNILYTAPTAIRaLMAKGNEAVEGTSRdSLRVMGSVGEPINPEAWEWYYKTIGNEqspIVDTWWQT 416
Cdd:cd05971 168 fdpkAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQV-KLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 417 EtGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTVHGDhdrfEQTYFSTFKGMY 496
Cdd:cd05971 243 E-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNN----PSATEKKMAGDW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 F-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAEL 575
Cdd:cd05971 318 LlTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 515671996 576 HKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 398 AREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
103-616 |
8.72e-66 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 222.72 E-value: 8.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 103 ADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKV 182
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 183 VITADegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhDAIAnvsadcppeemnaedplFIL 262
Cdd:cd05919 86 VVTSA---------------------------------------------------DDIA-----------------YLL 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 263 YTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADV--GWITGHTylVYGPLANGAKTILFegvPNYPNTS 340
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 341 RMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGG 420
Cdd:cd05919 173 RVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALR--SLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 421 ILIAPLPGAtdLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRtvhGDHDRFEQTYFSTFKGMYFTSD 500
Cdd:cd05919 248 IFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLV--RGPSAAV---GYWNNPEKSRATFNGGWYRTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 501 GARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVK 580
Cdd:cd05919 321 KFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIH 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 515671996 581 NWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
24-617 |
2.21e-61 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 216.15 E-value: 2.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 24 YLAMYQQSVSDPEGFWGEHG-KIVDWIKPFTQVknTSFDPGHIDirWFEDGTLNVSANCIDRHL--AERGDEVAIIWEGd 100
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAkKYVHWDKMYDKV--YSGDEIYPD--WFKGGELNTCYNVLDIHVknPLKRDQDALIYEC- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 101 dPADDKT--LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDS 178
Cdd:PTZ00237 85 -PYLKKTikLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 179 NSKVVITADEGVRGGRAVPLKKNVDEA-------------------LTNPEVKNIEKVVVFKRTggdvawhehrdVWWHD 239
Cdd:PTZ00237 164 TPKLIITTNYGILNDEIITFTPNLKEAielstfkpsnvitlfrndiTSESDLKKIETIPTIPNT-----------LSWYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 240 AIANVSA-------DCPPEEMNaeDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITG 312
Cdd:PTZ00237 233 EIKKIKEnnqspfyEYVPVESS--HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 313 HTYLvYGPLANGAKTILFEG--VPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSR---DSLRVMGSVG 387
Cdd:PTZ00237 311 HGFL-YGSLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 388 EPINPEAWEWYYKTIGNEQSPIvdtWWQTETGGILIAPLPGATdlKPGSAT-RPFFGVQPALVDNMGNIIEGATDGNLVI 466
Cdd:PTZ00237 390 EVIEESIPEYIENKLKIKSSRG---YGQTEIGITYLYCYGHIN--IPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 467 -LDSWPGQMRTVHGDHDRFEQTyFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEA 545
Cdd:PTZ00237 465 kLPMPPSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLEC 543
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515671996 546 AIVGIPH-DIKGQAIYAYITLNDGEFPTAELHK---EVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 544 CSIGIYDpDCYNVPIGLLVLKQDQSNQSIDLNKlknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
96-617 |
1.90e-59 |
|
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: 208.09 E-value: 1.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 96 IWEGDDPADDKTLTFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGR 174
Cdd:cd05928 30 LWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 175 IIDSNSKVVITADEgvrggravpLKKNVDE-ALTNPEVKNieKVVVFkrtggdvawHEHRDVW--WHDAIANVSADCPPE 251
Cdd:cd05928 110 LQASKAKCIVTSDE---------LAPEVDSvASECPSLKT--KLLVS---------EKSRDGWlnFKELLNEASTEHHCV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 252 EMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAkTILFE 331
Cdd:cd05928 170 ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGA-CVFVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 332 GVPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMakgNEAVEGTSRDSLRVMGSVGEPINPEAWE-WYYKTiGNEqspIV 410
Cdd:cd05928 249 HLPRF-DPLVILKTLSSYPITTFCGAPTVYRMLV---QQDLSSYKFPSLQHCVTGGEPLNPEVLEkWKAQT-GLD---IY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 411 DTWWQTETGgiLIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVI--LDSWPGQMRTVHGDHDrfEQTY 488
Cdd:cd05928 321 EGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvKPIRPFGLFSGYVDNP--EKTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 489 fSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLN- 566
Cdd:cd05928 397 -ATIRGdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAp 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 515671996 567 -----DGEFPTAELHKEVKNwvrkEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 476 qflshDPEQLTKELQQHVKS----VTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-616 |
3.88e-59 |
|
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: 205.49 E-value: 3.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGA--VHT 160
Cdd:cd05936 6 EEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAvvVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 161 VVFggFSPEALSGRIIDSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrDVWWHDA 240
Cdd:cd05936 80 NPL--YTPRELEHILNDSGAKALIV------------------------------------------------AVSFTDL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 241 IANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEG-ETFWCTADVGWITGHTYLVYG 319
Cdd:cd05936 110 LAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGdDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 320 PLANGAKTILfegVPNyPNTSRMSEVVDKHQVNILYTAPTAIRALMakGNEAVEGTSRDSLRVMGSVGEPINPEAWE-WY 398
Cdd:cd05936 190 PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALL--NAPEFKKRDFSSLRLCISGGAPLPVEVAErFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 399 YKTigneQSPIVDTWWQTETGGILIA-PLPGATdlKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRtv 477
Cdd:cd05936 264 ELT----GVPIVEGYGLTETSPVVAVnPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV--RGPQVMK-- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 478 hGDHDRFEQTYfSTFK-GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKG 556
Cdd:cd05936 334 -GYWNRPEETA-EAFVdGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSG 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 557 QAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 412 EAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-611 |
2.69e-56 |
|
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: 198.59 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 101 DPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 181 KVVITADEGVrggravplkKNVDEALTnpEVKNIEKVVVFkrtGGDVAWHEHRDVWWHD-AIANVSADCPPEEMNAEDPL 259
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAK--ELGPKDKIIVL---DDKPDGVLSIEDLLSPtLGEEDEDLPPPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 260 FILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFD-YQEGETFWCTADVGWITGHTYLVYGPLaNGAKTILFegvpNYPN 338
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM----PKFD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 339 TSRMSEVVDKHQVNILYTAPtAIRALMAKgNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQspIVDTWWQTET 418
Cdd:cd05911 225 SELFLDLIEKYKITFLYLVP-PIAAALAK-SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAT--IKQGYGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 419 GGILIAPLPGatDLKPGSATRPFFGVQPALVDnmgniiegaTDGNLVILDSWPGQMRtVHGDH------DRFEQTYFSTF 492
Cdd:cd05911 301 GGILTVNPDG--DDKPGSVGRLLPNVEAKIVD---------DDGKDSLGPNEPGEIC-VRGPQvmkgyyNNPEATKETFD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 493 KGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFP 571
Cdd:cd05911 369 EDGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 515671996 572 TAelhKEVKNWVRKEIgpiatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 449 TE---KEVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
79-616 |
2.84e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 196.56 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK06187 9 GRILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 -HTV-VFggFSPEALSGRIIDSNSKVVITADEGVrggravPLKKNVdealtNPEVKNIEKVVVFK---RTGGDVAWHEhr 233
Cdd:PRK06187 83 lHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAI-----LPQLPTVRTVIVEGdgpAAPLAPEVGE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 234 dvwWHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTtggY--LVYAAMTFKYVFDyqegetfWCTADVGWIT 311
Cdd:PRK06187 148 ---YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS---HrnLFLHSLAVCAWLK-------LSRDDVYLVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 312 ---GHTY---LVYGPLANGAKTILfegVPNYPnTSRMSEVVDKHQVNILYTAPTAIRALMAkgneAVEGTSRD--SLRVM 383
Cdd:PRK06187 215 vpmFHVHawgLPYLALMAGAKQVI---PRRFD-PENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDfsSLRLV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 384 GSVGEPINP---EAWEWYYKTigneqsPIVDTWWQTETGGILIAPLPGATDL----KPGSATRPFFGVQPALVDNMGNII 456
Cdd:PRK06187 287 IYGGAALPPallREFKEKFGI------DLVQGYGMTETSPVVSVLPPEDQLPgqwtKRRSAGRPLPGVEARIVDDDGDEL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 457 E--GATDGNLVILDSWpgQMRTVHGDHDRFEQTYFstfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK06187 361 PpdGGEVGEIIVRGPW--LMQGYWNRPEATAETID---GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 535 ALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAelhKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK06187 436 ALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRV 512
|
..
gi 515671996 615 LR 616
Cdd:PRK06187 513 LR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
1.13e-54 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 192.83 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVItadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdai 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 anvsadcppeemnaEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 ANGAKTILFEGvpnyPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdSLRVMGSVGEPINP---EAWEWY 398
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIYGGAPMPErllRALQAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 399 YKtigneqsPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRtvh 478
Cdd:cd17631 237 GV-------KFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA--- 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 GDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQA 558
Cdd:cd17631 305 GYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEA 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 515671996 559 IYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 385 VVAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
105-616 |
1.51e-53 |
|
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: 189.61 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALK-EQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALsGRIIDsnskvv 183
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL-AYILD------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 itadegvRGGRAVPLkknVDEALTNpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnAEDPLFILY 263
Cdd:cd05958 81 -------KARITVAL---CAHALTA----------------------------------------------SDDICILAF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEG-VPnypntSRM 342
Cdd:cd05958 105 TSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEaTP-----DLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 SEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGIL 422
Cdd:cd05958 180 LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLS--SLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIF 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 423 IAPLPGatDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldswpgQMRTV-HGDHDRFEQTYFStfKGMYFTSDG 501
Cdd:cd05958 255 ISARPG--DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV------RGPTGcRYLADKRQRTYVQ--GGWNITGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 502 ARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKN 581
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQD 404
|
490 500 510
....*....|....*....|....*....|....*
gi 515671996 582 WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 405 HAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-617 |
1.94e-52 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 192.60 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 28 YQQSVSDPEGFWG---EHGKIVDWIKPFTQVKNTSF-DPGHidiRWFEDGTLNVSANCIDRHLAERGDEVAIIW--EGDD 101
Cdd:PLN03052 126 QRFSVENPEVYWSivlDELSLVFSVPPRCILDTSDEsNPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 102 PADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSK 181
Cdd:PLN03052 203 DLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 182 VVITADEGVRGGRAVPLKKNVDEAltnpevkNIEKVVVFKRTGGDVAWH-EHRDVWWHDAIANVSADCPPEE-----MNA 255
Cdd:PLN03052 283 AIFTQDVIVRGGKSIPLYSRVVEA-------KAPKAIVLPADGKSVRVKlREGDMSWDDFLARANGLRRPDEykaveQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVfDYQEGETF-WCTaDVGWITGHtYLVYGPLANGAKTILFEGVp 334
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGS- 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 335 nyPNTSRMSEVVDKHQVNILYTAPTAIRALmaKGNEAVEGTSRDSLRVMGSVGEPINPEAWEW-----YYKtigneqsPI 409
Cdd:PLN03052 432 --PLGRGFAKFVQDAKVTMLGTVPSIVKTW--KNTNCMAGLDWSSIRCFGSTGEASSVDDYLWlmsraGYK-------PI 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 410 VDTWWQTETGGILIAplpgATDLKP---GSATRPFFGVQPALVDNMGNII--EGATDGNLVILDSWPGQMRT-VHGDHDr 483
Cdd:PLN03052 501 IEYCGGTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFILDDSGNPYpdDAPCTGELALFPLMFGASSTlLNADHY- 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 484 feQTYFS---TFKGMYFTSDGA--RRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL-VAFDKIAEAAIVGIPHDIKGQ 557
Cdd:PLN03052 576 --KVYFKgmpVFNGKILRRHGDifERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGP 653
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 558 ---AIYAYITLNDGEFP-TAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 654 eqlVIAAVLKDPPGSNPdLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
102-617 |
4.45e-52 |
|
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: 187.13 E-value: 4.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 102 PADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSK 181
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 182 VVITADEGvrGGRAVPLKKNVDEALTNPEVKNIEKVVVFKrtGGDVAWHEhrdvwwhDAIANVSADCPPEEmnaEDPLFI 261
Cdd:cd05926 89 LVLTPKGE--LGPASRAASKLGLAILELALDVGVLIRAPS--AESLSNLL-------ADKKNAKSEGVPLP---DDLALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 262 LYTSGSTGKPKGVMHTTGGYLV---YAAMTFKYVFDyqegetfwctaDVGWITGHTYLVYG-------PLANGAKTILfe 331
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPD-----------DRTLVVMPLFHVHGlvasllsTLAAGGSVVL-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 332 gvpnyPNTSRMSEV---VDKHQVNiLYTA-PTAIRALMAKGNEAVEgTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqS 407
Cdd:cd05926 222 -----PPRFSASTFwpdVRDYNAT-WYTAvPTIHQILLNRPEPNPE-SPPPKLRFIRSCSASLPPAVLEALEATFG---A 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 408 PIVDTWWQTETGGILIA-PLPGATDlKPGSATRPFfGVQPALVDNMGNIIEGATDGNLVILDSwpgqmRTVHGDHDRFEQ 486
Cdd:cd05926 292 PVLEAYGMTEAAHQMTSnPLPPGPR-KPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 487 TYFSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITL 565
Cdd:cd05926 365 NAEAAFKDGWFrTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 515671996 566 NDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 445 REGASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
1.15e-50 |
|
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: 181.61 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIiDSNSKVVITAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EGVRggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnAEDPLFILYTSGS 267
Cdd:cd05974 80 ENTH---------------------------------------------------------------ADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGGYLVYAAMTFkYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFegvpNYP--NTSRMSEV 345
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 346 VDKHQVNILYTAPTAIRALMakgnEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGgILIAP 425
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLI----QQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETT-ALVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 426 LPGATdLKPGSATRPFFGVQPALVDNMGNiieGATDGN--LVILDSWP-GQMRTVHGDHDRfeqTYFSTFKGMYFTSDGA 502
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGA---PATEGEvaLDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 503 RRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNW 582
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 515671996 583 VRKEIGPIATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
2.24e-49 |
|
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: 180.03 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 73 GTLNVSANCIDRHLAE-RGDEVAIIwegdDPAddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI----DDI--SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 152 CTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEgvrggravpLKKNVDEALTnpEVKNIEKVVVfkrTGGDVAWHe 231
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA---------LLPVIKAALG--KSPHLEHRVV---VGRPEAGE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 232 hrdvwwhDAIANVSADCPPEEMNA----EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADV 307
Cdd:TIGR02262 140 -------VQLAELLATESEQFKPAatqaDDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 308 GWITGHTYLVYGPLANGAKTILFegvPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGtsRDSLRVMGSVG 387
Cdd:TIGR02262 213 FFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSED--QVRLRLCTSAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 388 EPINPEAWEWYYKTIGNEqspIVDTWWQTETGGILIAPLPGatDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIL 467
Cdd:TIGR02262 288 EALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPG--DVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 468 DSWPGQMRTVHGDHDRfeqtyfSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:TIGR02262 363 GPSSATMYWNNRAKSR------DTFQGEWTrSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAA 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 547 IVGIP---HDIKGQaiyAYITLNDGEfptAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 437 VVGVAdedGLIKPK---AFVVLRPGQ---TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-616 |
1.12e-48 |
|
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: 175.94 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtvvfggfspealsgriidsnskvvitade 188
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 189 gvrggrAVPLkknvdealtNPevkniekvvvfKRTGGDVAWhehrdvwwhdAIANvsADCppeEMNAEDPLFILYTSGST 268
Cdd:cd05934 55 ------LVPI---------NT-----------ALRGDELAY----------IIDH--SGA---QLVVVDPASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 269 GKPKGVMhTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILfegVPNYpNTSRMSEVVDK 348
Cdd:cd05934 94 GPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRFWSDVRR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 349 HQVNILYTAPTAIRALMAKgnEAVEGTSRDSLRVMGsvGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPLPG 428
Cdd:cd05934 169 YGATVTNYLGAMLSYLLAQ--PPSPDDRAHRLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 429 ATdlKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIlDSWPGQMRTvHGDHDRFEQTYFSTFKGMYFTSDGARRDEDG 508
Cdd:cd05934 242 PR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI-RGLRGWGFF-KGYYNMPEATAEAMRNGWFHTGDLGYRDADG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 509 YYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIG 588
Cdd:cd05934 318 FFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 515671996 589 PIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
99-617 |
5.20e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 170.86 E-value: 5.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 99 GDDPA---DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRI 175
Cdd:PRK07656 19 GDKEAyvfGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 176 IDSNSKVVITADEGVrggravplkkNVDEALTnPEVKNIEKVVVFKRTGGDVAWHEHRDvwWHDAIANVSADCPPEEMNA 255
Cdd:PRK07656 99 ARGDAKALFVLGLFL----------GVDYSAT-TRLPALEHVVICETEEDDPHTEKMKT--FTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHT----------TGGYL-------VYAAMTFKYVFDYQegetfwctadVGWITghtylvy 318
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLThrqllsnaadWAEYLgltegdrYLAANPFFHVFGYK----------AGVNA------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 319 gPLANGAkTILFegVPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAkgneAVEGTSRD--SLRVMGSVGEPINPEAWE 396
Cdd:PRK07656 229 -PLMRGA-TILP--LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQ----HPDRSAEDlsSLRLAVTGAASMPVALLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 WYYKTIGNEqspIVDTWWQ-TETGGIL-IAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQM 474
Cdd:PRK07656 300 RFESELGVD---IVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV--RGPNVM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 475 RTVHGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDI 554
Cdd:PRK07656 375 KGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515671996 555 KGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 453 LGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
1.07e-45 |
|
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: 168.09 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVfggfSPEA 170
Cdd:cd05930 2 DAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRII----DSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsa 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 247 dcppeemNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAmTFKYVFDYQEGETFWCTADVGWItGHTYLVYGPLANGAK 326
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGAT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 327 TILF-EGVPNYPNtsRMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNE 405
Cdd:cd05930 162 LVVLpEEVRKDPE--ALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVRRWRELLPGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 406 QspIVDTWWQTE-TGGILIAPLPGAtDLKPGSAT--RPFFGVQPALVDNMGNII-EGATdGNLVIldSWPGQMRTVHGDH 481
Cdd:cd05930 236 R--LVNLYGPTEaTVDATYYRVPPD-DEEDGRVPigRPIPNTRVYVLDENLRPVpPGVP-GELYI--GGAGLARGYLNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 482 D----RFEQTYFSTFKGMYFTSDGARRDEDG--YYwiTGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIK 555
Cdd:cd05930 310 EltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDG 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 556 GQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 388 EKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-617 |
1.97e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 169.34 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITADEgvrggravpLKKNVDEALTNPEVKNIEKVVVFKRTGGDVAWHEhrdvwWHDAIANVSADCPP 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREAPGGWLD-----FADWAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 EEMNAEDPLFILYTSGSTGKPKGVMHTTGgylvyaAMTFKYVFdyqegetfwCTADVGW----ITGHTYLVY-------- 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVS---------CIVAGDMsaddIPLHALPLYhcaqldvf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 319 -GP-LANGAKTILFEGvpnyPNTSRMSEVVDKHQVNILYTAPTAIRALMakgNEAVEGTsRD--SLRvMGSVGEPINPEa 394
Cdd:PRK08316 231 lGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLL---RHPDFDT-RDlsSLR-KGYYGASIMPV- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 395 wewyykTIGNE---QSPIVDTW---WQTEtggilIAPL-----PGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGN 463
Cdd:PRK08316 301 ------EVLKElreRLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 464 LVildswpgqMRTVH---GDHDRFEQTYfSTFKGMYFTS-DGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:PRK08316 370 IV--------HRSPQlmlGYWDDPEKTA-EAFRGGWFHSgDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTH 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 540 DKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK08316 441 PAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
107-617 |
5.50e-44 |
|
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: 163.32 E-value: 5.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 107 TLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITA 186
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 187 DEgvrggravplkknvdealtnpevkniekvvvfkrtggdvaWHEHRdvwwhdaianvsadcpPEEMNAeDPLFILYTSG 266
Cdd:cd05903 81 ER----------------------------------------FRQFD----------------PAAMPD-AVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 267 STGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVpnypNTSRMSEVV 346
Cdd:cd05903 104 TTGEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 347 DKHQVNILYTAPTAIRALMAKGNEAveGTSRDSLRVMGSVGEPINP----EAWEWYyktigneQSPIVDTWWQTETGGIL 422
Cdd:cd05903 179 REHGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRslarRAAELL-------GAKVCSAYGSTECPGAV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 423 IAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDswPGqmrTVHGDHDRFEQTYFSTFKGMYFTSDGA 502
Cdd:cd05903 250 TSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRG--PS---VFLGYLDRPDLTADAAPEGWFRTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 503 RRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVknW 582
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY--L 402
|
490 500 510
....*....|....*....|....*....|....*
gi 515671996 583 VRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 403 DRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
6.81e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 164.60 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 139 MPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEAltnpevkNIEKVV 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA-------APAKAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 219 VFKRTGGDVAWH-EHRDVWWHDAIANVSA-DCP------PEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFLGVAAAqGSVggneysPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 291 YVfDYQEGETFWCTADVGWITGhTYLVYGPLANGAKTILFEGVPnypnTSR-MSEVVDKHQVNILYTAPTAIRALMAKGN 369
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAP----LGRgFGKFVQDAGVTVLGLVPSIVKAWRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 370 EAVEGTSRDSLRVMGSVGEPINPEAWEW------YYKtigneqsPIVDTWWQTETGG--ILIAPL-PGAtdlkPGSATRP 440
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDVLWlssvrgYYK-------PVIEYCGGTELASgyISSTLLqPQA----PGAFSTA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 441 FFGVQPALVDNMGniiEGATDGNLVI--LDSWPGQM----RTVHGDHDrfeQTYfstFKGM-YFTSDGA--RRDED---- 507
Cdd:PLN03051 297 SLGTRFVLLNDNG---VPYPDDQPCVgeVALAPPMLgasdRLLNADHD---KVY---YKGMpMYGSKGMplRRHGDimkr 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 508 ---GYYWITGRVDDVLNVSGHRMGTAEIESALVAFDK-IAEAAIVGIPhDIKGQAIYAYITLNDGEFPT-------AELH 576
Cdd:PLN03051 368 tpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQ 446
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 515671996 577 KEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 447 KKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
1.01e-42 |
|
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: 161.25 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 87 AERGDEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 167 SPEALSGRIIDSNSKVVITADEGVrggravplkknvdealtnPEVKNIEKVVVfkrTGGDVawHEHRDVWWHDAIANVSA 246
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELA------------------EKLASLALPVV---LLDSA--EFDSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 247 DCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGylvYAAMTFKYVFDYQEG----ETFWCTADVGWITGHTYLVYGPLA 322
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN---LIAMVAQFVAGEGSNsdseDVFLCVLPMFHIYGLSSFALGLLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 323 NGAKTILfegVPNYpNTSRMSEVVDKHQVNILYTAPTAIRAlMAKgNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTI 402
Cdd:cd05904 226 LGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLA-LVK-SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 403 GNeqSPIVDTWWQTETGGILIA-PLPGATDLKPGSATRPFFGVQPALVD-NMGNIIEGATDGNLvildsW---PGQMRTV 477
Cdd:cd05904 300 PN--VDLGQGYGMTESTGVVAMcFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGEL-----WirgPSIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 478 HGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQ 557
Cdd:cd05904 373 LNNPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGE 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 558 AIYAYITLNDGEFPTAelhKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 451 VPMAFVVRKPGSSLTE---DEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-622 |
9.64e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 159.06 E-value: 9.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIWEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK13295 31 DACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVItadegvrggraVP-LKKNVD-EALTN---PEVKNIEKVVV--------FKRTGGDVAW 229
Cdd:PRK13295 111 MPIFRERELSFMLKHAESKVLV-----------VPkTFRGFDhAAMARrlrPELPALRHVVVvggdgadsFEALLITPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 230 HEHRDvwwhdAIANVSADCPpeemNAEDPLFILYTSGSTGKPKGVMHTT----GGYLVYAAMtfkyvFDYQEGETFWCTA 305
Cdd:PRK13295 180 EQEPD-----APAILARLRP----GPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 306 DVGWITGHTYLVYGPLANGAKTILFEgvpnYPNTSRMSEVVDKHQVNilYT-APTAIRALMAkgnEAVEGTSRD--SLRV 382
Cdd:PRK13295 246 PMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT--FTmASTPFLTDLT---RAVKESGRPvsSLRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 383 MGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDG 462
Cdd:PRK13295 317 FLCAGAPIPGALVERARAALG---AKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLvildswpgQMR--TVHGDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFD 540
Cdd:PRK13295 394 RL--------QVRgcSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 541 KIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVR-KEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK13295 466 AIAQVAIVAYPDERLGERACAFVVPRPGQSLDFE---EMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
...
gi 515671996 620 TGD 622
Cdd:PRK13295 543 RGE 545
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
8.57e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 157.81 E-value: 8.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIW--EGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLActriGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 160 TVVF---GGFSPEALSGRIIDSNSKVVITA--DEGVRGGRAVplKKNVDEAltnPEVKNIEKVVVFKRTGGDVAW----- 229
Cdd:PRK07529 107 GIANpinPLLEPEQIAELLRAAGAKVLVTLgpFPGTDIWQKV--AEVLAAL---PELRTVVEVDLARYLPGPKRLavpli 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 230 ---HEHRDVWWHDAIANVSADC--PPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCt 304
Cdd:PRK07529 182 rrkAHARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFC- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 305 advGWITGHTYLVYG----PLANGAkTILFEGVPNYPNTSRMS---EVVDKHQVNILYTAPTAIRALMAKgneAVEGTSR 377
Cdd:PRK07529 260 ---GLPLFHVNALLVtglaPLARGA-HVVLATPQGYRGPGVIAnfwKIVERYRINFLSGVPTVYAALLQV---PVDGHDI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 378 DSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTE-TGGILIAPLPGatDLKPGSATRPFFG--VQPALVDNMGN 454
Cdd:PRK07529 333 SSLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 455 II-EGATD--GNLVIldSWPGQMRT-VHGDHDR---FEQTYFSTfkgmyftSDGARRDEDGYYWITGRVDDVLNVSGHRM 527
Cdd:PRK07529 408 YLrDCAVDevGVLCI--AGPNVFSGyLEAAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 528 GTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDG-EFPTAELhkevKNWVRKEIG-PIATPDVLHWTDSLPKT 605
Cdd:PRK07529 479 DPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGaSATEAEL----LAFARDHIAeRAAVPKHVRILDALPKT 554
|
570
....*....|....*
gi 515671996 606 RSGKIMRRILRKIAT 620
Cdd:PRK07529 555 AVGKIFKPALRRDAI 569
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
105-617 |
9.37e-39 |
|
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: 150.32 E-value: 9.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:TIGR03098 23 DRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADEgvrggRAVPLKknvdeaLTNPEVKNIEKVVVFKRTGGDVAWHEHRDVW-WHDAIANVSADcPPEEMNAEDPLFILY 263
Cdd:TIGR03098 103 TSSE-----RLDLLH------PALPGCHDLRTLIIVGDPAHASEGHPGEEPAsWPKLLALGDAD-PPHPVIDSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVM--HTTggyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGpLANGAKTILFegvpNYPNTSR 341
Cdd:TIGR03098 171 TSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLH----DYLLPRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 342 MSEVVDKHQVnilyTAPTAIRALMAK-GNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQspIVDTWWQTETGG 420
Cdd:TIGR03098 243 VLKALEKHGI----TGLAAVPPLWAQlAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMYGLTEAFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 421 ILIAPlPGATDLKPGSATRPFFGVQPALVDNMGN------IIEGATDGNLVILDSWPGQMRTVhgdhDRFE----QTYFS 490
Cdd:TIGR03098 317 STYLP-PEEVDRRPDSIGKAIPNAEVLVLREDGSecapgeEGELVHRGALVAMGYWNDPEKTA----ERFRplppFPGEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 491 TFKGM-YFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDG- 568
Cdd:TIGR03098 392 HLPELaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGe 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 515671996 569 EFPTAELHKEvknwVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 472 ELDRAALLAE----CRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
1.47e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 147.49 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 ADEGVRGGRAVPLKKNVDEALTN------PEVKN-IEKVVVFKRTGGDVAWHEHRDVWWHDAI-----ANVSADCPPEEm 253
Cdd:PRK06710 128 LDLVFPRVTNVQSATKIEHVIVTriadflPFPKNlLYPFVQKKQSNLVVKVSESETIHLWNSVekevnTGVEVPCDPEN- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 naeDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGE-TFWCTADVGWITGHTYLVYGPLANGAKTILfeg 332
Cdd:PRK06710 207 ---DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEeVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 333 VPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMakGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIG--------- 403
Cdd:PRK06710 281 IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGgklvegygl 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 404 NEQSPIVDT--WWQTETGGILIAPLPGA----TDLKPGSATRPffgvqpalvdnmGNIIEGATDGNLVILDSWpgqmrtv 477
Cdd:PRK06710 358 TESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKGPQIMKGYW------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 478 hgdhDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQ 557
Cdd:PRK06710 419 ----NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGE 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 558 AIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 495 TVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
2.73e-37 |
|
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: 145.50 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVIT-ADEGVRGGRAVPLKKNVDEALTNPevkniekvvvfkrtggdvawhehrdvwwhda 240
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTtADLAARLPAGGDVALLGDEALAAP------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 241 ianvSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGG-----------YLVYA--AMTFK--YVFDYQEGETFWcta 305
Cdd:cd17646 127 ----PATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGivnrllwmqdeYPLGPgdRVLQKtpLSFDVSVWELFW--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 306 dvgwitghtylvygPLANGAKTILFE----GVPNYpntsrMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRDSLR 381
Cdd:cd17646 200 --------------PLVAGARLVVARpgghRDPAY-----LAALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 382 VMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETG-GILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGAT 460
Cdd:cd17646 257 RVFCSGEALPPELAARFLALPG---AELHNLYGPTEAAiDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 461 DGNLVIldswpGQMRTVHGDHDRFEQTY-------FSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIE 533
Cdd:cd17646 334 PGELYL-----GGVQLARGYLGRPALTAerfvpdpFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 534 SALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFP--TAELHKevknWVRKEIGPIATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17646 409 AALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpdTAALRA----HLAERLPEYMVPAAFVVLDALPLTANGKLD 484
|
....
gi 515671996 612 RRIL 615
Cdd:cd17646 485 RAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-616 |
5.13e-37 |
|
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: 144.79 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:cd17651 1 FERQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITADEgVRGGRAVPLkknvdealtnpevkniekvvvfkrtggdvawhehRDVWWHDAI 241
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLTHPA-LAGELAVEL----------------------------------VAVTLLDQP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 ANVSADC--PPEEMNAEDPLFILYTSGSTGKPKGVM--HTTGGYLVYA----------AMTFKYV---FDYQEGETFwct 304
Cdd:cd17651 120 GAAAGADaePDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWqarasslgpgARTLQFAglgFDVSVQEIF--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 305 advgwitghTYLVYGplangaKTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAveGTSRDSLRVMG 384
Cdd:cd17651 197 ---------STLCAG------ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEP--INPEAWEWY----YKTIGNEQSPivdtwwqTETGGILIAPLPGATDLKPGSAT--RPFFGVQPALVDNMGNII 456
Cdd:cd17651 260 TGGEQlvLTEDLREFCaglpGLRLHNHYGP-------TETHVVTALSLPGDPAAWPAPPPigRPIDNTRVYVLDAALRPV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 457 EGATDGNLVIldSWPGQMRTVHGD----HDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:cd17651 333 PPGVPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEI 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 533 ESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17651 411 EAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
....
gi 515671996 613 RILR 616
Cdd:cd17651 488 RALP 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
2.69e-35 |
|
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: 138.92 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 86 LAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 166 FSPEALSgRIIDSNSKVVITADEGvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvs 245
Cdd:cd05945 75 SPAERIR-EILDAAKPALLIADGD-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 adcppeemnaeDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYvFDYQEGETFWCTA----DVGwitghTYLVYGPL 321
Cdd:cd05945 98 -----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQApfsfDLS-----VMDLYPAL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 ANGAKTILfegVPN--YPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTsrDSLRVMGSVGEPI-NPEAWEWY 398
Cdd:cd05945 161 ASGATLVP---VPRdaTADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESL--PSLRHFLFCGEVLpHKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 399 YKTignEQSPIVDTWWQTET----GGILIAPLPgATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQM 474
Cdd:cd05945 236 QRF---PDARIYNTYGPTEAtvavTYIEVTPEV-LDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVI--SGPSVS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 475 RTVHGDHDRFEQTYFSTFK-GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHD 553
Cdd:cd05945 310 KGYLNNPEKTAAAFFPDEGqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKG 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 554 IKGQAIYAYITLNDGEfpTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 390 EKVTELIAFVVPKPGA--EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-615 |
4.78e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 139.71 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 87 AER-GDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFG 164
Cdd:PRK08314 20 ARRyPDKTAIVFYG------RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 165 GFSPEALSGRIIDSNSKVVITADEGVrgGRAVPLKKNVdealtnpevkNIEKVVV------FKRTGGDV--AW------- 229
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELA--PKVAPAVGNL----------RLRHVIVaqysdyLPAEPEIAvpAWlraeppl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 230 ---HEHRDVWWHDAIAnvSADCPPEEMNAEDPLFIL-YTSGSTGKPKGVMHTTGGYLVYAAmtfkyvfdyqeGETFWCTA 305
Cdd:PRK08314 162 qalAPGGVVAWKEALA--AGLAPPPHTAGPDDLAVLpYTSGTTGVPKGCMHTHRTVMANAV-----------GSVLWSNS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 306 DVG----------WITGHTYLVYGPLANGAKTILFegvpnyPNTSR--MSEVVDKHQVNILYTAPTAIRALMAKGNEAve 373
Cdd:PRK08314 229 TPEsvvlavlplfHVTGMVHSMNAPIYAGATVVLM------PRWDReaAARLIERYRVTHWTNIPTMVVDFLASPGLA-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 374 gtSRD--SLRVMGSVGEPInPEAwewyyktIGN---EQS--PIVDTWWQTETggilIAPlpgaTDLKPGSATR------P 440
Cdd:PRK08314 301 --ERDlsSLRYIGGGGAAM-PEA-------VAErlkELTglDYVEGYGLTET----MAQ----THSNPPDRPKlqclgiP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 441 FFGVQPALVD----------NMGNIIegaTDGNLVILDSWpgqmrtvhgdhDRFEQT--YFSTFKGMYF--TSDGARRDE 506
Cdd:PRK08314 363 TFGVDARVIDpetleelppgEVGEIV---VHGPQVFKGYW-----------NRPEATaeAFIEIDGKRFfrTGDLGRMDE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 507 DGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElHKEVKNWVRKE 586
Cdd:PRK08314 429 EGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREH 507
|
570 580
....*....|....*....|....*....
gi 515671996 587 IGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08314 508 MAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-615 |
9.19e-35 |
|
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: 138.10 E-value: 9.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVITaDEGVRGGRAVPLkknvdealtnpevkniekvvvfkrtggdvawhehRDVWWHDAIA 242
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLT-DRSLAGRAGGLE----------------------------------VAVVIDEALD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 243 NVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVfDYQEGETFWCTADVGWiTGHTYLVYGPLA 322
Cdd:cd12117 123 AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 323 NGAKTILFE-GVPNYPNtsRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGtsrdsLRVMGSVGEPINPEAWEWYYK- 400
Cdd:cd12117 200 NGARLVLAPkGTLLDPD--ALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPPHVRRVLAa 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 401 ----TIGNEQSPivdtwwqTETGGI----LIAPLPGATDLKP-GsatRPFFGVQPALVDNMGNIIEGATDGNLVIldswp 471
Cdd:cd12117 273 cpglRLVNGYGP-------TENTTFttshVVTELDEVAGSIPiG---RPIANTRVYVLDEDGRPVPPGVPGELYV----- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTVHGDHDRFEQT--YFST--FKG---MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAE 544
Cdd:cd12117 338 GGDGLALGYLNRPALTaeRFVAdpFGPgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVRE 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 545 AAIVGIPHDIKGQAIYAYITLnDGEFPTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 418 AVVVVREDAGGDKRLVAYVVA-EGALDAAEL----RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-616 |
1.68e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 137.81 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 73 GTLNVSAncidrhLAERGDEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLAC 152
Cdd:PRK06188 15 GHLLVSA------LKRYPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 153 TRIGAVHTVVFGGFSPEALSGRIIDSNSKVVItADEGVRGGRAVPLKKNVdealtnPEVKNIEkvvvfkrTGGDVAwhEH 232
Cdd:PRK06188 83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARV------PSLKHVL-------TLGPVP--DG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 233 RDVWwhDAIAN------VSADCPPeemnaeDPLFILYTSGSTGKPKGVMHTTGGYLVYAAmtfkyvfdyqegetfWCTAD 306
Cdd:PRK06188 147 VDLL--AAAAKfgpaplVAAALPP------DIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 307 VGWITGHTYLVYGPL--ANGAKTI--LFEG-----VPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAKGneAVEGTSR 377
Cdd:PRK06188 204 WEWPADPRFLMCTPLshAGGAFFLptLLRGgtvivLAKF-DPAEVLRAIEEQRITATFLVPTMIYALLDHP--DLRTRDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 378 DSLRVMGSVGEPINP----EAWEwyykTIGneqsPI-VDTWWQTETgGILIAPLPGA--TDLKP---GSATRPFFGVQPA 447
Cdd:PRK06188 281 SSLETVYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEA-PMVITYLRKRdhDPDDPkrlTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 448 LVDNMGNIIEGATDGNLVIldSWPGQMRtvhGDHDRFEQTYfSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK06188 352 LLDEDGREVAQGEVGEICV--RGPLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGFN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 527 MGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTR 606
Cdd:PRK06188 426 VFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLTA 502
|
570
....*....|
gi 515671996 607 SGKIMRRILR 616
Cdd:PRK06188 503 LGKPDKKALR 512
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-546 |
2.27e-34 |
|
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: 135.47 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHtVVFGGFSPEALSGRII-DSNSKVVITA 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAY-VPLDPAYPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 187 DEGvrggravplkkNVDEALTNPEVKNIEkvvvfkrtggdvawhehrDVWWHDAIANVSADCPPEEMNAEDPLFILYTSG 266
Cdd:TIGR01733 80 SAL-----------ASRLAGLVLPVILLD------------------PLELAALDDAPAPPPPDAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 267 STGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTA----DVGwitghTYLVYGPLANGAKTILFEGVPNYPNTSRM 342
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFAslsfDAS-----VEEIFGALLAGATLVVPPEDEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 SEVVDKHQVNILYTAPTAIRALMAkgneaVEGTSRDSLRVMGSVGEPINPEA---WEWYYktignEQSPIVDTWWQTETG 419
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALTPALvdrWRARG-----PGARLINLYGPTETT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 420 ---GILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNII-EGATdGNLVIldSWPGQMRTVHGDHD----RFEQTYFST 491
Cdd:TIGR01733 275 vwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVpVGVV-GELYI--GGPGVARGYLNRPEltaeRFVPDPFAG 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515671996 492 FKG--MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:TIGR01733 352 GDGarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
5.64e-34 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 135.13 E-value: 5.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17643 2 EAVAVVD------EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcpp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 eemNAEDPLFILYTSGSTGKPKGVMHTTGGYL-VYAAMTFKYVFDYQegetfwctaDVgWITGHTYL-------VYGPLA 322
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFNED---------DV-WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 323 NGAKTILfegVPNYpnTSRMSE----VVDKHQVNILYTAPTAIRALMAKgnEAVEGTSRDSLR--VMGsvGEPINPEAWE 396
Cdd:cd17643 158 HGGRLVV---VPYE--VARSPEdfarLLRDEGVTVLNQTPSAFYQLVEA--ADRDGRDPLALRyvIFG--GEALEAAMLR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 WYYKTIGNEQSPIVDTWWQTETG-GILIAPLpGATDLKPGSAT---RPFFGVQPALVDNMGNIIEGATDGNLVIldSWPG 472
Cdd:cd17643 229 PWAGRFGLDRPQLVNMYGITETTvHVTFRPL-DAADLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 473 QMRTVHG----DHDRF-EQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAi 547
Cdd:cd17643 306 VARGYLGrpelTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAA- 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 548 VGIPHDIKG-QAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 385 VIVREDEPGdTRLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
1.11e-33 |
|
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: 133.76 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITAD 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EgvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnAEDPLFILYTSGS 267
Cdd:cd05935 82 E------------------------------------------------------------------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVpnypNTSRMSEVVD 347
Cdd:cd05935 96 TGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARW----DRETALELIE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 348 KHQVNILYTAPTAIRALMAkgneAVEGTSRD--SLRVMGSVGEPINPEAWEWYYKTIGNEqspIVDTWWQTETggilIAP 425
Cdd:cd05935 171 KYKVTFWTNIPTMLVDLLA----TPEFKTRDlsSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTET----MSQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 426 LPGATDLKPGSATR--PFFGVQPALVD-NMGNIIEGATDGNLVIldSWPGQMRtvhGDHDRFEQTY--FSTFKGMYF--T 498
Cdd:cd05935 240 THTNPPLRPKLQCLgiP*FGVDARVIDiETGRELPPNEVGEIVV--RGPQIFK---GYWNRPEETEesFIEIKGRRFfrT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 499 SDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDgEFPTAELHKE 578
Cdd:cd05935 315 GDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGKVTEED 393
|
490 500 510
....*....|....*....|....*....|....*..
gi 515671996 579 VKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 394 IIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
257-617 |
3.88e-33 |
|
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: 132.41 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGgylVYAAMTFKYVFDYQegetfWCTADV-----------GWITGhtylVYGPLANGA 325
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHA---NLAANVRALVDAWR-----WTEDDVllhvlplhhvhGLVNA----LLCPLFAGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 326 KTI--------------------LFEGVPN-YpntSRMSEVVDKHqvnilYTAPTAIRALMAKGneavegtsrdsLRVM- 383
Cdd:cd05941 158 SVEflpkfdpkevaisrlmpsitVFMGVPTiY---TRLLQYYEAH-----FTDPQFARAAAAER-----------LRLMv 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 384 -GSVGEPInPEAWEWYYKTiGNeqsPIVDTWWQTETGGILIAPLPGatDLKPGSATRPFFGVQPALVD-NMGNIIEGATD 461
Cdd:cd05941 219 sGSAALPV-PTLEEWEAIT-GH---TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDeETGEPLPRGEV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 462 GNL------VILDSWPGQMRTVhgdhDRFeqtyfsTFKGMYFTSDGARRDEDGYYWITGRV-DDVLNVSGHRMGTAEIES 534
Cdd:cd05941 292 GEIqvrgpsVFKEYWNKPEATK----EEF------TDDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIER 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 535 ALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:cd05941 362 VLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE--ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKE 439
|
...
gi 515671996 615 LRK 617
Cdd:cd05941 440 LRK 442
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
4.46e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 133.75 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGN------TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 HTVVFGGFSPEALSGRIIDSNSKVVITadEGVrggrAVPLKKNVDEAltNPEVKNIekVVVFKRTGGDVAWHEhrdvwwh 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAA----LAPVATAVRDI--VPLLSTV--VVAGGSSDDSVLGYE------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 239 DAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVM--HTTggyLVYAAMTFKYVFDYQEGEtfwctaDVGWITGHTYL 316
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVltHAN---LTGQAMTCLRTNGADINS------DVGFVGVPLFH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 VYG------PLANGAKTILfegvpnYP----NTSRMSEVVDKHQVNILYTAPTAIRALMAkgneAVEGTSRD-SLRVMGS 385
Cdd:PRK07786 228 IAGigsmlpGLLLGAPTVI------YPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCA----EQQARPRDlALRVLSW 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 386 VGEPINPEAWEWYYKTIGNEQspIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVD-NMGNIIEGaTDGNL 464
Cdd:PRK07786 298 GAAPASDTLLRQMAATFPEAQ--ILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDeNMNDVPVG-EVGEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 465 VIldSWPGQMRtvhGDHDRFEQTYfSTFKGMYFTS-DGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIA 543
Cdd:PRK07786 375 VY--RAPTLMS---GYWNNPEATA-EAFAGGWFHSgDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 544 EAAIVGIPHDIKGQAIYAYITLNDGefpTAELH-KEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK-IATG 621
Cdd:PRK07786 449 EVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErYGAC 525
|
570
....*....|
gi 515671996 622 DTGNLGDTST 631
Cdd:PRK07786 526 VNVERRSASA 535
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-615 |
5.96e-33 |
|
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: 133.02 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITAD-----EGVRGGRAVPLKKNVDEALTNPEVKNiekvvvfkrtggdvawhehrdvwwhDAIAnvs 245
Cdd:cd05923 92 LAELIERGEMTAAVIAVdaqvmDAIFQSGVRVLALSDLVGLGEPESAG-------------------------PLIE--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 aDCPPEemnAEDPLFILYTSGSTGKPKGV-------------MHTTGGYL------------VYAAMTFKYVFDYQ-EGE 299
Cdd:cd05923 144 -DPPRE---PEQPAFVFYTSGTTGLPKGAvipqraaesrvlfMSTQAGLRhgrhnvvlglmpLYHVIGFFAVLVAAlALD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 300 TFWCtadvgwitghtylvygplangaktilfegVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDS 379
Cdd:cd05923 220 GTYV-----------------------------VVEEFDPADALKLIEQERVTSLFATPTHLDALAA--AAEFAGLKLSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 380 LRVMGSVGEPINPEAWEWYYKTIgneQSPIVDTWWQTETGGILIAPlpgatDLKPGSATRPFFGVQPALVDNMGNIIEGA 459
Cdd:cd05923 269 LRHVTFAGATMPDAVLERVNQHL---PGEKVNIYGTTEAMNSLYMR-----DARTGTEMRPGFFSEVRIVRIGGSPDEAL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 460 TDGN----LVILDS---WPGQMRtvhgdhdRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:cd05923 341 ANGEegelIVAAAAdaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 533 ESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEfPTAELHKEVknWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05923 414 ERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQF--CRASELADFKRPRRYFFLDELPKNAMNKVLR 490
|
...
gi 515671996 613 RIL 615
Cdd:cd05923 491 RQL 493
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
104-616 |
1.22e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 131.95 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 104 DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVV 183
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 ITADEGVRGGRAVPlkknvdEALTNPevkniekVVVFKRTGGDVAWHEHrdvwWHDAIANVSADCPPEEMNAEDplfILY 263
Cdd:PRK08276 88 IVSAALADTAAELA------AELPAG-------VPLLLVVAGPVPGFRS----YEEALAAQPDTPIADETAGAD---MLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVMHTTGGYLVYAA---MTFKYVFDYQEGEtfwctadvgwitGHTYLVYGPL-------------ANGAKT 327
Cdd:PRK08276 148 SSGTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYGGP------------DSVYLSPAPLyhtaplrfgmsalALGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 328 ILFEGVpnypNTSRMSEVVDKHQVNILYTAPTA-IRalMAKGNEAVEgTSRD--SLRVMGSVGEPINPEA----WEWYyk 400
Cdd:PRK08276 216 VVMEKF----DAEEALALIERYRVTHSQLVPTMfVR--MLKLPEEVR-ARYDvsSLRVAIHAAAPCPVEVkramIDWW-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 401 tigneqSPIVD-TWWQTETGGI-LIAPLPGATdlKPGSATRPFFGVQPALVDNmGNIIEGATDGNlvILDSWPGQMRTVH 478
Cdd:PRK08276 287 ------GPIIHeYYASSEGGGVtVITSEDWLA--HPGSVGKAVLGEVRILDED-GNELPPGEIGT--VYFEMDGYPFEYH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 GDHDRFEQTYFStfKGMYFTSDGARRDEDGYYWITGRVDDVLnVSGhrmGT----AEIESALVAFDKIAEAAIVGIPHDI 554
Cdd:PRK08276 356 NDPEKTAAARNP--HGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAVFGVPDEE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 555 KGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 430 MGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
72-617 |
5.28e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 130.89 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 72 DGTLnvsANCIDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLA 151
Cdd:PRK05605 31 DTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 152 CTRIGAVhtVVFGG--FSPEALSGRIIDSNSKVVITAD------EGVRGG------------RAVPLKKNVdeALTNPeV 211
Cdd:PRK05605 102 VLRLGAV--VVEHNplYTAHELEHPFEDHGARVAIVWDkvaptvERLRRTtpletivsvnmiAAMPLLQRL--ALRLP-I 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 212 KNIEKvvvfKR---TG---GDVAWHEHRDvwwhDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYA 285
Cdd:PRK05605 177 PALRK----ARaalTGpapGTVPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 286 AMTFKYVFDYQEG-ETFWCTADVGWITGHTYLVYGPLANGAKTILFegvPnypnTSRMSEVVD---KHQVNILYTAPTAI 361
Cdd:PRK05605 249 AQGKAWVPGLGDGpERVLAALPMFHAYGLTLCLTLAVSIGGELVLL---P----APDIDLILDamkKHPPTWLPGVPPLY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 362 RALMAKGNEavEGTSRDSLRVMGSVGEPINPEAWE-WYYKTIGNeqspIVDTWWQTETGGILIAPlPGATDLKPGSATRP 440
Cdd:PRK05605 322 EKIAEAAEE--RGVDLSGVRNAFSGAMALPVSTVElWEKLTGGL----LVEGYGLTETSPIIVGN-PMSDDRRPGYVGVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 441 FFGVQPALVD--NMGNIIEGATDGNLVIldSWPgqmRTVHGDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDD 518
Cdd:PRK05605 395 FPDTEVRIVDpeDPDETMPDGEEGELLV--RGP---QVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 519 VLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGefptAELHKE-VKNWVRKEIGPIATPDVLH 597
Cdd:PRK05605 470 LIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG----AALDPEgLRAYCREHLTRYKVPRRFY 545
|
570 580
....*....|....*....|
gi 515671996 598 WTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 546 HVDELPRDQLGKVRRREVRE 565
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
83-620 |
1.15e-31 |
|
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: 129.50 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtVV 162
Cdd:COG1021 32 RRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FggfspeALSG-RIID-------SNSKVVITADEgVRGGRAVPLkknVDEALTnpEVKNIEKVVVFKRTGGDVAWhehrd 234
Cdd:COG1021 104 F------ALPAhRRAEishfaeqSEAVAYIIPDR-HRGFDYRAL---ARELQA--EVPSLRHVLVVGDAGEFTSL----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 235 vwwhDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLvyaamtfkyvfdYqegeTFWCTADVGWITGHT 314
Cdd:COG1021 167 ----DALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL------------Y----SVRASAEICGLDADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 -YLV---------------YGPLANGAKTILfegVPNyPNTSRMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRD 378
Cdd:COG1021 227 vYLAalpaahnfplsspgvLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWL----DAAERSRYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 379 --SLRVMGSVGEPINPEAWEWYYKTIG--------------NEQSPIVDTWWQTETGGILIAPlpgATDLKpgsatrpff 442
Cdd:COG1021 299 lsSLRVLQVGGAKLSPELARRVRPALGctlqqvfgmaeglvNYTRLDDPEEVILTTQGRPISP---DDEVR--------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 443 gvqpaLVDNMGNII-EGATdGNLVildswpgqmrtVHGDHdrfeqtyfsTFKGMY---------FTSDG-------ARRD 505
Cdd:COG1021 367 -----IVDEDGNPVpPGEV-GELL-----------TRGPY---------TIRGYYrapehnaraFTPDGfyrtgdlVRRT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 506 EDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELhkevKNWVRk 585
Cdd:COG1021 421 PDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAEL----RRFLR- 495
|
570 580 590
....*....|....*....|....*....|....*...
gi 515671996 586 EIGpIAT---PDVLHWTDSLPKTRSGKIMRRILRKIAT 620
Cdd:COG1021 496 ERG-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
1.32e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 127.14 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGDDPAddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIW--QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITADEGVrggravpLKKnVDEALtnPEVKNIEKVVVFKRTGGDvawHEHRDVWWHDAI 241
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVR--DELPSLRHIVVLDPRGLR---DDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 ANVSADCPPEEMNA-------EDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETF-----WCtadvgW 309
Cdd:COG1022 162 ALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 310 ITGHTYLVYGpLANGAKTILFEGVPNYPNTsrMSEVvdkhQVNILYTAP-------TAIRALMAKG--------NEAVE- 373
Cdd:COG1022 236 VFERTVSYYA-LAAGATVAFAESPDTLAED--LREV----KPTFMLAVPrvwekvyAGIQAKAEEAgglkrklfRWALAv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 374 ----GTSRDS------------------------------LRVMGSVGEPINPEAWEWYYkTIGneqSPIVDTWWQTETG 419
Cdd:COG1022 309 grryARARLAgkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFR-ALG---IPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 420 GILIAPLPGatDLKPGSATRPFFGVQPALvdnmgniiegATDGnlVILdswpgqmrtVHGDHdrfeqtyfsTFKGMY--- 496
Cdd:COG1022 385 PVITVNRPG--DNRIGTVGPPLPGVEVKI----------AEDG--EIL---------VRGPN---------VMKGYYknp 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 ------FTSDG-------ARRDEDGYYWITGRVDDVLNVSGhrmGT----AEIESALVAFDKIAEAAIVG 549
Cdd:COG1022 433 eataeaFDADGwlhtgdiGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
3.49e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 124.30 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtVVF--GGFSP 168
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLlnTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 169 EALSGRIIDSNSKVVITADEGVRggravplKKNVDEALTNPEVKNIEKVVVFkrtggdvawhehrdvwwhdaianvsadc 248
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDFEA-------KLIPGISVKFAELMNGPKEEAE---------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 249 PPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLvYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVygplangaKTI 328
Cdd:PRK03640 134 IQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILM--------RSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 329 LFeGVPNYP----NTSRMSEVVDKHQVNILYTAPTAIRALMAkgnEAVEGTSRDSLRVMGSVGEPINP----EAWEWyyk 400
Cdd:PRK03640 205 IY-GMRVVLvekfDAEKINKLLQTGGVTIISVVSTMLQRLLE---RLGEGTYPSSFRCMLLGGGPAPKplleQCKEK--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 401 tigneQSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNmGNIIEGATDGNLVIldswPGQMRTVhGD 480
Cdd:PRK03640 278 -----GIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV----KGPNVTK-GY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 481 HDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIY 560
Cdd:PRK03640 347 LNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 561 AYITLnDGEFPTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 427 AFVVK-SGEVTEEEL----RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
3.97e-30 |
|
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: 123.63 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17649 2 DAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITADegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcpp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLTHH--------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 eemnAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYvFDYQEGETFWCTADVGWITGHTYLvYGPLANGAkTILF 330
Cdd:cd17649 93 ----PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 EGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAkgnEAVEGTSRD--SLRVMGSVGEPINPEAW-------EWYYKT 401
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAE---EADRTGDGRppSLRLYIFGGEALSPELLrrwlkapVRLFNA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IGNEQSPIVDTWWQTEtggiliaplPGATDLKPGSAT-RPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHG- 479
Cdd:cd17649 243 YGPTEATVTPLVWKCE---------AGAARAGASMPIgRPLGGRSAYILDADLNPVPVGVTGELYI--GGEGLARGYLGr 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 480 ---DHDRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIk 555
Cdd:cd17649 312 pelTAERFVPDPFGAPGSrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG- 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 556 GQAIYAYITLNDGEfPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 391 GKQLVAYVVLRAAA-AQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
104-615 |
4.85e-30 |
|
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: 123.94 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 104 DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVV 183
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 ITADEGVRGGRavplkknvdealtnpevkniekvvvfkrtGGDVAWHehrDVWWHDAianVSADCPPEEMNAEDPLFILY 263
Cdd:cd12116 89 LTDDALPDRLP-----------------------------AGLPVLL---LALAAAA---AAPAAPRTPVSPDDLAYVIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVMHTTGGYLVY-AAMtfkyvfdyqeGETFWCTADVGWITGHTYL-------VYGPLANGAKTILFEGVPN 335
Cdd:cd12116 134 TSGSTGRPKGVVVSHRNLVNFlHSM----------RERLGLGPGDRLLAVTTYAfdislleLLLPLLAGARVVIAPRETQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 YpNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAvegtsRDSLRVM-GsvGEPINPEAWEWYYKTIG---NEQSPIVD 411
Cdd:cd12116 204 R-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG--GEALPPDLAARLLSRVGslwNLYGPTET 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 412 TWWQTetggilIAPLPGAtdLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHGDHD----RFEQT 487
Cdd:cd12116 276 TIWST------AARVTAA--AGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYI--GGDGVAQGYLGRPAltaeRFVPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 488 YFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQaIYAYITLN 566
Cdd:cd12116 346 PFAGPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 515671996 567 DGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12116 425 AGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
5.19e-30 |
|
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: 123.58 E-value: 5.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAERGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 164 GGFSPEALSGRIIDSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaian 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 244 vsadcppeemNAEDPLFILYTSGSTGKPKGVM---HTTGGYLVYAAMTF------------KYVFDYQEGETFwctadvg 308
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSICFDLSVFELF------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 309 witghtylvyGPLANGAKTILFEGVPNYPNTSRMSEVvdkhqvNILYTAPTAIRALMAKGneAVEGtsrdSLRVMGSVGE 388
Cdd:cd12115 166 ----------GPLATGGKVVLADNVLALPDLPAAAEV------TLINTVPSAAAELLRHD--ALPA----SVRVVNLAGE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 389 PINPEAWEWYYKTIGNEQ-----SPIVDTWWQTetggilIAPLPgATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGN 463
Cdd:cd12115 224 PLPRDLVQRLYARLQVERvvnlyGPSEDTTYST------VAPVP-PGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGE 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 464 LVIldSWPGQMRTVHGD----HDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:cd12115 297 LYI--GGAGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515671996 540 DKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 375 PGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-609 |
5.21e-29 |
|
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: 123.81 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV--- 158
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAyvp 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 ----HtvvfggfsPEALSGRII-DSNSKVVITADEgvrggravplkknVDEALTNPEVKniekVVVFkrtggDVAwhehr 233
Cdd:COG1020 556 ldpaY--------PAERLAYMLeDAGARLVLTQSA-------------LAARLPELGVP----VLAL-----DAL----- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 234 dvwwhdAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETF-WCTA---DVGw 309
Cdd:COG1020 601 ------ALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDRVlQFASlsfDAS- 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 310 itghTYLVYGPLANGAKTILF-EGVPnyPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVegtsrDSLRVMGSVGE 388
Cdd:COG1020 673 ----VWEIFGALLSGATLVLApPEAR--RDPAALAELLARHRVTVLNLTPSLLRALLDAAPEAL-----PSLRLVLVGGE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 389 PINPEAWEWYYKTIG-----NEQSPivdtwwqTETG-GILIAPLPgATDLKPGSAT--RPFFGVQpalvdnmgniiegat 460
Cdd:COG1020 742 ALPPELVRRWRARLPgarlvNLYGP-------TETTvDSTYYEVT-PPDADGGSVPigRPIANTR--------------- 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 461 dgnLVILDSW--------PGQMrTVHGD------HDRFEQT--YF----STFKG--MYFTSDGARRDEDG---YywiTGR 515
Cdd:COG1020 799 ---VYVLDAHlqpvpvgvPGEL-YIGGAglargyLNRPELTaeRFvadpFGFPGarLYRTGDLARWLPDGnleF---LGR 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 516 VDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKnwvRKEIGPIATPDV 595
Cdd:COG1020 872 ADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAA 948
|
570
....*....|....
gi 515671996 596 LHWTDSLPKTRSGK 609
Cdd:COG1020 949 VVLLLPLPLTGNGK 962
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
6.01e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 121.53 E-value: 6.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 90 GDEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC------GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 170 ALSGRIIDSNSKVVITADEgvRGGRAVPLKKNVdealtnPEVKNIekVVVFKRTGGDVawhEHRDVWWHDAIANVSADCP 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPRVAEVLPRL------PKLRTL--VVVEDGSGNDL---LPGAVDYEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 250 PEEMNAEDpLFILYTSGSTGKPKGVMHTTGG-YLV----YAAMTFKYVFDYQEGetfwcTADVGWITGHTYLVYGPLANG 324
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMWRQEDiFRVllggRDFATGEPIEDEEEL-----AKRAAAGPGMRRFPAPPLMHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 325 AKTI-----LFEG--VPNYPNTS----RMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPE 393
Cdd:PRK07798 232 AGQWaafaaLFSGqtVVLLPDVRfdadEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 394 AWEWYYKTIgnEQSPIVDTWWQTETGgiliAPLPGATDLKPGSATRPFFGVQP--ALVDNMGNIIEGATDGnlvilDSWP 471
Cdd:PRK07798 312 VKEALLELL--PNVVLTDSIGSSETG----FGGSGTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVEPGSGE-----IGWI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTV----HGDHDRFEQTYFsTFKGM-Y-FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEA 545
Cdd:PRK07798 381 ARRGHIplgyYKDPEKTAETFP-TIDGVrYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 546 AIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-617 |
7.47e-29 |
|
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: 120.81 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 96 IWEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV-HTV---VFggfsPEAL 171
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTInprLF----PEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 172 SGRIIDSNSKVVITADEgvrggrAVPLKKNVDealtnPEVKNIEKVVVFkrtGGDVAWHEHRDVWWH---DAIANVSADC 248
Cdd:cd12119 90 AYIINHAEDRVVFVDRD------FLPLLEAIA-----PRLPTVEHVVVM---TDDAAMPEPAGVGVLayeELLAAESPEY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 249 PPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTF--KYVFDYQEGETF-----------WCTADVGWITGHTY 315
Cdd:cd12119 156 DWPDFDENTAAAICYTSGTTGNPKGVVYSHRS-LVLHAMAAllTDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 LVYGPLANGAKTIlfegvpnypntsrmsEVVDKHQVNILYTAPTAIRALMAkgneAVEGTSRD--SLRVM---GSVGEPI 390
Cdd:cd12119 235 VLPGPYLDPASLA---------------ELIEREGVTFAAGVPTVWQGLLD----HLEANGRDlsSLRRVvigGSAVPRS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 391 NPEAWEWYYktigneqSPIVDTWWQTETGGILIA--PLPGATDLKPG-------SATRPFFGVQPALVDNMGNIIE--GA 459
Cdd:cd12119 296 LIEAFEERG-------VRVIHAWGMTETSPLGTVarPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPwdGK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 460 TDGNLVILDSWPGQmRTVHGDhdrfEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:cd12119 369 AVGELQVRGPWVTK-SYYKND----EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 540 DKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd12119 444 PAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
84-617 |
1.59e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 120.15 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAER-GDEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK07470 14 RQAARRfPDRIALVW------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVplkknvdeALTNPEVKNiekVVVFKRTGGDvawhehRDVwwhDAI- 241
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHADFPEHAAAV--------RAASPDLTH---VVAIGGARAG------LDY---EALv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 -ANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGgylvyaAMTF---KYVFDYQEGETfwcTADVGwitghtyLV 317
Cdd:PRK07470 148 aRHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG------QMAFvitNHLADLMPGTT---EQDAS-------LV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 YGPL------------ANGAKTILfegvpnyPNTSRM--SEV---VDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSL 380
Cdd:PRK07470 212 VAPLshgagihqlcqvARGAATVL-------LPSERFdpAEVwalVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 381 RVMGSVGEPINPEAWEWYYKTIGNEqspIVDTWWQTE-TGGILIAPLPG-----ATDLKPGSATRPFFGVQPALVDNMGN 454
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEvTGNITVLPPALhdaedGPDARIGTCGFERTGMEVQIQDDEGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 455 IIEGATDGNLVILDswPGqmrTVHGDHDRFEQTYfSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIE 533
Cdd:PRK07470 360 ELPPGETGEICVIG--PA---VFAGYYNNPEANA-KAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 534 SALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK07470 434 EKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
....
gi 515671996 614 ILRK 617
Cdd:PRK07470 511 MVRE 514
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
84-618 |
2.33e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 119.65 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAERG-DEVAIIwegdDpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCL----YMPMVpeaaVAMLACTRIGAV 158
Cdd:PRK07788 56 AHAARRApDRAALI----D--ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 HTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVPlkknvdealtnPEVKNIEKVVVFKRTGGDVA--WHEHRDVw 236
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRLRAWGGNPDDDEPSGstDETLDDL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 whdaIANVSADCPPEemnAEDP-LFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVfDYQEGETFWCTADVGWITGHTY 315
Cdd:PRK07788 194 ----IAGSSTAPLPK---PPKPgGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV-PFRAGETTLLPAPMFHATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 LVYGpLANGAKTIL---FEgvPnyPNTSRMsevVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINP 392
Cdd:PRK07788 266 LTLA-MALGSTVVLrrrFD--P--EATLED---IAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 393 EAWEWYYKTIGneqsPIV-DTWWQTEtggILIAPLPGATDLK--PGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDS 469
Cdd:PRK07788 338 ELATRALEAFG----PVLyNLYGSTE---VAFATIATPEDLAeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 470 WPGQMRTVHGDHDRFeqtyfstfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVG 549
Cdd:PRK07788 411 FPFEGYTDGRDKQII--------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 550 IPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK07788 483 VDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
4.15e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 117.93 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 117 VCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEalsgrIIDSNSKVVItADEGVRggRAV 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLV-ADAGGR--IVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 197 PLKKNVDEALTNPEVKNIEKVVVfkrtGGDVAWHEHrdvwwHDAIANVSADcppeemnaEDPLFILYTSGSTGKPKGVM- 275
Cdd:cd05922 75 ADAGAADRLRDALPASPDPGTVL----DADGIRAAR-----ASAPAHEVSH--------EDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 276 -HTTggyLVYAAMTFKYVFDYQEGETFWCTADVGWITGhTYLVYGPLANGAKTILFE-GVPNypntsrmSEVVD---KHQ 350
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNdGVLD-------DAFWEdlrEHG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 351 VNILYTAPTaIRALMAKGNEAVEGTSrdSLRVMGSVGEPINPEawewyykTIG--NEQSP---IVDTWWQTE-TGGILIA 424
Cdd:cd05922 207 ATGLAGVPS-TYAMLTRLGFDPAKLP--SLRYLTQAGGRLPQE-------TIArlRELLPgaqVYVMYGQTEaTRRMTYL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 425 PlPGATDLKPGSATRPFFGVQPALVDNMGNII------EGATDGNLVILDSWpgqmrtvhgdHDRFEQTYFSTFKGMYFT 498
Cdd:cd05922 277 P-PERILEKPGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYW----------NDPPYRRKEGRGGGVLHT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 499 SDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPhDIKGQAIYAYITLNDGEFPtaelhKE 578
Cdd:cd05922 346 GDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDP-----KD 419
|
490 500 510
....*....|....*....|....*....|....*...
gi 515671996 579 VKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 420 VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
101-616 |
1.01e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.13 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 101 DPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNS 180
Cdd:PRK09088 16 DLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 181 KVvITADEGVRGGRAVPLkknvdealtnpevkniekvvvfkrtggDVAwhehrdvwwhDAIANVSADCPP--EEMNAEDP 258
Cdd:PRK09088 96 RL-LLGDDAVAAGRTDVE---------------------------DLA----------AFIASADALEPAdtPSIPPERV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 259 LFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPN 338
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 339 TSRMSEVvdKHQVNILYTAPTAIRALMAKgnEAVEGTSRDSLRVMGSVGEPINPEAWEWYYktigNEQSPIVDTWWQTET 418
Cdd:PRK09088 217 LGRLGDP--ALGITHYFCVPQMAQAFRAQ--PGFDAAALRHLTALFTGGAPHAAEDILGWL----DDGIPMVDGFGMSEA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 419 GGILIAPL-PGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIL--DSWPGQMRTVHGDHDRFeqtyfsTFKGM 495
Cdd:PRK09088 289 GTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAF------TGDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 496 YFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGefpTAEL 575
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 515671996 576 HKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK09088 440 LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
1.58e-26 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 103.01 E-value: 1.58e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 531 EIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
1.69e-26 |
|
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: 111.42 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 263 YTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKtILFEGVPNYPNTSRM 342
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 SE---VVDKHQVNILYTAPTAIRALMAKGNEAVEGtsrdSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETG 419
Cdd:cd05944 87 DNfwkLVERYRITSLSTVPTVYAALLQVPVNADIS----SLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 420 gILIAPLPGATDLKPGSATR--PFFGVQPALVDNMGNIIE---GATDGNLVIldswpgQMRTVHGDHDRFEQTYFSTFKG 494
Cdd:cd05944 160 -CLVAVNPPDGPKRPGSVGLrlPYARVRIKVLDGVGRLLRdcaPDEVGEICV------AGPGVFGGYLYTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 495 MYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTA 573
Cdd:cd05944 233 GWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515671996 574 ElhkEVKNWVRKEIGP-IATPDVLHWTDSLPKTRSGKIMRRILRKIAT 620
Cdd:cd05944 313 E---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
104-616 |
2.01e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 113.64 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 104 DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVV 183
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 IT-AD--EGVRGgrAVPLKKNVDEALTNPEVKNIEKVVVFKRT--GGDVAWhehrDVWwhdaianVSADCPPEEMNAEDP 258
Cdd:PRK12406 88 IAhADllHGLAS--ALPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDW----EGW-------LAQQEPYDGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 259 LFILYTSGSTGKPKGVMHT--TGGYLVYAAMTFKYVFdyqegetfwctadvGWITGHTYLVYGPL------ANGAKTILF 330
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIY--------------GLKPGIRALLTGPLyhsapnAYGLRAGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 EGV----PNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEA----WEWYykti 402
Cdd:PRK12406 221 GGVlvlqPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWW---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 403 gneqSP-IVDTWWQTETGGILIAPLPGATDlKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVildswpgqMR------ 475
Cdd:PRK12406 296 ----GPvIYEYYGSTESGAVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIY--------SRiagnpd 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 476 -TVHGDHDR---FEQTYFSTfkgmyfTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIP 551
Cdd:PRK12406 363 fTYHNKPEKraeIDRGGFIT------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 552 HDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
107-617 |
4.29e-26 |
|
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: 111.28 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 107 TLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtvvfggfspealsgriidsnskvvita 186
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 187 degvrggrAVPLKKNVDEALTNPEVKNIEKVVvfkrtggdvawhehrdvwwhDAIANvsadcppeemnaedplfILYTSG 266
Cdd:cd05912 53 --------AVLLNTRLTPNELAFQLKDSDVKL--------------------DDIAT-----------------IMYTSG 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 267 STGKPKGVMHTTGGYLVYAAMTfkyvfdyqeGETFWCTADVGW--------ITGHTYLVYGpLANGAKTILFEGVpnypN 338
Cdd:cd05912 88 TTGKPKGVQQTFGNHWWSAIGS---------ALNLGLTEDDNWlcalplfhISGLSILMRS-VIYGMTVYLVDKF----D 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 339 TSRMSEVVDKHQVNILYTAPTAIRALMAKGNEavegTSRDSLRVMGSVGEPINPEAWEwyykTIGNEQSPIVDTWWQTET 418
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQRLLEILGE----GYPNNLRCILLGGGPAPKPLLE----QCKEKGIPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 419 GGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIiegATDGNLVIldswPGQMRTvHGDHDRFEQTYFSTFKGMYFT 498
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILL----KGPNVT-KGYLNRPDATEESFENGWFKT 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 499 SDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNdGEFPTAELhke 578
Cdd:cd05912 298 GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-RPISEEEL--- 373
|
490 500 510
....*....|....*....|....*....|....*....
gi 515671996 579 vKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 374 -IAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-622 |
6.72e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 114.28 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADegvRGGRAVPLKKNVDealtnpevkniekVVVFKRTGgdvAWhehrdvwwhdaIANVSADCPPEEMNAEDPLFILYT 264
Cdd:PRK12316 614 SQS---HLGRKLPLAAGVQ-------------VLDLDRPA---AW-----------LEGYSEENPGTELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGYLVY-AAMTFKYVFDyqEGETFWCTADVGWITGHTYLvYGPLANGAKTILfEGVPNYPNTSRMS 343
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNRlCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVV-AAPGDHRDPAKLV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 344 EVVDKHQVNILYTAPTAIRALMAKGNEAvegtSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQspIVDTWWQTETGgili 423
Cdd:PRK12316 740 ELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAG--LYNLYGPTEAA---- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 424 APLPGATDLKPGSAT----RPFFGVQPALVDNMGNIIEGATDGNLVILDSwpGQMRTVHG----DHDRFEQTYFSTFKGM 495
Cdd:PRK12316 810 IDVTHWTCVEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAGERM 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 496 YFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGiphdIKGQAIYAYITLNDgefPTAEL 575
Cdd:PRK12316 888 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLES---EGGDW 960
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 515671996 576 HKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATGD 622
Cdd:PRK12316 961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
87-615 |
7.84e-26 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 111.65 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 87 AERG-DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGG 165
Cdd:cd17655 7 AEKTpDHTAVVFE------DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 166 FSPEALSGRIIDSNSKVVITADEgvrggraVPLKKNVDEALTNPEVKNIEkvvvfkrtggdvawhehrdvwwHDAIANVS 245
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSH-------LQPPIAFIGLIDLLDEDTIY----------------------HEESENLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 ADCppeemNAEDPLFILYTSGSTGKPKGVMHTTGG---YLVYA------------AMTFKYVFDyqegetfwctADVGWI 310
Cdd:cd17655 132 PVS-----KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnLVEWAnkviyqgehlrvALFASISFD----------ASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 311 tghtylvYGPLANGAKTILfegvpnYPNTSRMS-----EVVDKHQVNILYTAPTAIRALmakgnEAVEGTSRDSLRVMGS 385
Cdd:cd17655 197 -------FASLLSGNTLYI------VRKETVLDgqaltQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 386 VGEPINPE-AWEWYYK-----TIGNEQSPivdtwwqTETG-GILIAPLPGATDLKPG-SATRPFFGVQPALVDNMGNIIE 457
Cdd:cd17655 259 GGEALSTElAKKIIELfgtnpTITNAYGP-------TETTvDASIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 GATDGNLVIldswpGQMRTVHGDHDRFEQTY-------FSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTA 530
Cdd:cd17655 332 VGVAGELYI-----GGEGVARGYLNRPELTAekfvddpFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 531 EIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITlNDGEFPTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17655 407 EIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-SEKELPVAQL----REFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
....*
gi 515671996 611 MRRIL 615
Cdd:cd17655 482 DRKAL 486
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
91-615 |
2.45e-25 |
|
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: 109.48 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17650 2 DAIAVSD------ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVitadegvrggravplkknvdeaLTNPEvkniekvvvfkrtggdvawhehrdvwwhdaianvsadcpp 250
Cdd:cd17650 76 LQYMLEDSGAKLL----------------------LTQPE---------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 eemnaeDPLFILYTSGSTGKPKGVMHTTGGYL-VYAAMTFKYVFDYQegetfwcTADVGWITGHTYLVYGplANGAKTIL 329
Cdd:cd17650 94 ------DLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSF-------PVRLLQMASFSFDVFA--GDFARSLL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 330 FEG----VPN--YPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEavEGTSRDSLR--VMGSVGEPINPEAWEwyYKT 401
Cdd:cd17650 159 NGGtlviCPDevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRllIVGSDGCKAQDFKTL--AAR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IGnEQSPIVDTWWQTETGgILIAPLPGATDLKPGSAT----RPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTV 477
Cdd:cd17650 235 FG-QGMRIINSYGVTEAT-IDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQPVGVAGELYI--GGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 478 HGDHD----RFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVgIPHD 553
Cdd:cd17650 311 LNRPEltaeRFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VRED 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515671996 554 IKGQA-IYAYI----TLNdgefpTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 390 KGGEArLCAYVvaaaTLN-----TAEL----RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
105-616 |
4.68e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 109.21 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 tadegvrggravplkknVDEALTNPEVKNIEKVVVFKRTGGDVAwhehrdvwwhdAIANVSADCPPEEMNAEDPLF-ILY 263
Cdd:PRK06145 105 -----------------VDEEFDAIVALETPKIVIDAAAQADSR-----------RLAQGGLEIPPQAAVAPTDLVrLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGVMHTTGGYlvyaamtfkyvfdyqegetFWCTAD----VGWITGHTYLVYGPLAN-GA-----KTILFEG- 332
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNL-------------------HWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 333 ---VPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAkgneaVEGTSR---DSLRVMGSVGEPiNPE----AWEWYYKti 402
Cdd:PRK06145 218 tlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLT-----VPDRDRfdlDSLAWCIGGGEK-TPEsrirDFTRVFT-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 403 gneQSPIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSwpgqmRTVHGDHD 482
Cdd:PRK06145 290 ---RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP-----KVTKGYWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 483 RFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAY 562
Cdd:PRK06145 362 DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 515671996 563 ITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06145 442 VVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
4.68e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 109.39 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 90 GDEVAIIWEgDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 170 AlSGRIIDSN--SKVVITAD-----EGVRGGRAVPLKKNVdeaLTNPEVKNIEKVVVFKRtggdvawhehrdvwwhdAIA 242
Cdd:PRK08008 100 E-SAWILQNSqaSLLVTSAQfypmyRQIQQEDATPLRHIC---LTRVALPADDGVSSFTQ-----------------LKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 243 NVSA---DCPPeeMNAEDPLFILYTSGSTGKPKGVMHTT-----GGYL-----------VYAAMTFKYVFDYQegetfwC 303
Cdd:PRK08008 159 QQPAtlcYAPP--LSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYsawqcalrdddVYLTVMPAFHIDCQ------C 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 304 TADVGWITGhtylvygplanGAKTILFEgvpNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAKgnEAVEGTSRDSLRVM 383
Cdd:PRK08008 231 TAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMVQ--PPSANDRQHCLREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 384 gsvgepinpeaweWYYKTIGNEQSP---------IVDTWWQTETGGILIAPLPGATDLKPgSATRPFFGVQPALVDNMGN 454
Cdd:PRK08008 294 -------------MFYLNLSDQEKDafeerfgvrLLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 455 IIEGATDGNLVIlDSWPGQ--MRTVHGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:PRK08008 360 PLPAGEIGEICI-KGVPGKtiFKEYYLDPKATAKVL--EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 533 ESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
....
gi 515671996 613 RILR 616
Cdd:PRK08008 514 KNLK 517
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
5.68e-25 |
|
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: 106.26 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYV-FDyqeGETFW-CTADVGWITGHTYLVYGPLANGAKTILfegvp 334
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG---GGDSWlLSLPLYHVGGLAILVRSLLAGAELVLL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 335 nypnTSRMSEVVDKHQVNILYTA--PTAIRALMAKGNEAvegTSRDSLRVMGSVGEPINPEAWEwyykTIGNEQSPIVDT 412
Cdd:cd17630 73 ----ERNQALAEDLAPPGVTHVSlvPTQLQRLLDSGQGP---AALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 413 WWQTETGGILIAPLPGATDLkpGSATRPFFGVQPALVDNmGNI-IEGATdgnlVILDSWPGQMRTvhgdhDRFEQtyfst 491
Cdd:cd17630 142 YGMTETASQVATKRPDGFGR--GGVGVLLPGRELRIVED-GEIwVGGAS----LAMGYLRGQLVP-----EFNED----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 492 fkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGefp 571
Cdd:cd17630 205 --GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515671996 572 taELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 280 --ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
106-549 |
1.10e-24 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 107.68 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 ADegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnAEDPLFILYTS 265
Cdd:cd05907 84 ED-------------------------------------------------------------------PDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 266 GSTGKPKGVMHTTGGYLVYAAMTFKYVfDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPNYPNTSRMSE- 344
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRp 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 345 --------VVDKHQVNILYTAPTAIRALM---AKGneavegtsrDSLRVMGSVGEPINPEAWEWYYKtIGneqSPIVDTW 413
Cdd:cd05907 176 tvflavprVWEKVYAAIKVKAVPGLKRKLfdlAVG---------GRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGY 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 414 WQTETGGILIAPLPGatDLKPGSATRPFFGVQPALVDnmgniiegatDGNLVIldSWPGQMRtvhGDHDRFEQTYFSTFK 493
Cdd:cd05907 243 GLTETSAVVTLNPPG--DNRIGTVGKPLPGVEVRIAD----------DGEILV--RGPNVML---GYYKNPEATAEALDA 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 494 -GMYFTSDGARRDEDGYYWITGRVDDVL-NVSGHRMGTAEIESALVAFDKIAEAAIVG 549
Cdd:cd05907 306 dGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
109-617 |
1.15e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 108.30 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNEL-HKEVCLfSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITAD 187
Cdd:PRK06087 51 TYSALdHAASRL-ANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EgvrggravpLKKNVDEALTNP---EVKNIEKVVVFkrtggDVAWHEHRDvwwhDAIANVSADCPPEE----MNAEDPLF 260
Cdd:PRK06087 130 L---------FKQTRPVDLILPlqnQLPQLQQIVGV-----DKLAPATSS----LSLSQIIADYEPLTtaitTHGDELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 261 ILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVpnypNTS 340
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF----TPD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 341 RMSEVVDKHQVNILYTAPTAIRALMAKGNEAveGTSRDSLRVMGSVGEPInP-----EAWEWYYKtigneqspIVDTWWQ 415
Cdd:PRK06087 267 ACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PkkvarECQQRGIK--------LLSVYGS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPLPGATDLKPGSATRPFFGVQPALVDN------MGNIIEGATDGNLVILDSWPGQMRTVHG-DHDrfeqty 488
Cdd:PRK06087 336 TESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlpPGCEGEEASRGPNVFMGYLDEPELTARAlDEE------ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 489 fstfkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDG 568
Cdd:PRK06087 410 -----GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 515671996 569 EF-PTAElhkEVKNWV-RKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 485 HHsLTLE---EVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
1.39e-24 |
|
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: 96.77 E-value: 1.39e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 24 YLAMYQQSVSDPEGFWGEHGKIVDWIKPFTQVKNTSFDPghiDIRWFEDGTLNVSANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGP---FAKWFVGGKLNVCYNC 55
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
105-619 |
1.86e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.94 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADE-------GVRGGRAVPLKKNVDEALTNPEVKNIEKVVVF--KRTGGDVAWHE---HRDVWWHDAIANVSAdcppeE 252
Cdd:PRK12583 123 CADAfktsdyhAMLQELLPGLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHElqaRGETVSREALAERQA-----S 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 253 MNAEDPLFILYTSGSTGKPKGVMHT-----TGGYLVYAAMTFkyvfdyqeGETFWCTADVGWIT--GHTYLVYGPLANGA 325
Cdd:PRK12583 198 LDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGL--------TEHDRLCVPVPLYHcfGMVLANLGCMTVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 326 KTIlfegvpnYPNTS----RMSEVVDKHQVNILYTAPTAIRAlmakgneAVEGTSRD-----SLRVMGSVGEPINPEAWE 396
Cdd:PRK12583 270 CLV-------YPNEAfdplATLQAVEEERCTALYGVPTMFIA-------ELDHPQRGnfdlsSLRTGIMAGAPCPIEVMR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 wyyKTIGNEQSP-IVDTWWQTETGGILIapLPGATD---LKPGSATRPFFGVQPALVDNMGNII------EGATDGNLVI 466
Cdd:PRK12583 336 ---RVMDEMHMAeVQIAYGMTETSPVSL--QTTAADdleRRVETVGRTQPHLEVKVVDPDGATVprgeigELCTRGYSVM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 467 LDSWPGQMRTVHG-DHDrfeqtyfstfkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEA 545
Cdd:PRK12583 411 KGYWNNPEATAESiDED-----------GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 546 AIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
2.44e-24 |
|
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: 106.79 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITADEgvrggravplkknvdeaLTNPEVKNIEKVVVfkrtggdvawhehrdVWwhDAIANVSADCPP 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----------------LKSKLSFNKSTILL---------------ED--PSISQEDTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 EEMNAEDPLFILYTSGSTGKPKGVM-------------------HTTGGYLVYAAMTFKYVfdYQEGETFWCTAdvgwit 311
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQlehknmvnllhferektniNFSDKVLQFATCSFDVC--YQEIFSTLLSG------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 312 GHTYLVygplANGAKTilfegvpnypNTSRMSEVVDKHQVNILYTaPTAIRALMAKGNEAVEGTSrDSLRVMGSVGEP-- 389
Cdd:cd17656 195 GTLYII----REETKR----------DVEQLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFP-TCVKHIITAGEQlv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 390 INPEAWEWYYK---TIGNEQSP----IVDTWwqtetggiLIAPLPGATDLKPgsATRPFFGVQPALVDNMGNIIEGATDG 462
Cdd:cd17656 259 ITNEFKEMLHEhnvHLHNHYGPsethVVTTY--------TINPEAEIPELPP--IGKPISNTWIYILDQEQQLQPQGIVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLVIldSWPGQMRTVHGD----HDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVA 538
Cdd:cd17656 329 ELYI--SGASVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 539 FDKIAEAAIVGIPHDIKGQAIYAYI----TLNDGEFptaelhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAYFvmeqELNISQL---------REYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKA 477
|
.
gi 515671996 615 L 615
Cdd:cd17656 478 L 478
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
3.27e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.14 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAERGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALI------DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 HTVVFGGFSPEALSGRIIDSNSKVVITADegvrGGRAVPLKKNVDEAlTNPEVKNIEKVVVFKRTGGDVAWHEHRDvwWH 238
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAV-PPDALPPLRAIAVVDDAADATPAPAPGA--RV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 239 DAIANVSADCPP---EEMNAEDPLFILYT-SGSTGKPKGVMHTTGGYLVYAAMTFKyVFDYQEGETFWCTADVGWITGHT 314
Cdd:PRK06164 160 QLFALPDPAPPAaagERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 YLVyGPLANGAkTILFEGVPNYPNTSRMsevVDKHQVNILYTAPTAIRALMAkgneaVEGTSRD--SLRVMGSVGepINP 392
Cdd:PRK06164 239 TLL-GALAGGA-PLVCEPVFDAARTARA---LRRHRVTHTFGNDEMLRRILD-----TAGERADfpSARLFGFAS--FAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 393 eAWEWYYKTIGNEQSPIVDTWWQTEtggiLIApLPGATDLKPGSATRPFFGVQPA-------LVDNM-GNIIEGATDGNL 464
Cdd:PRK06164 307 -ALGELAALARARGVPLTGLYGSSE----VQA-LVALQPATDPVSVRIEGGGRPAspearvrARDPQdGALLPDGESGEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 465 VIldSWPGQMRTVHGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAE 544
Cdd:PRK06164 381 EI--RAPSLMRGYLDNPDATARAL--TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAA 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 545 AAIVGIPHDIKGQAiYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSG---KIMRRILRKIA 619
Cdd:PRK06164 457 AQVVGATRDGKTVP-VAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
89-620 |
5.92e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 105.71 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 89 RGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALK-EQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFS 167
Cdd:PRK06839 15 HPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 168 PEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEALTNPEVKNIEKvvvfkrtggdvawHEHRDVwwhdaianvsad 247
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIED-------------RKIDNF------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 248 cppEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKT 327
Cdd:PRK06839 144 ---VEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 328 IlfegVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNeaVEGTSRDSLRVMGSVGEPInPEAWEWYYKTIGneqS 407
Cdd:PRK06839 220 I----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPC-PEELMREFIDRG---F 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 408 PIVDTWWQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHgdhDRFEQT 487
Cdd:PRK06839 290 LFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI--RGPNVMKEYW---NRPDAT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 488 YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLND 567
Cdd:PRK06839 365 EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 515671996 568 GEFPTaelHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIAT 620
Cdd:PRK06839 445 SSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
84-623 |
1.56e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.12 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLA-ERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK06178 40 RAWArERPQRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVITAD------EGVRGGRAV------------------PLKKNVDEALTNPEvkniekvv 218
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDqlapvvEQVRAETSLrhvivtsladvlpaeptlPLPDSLRAPRLAAA-------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 219 vfkrtggdvawhehrdvWWHD---AIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTgGYLVYAAMTFKYV-FD 294
Cdd:PRK06178 186 -----------------GAIDllpALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ-RDMVYTAAAAYAVaVV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 295 YQEGETFWCTADVGWITGHTYLVYGPLANGAKTILF---------EGVPNYpNTSRMSEVVDKHqVNILYTAPTAIRALm 365
Cdd:PRK06178 248 GGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLarwdavafmAAVERY-RVTRTVMLVDNA-VELMDHPRFAEYDL- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 366 akgneavegTSRDSLRVMGSVgEPINPEawewYYKTigneqspivdtwWQTETGGILIAPLPGAT--------------- 430
Cdd:PRK06178 325 ---------SSLRQVRVVSFV-KKLNPD----YRQR------------WRALTGSVLAEAAWGMTethtcdtftagfqdd 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 431 --DLKpgsaTRPFF------GVQPALVD-NMGNIIEGATDGNLVIldswpgqmRT---VHGDHDRFEQTYFSTFKGMYFT 498
Cdd:PRK06178 379 dfDLL----SQPVFvglpvpGTEFKICDfETGELLPLGAEGEIVV--------RTpslLKGYWNKPEATAEALRDGWLHT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 499 SDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkE 578
Cdd:PRK06178 447 GDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---A 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 515671996 579 VKNWVRKEIGPIATPDVlHWTDSLPKTRSGKIMRRILRKIATGDT 623
Cdd:PRK06178 524 LQAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-619 |
2.64e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 104.19 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLF-SNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK08751 49 KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADEGVRGGRAV----PLKKNV-----------DEALTNPEVKNIEKVVVFKRTGGDVAWHEhrdvwwhdAIANVSA-DC 248
Cdd:PRK08751 129 VIDNFGTTVQQViadtPVKQVIttglgdmlgfpKAALVNFVVKYVKKLVPEYRINGAIRFRE--------ALALGRKhSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 249 PPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVF---DYQEGETFWCTADvgwitgHTYLVYGPLANGA 325
Cdd:PRK08751 201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgKLEEGCEVVITAL------PLYHIFALTANGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 326 KTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAK--GNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIG 403
Cdd:PRK08751 275 VFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 404 neqSPIVDTWWQTETG-GILIAPLpgatDLKP--GSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRtvhGD 480
Cdd:PRK08751 355 ---LTLVEAYGLTETSpAACINPL----TLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCI--KGPQVMK---GY 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 481 HDRFEQT-YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAI 559
Cdd:PRK08751 423 WKRPEETaKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIV 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 560 YAYITLNDGEFpTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08751 503 KVVIVKKDPAL-TAE---DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
5.04e-23 |
|
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: 102.73 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd12114 2 DATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITADEGVrggravplkKNVDEALTNPevkniekvvvfkrtggdvawhehrdVWWHDAIAnVSADCPP 250
Cdd:cd12114 76 REAILADAGARLVLTDGPDA---------QLDVAVFDVL-------------------------ILDLDALA-APAPPPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 EEMNAEDPLFILYTSGSTGKPKGVMHTTGGYL-VYAAMTFKYV--------------FDYQegetfwctadvgwitghTY 315
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAvgpddrvlalsslsFDLS-----------------VY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 LVYGPLANGAkTILFEGVPNYPNTSRMSEVVDKHQVNILYTAPtAIRALMAKGNEAVEGTSRdSLR-VMGSvGEPINPEa 394
Cdd:cd12114 184 DIFGALSAGA-TLVLPDEARRRDPAHWAELIERHGVTLWNSVP-ALLEMLLDVLEAAQALLP-SLRlVLLS-GDWIPLD- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 395 wewyyktigneqspIVDTWWQTETGGILIApLPGAT----------------DLKPGSATRPFFGVQPALVDNMGNIIEG 458
Cdd:cd12114 259 --------------LPARLRALAPDARLIS-LGGATeasiwsiyhpidevppDWRSIPYGRPLANQRYRVLDPRGRDCPD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 459 ATDGNLVIldSWPGQMRTVHGDHDRFEQTYFSTFKG--MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:cd12114 324 WVPGELWI--GGRGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAAL 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 537 VAFDKIAEAAIVGIPhDIKGQAIYAYITLNDGEFPTAELhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 402 QAHPGVARAVVVVLG-DPGGKRLAAFVVPDNDGTPIAPD--ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
104-617 |
5.32e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.24 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 104 DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVV 183
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 ITADEGVR------GGRAVPLkknvDEALtnpevkniekvvvfkrtggdvawhehrDVWWHDAIANVSADCPPEEMnaed 257
Cdd:PRK12467 614 LTQSHLLAqlpvpaGLRSLCL----DEPA---------------------------DLLCGYSGHNPEVALDPDNL---- 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 258 pLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYvfdyqegetFWCTADVGWITGHTY-------LVYGPLANGAKTILF 330
Cdd:PRK12467 659 -AYVIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 EgvpnyPNTSRMSE----VVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSvgepinpEAWEWYYKTIGNEQ 406
Cdd:PRK12467 729 P-----PDCARDAEafaaLMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCGG-------EALQVDLLARVRAL 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 407 SP---IVDTWWQTETG-GILIAPLPG-ATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHG-- 479
Cdd:PRK12467 795 GPgarLINHYGPTETTvGVSTYELSDeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYI--GGAGLARGYHRrp 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 480 --DHDRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKG 556
Cdd:PRK12467 873 alTAERFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL 952
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515671996 557 QAIyAYITLNDGEFPT--AELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 953 QLV-AYLVPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
5.93e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 102.85 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIWegddPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVITAdegvrggRAvplKKNVDEALTNpEVKNIEKVVVFKRTGGDVAWhehrdVWWHDAIA 242
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITS-------AA---KLDVARALLK-QCPGVRHRLVLDGDGELEGF-----VGYAEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 243 NVSADCPPEEMNAEDplfILYTSGSTGKPKGVMH--------TTGGYLvyaaMTFKYVFDYQEGETFWCTADVGwitgHT 314
Cdd:PRK13391 144 GLPATPIADESLGTD---MLYSSGTTGRPKGIKRplpeqppdTPLPLT----AFLQRLWGFRSDMVYLSPAPLY----HS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 ylvyGPLA-------NGAKTILFEGVpnypNTSRMSEVVDKHQVNILYTAPTA-IRalMAKGNEAVEGT-SRDSLRVMGS 385
Cdd:PRK13391 213 ----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMfSR--MLKLPEEVRDKyDLSSLEVAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 386 VGEPINPEAWEWYYKTIGneqsPIVDTWW-QTETGGILIAPLPGATDlKPGSATRPFFGVQPALVDNMGNIIEGaTDGNL 464
Cdd:PRK13391 283 AAAPCPPQVKEQMIDWWG----PIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGDLHILDDDGAELPPG-EPGTI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 465 vildsW--PGQMRTVHGDHDRFEQTYfSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKI 542
Cdd:PRK13391 357 -----WfeGGRPFEYLNDPAKTAEAR-HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 543 AEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13391 431 ADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
6.03e-23 |
|
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: 100.82 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHT-----TGGYLVYAAMtfkyvfDYQEGETFWCTADVGWITGhtyLVYGPLA---NGAKT 327
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERL------GLTEQDRLCIPVPLFHCFG---SVLGVLAcltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 328 IL----FEGVPNYpntsrmsEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdSLR--VMGsvGEPINPEAWEWYYKT 401
Cdd:cd05917 73 VFpspsFDPLAVL-------EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLS--SLRtgIMA--GAPCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IGNEQSPIVdtWWQTETGGILIAPLPGAT-DLKPGSATRPFFGVQPALVDNMGNII-------EGATDGNLVILDSW--P 471
Cdd:cd05917 142 MNMKDVTIA--YGMTETSPVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpgELCIRGYSVMKGYWndP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTVHgDHDRFeqtyfstfkgmYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIP 551
Cdd:cd05917 220 EKTAEAI-DGDGW-----------LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 552 HDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
107-616 |
6.35e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 102.91 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 107 TLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAvHTVVFG-GFSPEALSGRIIDSNSKVVIT 185
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 ADEgvrggravpLKKNVDEALTN-PEVKNIekvvvfkrtggdVAWHEHRDVWWHDAIANVSADCPPEEMNAEDPLfILYT 264
Cdd:PRK13382 147 DEE---------FSATVDRALADcPQATRI------------VAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGylvyAAMTFKYVFDyqegetfwctaDVGWITGHTYLVYGPL--ANGAKTILFEGVPNYPNTSRM 342
Cdd:PRK13382 205 SGTTGTPKGARRSGPG----GIGTLKAILD-----------RTPWRAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 S-------EVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNeqsPIVDTWWQ 415
Cdd:PRK13382 270 RfdpeatlDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPlpgATDLK--PGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSW------PGQMRTVHgdhdrfeqt 487
Cdd:PRK13382 347 TEAGMIATAT---PADLRaaPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTqfdgytSGSTKDFH--------- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 488 yfstfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLND 567
Cdd:PRK13382 415 -----DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 515671996 568 GefpTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 490 G---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
108-621 |
8.40e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.78 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITAD 187
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EGVRGGRAVPLKKNVDEALTnpevkniekvvvfKRTGGDVAWHEHrdvwwhdaiaNVSADCPPEEMN--AEDPLFILYTS 265
Cdd:PRK05857 122 GSKMASSAVPEALHSIPVIA-------------VDIAAVTRESEH----------SLDAASLAGNADqgSEDPLAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 266 GSTGKPKGVMhttggylvYAAMTFKYVFDYQEGETF-WctadVGWITGHTylVYGPLAngAKTI---------LFEG--- 332
Cdd:PRK05857 179 GTTGEPKAVL--------LANRTFFAVPDILQKEGLnW----VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 333 VPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAveGTSRDSLRVMGSVGEpinpeawewyyKTIGNEQSPIVDT 412
Cdd:PRK05857 243 VTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSLRLVGYGGS-----------RAIAADVRFIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 413 WWQT-------ETGGILIApLPgaTD------LKPGSATRPFFGVQPALVD------NMGNIIEGATDGNLVILDswPGQ 473
Cdd:PRK05857 310 GVRTaqvyglsETGCTALC-LP--TDdgsivkIEAGAVGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLWIKS--PAN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 474 MRTVHGDHDRFEQTYfstFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHD 553
Cdd:PRK05857 385 MLGYWNNPERTAEVL---IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 554 ----IKGQAIYAYITLNdgEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIATG 621
Cdd:PRK05857 462 efgaLVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
86-616 |
1.15e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 102.80 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 86 LAERGDEVAiiWEgDDPA--DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVf 163
Cdd:PRK06060 10 LAEQASEAG--WY-DRPAfyAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 164 ggfSPE------ALSGRiiDSNSKVVITAdeGVRGGRAVPlKKNVDEALTNPEVKNIEKVVvFKRTGGDVAwhehrdvww 237
Cdd:PRK06060 86 ---NPElhrddhALAAR--NTEPALVVTS--DALRDRFQP-SRVAEAAELMSEAARVAPGG-YEPMGGDAL--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 238 hdaianvsadcppeemnaedpLFILYTSGSTGKPKGVMHTtggylvyAAMTFKYVfdyqegETFWCTA------DVGWIT 311
Cdd:PRK06060 148 ---------------------AYATYTSGTTGPPKAAIHR-------HADPLTFV------DAMCRKAlrltpeDTGLCS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 312 GHTYLVYG-------PLANGAKTILfEGVPNYPNTSRMseVVDKHQVNILYTAPTairaLMAKGNEAVEGTSRDSLRVMG 384
Cdd:PRK06060 194 ARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAI--LSARFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPEAWEWYYKTIGNeqSPIVDTWWQTETGGILIAPlpGATDLKPGSATR--PFFGVQPALVDnmgniieGATDG 462
Cdd:PRK06060 267 SAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGRvlPPYEIRVVAPD-------GTTAG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLVILDSWpgqmrtVHGDhdRFEQTYFS------TFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:PRK06060 336 PGVEGDLW------VRGP--AIAKGYWNrpdspvANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLI 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 537 VAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 408 IEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-624 |
1.95e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.32 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITadegvrggravplKKNVDEALtnPEVKNIEKVVVfkrtggdvawheHRDVWWhdai 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLEQL--PAPAGDTALTL------------DRLDLN---- 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 aNVSADCPPEEMNAEDPLFILYTSGSTGKPKGV--------MHT---------TGGYLVYAAMTFKyvFDYQEGETFWct 304
Cdd:PRK12467 3224 -GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVgvrhgalaNHLcwiaeayelDANDRVLLFMSFS--FDGAQERFLW-- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 305 advgwitghtylvygPLANGAKTILFEGVPNYPNTSRmsEVVDKHQVNILYTAPTAIRALMAKGneavEGTSRDSLRVMG 384
Cdd:PRK12467 3299 ---------------TLICGGCLVVRDNDLWDPEELW--QAIHAHRISIACFPPAYLQQFAEDA----GGADCASLDIYV 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPEAWEWY---------YKTIGNEQSPIVDTWWQTETGGIliaplPGATDLKPGsatRPFFGVQPALVDNMGNI 455
Cdd:PRK12467 3358 FGGEAVPPAAFEQVkrklkprglTNGYGPTEAVVTVTLWKCGGDAV-----CEAPYAPIG---RPVAGRSIYVLDGQLNP 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 456 IEGATDGNLVIldswpGQMRTVHGDH-------DRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRM 527
Cdd:PRK12467 3430 VPVGVAGELYI-----GGVGLARGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 528 GTAEIESALVAFDKIAEAAIVGIPHDiKGQAIYAYITLNDgefPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRS 607
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPAD---PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPN 3580
|
570
....*....|....*..
gi 515671996 608 GKIMRRILRKIATGDTG 624
Cdd:PRK12467 3581 GKVDRKALPDPDAKGSR 3597
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
84-615 |
2.59e-22 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 100.48 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAERGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVF 163
Cdd:cd05920 23 RSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 164 GGFSPEALSGRIIDSNSKVVITADEgvrggravplkknvdealtnpevkniekvvvfkrtggdvawHEHRDvwwHDAIA- 242
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDR-----------------------------------------HAGFD---HRALAr 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 243 NVSADCPpeemnaeDPLFILYTSGSTGKPKGVMHTTGGYlVYAAMTfkyvfdyqegetfwcTADVGWITGHT-YL----- 316
Cdd:cd05920 133 ELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRA---------------SAEVCGLDQDTvYLavlpa 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 ----------VYGPLANGAKTILfegVPNyPNTSRMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRD--SLRVMG 384
Cdd:cd05920 190 ahnfplacpgVLGTLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWL----DAAASRRADlsSLRLLQ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPEAWEWYYKTIGneqsPIVDTWWQTETGGILIAPLPGATDLKPGSATRPffgVQP----ALVDNMGNIIEGAT 460
Cdd:cd05920 262 VGGARLSPALARRVPPVLG----CTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 461 DGNLVILDSWpgqmrTVHG-----DHDrfeQTYFsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESA 535
Cdd:cd05920 335 EGELLTRGPY-----TIRGyyrapEHN---ARAF-TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENL 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 536 LVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNwvrKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 406 LLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRE---RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
2.74e-22 |
|
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: 98.25 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGGYLvyaamtfkyvfdyqegETFWCTADVGWITGH-TYLVYGPLA-----NGAKTILF 330
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI----------------ESFVCNEDLFNISGEdAILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 EG----VPNYPNTSRMSEVVDKHQVNILYTAPTAIRALmakgneAVEGTSRDSLRVMGSVGEPINPEAwewyYKTIGNE- 405
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 406 -QSPIVDTWWQTETGgiLIAPLPGATDLKPGSATRPFFGVQPALVDNMGNII-----------EGATDGNLVILDSWpgq 473
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIgkifvksemvfSGYVRGGFSNPDGW--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 474 mrtvhgdhdrfeqtyfstfkgmYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHD 553
Cdd:cd17633 210 ----------------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 554 IKGQ---AIYAYITLNdgefptaelHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 268 RFGEiavALYSGDKLT---------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-621 |
3.08e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.83 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 81 CIDRhLAERGDEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHT 160
Cdd:PLN02246 29 CFER-LSEFSDRPCLI----DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 161 VVFGGFSPEALSGRIIDSNSKVVITadegvrggravplkknvdealtnpEVKNIEKVVVFKRTGGD--VAWHEHRDVWWH 238
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKLIIT------------------------QSCYVDKLKGLAEDDGVtvVTIDDPPEGCLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 239 --DAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAmtfKYV------FDYQEGETFWCTADVGWI 310
Cdd:PLN02246 160 fsELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 311 TGHTYLVYGPLANGAkTIL----FEgvpnypnTSRMSEVVDKHQVNILYTAPTAIRALmAKgNEAVEGTSRDSLRVMGSV 386
Cdd:PLN02246 237 YSLNSVLLCGLRVGA-AILimpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AK-SPVVEKYDLSSIRMVLSG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 387 GEPINPEAWEWYYKTIGNeqSPIVDTWWQTETGGILIAPLPGA---TDLKPGSAtrpffgvqpalvdnmGNIIEGATdgn 463
Cdd:PLN02246 307 AAPLGKELEDAFRAKLPN--AVLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC---------------GTVVRNAE--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 464 LVILD---------SWPGQMrTVHGDH------DRFEQTYFSTFK-GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRM 527
Cdd:PLN02246 367 LKIVDpetgaslprNQPGEI-CIRGPQimkgylNDPEATANTIDKdGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 528 GTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRS 607
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIHKVFFVDSIPKAPS 522
|
570
....*....|....*
gi 515671996 608 GKIMRRILR-KIATG 621
Cdd:PLN02246 523 GKILRKDLRaKLAAG 537
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
107-619 |
3.36e-22 |
|
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: 100.48 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 107 TLTFNELHKEVCLFSNALKEqGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITA 186
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 187 DEGVRGGRAVPLKknvdEALTNPEVKNIEKVVvfkrtgGDVAWhehrdvwWHDAIANVSADCPPEEM---------NAED 257
Cdd:cd05909 86 KQFIEKLKLHHLF----DVEYDARIVYLEDLR------AKISK-------ADKCKAFLAGKFPPKWLlrifgvapvQPDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 258 PLFILYTSGSTGKPKGVMHTTGGYL--VYAAMTfkyVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFegvPN 335
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH---PN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 YPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEavEGTSrdSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQ 415
Cdd:cd05909 223 PLDYKKIPELIYDKKATILLGTPTFLRGYARAAHP--EDFS--SLRLVVAGAEKLKDTLRQEFQEKFG---IRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPLPgATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSwPGQMRTVHGDHdrfEQTYFSTFKGM 495
Cdd:cd05909 296 TECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEP---ELTSFAFGDGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 496 YFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL-VAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEfpTAE 574
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTD--PSS 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 515671996 575 LHKEVKNwvrKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 449 LNDILKN---AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
88-617 |
1.83e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 98.51 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 88 ERGDEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtvvFGGFS 167
Cdd:PLN02330 40 LYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGAN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 168 PEALSGRIID----SNSKVVITADegvrggravplkknvdeaLTNPEVKNIE-KVVVFKRT--GGDVAWHEHRDVwwHDA 240
Cdd:PLN02330 112 PTALESEIKKqaeaAGAKLIVTND------------------TNYGKVKGLGlPVIVLGEEkiEGAVNWKELLEA--ADR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 241 IANVSADcppEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETfwctADVGWIT-----GHTY 315
Cdd:PLN02330 172 AGDTSDN---EEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIPffhiyGITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 LVYGPLANGAKTILfegVPNYPNTSRMSEVVdKHQVNILYTAPTAIRALMAkgNEAVE--GTSRDSLRVMGSVGEPINPE 393
Cdd:PLN02330 245 ICCATLRNKGKVVV---MSRFELRTFLNALI-TQEVSFAPIVPPIILNLVK--NPIVEefDLSKLKLQAIMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 394 AWEWYYKTIGNEQspIVDTWWQTETGGILIAPlpGATDLKPGSATRPFFG-VQPALVDNMGNiiegaTDGNLVILDSWPG 472
Cdd:PLN02330 319 LLTAFEAKFPGVQ--VQEAYGLTEHSCITLTH--GDPEKGHGIAKKNSVGfILPNLEVKFID-----PDTGRSLPKNTPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 473 QM--RT---VHGDHDRFEQTYFSTFK-GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:PLN02330 390 ELcvRSqcvMQGYYNNKEETDRTIDEdGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 547 IVGIPHDIKGQAIYAYITLNdgefPTA-ELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 470 VVPLPDEEAGEIPAACVVIN----PKAkESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-619 |
2.59e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 97.54 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLyMPMVPE-----AAVAMLACTRIGavhtvVFGG 165
Cdd:PRK07638 16 NKIAIKEN------DRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEflqlfAGAAMAGWTCVP-----LDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 166 FSPEALSGRIIDSNSKVVITADegvrggravpLKKNvdeALTNPEVKNIEkvvvfkrtggdvaWHEhrdvwWHDAIANVS 245
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTER----------YKLN---DLPDEEGRVIE-------------IDE-----WKRMIEKYL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 ADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLvyaamtfkyvfdyqegETFWCTADVGWITGH-TYLVYGPLAN- 323
Cdd:PRK07638 133 PTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL----------------HSFDCNVHDFHMKREdSVLIAGTLVHs 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 324 ----GAKTILFEG-----VPNY-PNtsRMSEVVDKHQVNILYTAPTAIRALmAKGNEAVEgtsrDSLRVMGSVGEpinpe 393
Cdd:PRK07638 197 lflyGAISTLYVGqtvhlMRKFiPN--QVLDKLETENISVMYTVPTMLESL-YKENRVIE----NKMKIISSGAK----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 394 aWEWYYKTIGNEQSPIVDTW--WQTETGGILIAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEgatdgnlvildswP 471
Cdd:PRK07638 265 -WEAEAKEKIKNIFPYAKLYefYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQ-------------K 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTVHGDHDRFEQTYFS--------TFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIA 543
Cdd:PRK07638 331 GEIGTVYVKSPQFFMGYIIggvlarelNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVD 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515671996 544 EAAIVGIPHDIKGQAIYAYItlnDGEfptaELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK07638 411 EIVVIGVPDSYWGEKPVAII---KGS----ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
99-623 |
3.07e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.91 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 99 GDDP---ADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRI 175
Cdd:PRK06155 35 PDRPllvFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHIL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 176 IDSNSKVVITADEGVRGGRAVPLKknvDEALtnPEVKNIekvvvfkrtGGDVAWHEHRDVwwhDAIANVSAD--CPPEEM 253
Cdd:PRK06155 115 RNSGARLLVVEAALLAALEAADPG---DLPL--PAVWLL---------DAPASVSVPAGW---STAPLPPLDapAPAAAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTfkyvfdyqegetfwcTADVGWITGHTYLVYGPL------------ 321
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPLfhtnalnaffqa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 -ANGAKTILFEGVpnypNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRdsLRVMGSVGEPinPEAWEWYYK 400
Cdd:PRK06155 243 lLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHR--VRVALGPGVP--AALHAAFRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 401 TIGneqSPIVDTWWQTETGGILIAPLPGAtdlKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWPGQMRTvhgD 480
Cdd:PRK06155 315 RFG---VDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFAT---G 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 481 HDRFEQTYFSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAI 559
Cdd:PRK06155 386 YFGMPEKTVEAWRNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 560 YAYITLNDGefpTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI-ATGDT 623
Cdd:PRK06155 466 MAAVVLRDG---TALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQgVTADT 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-617 |
6.22e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TadegvrggravplkknvDEALTNPEVKNIEKVVVFKrtgGDVAWHEHRdvwwhdaianvsadcPPEEMNAEDPLFILYT 264
Cdd:PRK12316 3160 S-----------------QSHLRLPLAQGVQVLDLDR---GDENYAEAN---------------PAIRTMPENLAYVIYT 3204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGYLVYAAMTfkyvfdyqeGETFWCTADVGWITGHTY-------LVYGPLANGAkTILFEGVPNYP 337
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWM---------QQAYGLGVGDRVLQFTTFsfdvfveELFWPLMSGA-RVVLAGPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 338 NTSRMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRDSLRVMGSVGEPINPE------AWEWYYKTIGNEQSPIVD 411
Cdd:PRK12316 3275 DPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADlqqqvfAGLPLYNLYGPTEATITV 3350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 412 TWWQTETGGILIAPLpgatdlkpgsaTRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRTVHGDHD----RFEQT 487
Cdd:PRK12316 3351 THWQCVEEGKDAVPI-----------GRPIANRACYILDGSLEPVPVGALGELYL--GGEGLARGYHNRPGltaeRFVPD 3417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 488 YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVgiphDIKGQAIYAYITLND 567
Cdd:PRK12316 3418 PFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPED 3493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 515671996 568 gefPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 3494 ---EAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
1.08e-20 |
|
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: 93.49 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVGWITGhTYLVYGPLANGAKTILFEGVpny 336
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 337 pNTSRMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRD--SLRVMGSVGEPINPEAWEwyyKTIGNeqspivdTWW 414
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSFPPILSNLL----DAAEKSGVDlsSLRHVLGLDAPETIQRFE---ETTGA-------TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 415 ----QTETGG-ILIAPlpgATDlKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldswPGQMrTVHGDHDRFEQTYF 489
Cdd:cd17637 141 slygQTETSGlVTLSP---YRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV----RGPL-VFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 490 STFKGMYFTSDGARRDEDGYYWITGRV--DDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPhDIK-GQAIYAYITLN 566
Cdd:cd17637 212 TFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGEGIKAVCVLK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515671996 567 DGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 291 PGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
106-616 |
2.71e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 94.69 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 AdegvrggraVPLKKNVDEALTNPEVKniekvVVFkrtGGDVAWhehrdvwWHDAIANVSADCPPEemnAEDPL--FILY 263
Cdd:PRK13390 103 S---------AALDGLAAKVGADLPLR-----LSF---GGEIDG-------FGSFEAALAGAGPRL---TEQPCgaVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 264 TSGSTGKPKGV--------MHTTGGYLVYAAMTFkyvFDYQEGETFWCTADV------GWITghtyLVYgplANGAKTIL 329
Cdd:PRK13390 156 SSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIyhaaplRWCS----MVH---ALGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 330 FEGVpNYPNTSRMsevVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEP------------INPEAWEW 397
Cdd:PRK13390 226 AKRF-DAQATLGH---VERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdvkhamidwLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 398 YYKTIGNEQSPIVDTWWQTEtggiliaplpgatdlkPGSATRPFFGVQPALVDnmgniiegatDGNlvilDSWPGQMRTV 477
Cdd:PRK13390 302 YSSTEAHGMTFIDSPDWLAH----------------PGSVGRSVLGDLHICDD----------DGN----ELPAGRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 478 HGDHDRFEQTYFSTFKGM---------YFTSDG--ARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:PRK13390 352 YFERDRLPFRYLNDPEKTaaaqhpahpFWTTVGdlGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVA 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 547 IVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13390 432 VIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
109-618 |
4.11e-20 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 94.13 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITAde 188
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 189 gvrggravplKKNVDEALT-NPEVKNIEKVVVFKrtgGDVAWHEHRD----VWWHDAIANVSADCPPEEMNAEDPL-FIL 262
Cdd:cd17642 124 ----------KKGLQKVLNvQKKLKIIKTIIILD---SKEDYKGYQClytfITQNLPPGFNEYDFKPPSFDRDEQVaLIM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 263 YTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGH-TYLVYGPLANGAKTILfegVPNYPNTSR 341
Cdd:cd17642 191 NSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFgMFTTLGYLICGFRVVL---MYKFEEELF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 342 MSEVVDkHQVNILYTAPTaIRALMAKgNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGneQSPIVDTWWQTE-TGG 420
Cdd:cd17642 268 LRSLQD-YKVQSALLVPT-LFAFFAK-STLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFK--LPGIRQGYGLTEtTSA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 421 ILIAPlpgATDLKPGSATR--PFFGVQpaLVD-NMGNIIEGATDGNLVIldSWPGQMRTVHGDHdrfEQTYFSTFK-GMY 496
Cdd:cd17642 343 ILITP---EGDDKPGAVGKvvPFFYAK--VVDlDTGKTLGPNERGELCV--KGPMIMKGYVNNP---EATKALIDKdGWL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTaelH 576
Cdd:cd17642 413 HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT---E 489
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 515671996 577 KEVKNWVRKEIGPIA-TPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:cd17642 490 KEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
249-616 |
4.84e-20 |
|
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: 93.60 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 249 PPEEMNAEDplfILYTSGSTGKPKGVMHTTGGYLVYAAMTFKyvfdyqegetfwCTADVGWITGHTYLVYGPLANGAKTI 328
Cdd:cd05929 121 IEDEAAGWK---MLYSGGTTGRPKGIKRGLPGGPPDNDTLMA------------AALGFGPGADSVYLSPAPLYHAAPFR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 329 LFEGVPNYPNTSRMSE---------VVDKHQVNILYTAPTaIRALMAKGNEAVEGtSRD--SLRVMGSVGEPINPEA--- 394
Cdd:cd05929 186 WSMTALFMGGTLVLMEkfdpeeflrLIERYRVTFAQFVPT-MFVRLLKLPEAVRN-AYDlsSLKRVIHAAAPCPPWVkeq 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 395 ---------WEWYYKTIGNEQSPIVDTWWQTEtggiliaplpgatdlkPGSATRPFFGVQPALVDNMGNIIEGATdGNLV 465
Cdd:cd05929 264 widwggpiiWEYYGGTEGQGLTIINGEEWLTH----------------PGSVGRAVLGKVHILDEDGNEVPPGEI-GEVY 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 466 ILDSWPgqmRTVHGDHDRFEQTYFStfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEA 545
Cdd:cd05929 327 FANGPG---FEYTNDPEKTAAARNE--GGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDA 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 546 AIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 402 AVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
5.03e-20 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 91.94 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTIlfeGVPN 335
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT---GGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 YPNTSrMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTsrDSLRVMGSVGE-PINPEA--WEWyyktigNEQSPIVDT 412
Cdd:cd17635 78 TTYKS-LFKILTTNAVTTTCLVPTLLSKLVSELKSANATV--PSLRLIGYGGSrAIAADVrfIEA------TGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 413 WWQTETGGILIapLPGATDLKP-GSATRPFFGVQPALVDNMGNIIEGATDGNLVILDSWpgqmrTVHGDHDRFEQTYFST 491
Cdd:cd17635 149 YGLSETGTALC--LPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 492 FKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLN---DG 568
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASaelDE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 515671996 569 EFPTAELHKevknwVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 302 NAIRALKHT-----IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-620 |
7.56e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.37 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 48 WIKPFTQVKNTSFDPGHIDIrwfeDGTLNVSANCIDRHlaERGDEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQ 127
Cdd:PLN02574 17 WYSPETGIYSSKHPPVPLPS----DPNLDAVSFIFSHH--NHNGDTALI----DSSTGFSISYSELQPLVKSMAAGLYHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 128 -GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVrgGRAVPLKKNVdeaL 206
Cdd:PLN02574 87 mGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPV---I 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 207 TNPEVKNI-EKVVVFKRtggdvawhehrdvwWHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYA 285
Cdd:PLN02574 162 GVPENYDFdSKRIEFPK--------------FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 286 AMTFKY---VFDYQEGETFWCTA-DVGWITGHTYLVYGPLANGAKTILFEGVpnypNTSRMSEVVDKHQVNILYTAPTAI 361
Cdd:PLN02574 228 ELFVRFeasQYEYPGSDNVYLAAlPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 362 RALMaKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIgneqsPIVD---TWWQTETGGILIAPLPGATDLKPGSAT 438
Cdd:PLN02574 304 MALT-KKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDfiqGYGMTESTAVGTRGFNTEKLSKYSSVG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 439 RPFFGVQPALVD-NMGNIIEGATDGNLVIldSWPGQMRTVHGDHdrfEQTYFSTFK-GMYFTSDGARRDEDGYYWITGRV 516
Cdd:PLN02574 378 LLAPNMQAKVVDwSTGCLLPPGNCGELWI--QGPGVMKGYLNNP---KATQSTIDKdGWLRTGDIAYFDEDGYLYIVDRL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 517 DDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVL 596
Cdd:PLN02574 453 KEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPYKKVRKV 529
|
570 580
....*....|....*....|....
gi 515671996 597 HWTDSLPKTRSGKIMRRILRKIAT 620
Cdd:PLN02574 530 VFVQSIPKSPAGKILRRELKRSLT 553
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-615 |
3.70e-19 |
|
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: 90.39 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17652 2 DAPAVV------FGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcpp 250
Cdd:cd17652 76 IAYMLADARPALLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 eemNAEDPLFILYTSGSTGKPKGVM--HTTGGYLVYAAMTFkyvFDYQEGE------------TFW--CTAdvgWITGHT 314
Cdd:cd17652 91 ---TPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSrvlqfaspsfdaSVWelLMA---LLAGAT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 yLVYGPlangAKTILFeGVPnypntsrMSEVVDKHQVNILYTAPTAIRALmakgneavEGTSRDSLRVMGSVGEPINPEa 394
Cdd:cd17652 162 -LVLAP----AEELLP-GEP-------LADLLREHRITHVTLPPAALAAL--------PPDDLPDLRTLVVAGEACPAE- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 395 wewyyktigneqspIVDTWWQ----------TET--GGILIAPLPGATDLKPGsatRPFFGVQPALVDNMGNIIEGATDG 462
Cdd:cd17652 220 --------------LVDRWAPgrrminaygpTETtvCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLVIldSWPGQMRTVHGDHD----RFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:cd17652 283 ELYI--AGAGLARGYLNRPGltaeRFVADPFGAPGSrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALT 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 538 AFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 361 EHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
4.13e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 91.47 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV--- 158
Cdd:PRK08279 43 FEEAAARHPDRPALLFE------DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 -HTVVFGgfspEALSGRIIDSNSKVVITADEgvrggravpLKKNVDEALtnPEVKNIEKVVVFkrtGGDVAWHEHRDVWW 237
Cdd:PRK08279 117 lNTQQRG----AVLAHSLNLVDAKHLIVGEE---------LVEAFEEAR--ADLARPPRLWVA---GGDTLDDPEGYEDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 238 HDAIANVSADCPPE--EMNAEDPLFILYTSGSTGKPK-GVMH---TTGGYLVYAAMTfkyvfDYQEGETFWCTADVGWIT 311
Cdd:PRK08279 179 AAAAAGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPKaAVMShmrWLKAMGGFGGLL-----RLTPDDVLYCCLPLYHNT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 312 GHTYLVYGPLANGAKTIL---FegvpnypNTSRMSEVVDKHQVnilyTAPTAI----RALMakgNEAVEGTSRD-SLRVM 383
Cdd:PRK08279 254 GGTVAWSSVLAAGATLALrrkF-------SASRFWDDVRRYRA----TAFQYIgelcRYLL---NQPPKPTDRDhRLRLM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 384 gsVGEPINPEAWEWYYKTIGNEQspIVDTWWQTE--TGGILIAPLPGATDLKPGSATRPFfgvqpALV----DNmGNIIE 457
Cdd:PRK08279 320 --IGNGLRPDIWDEFQQRFGIPR--ILEFYAASEgnVGFINVFNFDGTVGRVPLWLAHPY-----AIVkydvDT-GEPVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 GAtDGNLV-------------ILDSWP--GqmrtvHGD---------HDRFEqtyfstfKG-MYF-TSDGARRDEDGYYW 511
Cdd:PRK08279 390 DA-DGRCIkvkpgevglligrITDRGPfdG-----YTDpeasekkilRDVFK-------KGdAWFnTGDLMRDDGFGHAQ 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 512 ITGRVDDVL-----NVSghrmgTAEIESALVAFDKIAEAAIVG--IP-HDikGQAIYAYITLNDG-EFPTAELHKEVK 580
Cdd:PRK08279 457 FVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGveVPgTD--GRAGMAAIVLADGaEFDLAALAAHLY 527
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
237-622 |
4.25e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 90.90 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 WHDAIA-NVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMhTTGGYLVYAAMTFKYVFDYQEGETFWCTAD--------V 307
Cdd:PRK07867 132 WADELAaHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 308 GWITGhtylvygpLANGAKTIL---FEGVPNYPNTSRM----SEVVDKHQVNILYTAP------TAIRALMakGNEAVEG 374
Cdd:PRK07867 211 GWAVA--------LAAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPErpddadNPLRIVY--GNEGAPG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 375 TSRDSLRVMGSVgepinpeawewyyktigneqspIVDTWWQTEtGGILIAPLPGAtdlKPGSATRPFFGVQ--------- 445
Cdd:PRK07867 281 DIARFARRFGCV----------------------VVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgte 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 446 --PALVDNMGNIIEGATDGNLVILDSwPGQMRTVHGDHDRFEQtyfSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK07867 335 cpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 524 GHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDG---------EFPTAelhkevknwvRKEIGPIATPD 594
Cdd:PRK07867 411 GENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGakfdpdafaEFLAA----------QPDLGPKQWPS 480
|
410 420 430
....*....|....*....|....*....|
gi 515671996 595 VLHWTDSLPKTRSGKIMRRILRK--IATGD 622
Cdd:PRK07867 481 YVRVCAELPRTATFKVLKRQLSAegVDCAD 510
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-619 |
5.40e-19 |
|
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: 90.29 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 81 CIDRHLAERGDEVAI-IWEGDdpaddktLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAvh 159
Cdd:cd05918 4 LIEERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 160 TVVFGGFS-PEA-LSGRIIDSNSKVVITADegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvww 237
Cdd:cd05918 75 AFVPLDPShPLQrLQEILQDTGAKVVLTSS-------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 238 hdaianvsadcppeemnAEDPLFILYTSGSTGKPKGVM--HTTggyLVYAAMTFKYVFDYQEG--------ETFwctaDV 307
Cdd:cd05918 105 -----------------PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSEsrvlqfasYTF----DV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 308 gwitgHTYLVYGPLANGAkTILfegVPnyPNTSRMS---EVVDKHQVNILYTAPTAIRALmakGNEAVEgtsrdSLRVMG 384
Cdd:cd05918 161 -----SILEIFTTLAAGG-CLC---IP--SEEDRLNdlaGFINRLRVTWAFLTPSVARLL---DPEDVP-----SLRTLV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPEawewyyktigneqspIVDTWWQ----------TET--GGILIAPLPGATDLKPGSAtrpfFGVQPALVDNm 452
Cdd:cd05918 222 LGGEALTQS---------------DVDTWADrvrlinaygpAECtiAATVSPVVPSTDPRNIGRP----LGATCWVVDP- 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 453 GNIIE----GATdGNLVIldSWPGQMRtvhGDHDRFEQTYFSTFKG--------------MYFTSDGARRDEDG--YYwi 512
Cdd:cd05918 282 DNHDRlvpiGAV-GELLI--EGPILAR---GYLNDPEKTAAAFIEDpawlkqegsgrgrrLYRTGDLVRYNPDGslEY-- 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 513 TGRVDDVLNVSGHRMGTAEIESAL---VAFDKIAEAAIVGIPHDIKGQAIYAYITLnDGEFPTAELHKEVKNWVRKEIGP 589
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLrqsLPGAKEVVVEVVKPKDGSSSPQLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRA 432
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 515671996 590 IAT---------------PDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05918 433 LVAelrsklrqrlpsymvPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-617 |
7.46e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 81 CIDRHLAERG----DEVAIIWegddpaDDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIG 156
Cdd:PRK12316 4552 CVHQLVAERArmtpDAVAVVF------DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 157 AVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGgraVPLKKNVDEaltnpevkniekvVVFKRTGGdvawhehrdvw 236
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR---LPIPDGLAS-------------LALDRDED----------- 4678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 WHDaianVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTfkyvfdyqeGETFWCTAD--VGWITGHT 314
Cdd:PRK12316 4679 WEG----FPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDdrVLQFMSFS 4745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 YLV-----YGPLANGAKTILFEgvPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSrdsLRVMGSVGEP 389
Cdd:PRK12316 4746 FDGsheglYHPLINGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPS---LRVYCFGGEA 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 390 INPEAWEWYYKTIGNEQspIVDTWWQTETggiLIAPLPGAT--DLKPGSATRPFFGVQPA----LVDNMGNIIEGATDGN 463
Cdd:PRK12316 4821 VAQASYDLAWRALKPVY--LFNGYGPTET---TVTVLLWKArdGDACGAAYMPIGTPLGNrsgyVLDGQLNPLPVGVAGE 4895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 464 LVIldswpGQMRTVHGDH-------DRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESA 535
Cdd:PRK12316 4896 LYL-----GGEGVARGYLerpaltaERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEAR 4970
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 536 LVAFDKIAEAAIVGIPHDIkGQAIYAYIT-----LNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK12316 4971 LREHPAVREAVVIAQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
....*..
gi 515671996 611 MRRILRK 617
Cdd:PRK12316 5050 DRKALPQ 5056
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
249-616 |
7.78e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 89.66 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 249 PPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGylvyAAMTFKYVFDYQEgetfWCTADV-----------GWITGhtylV 317
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRA----IAADLDALAEAWQ----WTADDVlvhglplfhvhGLVLG----V 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 YGPL--------------------ANGAKTILFeGVPnypnT--SRMSEvvdkhqvnilytAPTAIRALmakgneaveGT 375
Cdd:PRK07787 189 LGPLrignrfvhtgrptpeayaqaLSEGGTLYF-GVP----TvwSRIAA------------DPEAARAL---------RG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 376 SRdsLRVMGSVGEPInPEAwEWYYKTIGNEqspIVDTWWQTETGGILIAPLPGatDLKPGSATRPFFGVQPALVDNMGNI 455
Cdd:PRK07787 243 AR--LLVSGSAALPV-PVF-DRLAALTGHR---PVERYGMTETLITLSTRADG--ERRPGWVGLPLAGVETRLVDEDGGP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 456 I--EGATDGNLvildswpgQMR--TVH-GDHDRFEQTYFS-TFKGMYFTSDGARRDEDGYYWITGRVD-DVLNVSGHRMG 528
Cdd:PRK07787 314 VphDGETVGEL--------QVRgpTLFdGYLNRPDATAAAfTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 529 TAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGefPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:PRK07787 386 AGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAAD---ELIDFVAQQLSVHKRPREVRFVDALPRNAMG 460
|
....*...
gi 515671996 609 KIMRRILR 616
Cdd:PRK07787 461 KVLKKQLL 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
237-643 |
1.83e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 WHDAIANVSADCPPEEMNAEDPL-FILYTSGSTGKPKGVMHTTGGYL-------VYAAMTFKYVFDYQEGETFwctaDVG 308
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLnnqlskvPYLALSEADVIAQTASQSF----DIS 3924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 309 -WitghtYLVYGPLAnGAKTilfEGVPN---YPNTSRMSEVVDKhQVNILYTAPTAIRALMAKGNEAVegtsrDSLRVMG 384
Cdd:PRK05691 3925 vW-----QFLAAPLF-GARV---EIVPNaiaHDPQGLLAHVQAQ-GITVLESVPSLIQGMLAEDRQAL-----DGLRWML 3989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 385 SVGEPINPE-AWEWY--YKTIGneqspIVDTWWQTETggiliaplpgatdlkpgSATRPFFGVQPALVDNMGNIIEGATD 461
Cdd:PRK05691 3990 PTGEAMPPElARQWLqrYPQIG-----LVNAYGPAEC-----------------SDDVAFFRVDLASTRGSYLPIGSPTD 4047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 462 GN-LVILD----------------SWPGQMRTVHGDHDRFEQTYFSTFKG-----MYFTSDGARRDEDGYYWITGRVDDV 519
Cdd:PRK05691 4048 NNrLYLLDealelvplgavgelcvAGTGVGRGYVGDPLRTALAFVPHPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 520 LNVSGHRMGTAEIESALVAFDKIAEAAiVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWT 599
Cdd:PRK05691 4128 VKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWL 4206
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 515671996 600 DSLPKTRSGKIMRRILRKIatgDTGNLGDTSTLADPSVVDKLIA 643
Cdd:PRK05691 4207 DRLPLNANGKLDRKALPAL---DIGQLQSQAYLAPRNELEQTLA 4247
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-617 |
2.22e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.40 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 87 AERGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGF 166
Cdd:PRK12316 2014 ARAPEAIAVV------FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 167 SPEALSGRIIDSNSKVVITadegvrggravplKKNVDEALTNPEvknieKVVVFKRTggdvawhehRDVWWHDaianvSA 246
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLT-------------QRHLLERLPLPA-----GVARLPLD---------RDAEWAD-----YP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 247 DCPPEEMNAEDPL-FILYTSGSTGKPKGV----------MHTTGGYL-------VYAAMTFKyvFDYQEGETFWctadvg 308
Cdd:PRK12316 2136 DTAPAVQLAGENLaYVIYTSGSTGLPKGVavshgalvahCQAAGERYelspadcELQFMSFS--FDGAHEQWFH------ 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 309 witghtylvygPLANGAKTILFEGVPNYPntSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGtSRDSLRVMGSVGE 388
Cdd:PRK12316 2208 -----------PLLNGARVLIRDDELWDP--EQLYDEMERHGVTILDFPPVYLQQLAE--HAERDG-RPPAVRVYCFGGE 2271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 389 PINPEAWEWYYKTIGNEQspIVDTWWQTETggiLIAPL---PGATDlkPGSATRPFFGVqpALVDNMGNIIEGATD---- 461
Cdd:PRK12316 2272 AVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLlwkCRPQD--PCGAAYVPIGR--ALGNRRAYILDADLNllap 2342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 462 ---GNLVIldswpGQMRTVHGDHDRFEQT--------YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTA 530
Cdd:PRK12316 2343 gmaGELYL-----GGEGLARGYLNRPGLTaerfvpdpFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELG 2417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 531 EIESALVAFDKIAEAAIVGIpHDIKGQAIYAYITLNDgefPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK12316 2418 EIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDD---AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
....*..
gi 515671996 611 MRRILRK 617
Cdd:PRK12316 2494 DRKALPK 2500
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
5.06e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 87.63 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAERGDEVAIIWEGDDPAddktLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVVTADRIA----ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 159 HTVVFGGFSPEALSGRIIDSNSKVVITADEGVrGGRAVPLKKNVDEALTnpevkniekvVVFKRTGGDVAWHEHRDvwwh 238
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVVLIDADGP-HDRAEPTTRWWPLTVN----------VGGDSGPSGGTLSVHLD---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 239 DAIANVSADCPPEEMNAEDPLfILYTSGSTGKPKGVMHTTGGYlvyAAMTFKYVFDYQEGETFWCTADVGWITGHTYL-- 316
Cdd:PRK05852 160 AATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 VYGPLANGAKTILfegvpnyPNTSRMSEVV---DKHQVN-ILYTA-PTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPIN 391
Cdd:PRK05852 236 LLATLASGGAVLL-------PARGRFSAHTfwdDIKAVGaTWYTAvPTIHQILLERAATEPSGRKPAALRFIRSCSAPLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 392 PEAWEWYYKTIGneqSPIVDTWWQTET---------GGILIAPLPGATDLKPGSATrpffGVQPALVDNMGNIIEGATDG 462
Cdd:PRK05852 309 AETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLVIldSWPGQMRTVHGDHdrfEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKI 542
Cdd:PRK05852 382 EVWL--RGTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 543 AEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK05852 457 MEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
3.50e-17 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 83.32 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 261 ILYTSGSTGKPKGVM--HTTGgYLVYAAmtfkyvfdyqegetfWCtaDVGWIT-GHTYLVYGPLAN------GAKTILFE 331
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPFFHtfgykaGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 332 GVPNYP----NTSRMSEVVDKHQVNILYTAPTAIRALMakGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEQs 407
Cdd:cd17638 67 GATVVPvavfDVDAILEAIERERITVLPGPPTLFQSLL--DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFET- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 408 pIVDTWWQTETG-GILIAPLPGATDLKPGSAtRPFFGVQPALVDNmGNIIEGATDGNLVILDSWPGQMRTVHGDhdrfeq 486
Cdd:cd17638 144 -VLTAYGLTEAGvATMCRPGDDAETVATTCG-RACPGFEVRIADD-GEVLVRGYNVMQGYLDDPEATAEAIDAD------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 487 tyfstfkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLN 566
Cdd:cd17638 215 -------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515671996 567 DGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 288 PGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
92-617 |
7.28e-17 |
|
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: 84.02 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 92 EVAIIWEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEAL 171
Cdd:cd05915 9 GRKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 172 SGRIIDSNSKVVITADEGVR-GGRAVPLKKNVDEaltNP-EVKNIEKVVVFKRTGGdvawhehrdvwwhdaiANVSADCP 249
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLPlVEAIRGELKTVQH---FVvMDEKAPEGYLAYEEAL----------------GEEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 250 PEEMnaeDPLFILYTSGSTGKPKGVMHT-TGGYLVYAAMTFKYVFDYQEGETFWCTADVGWITGHTYlVYGPLANGAKTI 328
Cdd:cd05915 150 VPER---AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCL-PYAATLVGAKQV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 329 LFEGVPNypnTSRMSEVVDKHQVNILYTAPTAIRaLMAKGNEAVEGTSRDSLRVMGSVGEPinPEAWeWYYKTIGNEQsp 408
Cdd:cd05915 226 LPGPRLD---PASLVELFDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVE-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 409 IVDTWWQTETGGILIA----------PLPGATDLKPGSATRPFFGVQPALVDNMGNIiegATDGNLVILDSWPGQMrTVH 478
Cdd:cd05915 297 VRQGYGLTETSPVVVQnfvkshleslSEEEKLTLKAKTGLPIPLVRLRVADEEGRPV---PKDGKALGEVQLKGPW-ITG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 GDHDRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQ 557
Cdd:cd05915 373 GYYGNEEATRSALTPDgFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 558 AIYAYITLNDGEfptaELHKEVKNWVRKEIGPIAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 453 RPLAVVVPRGEK----PTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-615 |
1.54e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGE------QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITadegvrggravplkknvdEALTNPEVKNIEKVVVFKRTGGDvAWHEHRDvwwhdai 241
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT------------------QSHLQARLPLPDGLRSLVLDQED-DWLEGYS------- 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 anvsaDCPPEEMNAEDPL-FILYTSGSTGKPKGVMHTTGGYL-VYAAMtfkyvfdyqeGETFWCTADVGWITGHTYL--- 316
Cdd:PRK12467 1708 -----DSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT----------QEAYQLSAADVVLQFTSFAfdv 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 ----VYGPLANGAKTILfegVPnyPNTSRMSE----VVDKHQVNILYTAPTAIRALMaKGNEAVEGTSrdSLRVMGSVGE 388
Cdd:PRK12467 1773 svweLFWPLINGARLVI---AP--PGAHRDPEqliqLIERQQVTTLHFVPSMLQQLL-QMDEQVEHPL--SLRRVVCGGE 1844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 389 PINPEAWEWYYKTIGNEQspIVDTWWQTETGgilIAPLPGATDLKP--GSATRPfFGVqpaLVDNMGNIIegaTDGNL-- 464
Cdd:PRK12467 1845 ALEVEALRPWLERLPDTG--LFNLYGPTETA---VDVTHWTCRRKDleGRDSVP-IGQ---PIANLSTYI---LDASLnp 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 465 ----VILDSWPGQMRTVHGDH-------DRFEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:PRK12467 1913 vpigVAGELYLGGVGLARGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 533 ESALVAFDKIAEAAIvgIPHD-IKGQAIYAYITLNDGEFPTAE-----LHKEVKNWVRKEIGPIATPDVLHWTDSLPKTR 606
Cdd:PRK12467 1993 EARLREQGGVREAVV--IAQDgANGKQLVAYVVPTDPGLVDDDeaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTP 2070
|
....*....
gi 515671996 607 SGKIMRRIL 615
Cdd:PRK12467 2071 NGKLDRKAL 2079
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
106-616 |
2.45e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.50 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNAL-KEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSK-VV 183
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 184 ITAD-----EGV---RGGRAV----------PLKKnvdeALTNPEVKNIEKVVVfkrtggdvAWHEHRDVWWHDAIANvS 245
Cdd:PRK05677 128 CLANmahlaEKVlpkTGVKHVivtevadmlpPLKR----LLINAVVKHVKKMVP--------AYHLPQAVKFNDALAK-G 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 246 ADCPPEEMN--AEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVF--DYQEG-ETFWCTADVGWITGHTYLVYGP 320
Cdd:PRK05677 195 AGQPVTEANpqADDVAVLQYTGGTTGVAKGAMLTHRN-LVANMLQCRALMgsNLNEGcEILIAPLPLYHIYAFTFHCMAM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 321 LANGAKTILfegVPNYPNTSRMSEVVDKHQvnilYTAPTAIRALMAK--GNEAVEGTSRDSLRVMGSVGEPINPEAWEWY 398
Cdd:PRK05677 274 MLIGNHNIL---ISNPRDLPAMVKELGKWK----FSGFVGLNTLFVAlcNNEAFRKLDFSALKLTLSGGMALQLATAERW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 399 YKTIGneqSPIVDTWWQTETGGIliAPLPGATDLKPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMRtvh 478
Cdd:PRK05677 347 KEVTG---CAICEGYGMTETSPV--VSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV--KGPQVMK--- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 GDHDRFEQTYFS-TFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQ 557
Cdd:PRK05677 417 GYWQRPEATDEIlDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 558 AIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK05677 497 AIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
3.86e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 81.72 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV-HTVVFGGFsPEALSGRIIDSNSKVVITaD 187
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINHAEDRVVIT-D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EGVrggraVPLKknvdEALTnPEVKNIEKVVVFKRTGGDVAWHEHRDVWWHDAIANVSADCPPEEMNAEDPLFILYTSGS 267
Cdd:PRK06018 119 LTF-----VPIL----EKIA-DKLPSVERYVVLTDAAHMPQTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 268 TGKPKGVMHTTGGYLVYAAMTFKyvfdyqegetfwctADV-GWITGHTYLVYGPL--AN-----------GAKTIL---- 329
Cdd:PRK06018 189 TGDPKGVLYSHRSNVLHALMANN--------------GDAlGTSAADTMLPVVPLfhANswgiafsapsmGTKLVMpgak 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 330 FEGVPNYpntsrmsEVVDKHQVNILYTAPTAirALMAKGNEAVEGTSRDSLRVMGSVGEPInPEAWEWYYKTIGNEqspI 409
Cdd:PRK06018 255 LDGASVY-------ELLDTEKVTFTAGVPTV--WLMLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVE---V 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 410 VDTWWQTETGGI-LIAPLPGATDLKPGSAT--------RPFFGVQPALVDNMGNII--EGATDGNLVIldSWPgqmrTVH 478
Cdd:PRK06018 322 RHAWGMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGVEMKITDDAGKELpwDGKTFGRLKV--RGP----AVA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 GDHDRFEQTYFSTfKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQA 558
Cdd:PRK06018 396 AAYYRVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDER 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 515671996 559 IYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 475 PLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
82-617 |
5.94e-16 |
|
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: 80.43 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:cd17653 3 FERIAAAHPDAVAVESLGG------SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGfSPEALSGRIID-SNSKVVITADegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhda 240
Cdd:cd17653 77 LDAK-LPSARIQAILRtSGATLLLTTD----------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 241 ianvsadcppeemNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYA---------------AMTFKYVFDYQEGETFWCta 305
Cdd:cd17653 103 -------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsqpparldvgpgsrvAQVLSIAFDACIGEIFST-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 306 dvgwitghtylvygpLANGAKTILFEGVPNYPNTSRmsevvdkhQVNILYTAPTAIRALmakgneavEGTSRDSLRVMGS 385
Cdd:cd17653 168 ---------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL--------SPQDFPNLKTIFL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 386 VGEPINP---EAWeWYYKTIGNEQSP----IVDTWWQTETGG--ILIAPLPGATD--LKPGsatrpffgVQPALVDNMGN 454
Cdd:cd17653 217 GGEAVPPsllDRW-SPGRRLYNAYGPtectISSTMTELLPGQpvTIGKPIPNSTCyiLDAD--------LQPVPEGVVGE 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 455 I-IEGA--TDGNLvildswPGQMRTVhgdhDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAE 531
Cdd:cd17653 288 IcISGVqvARGYL------GNPALTA----SKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 532 IESALVAFDKIAE--AAIVgiphdiKGQAIYAYITlndgefpTAELHKE-VKNWVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:cd17653 358 IEEVVLQSQPEVTqaAAIV------VNGRLVAFVT-------PETVDVDgLRSELAKHLPSYAVPDRIIALDSFPLTANG 424
|
....*....
gi 515671996 609 KIMRRILRK 617
Cdd:cd17653 425 KVDRKALRE 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-622 |
7.88e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.98 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 90 GDEVAIIWEGDDPAddkTLTFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtvvfggFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQE---QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAV-------FNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 169 --EALSG----RIIDSNSKVVITADEGvrggravpLKKNVDEALtnPEVKNIEKVVVfkrTGGDVAWHEHRDVWWHDAIA 242
Cdd:PRK05620 94 lnKQLMNdqivHIINHAEDEVIVADPR--------LAEQLGEIL--KECPCVRAVVF---IGPSDADSAAAHMPEGIKVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 243 NV-------SADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYV--FDYQEGETFWCTADVgwitgH 313
Cdd:PRK05620 161 SYealldgrSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRS-LYLQSLSLRTTdsLAVTHGESFLCCVPI-----Y 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 314 TYLVYG-PLA---NGAKtILFEGVPNYPNTsrMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSVGEP 389
Cdd:PRK05620 235 HVLSWGvPLAafmSGTP-LVFPGPDLSAPT--LAKIIATAMPRVAHGVPTLWIQLMV--HYLKNPPERMSLQEIYVGGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 390 INP---EAWEWYYKTigneqsPIVDTWWQTETG--GILIAPLPGATdlkpGSATRPFFGVQ---PA----LVDNMGNIIE 457
Cdd:PRK05620 310 VPPiliKAWEERYGV------DVVHVWGMTETSpvGTVARPPSGVS----GEARWAYRVSQgrfPAsleyRIVNDGQVME 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 gATDGNLVILdswpgQMR--TVHG----DHDRFEQTYFSTFKGMY-------FTSDGARR-------DEDGYYWITGRVD 517
Cdd:PRK05620 380 -STDRNEGEI-----QVRgnWVTAsyyhSPTEEGGGAASTFRGEDvedandrFTADGWLRtgdvgsvTRDGFLTIHDRAR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 518 DVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLH 597
Cdd:PRK05620 454 DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWT 533
|
570 580
....*....|....*....|....*.
gi 515671996 598 WTDSLPKTRSGKIMRRILRK-IATGD 622
Cdd:PRK05620 534 FVDEIDKTSVGKFDKKDLRQhLADGD 559
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
9.88e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.46 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 WHDAIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYA-AMTFKYvfDYQEGETFWCTADV-------- 307
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLfhsnavma 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 308 GWitghtylvyGP-LANGAKTILfegvPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRdsLRVmgSV 386
Cdd:PRK13388 209 GW---------APaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 387 GEPINPEAWEWYYKTIGNEqspIVDTWWQTETGGILIAPlPGAtdlKPGSATRPFFGVqpaLVDNMGNIIEGAT-----D 461
Cdd:PRK13388 272 GNEASPRDIAEFSRRFGCQ---VEDGYGSSEGAVIVVRE-PGT---PPGSIGRGAPGV---AIYNPETLTECAVarfdaH 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 462 GNLVILDSWPGQMRTVHGDhDRFEQTYFS-------TFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK13388 342 GALLNADEAIGELVNTAGA-GFFEGYYNNpeataerMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 535 ALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGE-FPTAELHKEVKNwvRKEIGPIATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK13388 421 ILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAtFDPDAFAAFLAA--QPDLGTKAWPRYVRIAADLPSTATNKVLKR 498
|
...
gi 515671996 614 ILR 616
Cdd:PRK13388 499 ELI 501
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
106-616 |
3.30e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 78.94 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALK-EQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK08974 47 EVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 tadegVRGGRAVPLKKNVDEA--------------------LTNPEVKNIEKVV---------VFKRtggdvAWHEHRDV 235
Cdd:PRK08974 127 -----IVSNFAHTLEKVVFKTpvkhviltrmgdqlstakgtLVNFVVKYIKRLVpkyhlpdaiSFRS-----ALHKGRRM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 236 WWhdaianVSADcppeeMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFD--YQEGETFWCTADvgwitgH 313
Cdd:PRK08974 197 QY------VKPE-----LVPEDLAFLQYTGGTTGVAKGAMLTHRN-MLANLEQAKAAYGplLHPGKELVVTAL------P 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 314 TYLVYGPLAN-------GAKTILFEGVPNYPNTsrMSEVvDKHQVNILYTAPTAIRALMakGNEAVEGTSRDSLRVmgSV 386
Cdd:PRK08974 259 LYHIFALTVNcllfielGGQNLLITNPRDIPGF--VKEL-KKYPFTAITGVNTLFNALL--NNEEFQELDFSSLKL--SV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 387 GEpinpeawewyyktiGNEQSPIVDTWWQTETGGILI--------APLPGAT--DLK--PGSATRPFFGVQPALVDNMGN 454
Cdd:PRK08974 332 GG--------------GMAVQQAVAERWVKLTGQYLLegygltecSPLVSVNpyDLDyySGSIGLPVPSTEIKLVDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 455 IIEGATDGNLVIldSWPGQMRtvhGDHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK08974 398 EVPPGEPGELWV--KGPQVML---GYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 535 ALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFpTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK08974 473 VVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSL-TEE---ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRE 548
|
..
gi 515671996 615 LR 616
Cdd:PRK08974 549 LR 550
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
100-615 |
3.42e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 79.70 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 100 DDPA---DDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRII 176
Cdd:PRK10252 473 DAPAladARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 177 DSNSKVVITADEgvrggravplkknvdealtnpevkniekvVVFKRTGGDVAWHEHRDVWWHDAIANVSADCPPeemnaE 256
Cdd:PRK10252 553 DARPSLLITTAD-----------------------------QLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQP-----H 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVM--HTT-GGYLVYaaMTFKY--------------VFDYQEGETFWctadvgwitghtylvyg 319
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMvgQTAiVNRLLW--MQNHYpltaddvvlqktpcSFDVSVWEFFW----------------- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 320 PLANGAKTILFEgvpnyPNTSR----MSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAW 395
Cdd:PRK10252 660 PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLC 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 396 EWYYKTIG----NEQSPI---VD-TWWqtETGGILIAPLPGAtdlkPGSATRPFFGVQPALVDNMGNIIEGATDGNLVIl 467
Cdd:PRK10252 735 REWQQLTGaplhNLYGPTeaaVDvSWY--PAFGEELAAVRGS----SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYL- 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 468 dswpGQMRTVHGDHDRFEQTY-------FSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFD 540
Cdd:PRK10252 808 ----TGIQLAQGYLGRPDLTAsrfiadpFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALP 883
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 541 KIAEAAIV------GIPHDIKGQAIYAYITLNDGEFPTAELHKEvknWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK10252 884 DVEQAVTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQA---QLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA 960
|
.
gi 515671996 615 L 615
Cdd:PRK10252 961 L 961
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
105-616 |
1.13e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 77.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADEGVRGGRAVPLKKNVDE--------------ALTNPEVKNIEKVVVfkrtggdvAWHEHRDVWWHDAIA-NVSADCP 249
Cdd:PRK07059 126 VLENFATTVQQVLAKTAVKHvvvasmgdllgfkgHIVNFVVRRVKKMVP--------AWSLPGHVRFNDALAeGARQTFK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 250 PEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYL---------VYAAMTFKyvfDYQEGETFWCTADVGWITGHTYLVYGP 320
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawLQPAFEKK---PRPDQLNFVCALPLYHIFALTVCGLLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 321 LANGAKTILfegVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMakGNEAVEGTSRDSLRV-----MgSVGEPInpeAW 395
Cdd:PRK07059 275 MRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALL--NNPDFDKLDFSKLIVangggM-AVQRPV---AE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 396 EWYYKTigneQSPIVDTWWQTETGGILIAPLPGATDLKpGSATRPFFGVQPALVDNMGNIIEGATDGNLVIldSWPGQMR 475
Cdd:PRK07059 346 RWLEMT----GCPITEGYGLSETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICI--RGPQVMA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 476 tvhGDHDRFEQTYFSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDI 554
Cdd:PRK07059 419 ---GYWNRPDETAKVMTADGFFrTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 555 KGQAIYAYITLNDGEFpTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07059 496 SGEAVKLFVVKKDPAL-TEE---DVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
1.13e-14 |
|
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: 76.95 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEgddpadDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVItadegvrggravplkknVDEALTnpevkniekvvvfkrtggdvawhehrdvwWHDAI 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-----------------VDREFE-----------------------------YEDLL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 242 ANVSADCPPEEMNAE-DPLFILYTSGSTGKPKGVMHT-TGGYLvyAAMTFKYVFDYQEGETFWCTADV----GWitghTY 315
Cdd:cd12118 118 AEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGW----CF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 lVYGPLANGAKTILFEGVpNYPNTSRMsevVDKHQVNILYTAPTAIRALmAKGNEAVEGTSRDSLRVMgSVGEPinPEAw 395
Cdd:cd12118 192 -PWTVAAVGGTNVCLRKV-DAKAIYDL---IEKHKVTHFCGAPTVLNML-ANAPPSDARPLPHRVHVM-TAGAP--PPA- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 396 ewyyKTIGNEQS---PIVDTWWQTET-GGILIAP-------LPgaTDLKPGSATR---PFFGVQPALVDNMGNIIEGATD 461
Cdd:cd12118 262 ----AVLAKMEElgfDVTHVYGLTETyGPATVCAwkpewdeLP--TEERARLKARqgvRYVGLEEVDVLDPETMKPVPRD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 462 GNLVildswpGQ--MR--TVHGDHDRFEQTYFSTFKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:cd12118 336 GKTI------GEivFRgnIVMKGYLKNPEATAEAFRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 537 VAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDsLPKTRSGKIMRRILR 616
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
.
gi 515671996 617 K 617
Cdd:cd12118 486 D 486
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-618 |
3.26e-14 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 75.78 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 87 AERGDEVAIIWEGDDPADDkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACtrigavhtvVFGGF 166
Cdd:cd05906 20 AERGPTKGITYIDADGSEE-FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 167 SPEALSgriidsnskVVITADEGVRGGRAVplkKNVDEALTNPevknieKVVVFKRTGGDVAWHEHRDVWWHDAIANVSA 246
Cdd:cd05906 90 VPAPLT---------VPPTYDEPNARLRKL---RHIWQLLGSP------VVLTDAELVAEFAGLETLSGLPGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 247 --DCPPEEM----NAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKyVFDYQEGETF--WCTADvgWITGHTYLVY 318
Cdd:cd05906 152 llDTAADHDlpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLVELHL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 319 GPLANGAKTIlfegvpNYP------NTSRMSEVVDKHQVNILYtAPTAIRALMAKGNEAVEGTSRD--SLRVMGSVGEPI 390
Cdd:cd05906 229 RAVYLGCQQV------HVPteeilaDPLRWLDLIDRYRVTITW-APNFAFALLNDLLEEIEDGTWDlsSLRYLVNAGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 391 NPEAWEWYYKTIGNEQSP---IVDTWWQTETG-GILIAPLPGATDLKPG----SATRPFFGVQPALVDNMGNIIEGATDG 462
Cdd:cd05906 302 VAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLvildswpgqmrTVHGDhdrfeqtyfSTFKGMY---------FTSDGARR--D----EDGYYWITGRVDDVLNVSGHRM 527
Cdd:cd05906 382 RL-----------QVRGP---------VVTKGYYnnpeanaeaFTEDGWFRtgDlgflDNGNLTITGRTKDTIIVNGVNY 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 528 GTAEIESALVAFDKIAE----AAIVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVKNWVRKEIG-------PIAtpdvl 596
Cdd:cd05906 442 YSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGvspayliPLP----- 516
|
570 580
....*....|....*....|..
gi 515671996 597 hwTDSLPKTRSGKIMRRILRKI 618
Cdd:cd05906 517 --KEEIPKTSLGKIQRSKLKAA 536
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
3.36e-14 |
|
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: 74.73 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQEGETFWCTADVGwITGHTYLVYGPLANGAKTILFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAA-AAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 YPNT-----SRMS-----EVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNe 405
Cdd:cd05924 82 GGQTvvlpdDRFDpeevwRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 406 qSPIVDTWWQTETGGILIAPLPGAtdlkpGSATRPFFGVQP--ALVDNMGNIIEGATDGnlvilDSWPGQMRTV----HG 479
Cdd:cd05924 161 -ITLVDAFGSSETGFTGSGHSAGS-----GPETGPFTRANPdtVVLDDDGRVVPPGSGG-----VGWIARRGHIplgyYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 480 DHDRFEQTYFSTFKGMY-FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQA 558
Cdd:cd05924 230 DEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515671996 559 IYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 310 VVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
237-549 |
5.04e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 74.81 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 237 WHDAIA--NVSADCPPEEmnAEDPLFILYTSGSTGKPKGVMHTTGGYlVYAAMTFKYVFDYQEGETFWCTADVGWITGHT 314
Cdd:cd05932 118 WDDLIAqhPPLEERPTRF--PEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 315 YLVYGPLANG------------------AKTILFEGVPNYPNTSRMSeVVDK---HQVNILYTAPTaIRALMAKgnEAVE 373
Cdd:cd05932 195 FVEGGSLYGGvlvafaesldtfvedvqrARPTLFFSVPRLWTKFQQG-VQDKipqQKLNLLLKIPV-VNSLVKR--KVLK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 374 GTSRDSLRVMGSVGEPINPEAWEWYYKtIGneqSPIVDTWWQTETGGILIAPLPGATdlKPGSATRPFFGVQpalvdnmg 453
Cdd:cd05932 271 GLGLDQCRLAGCGSAPVPPALLEWYRS-LG---LNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVE-------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 454 niIEGATDGNLVILDswPGQMRTVHGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVS-GHRMGTAEI 532
Cdd:cd05932 337 --VRISEDGEILVRS--PALMMGYYKDPEATAEAF--TADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPI 410
|
330
....*....|....*..
gi 515671996 533 ESALVAFDKIAEAAIVG 549
Cdd:cd05932 411 ENKLAEHDRVEMVCVIG 427
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
5.85e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 82 IDRHLAERGDEVAIIWEGDdpaddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 162 VFGGFSPEALSGRIIDSNSKVVITAD------EGVRGGRAVPLkknvdEALtnpevkniekvvvfkrtggdvawheHRDV 235
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQShllerlPQAEGVSAIAL-----DSL-------------------------HLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 236 WWHDAianvsadcPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGY---LVYAAMTFKY------------VFDYQEGET 300
Cdd:PRK05691 1261 WPSQA--------PGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQATYALddsdvlmqkapiSFDVSVWEC 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 301 FWctadvgwitghtylvygPLANGAKTILfEGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMakgNEAVEGTSRdSL 380
Cdd:PRK05691 1333 FW-----------------PLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI---DEPLAAACT-SL 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 381 RVMGSVGEPINPEAWEWYYKTI---------GNEQSPIVDTWWQTETGGILIAPLpgatdlkpgsaTRPFFGVQPALVDN 451
Cdd:PRK05691 1391 RRLFSGGEALPAELRNRVLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 452 MGNIIEGATDGNLVIldSWPGQMRTVHG----DHDRF-EQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK05691 1460 ELNLLPPGVAGELCI--GGAGLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFR 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 527 MGTAEIESALVAFDKIAEAAIVgIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTR 606
Cdd:PRK05691 1538 VEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGP 1613
|
....*....
gi 515671996 607 SGKIMRRIL 615
Cdd:PRK05691 1614 SGKLDRRAL 1622
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
7.76e-14 |
|
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: 74.58 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAERGDEVAIIWEGDDPADDKTLTFNELHKEVCLFSNALKEQGvRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 164 GGFSPEA---LSGRIIDSNSKVVITADEgvrggravplkknVDEALtnpevkniekvvvfKRTGGDVAWHEHRDVWWHDA 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAA-------------ALAAV--------------RAFAASRPAAGTPRLLVVDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 241 IA-NVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKyVFDYQEGETFwctadVGWITghTY---- 315
Cdd:cd05931 133 LPdTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVV-----VSWLP--LYhdmg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 316 LVYG---PLANGAKTILfegvpnypnTSRMS---------EVVDKHQVNILYtAPT-----AIRALMAkgnEAVEGTSRD 378
Cdd:cd05931 205 LIGGlltPLYSGGPSVL---------MSPAAflrrplrwlRLISRYRATISA-APNfaydlCVRRVRD---EDLEGLDLS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 379 SLRVMGSVGEPINPEAWEWYYK--------------------------TIGNEQSPIVDTWWQTETGGILIAPL---PGA 429
Cdd:cd05931 272 SWRVALNGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAaddPAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 430 TDLKpgSATRPFFGVQPALVDnmgniiegaTDGNLVILDSWPGQMRtVHGD------HDRFEQTyFSTFK-------GMY 496
Cdd:cd05931 352 RELV--SCGRPLPDQEVRIVD---------PETGRELPDGEVGEIW-VRGPsvasgyWGRPEAT-AETFGalaatdeGGW 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 F-TSD-GARRdeDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDK---IAEAAIVGIPHDIKGQ-AIYAYITLNDGEF 570
Cdd:cd05931 419 LrTGDlGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDDGEERlVVVAEVERGADPA 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 515671996 571 PTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 497 DLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRA 543
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
105-612 |
8.26e-14 |
|
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: 74.02 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADEgvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnaEDPLFILYT 264
Cdd:cd05914 85 VSDE-------------------------------------------------------------------DDVALINYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGYLVYAAMTFKYVFdYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVPN--------- 335
Cdd:cd05914 98 SGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSakiialafa 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 336 --YPN--TSRMSEVVDKHQVNILYTAPTA--IRALMAKGN-------------EAVEGtsrdSLRVMGSVGEPINPEAwE 396
Cdd:cd05914 177 qvTPTlgVPVPLVIEKIFKMDIIPKLTLKkfKFKLAKKINnrkirklafkkvhEAFGG----NIKEFVIGGAKINPDV-E 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 WYYKTIGneqSPIVDTWWQTETGGILIAPLPGATDLkpGSATRPFFGVQPALVDNMGNIIEGAtdgnlvILDSWPGQMRT 476
Cdd:cd05914 252 EFLRTIG---FPYTIGYGMTETAPIISYSPPNRIRL--GSAGKVIDGVEVRIDSPDPATGEGE------IIVRGPNVMKG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 477 VHGDHDRFEQTYfsTFKGMYFTSDGARRDEDGYYWITGRVDDV-LNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIK 555
Cdd:cd05914 321 YYKNPEATAEAF--DKDGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515671996 556 GQAIYAYITLNDGEFPTAELHKEVKNWVRKEIGpIATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 399 ALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
254-621 |
1.17e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.90 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHT-TGGYLVyaamTFKYVFDYQEG---------ETFWCTadvGWItghtyLVYGPLAN 323
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVIShRGAYLS----TLSAIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAAR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 324 GAKTILFEGVpnypNTSRMSEVVDKHQVNILYTAPTAIRALMaKGNEAVEGTSRDSLRVMGSVGEPinPEAWEWYYKTIG 403
Cdd:PLN03102 252 GGTSVCMRHV----TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 404 ----------NEQSPIVDTWWQTETGGIliaPLPGATDLKPGSATRpFFGVQPALVDNMGNI----IEGATDGNLVILDS 469
Cdd:PLN03102 325 fqvmhaygltEATGPVLFCEWQDEWNRL---PENQQMELKARQGVS-ILGLADVDVKNKETQesvpRDGKTMGEIVIKGS 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 470 --WPGQMRTVHGDHDRFEQTYFSTfkgmyftSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAI 547
Cdd:PLN03102 401 siMKGYLKNPKATSEAFKHGWLNT-------GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 548 VGIPHDIKGQAIYAYITLNDGE---------FPTAElhKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PLN03102 474 VAMPHPTWGETPCAFVVLEKGEttkedrvdkLVTRE--RDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
...
gi 515671996 619 ATG 621
Cdd:PLN03102 552 AKG 554
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
254-615 |
1.22e-13 |
|
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: 73.62 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVM--------HTTGGYLVYAAMTFKYV-------FDYQEGETFwctadVGWITGHTYLVy 318
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 319 gplangaktilfegVPN--YPNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVeGTSRDSLRVMGSVGEPINPEAWE 396
Cdd:cd17644 178 --------------RPEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLST-IDLPSSLRLVIVGGEAVQPELVR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 WYYKTIGNEQSpIVDTWWQTEtgGILIAPLPGATDLKPGSATRPFFG-----VQPALVDNMGNIIEGATDGNLVIldswp 471
Cdd:cd17644 243 QWQKNVGNFIQ-LINVYGPTE--ATIAATVCRLTQLTERNITSVPIGrpianTQVYILDENLQPVPVGVPGELHI----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTVHGDHDRFEQT---------YFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKI 542
Cdd:cd17644 315 GGVGLARGYLNRPELTaekfishpfNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 543 AEAAIVgIPHDIKGQA-IYAYITlndGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17644 395 KTAVVI-VREDQPGNKrLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
79-277 |
1.56e-13 |
|
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: 73.64 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 79 ANCIDRHLAERGDEVAIIWEGDDPADD--------------KTLTFNELHKEVCLFSNALK-EQGVRKGDVVCLYMPMVP 143
Cdd:cd17632 25 AQIIATVMTGYADRPALGQRATELVTDpatgrttlrllprfETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 144 EAAVAMLACTRIGAVHTVVFGGFSPEALSGrIIDSNSKVVITAD--------EGVRGGRAVPlkknvdealtnpevknie 215
Cdd:cd17632 105 DYATVDLALTRLGAVSVPLQAGASAAQLAP-ILAETEPRLLAVSaehldlavEAVLEGGTPP------------------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 216 KVVVF--KRTGGDvawheHRD---------------VWWHDAIANVSADCPPEEMNAE----DPL-FILYTSGSTGKPKG 273
Cdd:cd17632 166 RLVVFdhRPEVDA-----HRAalesarerlaavgipVTTLTLIAVRGRDLPPAPLFRPepddDPLaLLIYTSGSTGTPKG 240
|
....
gi 515671996 274 VMHT 277
Cdd:cd17632 241 AMYT 244
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
254-615 |
2.63e-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: 72.43 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHTTGG-----------YLV----YAAMTF--KYVFDYQEGETfwCTAdvgWITGHTYL 316
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGrdngDEAVLFfsNYVFDFFVEQM--TLA---LLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 317 VYGPLANGAKtilfegvpnypntSRMSEVVDKHQVNILYTAPTAIralmakgnEAVEGTSRDSLRVMGSVGEPINPEAWE 396
Cdd:cd17648 167 VPPDEMRFDP-------------DRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 397 wyyKTIGNEQSPIVDTWWQTE---TGGILIAPLPGATDLKPGsatRPFFGVQP-ALVDNMGNIIEGATdGNLVI--LDSW 470
Cdd:cd17648 226 ---KLRSRFAGLIINAYGPTEttvTNHKRFFPGDQRFDKSLG---RPVRNTKCyVLNDAMKRVPVGAV-GELYLggDGVA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 471 PGQMRTVHGDHDRFEQTYFST--------FKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKI 542
Cdd:cd17648 299 RGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGV 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 543 AEAAIVGIPHDIKGQA-----IYAYITLNDGEFPTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17648 379 RECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPESDL----LSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
380-615 |
5.65e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 71.57 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 380 LRVMGSVGEPINPEAWEWYYKTIGNeqsPIVDTWWQTETGgilIAPLPGATDLK--PGSATRPFFGVQPALVDNMGNIIE 457
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVG---IGALATPADLRdaPETVGKPVAGCPVRILDRNNRPVG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 GATDGNLVILDSWPGQMRTVHGDHdrfeqtyfSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:PRK13383 368 PRVTGRIFVGGELAGTRYTDGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 538 AFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 440 AHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAA---QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
480-617 |
9.04e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.07 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 480 DHDRFEQtyfstfKGMYFTSDGARRDeDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAI 559
Cdd:PRK07824 226 DPDPFAE------PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 560 YAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 299 VAAVVGDGGPAPTLE---ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
106-450 |
1.37e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 70.78 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 adegvrGGRAVPlkkNVDEALTNPEVKNIeKVVVFKRTGGDVAWHEHRDVWWHDAIAN----VSADCPPEEMNAEDPLFI 261
Cdd:PTZ00216 200 ------NGKNVP---NLLRLMKSGGMPNT-TIIYLDSLPASVDTEGCRLVAWTDVVAKghsaGSHHPLNIPENNDDLALI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 262 LYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVF-----DYQEGEtfwctadvgwitghTYLVYGPLAN------------- 323
Cdd:PTZ00216 270 MYTSGTTGDPKGVMHTHGS-LTAGILALEDRLndligPPEEDE--------------TYCSYLPLAHimefgvtniflar 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 324 GA------------------------KTILFEGVPNYPNTsrMSEVVD---------KHQV-NILYTAPtaIRALMaKG- 368
Cdd:PTZ00216 335 GAligfgsprtltdtfarphgdltefRPVFLIGVPRIFDT--IKKAVEaklppvgslKRRVfDHAYQSR--LRALK-EGk 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 369 -----NEAVEGTSRDSL----RVMGSVGEPINPEAWEWYYKTIGneqsPIVDTWWQTET---GGIliaPLPGatDLKPGS 436
Cdd:PTZ00216 410 dtpywNEKVFSAPRAVLggrvRAMLSGGGPLSAATQEFVNVVFG----MVIQGWGLTETvccGGI---QRTG--DLEPNA 480
|
410
....*....|....
gi 515671996 437 ATRPFFGVQPALVD 450
Cdd:PTZ00216 481 VGQLLKGVEMKLLD 494
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
240-615 |
1.90e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 240 AIANVSADCPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYlvyaAMTFKYVFdyqegETFWCTADVGWItgHTYLV-- 317
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI----AMHCQAVI-----ERFGMRADDCEL--HFYSInf 2385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 -------YGPLANGAKTILfeGVPNYPNTSRMSEVVDKHQVNILYTAPTAIRAL---MAKGNEAVegtsrdSLRVMGSVG 387
Cdd:PRK05691 2386 daaserlLVPLLCGARVVL--RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLaqwLAGQGEQL------PVRMCITGG 2457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 388 EPINPEAWEWYYKTIGNEQspIVDTWWQTETGGILIAPLPGATdLKPGSATRPFFGVQPALV-----DNMGNIIEGATdG 462
Cdd:PRK05691 2458 EALTGEHLQRIRQAFAPQL--FFNAYGPTETVVMPLACLAPEQ-LEEGAASVPIGRVVGARVayildADLALVPQGAT-G 2533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 463 NLVIldswpGQMRTVHGDHDR-------FEQTYFSTFKG-MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK05691 2534 ELYV-----GGAGLAQGYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIES 2608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 535 ALVAFDKIAEAAI--VGIPhdiKGQAIYAYI---TLNDGEFPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGK 609
Cdd:PRK05691 2609 RLLEHPAVREAVVlaLDTP---SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
|
....*.
gi 515671996 610 IMRRIL 615
Cdd:PRK05691 2686 LDRRAL 2691
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
2.12e-12 |
|
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: 69.51 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 91 DEVAIIWEGddpaddKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG------QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 171 LSGRIIDSNSKVVITadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcpp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 251 eemNAEDPLFILYTSGSTGKPKGVM--HTTggyLVYAAMTFKYVFDYQEGETFWCTADVGWiTGHTYLVYGPLANGAKTI 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 329 LFEGVPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEavegtsrdSLRVMGSVGEPINPEAWEWY--YKTIGNEQ 406
Cdd:cd17645 175 VVPSERRL-DLDALNDYFNQEGITISFLPTGAAEQFMQLDNQ--------SLRVLLTGGDKLKKIERKGYklVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 407 SPIVDTWWQT--ETGGILIAplpgatdlKPGSATRPFF-----GVQPALVDNMGNII-EGATDGNLvildSWPGQMRtvh 478
Cdd:cd17645 246 NTVVATSFEIdkPYANIPIG--------KPIDNTRVYIldealQLQPIGVAGELCIAgEGLARGYL----NRPELTA--- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 479 gdhDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQA 558
Cdd:cd17645 311 ---EKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKY 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 515671996 559 IYAYITLndgefPTAELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 388 LVAYVTA-----PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
88-616 |
2.43e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 69.52 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 88 ERGDEVAIiwEGDDPAddkTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFS 167
Cdd:PRK07514 14 ADRDAPFI--ETPDGL---RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 168 PEALSGRIIDSNSKVVITADEGVRGGRAVPLKKNVDEALTNPEvkniekvvvfKRTGGDVawhehrdvwwhDAIANVSAD 247
Cdd:PRK07514 89 LAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDA----------DGTGSLL-----------EAAAAAPDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 248 CPPEEMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKyvfDYqegetfWctadvGWITG----------HTYLV 317
Cdd:PRK07514 148 FETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLV---DY------W-----RFTPDdvlihalpifHTHGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 Y----GPLANGAKTIL---FEgvpnypntsrMSEVVDK-HQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMGSVgeP 389
Cdd:PRK07514 213 FvatnVALLAGASMIFlpkFD----------PDAVLALmPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSA--P 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 390 INPEAW-EWYYKTiGNeqsPIVDTWWQTETGGILIAPLPGatDLKPGSATRPFFGVQPALVDNMgniiEGATDGnlvild 468
Cdd:PRK07514 281 LLAETHrEFQERT-GH---AILERYGMTETNMNTSNPYDG--ERRAGTVGFPLPGVSLRVTDPE----TGAELP------ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 469 swPGQ--MRTVHGDhdrfeqtyfSTFKGMY---------FTSDG-------ARRDEDGYYWITGRVDDVLNVSGHRMGTA 530
Cdd:PRK07514 345 --PGEigMIEVKGP---------NVFKGYWrmpektaeeFRADGffitgdlGKIDERGYVHIVGRGKDLIISGGYNVYPK 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 531 EIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPT-AELHKEVKnwvrkeiGPIA---TPDVLHWTDSLPKTR 606
Cdd:PRK07514 414 EVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDeAAILAALK-------GRLArfkQPKRVFFVDELPRNT 486
|
570
....*....|
gi 515671996 607 SGKIMRRILR 616
Cdd:PRK07514 487 MGKVQKNLLR 496
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
107-619 |
2.48e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 69.85 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 107 TLTFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI- 184
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVy 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 -----------TADEG------VRGGRAVPLKKNvdeALTNPEVKNIEKVVVfkrtggdvAWHEHRDVWWHDAIANVSAD 247
Cdd:PRK12492 129 lnmfgklvqevLPDTGieylieAKMGDLLPAAKG---WLVNTVVDKVKKMVP--------AYHLPQAVPFKQALRQGRGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 248 CP-PEEMNAEDPLFILYTSGSTGKPKGVMHTTGGYL-----VYAAMTfkyvfdyQEGETfwctadvgwitGHtylvygPL 321
Cdd:PRK12492 198 SLkPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlqVRACLS-------QLGPD-----------GQ------PL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 322 ANGAKTILFEGVPNY------PNTSRMSeVVDKHqvNILYTAP----------------------TAIRALMAkgNEAVE 373
Cdd:PRK12492 254 MKEGQEVMIAPLPLYhiyaftANCMCMM-VSGNH--NVLITNPrdipgfikelgkwrfsallglnTLFVALMD--HPGFK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 374 GTSRDSLRVMGSVGEPINPEAWEWYYKTIGneqSPIVDTWWQTETGGILIAPlPGATDLKPGSATRPFFGVQPALVDNMG 453
Cdd:PRK12492 329 DLDFSALKLTNSGGTALVKATAERWEQLTG---CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 454 NIIEGATDGNLVIldSWPGQMRtvhGDHDRFEQTYFS-TFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:PRK12492 405 NELPLGERGELCI--KGPQVMK---GYWQQPEATAEAlDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 533 ESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAELhkevKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK12492 480 EDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEEL----KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILR 555
|
....*..
gi 515671996 613 RILRKIA 619
Cdd:PRK12492 556 RELRDIA 562
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
106-619 |
3.06e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.95 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKeQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAV-----HTVvfggfSPEALSGRIIDSNS 180
Cdd:PRK08633 640 GELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGKVpvnlnYTA-----SEAALKSAIEQAQI 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 181 KVVITADEGVRggrAVPLKKNVDEALTNPEVKNIEKVVVfKRTGGDVAWhehrdvwwhdaiANVSADCPPEEM------- 253
Cdd:PRK08633 714 KTVITSRKFLE---KLKNKGFDLELPENVKVIYLEDLKA-KISKVDKLT------------ALLAARLLPARLlkrlygp 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 --NAEDPLFILYTSGSTGKPKGVM---HTTGGYLVYAAMtfkyVFDYQEGetfwctaDV-----------GwITGHTYLv 317
Cdd:PRK08633 778 tfKPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRND-------DVilsslpffhsfG-LTVTLWL- 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 318 ygPLANGAKTILfegVPNYPNTSRMSEVVDKHQVNILYTAPTAIRALMAkgNEAVEGTSRDSLRVMGSVGEPINPEAWEW 397
Cdd:PRK08633 845 --PLLEGIKVVY---HPDPTDALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 398 YYKTIG---------NEQSPIV----------DTWWQTETggiliaplpgatdlKPGSATRPFFGVQPALVD-NMGNIIE 457
Cdd:PRK08633 918 FEEKFGirilegygaTETSPVAsvnlpdvlaaDFKRQTGS--------------KEGSVGMPLPGVAVRIVDpETFEELP 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 458 GATDGNLVIldSWPGQMRTVHGDHDRF-EQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:PRK08633 984 PGEDGLILI--GGPQVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL 1061
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 537 VAF--DKIAEAAIVGIPHDIKGQAIYAYITLNDGEFptAELHKEVKNwvrKEIGPIATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK08633 1062 AKAlgGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDV--EELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKG 1136
|
....*
gi 515671996 615 LRKIA 619
Cdd:PRK08633 1137 LKELA 1141
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
83-619 |
1.03e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 67.91 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 83 DRHLAERGDEVAIIwegdDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK08315 23 DRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFSPEALSGRIIDSNSKVVITADeGVRGGR-------AVP-LKKNVDEALTNPEVKNIEKVVVF--KRTGGDVAWHE- 231
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAAD-GFKDSDyvamlyeLAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLNFDEl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 232 -----HRDVWWHDAIAnvsadcppEEMNAEDPLFILYTSGSTGKPKGVMHT-----TGGYLVYAAMTFkyvfdyqeGET- 300
Cdd:PRK08315 178 lalgrAVDDAELAARQ--------ATLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKL--------TEEd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 301 --------FWCtadVGWITGhtylVYGPLANGAKTIlfegvpnYPNTS----RMSEVVDKHQVNILYTAPTAIRALMakg 368
Cdd:PRK08315 242 rlcipvplYHC---FGMVLG----NLACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMFIAEL--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 369 nEAVEGTSRD--SLR------------VMGSVGEPIN-PEAwewyykTIG---NEQSPiVDTwwQTETGgiliAPLpgat 430
Cdd:PRK08315 305 -DHPDFARFDlsSLRtgimagspcpieVMKRVIDKMHmSEV------TIAygmTETSP-VST--QTRTD----DPL---- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 431 DLKPGSATRPFFGVQPALVD-NMGNII------EGATDGNLVILDSW--PGQMRTVHgDHDRFeqtyfstfkgMYfTSDG 501
Cdd:PRK08315 367 EKRVTTVGRALPHLEVKIVDpETGETVprgeqgELCTRGYSVMKGYWndPEKTAEAI-DADGW----------MH-TGDL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 502 ARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAElhkEVKN 581
Cdd:PRK08315 435 AVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---DVRD 511
|
570 580 590
....*....|....*....|....*....|....*...
gi 515671996 582 WVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
1.61e-11 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 66.17 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 257 DPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTfkyvfdyqegetfwctADVGWITGHT-YLVYGPL-----ANGAKTILF 330
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVL----------------AVLQAIDEGTvFLNSGPLfhigtLMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 EGVPNY--PNTS--RMSEVVDKHQVNILYTAPTAIRALMakgnEAVEGTSRD--SLRVMgsvgepinPEAWEWyyktigN 404
Cdd:cd17636 65 AGGTNVfvRRVDaeEVLELIEAERCTHAFLLPPTIDQIV----ELNADGLYDlsSLRSS--------PAAPEW------N 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 405 EQSPIVDTWW--------QTETGGILIAPLPGATDLkpGSATRPFFGVQPALVDNMGNII------EGATDGNLVILDSW 470
Cdd:cd17636 127 DMATVDTSPWgrkpggygQTEVMGLATFAALGGGAI--GGAGRPSPLVQVRILDEDGREVpdgevgEIVARGPTVMAGYW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 471 pgqmrtvhgdhDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGI 550
Cdd:cd17636 205 -----------NRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 551 PHDIKGQAIYAYITLNDGEFPTAElhkEVKNWVRKEIGPIATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 274 PDPRWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-549 |
3.24e-11 |
|
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: 66.29 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT 185
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 ADEgvrggravplkKNVDEALT-NPEVKNIEKVVVFKRTGgdvaWHEHRDVWWHD---------AIANVSADCPPEEMNA 255
Cdd:cd17641 90 EDE-----------EQVDKLLEiADRIPSVRYVIYCDPRG----MRKYDDPRLISfedvvalgrALDRRDPGLYEREVAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 ---EDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKyvFDYQE-GETFWCTADVGWITGHTYLVYGPLANG------- 324
Cdd:cd17641 155 gkgEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPLGpGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 325 -AKTI---LFEGVPNY----PNT---------SRMSEV------VDKHQVNILYTA----------PTAIRALMAKGNEA 371
Cdd:cd17641 233 ePETMmedLREIGPTFvllpPRVwegiaadvrARMMDAtpfkrfMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 372 VEGTSRDSL-----RVMGSVGEPINPEAWEwYYKTIGneqSPIVDTWWQTETGGILIAPLPGatDLKPGSATRPFFGVQp 446
Cdd:cd17641 313 LFRPLRDRLgfsrlRSAATGGAALGPDTFR-FFHAIG---VPLKQLYGQTELAGAYTVHRDG--DVDPDTVGVPFPGTE- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 447 ALVDNMGNIIeGATDGnlVILDSWPGQMRTvhgDHDRFEQTYFSTFKGMYFtsdgarrDEDGYYWITGRVDDVLNVS-GH 525
Cdd:cd17641 386 VRIDEVGEIL-VRSPG--VFVGYYKNPEAT---AEDFDEDGWLHTGDAGYF-------KENGHLVVIDRAKDVGTTSdGT 452
|
490 500
....*....|....*....|....
gi 515671996 526 RMGTAEIESALVAFDKIAEAAIVG 549
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
490-625 |
5.81e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.02 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 490 STFKGMY----------FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAI 559
Cdd:PRK07445 310 SLALGYYpqildsqgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVV 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 560 YAYITLNDGEFPTAELhkevKNWVRKEIGPIATPDvlHW--TDSLPKTRSGKIMRRILRKIATGDTGN 625
Cdd:PRK07445 390 TAIYVPKDPSISLEEL----KTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
492-619 |
1.82e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.81 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 492 FKGMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEF 570
Cdd:PRK08162 413 FAGGWFhTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS 492
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 515671996 571 PTAElhkEVKNWVRKEIGPIATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 493 ATEE---EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
494-619 |
1.85e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 63.86 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 494 GMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTA 573
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ 488
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 515671996 574 elhkeVKNWVRkEIGpIAT---PDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK10946 489 -----LRRFLR-EQG-IAEfklPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
109-619 |
3.05e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.86 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVIT--- 185
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVdqe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 186 ----ADEGVR-------GGRAVPLKKNVDEALTNPEVKN-------IEKVVVFKRTGGDVAWHEHRDVWwhDAIAnvsad 247
Cdd:PLN02479 127 fftlAEEALKilaekkkSSFKPPLLIVIGDPTCDPKSLQyalgkgaIEYEKFLETGDPEFAWKPPADEW--QSIA----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 248 cppeemnaedplfILYTSGSTGKPKGV-MHTTGGYLvyAAMTFKYVFDYQEGETF-----------WC-TADVGWITG-- 312
Cdd:PLN02479 200 -------------LGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMNEGAVYlwtlpmfhcngWCfTWTLAALCGtn 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 313 ------HTYLVYGPLANGAKT------ILFEGVPNYPNTSR---MSEVVDkhqVNILYTAPTAIraLMAKgneavegTSR 377
Cdd:PLN02479 265 iclrqvTAKAIYSAIANYGVThfcaapVVLNTIVNAPKSETilpLPRVVH---VMTAGAAPPPS--VLFA-------MSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 378 DSLRVMGSVG--EPINPE---AW--EWyyktigNEQSPIVDTWWQTETGGILIApLPG--ATDLKPGSATrpffgvqPAL 448
Cdd:PLN02479 333 KGFRVTHTYGlsETYGPStvcAWkpEW------DSLPPEEQARLNARQGVRYIG-LEGldVVDTKTMKPV-------PAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 449 VDNMGNIIegaTDGNLVIldswPGQMRTVHGDHDRFEQtyfstfkGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMG 528
Cdd:PLN02479 399 GKTMGEIV---MRGNMVM----KGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENIS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 529 TAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGEFPTAE--LHKEVKNWVRKEIGPIATPDVLHWtDSLPKTR 606
Cdd:PLN02479 465 SLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTA 543
|
570
....*....|...
gi 515671996 607 SGKIMRRILRKIA 619
Cdd:PLN02479 544 TGKIQKHVLRAKA 556
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
106-617 |
3.92e-09 |
|
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: 59.37 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALK-EQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 tadegvrggravplkknVDEaltnpevkniekvvvfkrtggdvawhehrdvwwhdaianvsadcppeemnaEDPLFILYT 264
Cdd:cd05937 84 -----------------VDP---------------------------------------------------DDPAILIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGYLVyAAMTFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILfegVPNYPNTSRMSE 344
Cdd:cd05937 96 SGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL---SRKFSASQFWKD 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 345 VVDKHQVNILYTAPTaIRALMAKGNEAVEgtsRDSlRVMGSVGEPINPEAW-------------EWYYKTIGneqspiVD 411
Cdd:cd05937 172 VRDSGATIIQYVGEL-CRYLLSTPPSPYD---RDH-KVRVAWGNGLRPDIWerfrerfnvpeigEFYAATEG------VF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 412 TWWQTETGGILIaplpGATDLKpGSATRPFFGVQPALVD---NMGNIIEGATDG-----------------NLVILDSWP 471
Cdd:cd05937 241 ALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVKmdpETDDPIRDPKTGfcvrapvgepgemlgrvPFKNREAFQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTVHGDHDRFEQTYFStfKG-MYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVG 549
Cdd:cd05937 316 GYLHNEDATESKLVRDVFR--KGdIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515671996 550 IP---HDikGQAIYAYITLNDGEFPTAELHK-EVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05937 394 VKvpgHD--GRAGCAAITLEESSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
74-396 |
2.07e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.22 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 74 TLNVSANcIDRHL----AERGDEVAII----WEGDDPADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEA 145
Cdd:PRK09274 1 MMASMAN-IARHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 146 AVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADEGVRGGRAVPLKKnvdealtnpevKNIEKVVVfkrTGG 225
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGK-----------PSVRRLVT---VGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 226 DVAW--HEHRDVWWHDAIANVS-ADCPPEEMNAedplfILYTSGSTGKPKGVMHTTGGYL--VYAAmtfKYVFDYQEGET 300
Cdd:PRK09274 146 RLLWggTTLATLLRDGAAAPFPmADLAPDDMAA-----ILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 301 fwctaDVgwitgHTYLVYG--PLANGAKTILFEGVPNYP---NTSRMSEVVDKHQVNILYTAPTAIRALmakGNEAVE-G 374
Cdd:PRK09274 218 -----DL-----PTFPLFAlfGPALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERL---GRYGEAnG 284
|
330 340
....*....|....*....|..
gi 515671996 375 TSRDSLRVMGSVGEPINPEAWE 396
Cdd:PRK09274 285 IKLPSLRRVISAGAPVPIAVIE 306
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
256-617 |
3.47e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 56.35 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 256 EDPLFILYTSGSTGKPKGVM--HTTggyLVYAAMTFKYVFDYQEGETFWCTADVGWITGhtylVYGPLAN---GAKTILf 330
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTisHSA---LIVQSLAKIAIVGYGEDDVYLHTAPLCHIGG----LSSALAMlmvGACHVL- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 331 egVPNYpNTSRMSEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVM----GSVGEPINPEAWEWY-----YKT 401
Cdd:PLN02860 244 --LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSRLLPDAKKLFpnaklFSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 402 IG----------------NEQSPIVDTWWQTETGGILIAPLPGATDLKPgsATRPFFGVQPALVDNMGNIIegaTDGNLV 465
Cdd:PLN02860 321 YGmteacssltfmtlhdpTLESPKQTLQTVNQTKSSSVHQPQGVCVGKP--APHVELKIGLDESSRVGRIL---TRGPHV 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 466 ILDSWpGQMRTVHGDhdrfeqtyfSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEA 545
Cdd:PLN02860 396 MLGYW-GQNSETASV---------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 546 AIVGIPHDIKGQAIYAYITLNDG------EFPTAE-----------LHKEVKNWVRKEIGPIatpdVLHWTDSLPKTRSG 608
Cdd:PLN02860 466 VVVGVPDSRLTEMVVACVRLRDGwiwsdnEKENAKknltlssetlrHHCREKNLSRFKIPKL----FVQWRKPFPLTTTG 541
|
....*....
gi 515671996 609 KIMRRILRK 617
Cdd:PLN02860 542 KIRRDEVRR 550
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
252-617 |
8.51e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 55.19 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 252 EMNAEDPLFILYTSGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETF--W--CTADVGWITGHtylvYGPLANGAK- 326
Cdd:cd05908 102 CELADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 327 ----TILFEGVPnypntSRMSEVVDKHQVNILYTAPTAIRALMAKGN-EAVEGTSRDSLRVMGSVGEPINPEAWEWYYK- 400
Cdd:cd05908 177 ylmpTRLFIRRP-----ILWLKKASEHKATIVSSPNFGYKYFLKTLKpEKANDWDLSSIRMILNGAEPIDYELCHEFLDh 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 401 ------------------------TIGNEQSPIVDTWWQTEtgGILIAPLPGATDLKPGSATR------PFFGVQPALVD 450
Cdd:cd05908 252 mskyglkrnailpvyglaeasvgaSLPKAQSPFKTITLGRR--HVTHGEPEPEVDKKDSECLTfvevgkPIDETDIRICD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 451 NMGNIIEGATDGNLVIldswPGQMRTvHGDHDRFEQTyfstfkGMYFTSDGARRDED------GYYWITGRVDDVLNVSG 524
Cdd:cd05908 330 EDNKILPDGYIGHIQI----RGKNVT-PGYYNNPEAT------AKVFTDDGWLKTGDlgfirnGRLVITGREKDIIFVNG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 525 HRMGTAEIESALVAFDKI--AEAAIVGIpHD--IKGQAIYAYITLNDGEFPTAELHKEVKN-------WVRKEIGPIATp 593
Cdd:cd05908 399 QNVYPHDIERIAEELEGVelGRVVACGV-NNsnTRNEEIFCFIEHRKSEDDFYPLGKKIKKhlnkrggWQINEVLPIRR- 476
|
410 420
....*....|....*....|....
gi 515671996 594 dvlhwtdsLPKTRSGKIMRRILRK 617
Cdd:cd05908 477 --------IPKTTSGKVKRYELAQ 492
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
489-615 |
9.65e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 54.90 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 489 FSTFKGM--YFTSDGARRDeDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLN 566
Cdd:PRK04813 369 FFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPK 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 515671996 567 DGEFPT-AELHKEVKNWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK04813 448 EEDFEReFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-580 |
1.12e-07 |
|
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: 54.77 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 255 AEDPLFILYTSGSTGKPKGVMHTTGgylVYAAM--TFKYVFDYQEGEtfwctadVGWITGHTYLVYGPlANGAKTILFEG 332
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHG---TFAAQidALRQLYGIRPGE-------VDLATFPLFALFGP-ALGLTSVIPDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 333 VPNYPNTSRMSEVVD---KHQVNILYTAPTAIRALMAKGneAVEGTSRDSLRVMGSVGEPINPEAWEWYYKTIGNEqSPI 409
Cdd:cd05910 153 DPTRPARADPQKLVGairQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDE-AEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 410 VDTWWQTETGGI-------LIAPLPGATDlkPGSAT---RPFFGVQPALVD-NMGNIiegATDGNLVILDSW-------P 471
Cdd:cd05910 230 LTPYGATEALPVssigsreLLATTTAATS--GGAGTcvgRPIPGVRVRIIEiDDEPI---AEWDDTLELPRGeigeitvT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 472 GQMRTvHGDHDRFEQTYFSTFKG-----MYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAA 546
Cdd:cd05910 305 GPTVT-PTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
330 340 350
....*....|....*....|....*....|....
gi 515671996 547 IVGIPHDIKGQAIYAYITLNDGEFPTAELHKEVK 580
Cdd:cd05910 384 LVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-322 |
1.55e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 54.74 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITAD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 188 EgvrggravPLKKNVDealTNPEVKNIEKVVVFKRTGGDVAW-HEHRDVWWHDAIANV-----SADCPPEEMNAEDPLFI 261
Cdd:PLN02387 187 K--------QLKKLID---ISSQLETVKRVIYMDDEGVDSDSsLSGSSNWTVSSFSEVeklgkENPVDPDLPSPNDIAVI 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515671996 262 LYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVfdyqegetfwctADVGwiTGHTYLVYGPLA 322
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVV------------PKLG--KNDVYLAYLPLA 302
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
105-617 |
4.25e-07 |
|
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: 52.74 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVhtvvfggfspealsGRIIDSNSkvvi 184
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--------------AALINYNL---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 tadegvrggRAVPLKKNVDeaLTNPevknieKVVVFkrtggdvawhehrdvwwhdaianvsadcppeemnaeDPLFILYT 264
Cdd:cd05940 63 ---------RGESLAHCLN--VSSA------KHLVV------------------------------------DAALYIYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGYLVYAAMtFKYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEgvpNYPNTSRMSE 344
Cdd:cd05940 90 SGTTGLPKAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRK---KFSASNFWDD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 345 VVdKHQVNILYTAPTAIRALMakgNEAVEGTSRD-SLRVMgsVGEPINPEAWEWYYKTIGNEQspIVDTWWQTE--TGGI 421
Cdd:cd05940 166 IR-KYQATIFQYIGELCRYLL---NQPPKPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFI 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 422 LIAPLPGATDLKPgSATRPFFGVQPALVD-NMGNIIEGAT-------DGNLVILDSWPGQMRTVHGDHDRFEQT---YFS 490
Cdd:cd05940 238 NFFGKPGAIGRNP-SLLRKVAPLALVKYDlESGEPIRDAEgrcikvpRGEPGLLISRINPLEPFDGYTDPAATEkkiLRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 491 TFK--GMYF-TSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIP---HDikGQAIYAYIT 564
Cdd:cd05940 317 VFKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGMAAIV 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 515671996 565 LNDG-EFPTAELHKEVKnwvrKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 395 LQPNeEFDLSALAAHLE----KNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
109-277 |
1.04e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 51.74 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 109 TFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVITADE 188
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 189 GVRGgravplkknvdeaLTNPEVKNIE--KVVVFKRTGGDVAWHEHRDVW-----WHDAI----ANVSADCPPEemnAED 257
Cdd:PLN02430 158 KIKE-------------LLEPDCKSAKrlKAIVSFTSVTEEESDKASQIGvktysWIDFLhmgkENPSETNPPK---PLD 221
|
170 180
....*....|....*....|
gi 515671996 258 PLFILYTSGSTGKPKGVMHT 277
Cdd:PLN02430 222 ICTIMYTSGTSGDPKGVVLT 241
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
439-616 |
1.19e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 51.63 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 439 RPFFGVQPALVDNMGNII--EGATDGNLVILDSWPGQmRTVHGDHDRFEQTYFSTfkgmyftSDGARRDEDGYYWITGRV 516
Cdd:PRK07008 360 RVIYGVDMKIVGDDGRELpwDGKAFGDLQVRGPWVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 517 DDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYAYITLNDGefptAELhkevknwVRKEI-----GPIA 591
Cdd:PRK07008 432 KDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPG----AEV-------TREELlafyeGKVA 500
|
170 180
....*....|....*....|....*...
gi 515671996 592 ---TPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 501 kwwIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
105-617 |
1.42e-06 |
|
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: 51.27 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALSGRIIDSNSKVVI 184
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TadegvrggravplkknvdealtnpevkniekvvvfkrtggdvawhEHRdvwwhDAIANVSADCPP--EEMNAEDPLFIL 262
Cdd:cd05939 81 F---------------------------------------------NLL-----DPLLTQSSTEPPsqDDVNFRDKLFYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 263 YTSGSTGKPKGVMHTTGGYLVYAAMTFkYVFDYQEGETFWCTADVGWITGHTYLVYGPLANGAKTILFEGVpnypNTSRM 342
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKF----SASNF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 SEVVDKHQVNILYTAPTAIRALMAKgnEAVEGTSRDSLRVMgsVGEPINPEAWEWYYKTIGNEQspIVDTWWQTETGGIL 422
Cdd:cd05939 186 WDDCVKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQ--IGEFYGATEGNSSL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 423 --IAPLPGATDLKP--GSATRPffgVQPALVD-NMGNIIEGaTDGnLVIL--DSWPGQM----------RTVHG------ 479
Cdd:cd05939 260 vnIDNHVGACGFNSriLPSVYP---IRLIKVDeDTGELIRD-SDG-LCIPcqPGEPGLLvgkiiqndplRRFDGyvnega 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 480 DHDRFEQTYFSTFKGMYFTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVG--IPHdIKGQ 557
Cdd:cd05939 335 TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGveVPG-VEGR 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 558 AIYAYITLNDGEFPTAELHKEvknwVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05939 414 AGMAAIVDPERKVDLDRFSAV----LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-555 |
1.67e-06 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 50.82 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 106 KTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHtVVFGGFSP-EALSGRIIDSNSKVVI 184
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVD-VVRGSDSSvEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 tadegvrggravplkknvdealtnpeVKNIEKvvvfkrtggDVAwhehrdvwwhdaianvsadcppeemnaedplFILYT 264
Cdd:cd17640 83 --------------------------VENDSD---------DLA-------------------------------TIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 265 SGSTGKPKGVMHTTGGyLVYAAMTFKYVFDYQEGETFWCTADVgWitgHTYlvygplANGAKTILFE--GVPNYPNTSRM 342
Cdd:cd17640 97 SGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSY------ERSAEYFIFAcgCSQAYTSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 343 SEVVDKHQVNILYTAPTAIRALMAKGNEAVEGTSRDSLRVMG---SVGE---PIN-----PEAWEWYYKTIGneqSPIVD 411
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 412 TWWQTETGGILIAPLPGATDLkpGSATRPFFGVQPALVD-NMGNIIEGATDGnlVILDSWPGQMRTVHGDHDRFEQTYFS 490
Cdd:cd17640 243 GYGLTETSPVVSARRLKCNVR--GSVGRPLPGTEIKIVDpEGNVVLPPGEKG--IVWVRGPQVMKGYYKNPEATSKVLDS 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515671996 491 tfKGMYFTSDGARRDEDGYYWITGRVDD--VLNvSGHRMGTAEIESALVAFDKIAEAAIVGipHDIK 555
Cdd:cd17640 319 --DGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG--QDQK 380
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
254-322 |
1.80e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 51.06 E-value: 1.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHTTGGylVYAAMtfkyvfdyqegetfwcTADVGWITGH-----TYLVYGPLA 322
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGN--LVAGI----------------AGLGDRVPELlgpddRYLAYLPLA 141
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-615 |
2.15e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.42 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 497 FTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPHDIKGQAIYA-YITlnDGEFPTAEL 575
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAkVIS--HEEIDPVQL 371
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515671996 576 HKevknWVRKEIGPIATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 372 RE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
84-289 |
1.30e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 47.94 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 84 RHLAE-RGDEVAIIwegddpADDKTLTFNELHKEVCLFSNALKEQGVRKGDVVCLYMPMVPEAAVAMLACTRIGAVHTVV 162
Cdd:PRK09029 10 RHWAQvRPQAIALR------LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 163 FGGFsPEALSGRIIDSNSKVVITADEgvrGGRAVPLKKNVDEALTNpevkniekvvvfkrtggdvawHEHRDVWWHDAIA 242
Cdd:PRK09029 84 NPQL-PQPLLEELLPSLTLDFALVLE---GENTFSALTSLHLQLVE---------------------GAHAVAWQPQRLA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515671996 243 NvsadcppeemnaedplFILyTSGSTGKPKGVMHTTGGYLVYAA-----MTF 289
Cdd:PRK09029 139 T----------------MTL-TSGSTGLPKAAVHTAQAHLASAEgvlslMPF 173
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
105-272 |
5.67e-05 |
|
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: 46.13 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 105 DKTLTFNELHKEVCLFSNALKEQ-GVRKGDVVCLYMPMVPEA-----AVAMLACtRIGAVHTVVFGGfspeALSGRIIDS 178
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFlwiwlGLAKLGC-PVAFLNTNIRSK----SLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 179 NSKVVITADEgvrggravpLKKNVDEALtnPEVKNiEKVVVFKRTGGDvawhEHRDVW-WHDAIANVSADCPPEEMNAE- 256
Cdd:cd05938 78 GAKVLVVAPE---------LQEAVEEVL--PALRA-DGVSVWYLSHTS----NTEGVIsLLDKVDAASDEPVPASLRAHv 141
|
170
....*....|....*....
gi 515671996 257 ---DPLFILYTSGSTGKPK 272
Cdd:cd05938 142 tikSPALYIYTSGTTGLPK 160
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
416-607 |
1.01e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.48 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 416 TETGGILIAPLPGAtdlKPGSATRPFFG-----------------------VQPALVDNMGNIIeGATDGNLvilDSWPG 472
Cdd:PRK07868 753 TTDGQAVLANVSGA---KIGSKGRPLPGagrvelaaydpehdlileddrgfVRRAEVNEVGVLL-ARARGPI---DPTAS 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 473 QMRTVHGDHDrfeqTYFSTfkGMYFtsdgaRRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPH 552
Cdd:PRK07868 826 VKRGVFAPAD----TWIST--EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEV 894
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515671996 553 DIKGQAIYAYITLNDGEFPTAELHKEVknwvrKEIGPIATPDVLHWTDSLPKTRS 607
Cdd:PRK07868 895 GGRQLAVAAVTLRPGAAITAADLTEAL-----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-322 |
2.00e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 44.51 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 108 LTFNELHKEVCLFSNALKEQGVR--KGDVVCLYMPMVPEAAVAMLACTRIGAVHTVVFGGFSPEALsgRIIDSNSKV-VI 184
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAI--EYILNHAEIsIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 185 TADEGVRggraVPLKKNVdEALTNpevKNIEKVVvfkrtggdvawhehrdvwwhdaianvsadcPPEemnAEDPLFILYT 264
Cdd:cd05927 84 FCDAGVK----VYSLEEF-EKLGK---KNKVPPP------------------------------PPK---PEDLATICYT 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 265 SGSTGKPKGVMHTTGGYLVYAAMTFKYVFDYQegetFWCTADVgwitghtYLVYGPLA 322
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFKILEILN----KINPTDV-------YISYLPLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
254-610 |
8.05e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.65 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 254 NAEDPLFILYTSGSTGKPKGVMHTTGGYLVYAAMTFKYVfDYQEGETFWCTADV----GwITGHTYLvygPLANGAKTIL 329
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVfhsfG-LTGGLVL---PLLSGVKVFL 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 330 FegvPNYPNTSRMSEVVdkHQVN--ILYTAPTairALMAKGNEAVEGTSRdSLRVMGSVGEPINPEAWEWYYKTIGNEqs 407
Cdd:PRK06814 866 Y---PSPLHYRIIPELI--YDTNatILFGTDT---FLNGYARYAHPYDFR-SLRYVFAGAEKVKEETRQTWMEKFGIR-- 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 408 pIVDTWWQTETGGILIAPLPGATdlKPGSATRPFFGVQPALVDNMGnIIEGatdGNL------VILdswpGQMRT----- 476
Cdd:PRK06814 935 -ILEGYGVTETAPVIALNTPMHN--KAGTVGRLLPGIEYRLEPVPG-IDEG---GRLfvrgpnVML----GYLRAenpgv 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671996 477 ----VHGDHDrfeqtyfstfkgmyfTSDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFDKIAEAAIVGIPH 552
Cdd:PRK06814 1004 leppADGWYD---------------TGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPD 1068
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515671996 553 DIKGQAIYAYITLNDGEfpTAELHKEVKnwvRKEIGPIATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK06814 1069 ARKGERIILLTTASDAT--RAAFLAHAK---AAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| |
