|
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: 1355.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 6 IYPVKQNIKAHTHADNDTYQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVkntsFDPGHIDIRWFEDGTLNISANCIDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPFDTV----LDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 86 LATRGDQVAIIWEGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 166 FSPEALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEALTNPEvkNISKVMVLKRTGGNVAWHEHRDIWWHEATAKVS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 246 DQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 326 KTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 406 KSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 486 QTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 566 NDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDTsNLGDTSTLADPSVVDRLIAEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
gi 258583962 646 AQLK 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: 1168.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 18 HADNDTYQAMYQQSITDPEGFWGEQGK-IVDWIKPFTKVKNTSFDPghiDIRWFEDGTLNISANCIDRHLATRGDQVAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 97 WEGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 177 DSNAKLVITADEGVRGGRAVPLKKNVDEALTNPEVKnISKVMVLKRTGGNVA-WHEHRDIWWHEATAKVSDQCQPEEMKA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS-VEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 YPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKSPIVDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 416 TETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGN-LVLLDSWPGQMRTVYGDHDRFEQTYFSTFKG 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 495 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 575 LHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDTSNLGDTSTLADPSVVDRLIAE 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: 1156.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 22 DTYQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVKNTSFDPghIDIRWFEDGTLNISANCIDRHLATRGDQVAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSKGP--PFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 102 PTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 182 LVITADEGVRGGRAVPLKKNVDEALTN-PEVKNiskVMVLKRTGGNVAWHEHRDIWWHEATAKVSDQCQPEEMKAEDPLF 260
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEKcPSVEK---VLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTA 340
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 341 RMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKSPIVDTWWQTETGG 420
Cdd:cd05966 316 RYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 421 ILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFEQTYFSTFKGMYFTGD 500
Cdd:cd05966 396 IMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 501 GARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVK 580
Cdd:cd05966 476 GARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELR 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 258583962 581 DWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGdTSNLGDTSTLAD 634
Cdd:cd05966 556 KHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 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: 923.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 68 RWFEDGTLNISANCIDRHLATRGDQVAIIWEGDDPTQdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 148 AMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEALtnPEVKNISKVMVLKRTGGNV 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAL--EELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 228 AWHEhrDIWWHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 308 GWITGHSYLVYGPLSNGAKTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 388 EPINPEAWEWYYRTIGnekSPIVDTWWQTETGGILITPLPGaTALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLL 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 468 DSWPGQMRTVYGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 548 VGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 258583962 628 DTSTLADPSVVDRLIA 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: 908.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 24 YQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVKNTSFDPGHIDIRWFEDGTLNISANCIDRHLATRGDQVAIIWEGDDPT 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 104 QDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEGVRGGRAVPLKKNVDEALtNPEVKNISKVMVLKRTGGNVAWHEHRDIWWHEATAKVSDQCQPEEMKAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTARMS 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 344 EVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKSPIVDTWWQTETGGILI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 424 TPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFEQTYFSTFKGMYFTGDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 504 RDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 258583962 584 RKEIGAIATPDVLHWTDALPKTRSDKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
24-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 835.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 24 YQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVK----NTSFDPGHIDIRWFEDGTLNISANCIDRHL-ATRGDQVAIIWE 98
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEvcseNLDVRKGPISIEWFKGGKTNICYNCLDRNVeAGNGDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 99 GDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDS 178
Cdd:PLN02654 112 GNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 179 NAKLVITADEGVRGGRAVPLKKNVDEALTNPEVKNIS--------KVMVLKRTggNVAWHEHRDIWWHEATAKVSDQCQP 250
Cdd:PLN02654 192 KPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSvgicltyeNQLAMKRE--DTKWQEGRDVWWQDVVPNYPTKCEV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILF 330
Cdd:PLN02654 270 EWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 331 EGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKSPIV 410
Cdd:PLN02654 350 EGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPIS 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 411 DTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFEQTYFS 490
Cdd:PLN02654 430 DTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 491 TFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVY 570
Cdd:PLN02654 510 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVP 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 571 PSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDTSNLGDTSTLADPSVVDRLIA 643
Cdd:PLN02654 590 YSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-639 |
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: 645.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 24 YQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVKNTSFDPGHidiRWFEDGTLNISANCIDRH-LATRGDQVAIIWEGDDP 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFT---RWFVGGRLNTCYNALDRHvEAGRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 103 TQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 183 VITADEGVRGGRAVPLKKNVDEALTNPEVKNIsKVMVLKRtgGNV---AWHEHRDIWWHEATAKV-SDQCQPEEmkAEDP 258
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSGHKPH-HVLVLNR--PQVpadLTKPGRDLDWSELLAKAePVDCVPVA--ATDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 259 LFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVP-NYP 337
Cdd:cd05967 233 LYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 338 TTARMSEVVDKHKVNILYTAPTAIRALmAKGD---EAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWW 414
Cdd:cd05967 313 DPGAFWRVIEKYQVNALFTAPTAIRAI-RKEDpdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 QTETGGILITPLPG--ATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVL-LDSWPGQMRTVYGDHDRFEQTYFST 491
Cdd:cd05967 389 QTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIkLPLPPGCLLTLWKNDERFKKLYLSK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 492 FKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYP 571
Cdd:cd05967 469 FPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 572 SAE-LHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDtsNLGDTSTLADPSVVD 639
Cdd:cd05967 549 TAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVLD 615
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-641 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 619.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 22 DTYQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVKNTSFDPGhidIRWFEDGTLNISANCIDRHLATRGDQVAIIWEGDD 101
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPF---ARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 102 PTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK 181
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 182 LVITADEGVRGGRAVPLKKNVDEALTNPEVKNiSKVMVLKRTGGNVAWHEHRDIWWHEATAKVSD-QCQPEEMKAEDPLF 260
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIALAQHKP-RHVLLVDRGLAPMARVAGRDVDYATLRAQHLGaRVPVEWLESNEPSY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTA 340
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 341 RMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGG 420
Cdd:PRK10524 318 IWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVIDNYWQTETGW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 421 ILITPLPG--ATALKPGSATRPFFGVQPALVD-NMGEIVEGATEGNLVLLDSW-PGQMRTVYGDHDRFEQTYFSTFKGM- 495
Cdd:PRK10524 395 PILAIARGveDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFGRQv 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 496 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDG-VYPSAE 574
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdSLADRE 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 575 ----LHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATG-DTsnlGDTSTLADPSVVDRL 641
Cdd:PRK10524 555 arlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI 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: 555.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 24 YQAMYQQSITDPEGFWGEQGKIVD--WIKPFTKVKNTSfdpGHIDI-RWFEDGTLNISANCIDRHLATRGDQVAIIWEGD 100
Cdd:cd05968 9 LEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS---GGKPWaAWFVGGRMNIVEQLLDKWLADTRTRPALRWEGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 101 DPTQdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNA 180
Cdd:cd05968 86 DGTS-RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 181 KLVITADEGVRGGRAVPLKKNVDEALTN-PEVKnisKVMVLKRTGGNVAWHEHRDIWWHEATAKVSDQCqpEEMKAEDPL 259
Cdd:cd05968 165 KALITADGFTRRGREVNLKEEADKACAQcPTVE---KVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGA--ERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 260 FILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGE-VFWCTaDVGWITGhSYLVYGPLSNGAKTILFEGVPNYPT 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 339 TARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKSPIVDTWWQTE- 417
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEi 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 418 TGGIL----ITPLpgatalKPGSATRPFFGVQPALVDNMGEIVEGaTEGNLVLLDSWPGQMRTVYGDHDRFEQTYFSTFK 493
Cdd:cd05968 398 SGGILgnvlIKPI------KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 494 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSA 573
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 574 ELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDtsNLGDTSTLADP 635
Cdd:cd05968 551 ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-628 |
5.29e-170 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 497.11 E-value: 5.29e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 69 WFEDGTLNISANCIDRHLAT-RGDQVAIIWEgdDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGgRKDKVALRYL--DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 148 AMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVRggravplKKNVDEAltnPEVKnisKVMVLKRTGGNv 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL---PSLK---HVLLVGEDVEE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 228 awhEHRDIWWHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADV 307
Cdd:PRK04319 180 ---GPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA-MLQHYQTGKYVLDLHEDDVYWCTADP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 308 GWITGHSYLVYGPLSNGAKTILFEGvpnypttaRMS-----EVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRI 382
Cdd:PRK04319 256 GWVTGTSYGIFAPWLNGATNVIDGG--------RFSperwyRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 383 MGSVGEPINPEAWEWYYRTIGNeksPIVDTWWQTETGGILITPLPgATALKPGSATRPFFGVQPALVDNMGEIVEGATEG 462
Cdd:PRK04319 328 ILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 463 NLVLLDSWPGQMRTVYGDHDRFEQtYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKI 542
Cdd:PRK04319 404 NLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 543 AEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK----I 618
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgL 560
|
570
....*....|
gi 258583962 619 ATGDTSNLGD 628
Cdd:PRK04319 561 PEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
108-619 |
1.68e-139 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 414.59 E-value: 1.68e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITad 187
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 egvrggravplkknvdealtNPEVKniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpEEMKAEDPLFILYTSGS 267
Cdd:cd05969 79 --------------------TEELY--------------------------------------ERTDPEDPTLLHYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTTGGYLVYAtMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGV--PNypttaRMSEV 345
Cdd:cd05969 101 TGTPKGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRfdAE-----SWYGI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 346 VDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGGILITP 425
Cdd:cd05969 175 IERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIAN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 426 LPGATAlKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFEQtYFSTfkGMYFTGDGARRD 505
Cdd:cd05969 252 YPCMPI-KPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 506 EDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRK 585
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQ 407
|
490 500 510
....*....|....*....|....*....|....
gi 258583962 586 EIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:cd05969 408 KLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
108-617 |
1.96e-113 |
|
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: 347.02 E-value: 1.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITad 187
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 egvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemKAEDPLFILYTSGS 267
Cdd:cd05972 79 ------------------------------------------------------------------DAEDPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTTGgYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTtaRMSEVVD 347
Cdd:cd05972 93 TGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 348 KHKVNILYTAPTAIRALMAKGDEAIKgtsRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGgILITPLP 427
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDLSSYK---FSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 428 GaTALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYGDHDRFEqtyfSTFKG-MYFTGDGARRDE 506
Cdd:cd05972 243 D-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTE----ASIRGdYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 507 DGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKE 586
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKV 397
|
490 500 510
....*....|....*....|....*....|.
gi 258583962 587 IGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05972 398 LAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
2.45e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 333.51 E-value: 2.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAiiWEGDDptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITADEgvrggravPLKKNVDEALTNPEVknISKVMVLKRTGGNVAWHEHrdiwwHEAT 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEV--VKLVLVLDRDPVLKEEPLP-----EEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 AKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTgGYLVYATMTFKYV----FDYQPGEVFWCTADVGWITGHSYLV 317
Cdd:pfam00501 141 PADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 318 YGPLSNGAKTILFEGVPNyPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEaiKGTSRDSLRIMGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP--KRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 398 YYRTIGNeksPIVDTWWQTETGGILITPLPGATAL-KPGSATRPFFGVQPALVD-NMGEIVEGATEGNLVLldSWPGQMR 475
Cdd:pfam00501 297 FRELFGG---ALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 258583962 476 TVYGDHDRFEQTYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:pfam00501 372 GYLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-623 |
1.78e-96 |
|
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: 303.66 E-value: 1.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITAdegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheat 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvsdqcqpeemkaedplFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTILFEGVpnypTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEPINPEAWEWYYRT 401
Cdd:COG0318 165 LAGATLVLLPRF----DPERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 402 IGnekSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRTVYGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 482 DRFEQTyfstFK-GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 561 AYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGDT 623
Cdd:COG0318 390 AFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-611 |
8.27e-90 |
|
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: 282.25 E-value: 8.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYvFDYQPGEVFWCTADVGWItGHSYLVYGPLSNGAKTILFEGvpny 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 337 PTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 417 ETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTvygdhDRFEQTYFSTFKGMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYW-----NNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 497 FTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElh 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 258583962 577 kEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
6.12e-88 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 280.94 E-value: 6.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 egvrggravplkknvdealtnpEVKNISKVmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkAEDPLFILYTSGS 267
Cdd:cd05973 79 ----------------------DAANRHKL-------------------------------------DSDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTT------GGYLVYAtmtfkyvFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTAR 341
Cdd:cd05973 100 TGLPKGVPVPLralaafGAYLRDA-------VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 mseVVDKHKVNILYTAPTAIRALMAKGDEA---IKGtsrdSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTET 418
Cdd:cd05973 173 ---VIERLGVTNLAGSPTAYRLLMAAGAEVparPKG----RLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTEL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 419 GGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEgategnlvlldswPGQMRTVYGDHDRFEQTYF--------S 490
Cdd:cd05973 243 GMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELG-------------PGEPGRLAIDIANSPLMWFrgyqlpdtP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 491 TFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGV 569
Cdd:cd05973 310 AIDGGYYlTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 258583962 570 YPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05973 390 EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
13-639 |
2.04e-83 |
|
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: 274.92 E-value: 2.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 13 IKAHTHADNDTYQAMYQQSITDPEGFWGEqgkIVDWIK-PFTKVKNTSFDPGHI--DIRWFEDGTLNIsANCIDRHlaTR 89
Cdd:cd05943 8 VNARHGLSLADYAALHRWSVDDPGAFWAA---VWDFSGvRGSKPYDVVVVSGRImpGARWFPGARLNY-AENLLRH--AD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIWEGDDPTQDKtLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:cd05943 82 ADDPAAIYAAEDGERTE-VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEALTnpEVKNISKVMVLKRTGGNV---AWHEHRDIWWHEATAKVSD 246
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVAAGqpdLSKIAKALTLEDFLATGAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 -QCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHsYLVYGpLSNGA 325
Cdd:cd05943 239 gELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWN-WLVSG-LAVGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 326 KTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNe 405
Cdd:cd05943 317 TIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 406 kspivDTWWQTETGGiliTPLPGATALK-------PGSATRPFFGVQPALVDNMGEIVEGATeGNLVLLDSWPGQMRTVY 478
Cdd:cd05943 396 -----DVLLASISGG---TDIISCFVGGnpllpvyRGEIQCRGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPSMPVGFW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 479 GDHD--RFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKG 556
Cdd:cd05943 467 NDPDgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 557 QAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGdtSNLGDTSTLADPS 636
Cdd:cd05943 547 ERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPE 624
|
...
gi 258583962 637 VVD 639
Cdd:cd05943 625 SLD 627
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
11-649 |
6.79e-83 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 274.36 E-value: 6.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 11 QNIKAHTHADNDTYQAMYQQSITDPEGFWGEqgkIVDWI-----KPFTKVKNtsfDPGHIDIRWFEDGTLNISANcIDRH 85
Cdd:PRK03584 23 RWLAARRGLSFDDYAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLA---GRRMPGARWFPGARLNYAEN-LLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 86 laTRGDQVAIIWEGDDpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGG 165
Cdd:PRK03584 96 --RRDDRPAIIFRGED-GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 166 FSPEALAGRIIDSNAKLVITADeGVR-GGRAVPLKKNVDEALtnPEVKNISKVMVLKRTG-GNVAWHEHRDIWWHEATAK 243
Cdd:PRK03584 173 FGVQGVLDRFGQIEPKVLIAVD-GYRyGGKAFDRRAKVAELR--AALPSLEHVVVVPYLGpAAAAAALPGALLWEDFLAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 244 VSD-QCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGE-VFWCTAdVGWITgHSYLVYGPL 321
Cdd:PRK03584 250 AEAaELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMM-WNWLVSGLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SnGAKTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRT 401
Cdd:PRK03584 328 V-GATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEH 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 402 IGNekspivDTWWQTETGGiliTPLPGATALkpGSATRP---------FFGVQPALVDNMGEIVEGATeGNLVLLDSWPG 472
Cdd:PRK03584 407 VKA------DVWLASISGG---TDICSCFVG--GNPLLPvyrgeiqcrGLGMAVEAWDEDGRPVVGEV-GELVCTKPFPS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 473 QMRTVYGDHD--RFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGV 550
Cdd:PRK03584 475 MPLGFWNDPDgsRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 551 PHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIM----RRILRKIATGDTSNL 626
Cdd:PRK03584 555 EWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAVNR 634
|
650 660
....*....|....*....|...
gi 258583962 627 GdtsTLADPSVVDrLIAEKAQLK 649
Cdd:PRK03584 635 D---ALANPEALD-WFADLAELR 653
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
79-616 |
2.84e-75 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 249.98 E-value: 2.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 79 ANCIDRHLA-TRGDQVAIIwegdDPTqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGA 157
Cdd:cd05959 6 ATLVDLNLNeGRGDKTAFI----DDA--GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 158 VHTIVFGGFSPEALAGRIIDSNAKLVITADEgvrggravpLKKNVDEALTNPEVKNisKVMVLKRTGGNVAWHEH-RDIW 236
Cdd:cd05959 80 VPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTKSEHTL--VVLIVSGGAGPEAGALLlAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 237 WHEAtakvsDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYL 316
Cdd:cd05959 149 AAEA-----EQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 VYGPLSNGAKTILFegvPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 397 WYYRTIGNEkspIVDTWWQTETGGILITPLPGAtaLKPGSATRPFFGVQPALVDNMGEIVEGATEGNL-VLLDSwpgqMR 475
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELyVRGPS----SA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 476 TVYgdHDRFEQTYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDI 554
Cdd:cd05959 370 TMY--WNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 555 KGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
106-616 |
7.02e-74 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 244.26 E-value: 7.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 adegvrggravplkknvDEAltnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaEDPLFILYTS 265
Cdd:cd05971 85 -----------------DGS--------------------------------------------------DDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 266 GSTGKPKGVLHTTG---GYLVYATMTFKyvFDYQPGEVFWCTADVGWItghsylvyGPLSNGAKTILFEGVP--NYPTTA 340
Cdd:cd05971 98 GTTGPPKGALHAHRvllGHLPGVQFPFN--LFPRDGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlAHRMTK 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 341 ----RMSEVVDKHKVNILYTAPTAIRALMAKGDEaiKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEkspIVDTWWQT 416
Cdd:cd05971 168 fdpkAALDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFGVE---VNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 417 EtGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTvYGDHDRFEQtyfSTFKGMY 496
Cdd:cd05971 243 E-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLG-YWNNPSATE---KKMAGDW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 497 F-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAEL 575
Cdd:cd05971 318 LlTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 258583962 576 HKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05971 398 AREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
74-616 |
5.22e-70 |
|
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: 236.62 E-value: 5.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 74 TLNISANCIDRHLATRGDQVAIIWeGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACT 153
Cdd:cd05970 15 NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 154 RIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVrggravpLKKNVDEALtnPEVKNISKvmvLKRTGGNVawhehR 233
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAA--PECPSKPK---LVWVGDPV-----P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 234 DIW--WHEATAKVSDQCQP----EEMKAEDPLFILYTSGSTGKPKGVLHTTGgYLVYATMTFKYVFDYQPGEVFWCTADV 307
Cdd:cd05970 157 EGWidFRKLIKNASPDFERptanSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 308 GWITGHSYLVYGPLSNGAKTILFEGVPNYPttARMSEVVDKHKVNILYTAPTAIRALMakgDEAIKGTSRDSLRIMGSVG 387
Cdd:cd05970 236 GWGKAVWGKIYGQWIAGAAVFVYDYDKFDP--KALLEKLSKYGVTTFCAPPTIYRFLI---REDLSRYDLSSLRYCTTAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 388 EPINPEAWEWYYRTIGNEkspIVDTWWQTETGgILITPLPGATAlKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVL- 466
Cdd:cd05970 311 EALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIr 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 467 -LDSWP-GQMRTVYGDHDRFEQTYFStfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAE 544
Cdd:cd05970 386 tSKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 545 AAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05970 463 CAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
103-616 |
6.63e-69 |
|
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: 230.81 E-value: 6.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 103 TQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKL 182
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 183 VITAdegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkAEDPLFIL 262
Cdd:cd05919 86 VVTS--------------------------------------------------------------------ADDIAYLL 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 263 YTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADV--GWITGHSylVYGPLSNGAKTILFegvPNYPTTA 340
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 341 RMSEVVDKHKVNILYTAPTAIRALMAKGDeaikGTSRD--SLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTET 418
Cdd:cd05919 173 RVLATLARFRPTVLYGVPTFYANLLDSCA----GSPDAlrSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 419 GGILITPLPGAtaLKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRTVYgdhDRFEQTYFSTFKGMYFT 498
Cdd:cd05919 246 GHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLV--RGPSAAVGYW---NNPEKSRATFNGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 499 GDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKE 578
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARD 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 258583962 579 VKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05919 399 IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
24-617 |
2.66e-68 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 235.02 E-value: 2.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 24 YQAMYQQSITDPEGFWGEQG-KIVDWIKPFTKVknTSFDPGHIDirWFEDGTLNISANCIDRHL--ATRGDQVAIIWEGd 100
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAkKYVHWDKMYDKV--YSGDEIYPD--WFKGGELNTCYNVLDIHVknPLKRDQDALIYEC- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 101 dPTQDKT--LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDS 178
Cdd:PTZ00237 85 -PYLKKTikLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 179 NAKLVITADEGVRGGRAVPLKKNVDEALTNPEVKNiSKVMVLKRtggNVAWHEHRDIW------------WHEATAKVSD 246
Cdd:PTZ00237 164 TPKLIITTNYGILNDEIITFTPNLKEAIELSTFKP-SNVITLFR---NDITSESDLKKietiptipntlsWYDEIKKIKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 QCQ-------PEEmkAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLvYG 319
Cdd:PTZ00237 240 NNQspfyeyvPVE--SSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 320 PLSNGAKTILFEG--VPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSR---DSLRIMGSVGEPINPEA 394
Cdd:PTZ00237 317 SLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEVIEESI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 395 WEWYYRTIGNEKSPIvdtWWQTETGgilITPLPGATAL-KPGSAT-RPFFGVQPALVDNMGEIVEGATEGNLVL-LDSWP 471
Cdd:PTZ00237 397 PEYIENKLKIKSSRG---YGQTEIG---ITYLYCYGHInIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFkLPMPP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 GQMRTVYGDHDRFEQTyFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVP 551
Cdd:PTZ00237 471 SFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIY 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 552 H-DIKGQAIYAYITLNDGVYPSAELHKevkdwVRKEIGAIATPDVLHWT--------DALPKTRSDKIMRRILRK 617
Cdd:PTZ00237 550 DpDCYNVPIGLLVLKQDQSNQSIDLNK-----LKNEINNIITQDIESLAvlrkiiivNQLPKTKTGKIPRQIISK 619
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
119-617 |
1.19e-62 |
|
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: 216.95 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 119 RFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEgvrggravp 197
Cdd:cd05928 53 KAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE--------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 198 LKKNVDE-ALTNPEVKniSKVMVLkrtggnvawHEHRDIW--WHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGV 274
Cdd:cd05928 124 LAPEVDSvASECPSLK--TKLLVS---------EKSRDGWlnFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 275 LHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAkTILFEGVPNYPTTARMsEVVDKHKVNIL 354
Cdd:cd05928 193 EHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRFDPLVIL-KTLSSYPITTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 355 YTAPTAIRALMAKGDEAIKgtsRDSLRIMGSVGEPINPEAWEWYYRTIGNEkspIVDTWWQTETGgiLITPLPGATALKP 434
Cdd:cd05928 271 CGAPTVYRMLVQQDLSSYK---FPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 435 GSATRPFFGVQPALVDNMGEIVEGATEGNLVL--LDSWPGQMRTVYGDHDrfEQTYfSTFKG-MYFTGDGARRDEDGYYW 511
Cdd:cd05928 343 GSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvKPIRPFGLFSGYVDNP--EKTA-ATIRGdFYLTGDRGIMDEDGYFW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 512 ITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGV--YPSAELHKEVKDWVRKEIGA 589
Cdd:cd05928 420 FMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlsHDPEQLTKELQQHVKSVTAP 499
|
490 500
....*....|....*....|....*...
gi 258583962 590 IATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05928 500 YKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
2.53e-61 |
|
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: 210.54 E-value: 2.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVItadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheat 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvsdqcqpeemkaEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTILFEGvpnyPTTARMSEVVDKHKVNILYTAPTAIRALMAKgdEAIKGTSRDSLRIMGSVGEPInPEAWEWYYRT 401
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATTDLSSLRAVIYGGAPM-PERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 402 IGNEkspIVDTWWQTETGGiLITPLPGATAL-KPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRtvyGD 480
Cdd:cd17631 236 RGVK---FVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA---GY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 HDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIY 560
Cdd:cd17631 307 WNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 258583962 561 AYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17631 387 AVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
83-616 |
2.89e-60 |
|
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: 208.57 E-value: 2.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIWegddptQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGA--VHT 160
Cdd:cd05936 6 EEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAvvVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 161 IVFggFSPEALAGRIIDSNAKLVITAdegvrggraVPLKKNVDEALTNPEvkniskvmvlkrtggnvawhehrdiwwhea 240
Cdd:cd05936 80 NPL--YTPRELEHILNDSGAKALIVA---------VSFTDLLAAGAPLGE------------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 takvsdqcqPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPG-EVFWCTADVgwitghsYLVYG 319
Cdd:cd05936 119 ---------RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGdDVVLAALPL-------FHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 320 -------PLSNGAKTILfegVPNyPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSrdSLRIMGSVGEPINP 392
Cdd:cd05936 183 ltvalllPLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFS--SLRLCISGGAPLPV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 393 EAWEWYYRTIGnekSPIVDTWWQTETG-GILITPLPGATalKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWP 471
Cdd:cd05936 257 EVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV--RGP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 GQMRtvyGDHDRFEQTYfSTFK-GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGV 550
Cdd:cd05936 330 QVMK---GYWNRPEETA-EAFVdGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 551 PHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05936 406 PDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-616 |
4.39e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 209.66 E-value: 4.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 72 DGTLNIsANCIDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTI-GRILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 152 CTRIGAV-HTI-VFggFSPEALAGRIIDSNAKLVITADEGVrggravPLKKNVDEALtnPEVKNISKVMVLKRTGGNVAW 229
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQL--PTVRTVIVEGDGPAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 230 HEHRDiwWHEATAKVSDQCQPEEMkaeDPLFILYTSGSTGKPKGVLHTtggY--LVYATMTFKYVFDYQPGEVF------ 301
Cdd:PRK06187 146 GEYEE--LLAAASDTFDFPDIDEN---DAAAMLYTSGTTGHPKGVVLS---HrnLFLHSLAVCAWLKLSRDDVYlvivpm 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 302 -----WctadvGWItghsylvYGPLSNGAKTILfegVPNYPTTaRMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTS 376
Cdd:PRK06187 218 fhvhaW-----GLP-------YLALMAGAKQVI---PRRFDPE-NLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 377 rdSLRIMGSVGEPINP---EAWEWYYrtigneKSPIVDTWWQTETGGIL-ITPLP---GATALKPGSATRPFFGVQPALV 449
Cdd:PRK06187 282 --SLRLVIYGGAALPPallREFKEKF------GIDLVQGYGMTETSPVVsVLPPEdqlPGQWTKRRSAGRPLPGVEARIV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 450 DNMGEIVE--GATEGNLVLLDSWpgQMRTVYGDHDRFEQTYFstfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRM 527
Cdd:PRK06187 354 DDDGDELPpdGGEVGEIIVRGPW--LMQGYWNRPEATAETID---GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 528 GTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAelhKEVKDWVRKEIGAIATPDVLHWTDALPKTRS 607
Cdd:PRK06187 429 YPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDELPRTSV 505
|
....*....
gi 258583962 608 DKIMRRILR 616
Cdd:PRK06187 506 GKILKRVLR 514
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
100-611 |
4.89e-58 |
|
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: 203.21 E-value: 4.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 100 DDPTqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSN 179
Cdd:cd05911 4 DADT-GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 180 AKLVITADEGVrggravplkKNVDEALTnpEVKNISKVMVLkrtGGNVAWHEHR-DIWWHEATAKVSDQCQPEEMKAEDP 258
Cdd:cd05911 83 PKVIFTDPDGL---------EKVKEAAK--ELGPKDKIIVL---DDKPDGVLSIeDLLSPTLGEEDEDLPPPLKDGKDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 259 LFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFD-YQPGEVFWCTADVGWITGHSYLVYGPLsNGAKTILFegvpNYP 337
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM----PKF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 338 TTARMSEVVDKHKVNILYTAPtAIRALMAKGDEAIKGTSRdSLRIMGSVGEPINPEAWEWYYRTIGNEKspIVDTWWQTE 417
Cdd:cd05911 224 DSELFLDLIEKYKITFLYLVP-PIAAALAKSPLLDKYDLS-SLRVILSGGAPLSKELQELLAKRFPNAT--IKQGYGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 418 TGGILITPLPGAtaLKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSwPGQMRTVYGDHdrfEQTYFSTFKGMYF 497
Cdd:cd05911 300 TGGILTVNPDGD--DKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRG-PQVMKGYYNNP---EATKETFDEDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 498 -TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGvyPSAELh 576
Cdd:cd05911 374 hTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG--EKLTE- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 258583962 577 KEVKDWVRKEIgaiatPDVLHW------TDALPKTRSDKIM 611
Cdd:cd05911 451 KEVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
103-616 |
1.40e-57 |
|
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: 200.78 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 103 TQDKTLTYKQLHQEVCRFSNALK-EQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAgRIIDsnak 181
Cdd:cd05958 6 SPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA-YILD---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 182 lvitadegvRGGRAVPLkknVDEALTnpevkniskvmvlkrtggnvawheHRDiwwheatakvsDQCqpeemkaedplFI 261
Cdd:cd05958 81 ---------KARITVAL---CAHALT------------------------ASD-----------DIC-----------IL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 262 LYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVpnypTTAR 341
Cdd:cd05958 103 AFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 MSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGGI 421
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHI 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 422 LITPLPGAtaLKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldswpgQMRTVY-GDHDRFEQTYFStfKGMYFTGD 500
Cdd:cd05958 254 FISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV------RGPTGCrYLADKRQRTYVQ--GGWNITGD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 501 GARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVK 580
Cdd:cd05958 324 TYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQ 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 258583962 581 DWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05958 404 DHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
9.45e-53 |
|
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: 187.39 E-value: 9.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtivfggfspealagrIIDsnAKLVITAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------VIP--ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EgvrggravpLKKNVDealtnpevkniskvmvlkRTGGNVAwhehrdiwwheatakvsdqCQPEEMKAEDPLFILYTSGS 267
Cdd:cd05974 63 D---------LRDRVD------------------RGGAVYA-------------------AVDENTHADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTTGGYLV--YATMtfkYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFegvpNYP--TTARMS 343
Cdd:cd05974 97 TSKPKLVEHTHRSYPVghLSTM---YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 344 EVVDKHKVNILYTAPTAIRALMakgdEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGgILI 423
Cdd:cd05974 170 AALVRYGVTTLCAPPTVWRMLI----QQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETT-ALV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 424 TPLPGATaLKPGSATRPFFGVQPALVDNMGEiveGATEGN--LVLLDSWP-GQMRTVYGDHDRfeqTYFSTFKGMYFTGD 500
Cdd:cd05974 242 GNSPGQP-VKAGSMGRPLPGYRVALLDPDGA---PATEGEvaLDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 501 GARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVK 580
Cdd:cd05974 315 IAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIF 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 258583962 581 DWVRKEIGAIATPDVLHWTDaLPKTRSDKIMRRILRKIA 619
Cdd:cd05974 395 RFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
68-617 |
2.41e-52 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 192.22 E-value: 2.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 68 RWFEDGTLNISANCIDRHLATRGDQVAIIW--EGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEA 145
Cdd:PLN03052 167 QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 146 AVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEAltnpevkNISKVMVLKRTGG 225
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA-------KAPKAIVLPADGK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 226 NVAWH-EHRDIWWHEATAKVSDQCQPEEMKA-----EDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVfDYQPGE 299
Cdd:PLN03052 320 SVRVKlREGDMSWDDFLARANGLRRPDEYKAveqpvEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGD 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 300 VF-WCTaDVGWITGHsYLVYGPLSNGAKTILFEGVPNYPTTARMsevVDKHKVNILYTAPTAIRALmaKGDEAIKGTSRD 378
Cdd:PLN03052 399 IVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTW--KNTNCMAGLDWS 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 SLRIMGSVGEPINPEAWEW-----YYRtigneksPIVDTWWQTETGGILITplpgATALKP---GSATRPFFGVQPALVD 450
Cdd:PLN03052 472 SIRCFGSTGEASSVDDYLWlmsraGYK-------PIIEYCGGTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFILD 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 451 NMGEIV--EGATEGNLVLLDSWPGQMRTVY-GDHDrfeQTYfstFKGM-YFTGDGARRDED-------GYYWITGRVDDV 519
Cdd:PLN03052 541 DSGNPYpdDAPCTGELALFPLMFGASSTLLnADHY---KVY---FKGMpVFNGKILRRHGDifertsgGYYRAHGRADDT 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 520 LNVSGHRMGTAEIESAL-VAFSKIAEAAVVGVPHDIKGQ---AIYAYITLNDGVYPSA-ELHKEVKDWVRKEIGAIATPD 594
Cdd:PLN03052 615 MNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPeqlVIAAVLKDPPGSNPDLnELKKIFNSAIQKKLNPLFKVS 694
|
570 580
....*....|....*....|...
gi 258583962 595 VLHWTDALPKTRSDKIMRRILRK 617
Cdd:PLN03052 695 AVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
102-617 |
2.25e-51 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 185.21 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 102 PTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK 181
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 182 LVITADEGvrGGRAVPLKKNVDEALTNPEVkniskvmvlkRTGGNVAWHEHRDIWWHEATAKVSDQcqPEEMKAEDPLFI 261
Cdd:cd05926 89 LVLTPKGE--LGPASRAASKLGLAILELAL----------DVGVLIRAPSAESLSNLLADKKNAKS--EGVPLPDDLALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 262 LYTSGSTGKPKGVLHTTGGYLV---YATMTFKYVFDyqpgevfwctaDVGWITGHSYLVYG-------PLSNGAKTILfe 331
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHRNLAAsatNITNTYKLTPD-----------DRTLVVMPLFHVHGlvasllsTLAAGGSVVL-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 332 gVPNYPTTARMSEVVDkHKVNiLYTA-PTAIRALMAKGDEAiKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIV 410
Cdd:cd05926 222 -PPRFSASTFWPDVRD-YNAT-WYTAvPTIHQILLNRPEPN-PESPPPKLRFIRSCSASLPPAVLEALEATFG---APVL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 411 DTWWQTETGG-ILITPLPgATALKPGSATRPFfGVQPALVDNMGEIVEGATEGNLVLLDswPGQMRTVYGDHdrfEQTYF 489
Cdd:cd05926 295 EAYGMTEAAHqMTSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNP---EANAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 490 STFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDG 568
Cdd:cd05926 368 AAFKDGWFrTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 258583962 569 VYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05926 448 ASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
9.78e-51 |
|
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: 183.89 E-value: 9.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 73 GTLNISANCIDRHLAT-RGDQVAIIwegdDPTqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI----DDI--SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 152 CTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEgvrggravpLKKNVDEALTN-PEVKNIskVMVLKRTGGNVAWH 230
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA---------LLPVIKAALGKsPHLEHR--VVVGRPEAGEVQLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 231 EhrdiwwheATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWI 310
Cdd:TIGR02262 144 E--------LLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 311 TGHSYLVYGPLSNGAKTILFegvPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSVGEPI 390
Cdd:TIGR02262 216 YGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLA--DPNLPSEDQVRLRLCTSAGEAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 391 NPEAWEWYYRTIGNEkspIVDTWWQTETGGILITPLPGAtaLKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSW 470
Cdd:TIGR02262 291 PAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLI--SG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 PGQMRTVYGDHDRFEqtyfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:TIGR02262 364 PSSATMYWNNRAKSR----DTFQGEWTrSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVG 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258583962 550 VP---HDIKGQaiyAYITLNDGvypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:TIGR02262 440 VAdedGLIKPK---AFVVLRPG---QTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-616 |
1.27e-50 |
|
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: 181.34 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITade 188
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 189 gvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaeDPLFILYTSGST 268
Cdd:cd05934 82 --------------------------------------------------------------------DPASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 269 GKPKGVLhTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILfegVPNYPTTARMSEVvDK 348
Cdd:cd05934 94 GPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRFSASRFWSDV-RR 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 349 HKVNILYTAPTAIRALMAkgdEAIKGTSRDS-LRIMGsvGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGGILITPLP 427
Cdd:cd05934 169 YGATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 428 GATalKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYgdHDRFEQTYFSTFKGMYFTGDGARRDED 507
Cdd:cd05934 241 EPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGY--YNMPEATAEAMRNGWFHTGDLGYRDAD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 508 GYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEI 587
Cdd:cd05934 317 GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCEGQL 393
|
490 500
....*....|....*....|....*....
gi 258583962 588 GAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05934 394 AYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
1.09e-49 |
|
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: 179.26 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVfggfSPEA 170
Cdd:cd05930 2 DAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRII----DSNAKLVITAdegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsd 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLTD------------------------------------------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 qcqpeemkAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATmTFKYVFDYQPGEVFWCTA----DVGWitghsYLVYGPLS 322
Cdd:cd05930 92 --------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WMQEAYPLTPGDRVLQFTsfsfDVSV-----WEIFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 NGAKTILF-EGVPNYPttARMSEVVDKHKVNILYTAPTAIRALMakgdEAIKGTSRDSLRIMGSVGEPINPEAWEWYYR- 400
Cdd:cd05930 158 AGATLVVLpEEVRKDP--EALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVRRWREl 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 401 ----TIGNEKSP----IVDTWWQTETGGILITPLP-GatalkpgsatRPFFGVQPALVD-NMGEIVEGATeGNLVLldSW 470
Cdd:cd05930 232 lpgaRLVNLYGPteatVDATYYRVPPDDEEDGRVPiG----------RPIPNTRVYVLDeNLRPVPPGVP-GELYI--GG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 PGQMRTVYGDHD----RFEQTYFSTFKGMYFTGDGARRDEDG--YYwiTGRVDDVLNVSGHRMGTAEIESALVAFSKIAE 544
Cdd:cd05930 299 AGLARGYLNRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVRE 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 545 AAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRR 613
Cdd:cd05930 377 AAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
84-617 |
9.92e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 178.17 E-value: 9.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLATR-GDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV---- 158
Cdd:PRK07656 12 ARAARRfGDKEAYV------FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVvvpl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 159 HTIvfggFSPEALAGRIIDSNAKLVITADEgvrggrAVPLKKNVDEALtnPEVKNIskvmVLKRTGGNVAwHEHRDIWWH 238
Cdd:PRK07656 86 NTR----YTADEAAYILARGDAKALFVLGL------FLGVDYSATTRL--PALEHV----VICETEEDDP-HTEKMKTFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 239 EATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHT----------TGGYL-------VYATMTFKYVFDYQpgevf 301
Cdd:PRK07656 149 DFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLThrqllsnaadWAEYLgltegdrYLAANPFFHVFGYK----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 302 wctadVGWITghsylvygPLSNGAkTILFEGVPNyptTARMSEVVDKHKVNILYTAPTAIRALMAkgdeAIKGTSRD--S 379
Cdd:PRK07656 224 -----AGVNA--------PLMRGA-TILPLPVFD---PDEVFRLIETERITVLPGPPTMYNSLLQ----HPDRSAEDlsS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 380 LRIMGSVGEPINPEAWEWYYRTIGNEkspIVDTWWQ-TETGGIL-ITPLPGATALKPGSATRPFFGVQPALVDNMGEIVE 457
Cdd:PRK07656 283 LRLAVTGAASMPVALLERFESELGVD---IVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 458 GATEGNLVLldSWPGQMRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:PRK07656 360 VGEVGELLV--RGPNVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 538 AFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
107-617 |
2.71e-46 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 169.87 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 107 TLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITA 186
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 187 DEgvrggravplkknvdealtnpevkniskvmvlkrtggnvaWHEHRdiwwheatakvsdqcqPEEMKAeDPLFILYTSG 266
Cdd:cd05903 81 ER----------------------------------------FRQFD----------------PAAMPD-AVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 267 STGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVpnypTTARMSEVV 346
Cdd:cd05903 104 TTGEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 347 DKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEPINP----EAWEwyyrtIGNEKspIVDTWWQTETGGIL 422
Cdd:cd05903 179 REHGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRslarRAAE-----LLGAK--VCSAYGSTECPGAV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 423 ITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDswPGqmrTVYGDHDRFEQTYFSTFKGMYFTGDGA 502
Cdd:cd05903 250 TSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRG--PS---VFLGYLDRPDLTADAAPEGWFRTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 503 RRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDw 582
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLD- 403
|
490 500 510
....*....|....*....|....*....|....*
gi 258583962 583 vRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05903 404 -RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
90-615 |
4.23e-46 |
|
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: 170.88 E-value: 4.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIwegdDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVITADEGVrggravplkknvdealtnPEVKNISKVMVLKRTGGNVAWHEHRDIwwHEATakvSDQCQ 249
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELA------------------EKLASLALPVVLLDSAEFDSLSFSDLL--FEAD---EAEPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 PEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQ--PGEVFWCTADVGWITGHSYLVYGPLSNGAKT 327
Cdd:cd05904 152 VVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 328 ILfegVPNYPTTArMSEVVDKHKVNILYTAPTAIRAlMAKGDEAIKGtSRDSLRIMGSVGEPINPEAWEWYYRTIGNekS 407
Cdd:cd05904 231 VV---MPRFDLEE-LLAAIERYKVTHLPVVPPIVLA-LVKSPIVDKY-DLSSLRQIMSGAAPLGKELIEAFRAKFPN--V 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 408 PIVDTWWQTETGGIL-ITPLPGATALKPGSATRPFFGVQPALVD-NMGEIVEGATEGNLvlldsW---PGQMRTVYGDHD 482
Cdd:cd05904 303 DLGQGYGMTESTGVVaMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGEL-----WirgPSIMKGYLNNPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 483 RFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAY 562
Cdd:cd05904 378 ATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAF 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 258583962 563 ITLNdgvyPSAEL-HKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd05904 456 VVRK----PGSSLtEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-617 |
8.88e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 167.42 E-value: 8.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEgvrggravpLKKNVDEALTNPEVKNISKVMVLKRTGGNVAWHEHRDiwWHEATAKVSDQcqp 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFAD--WAEAGSVAEPD--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYatmtfKYVFdyqpgevfwCTADVGW----ITGHSYLVY-------- 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHRA-LIA-----EYVS---------CIVAGDMsaddIPLHALPLYhcaqldvf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 -GP-LSNGAKTILFEGvpnyPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikgtSRD--SLRiMGSVGEPINPea 394
Cdd:PRK08316 231 lGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPDFD----TRDlsSLR-KGYYGASIMP-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 395 wewyyRTIGNE---KSPIVDTW---WQTEtggilITPLpgATAL-------KPGSATRPFFGVQPALVDNMGEIVEGATE 461
Cdd:PRK08316 300 -----VEVLKElreRLPGLRFYncyGQTE-----IAPL--ATVLgpeehlrRPGSAGRPVLNVETRVVDDDGNDVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 462 GNLVLLDswPGQMRTVYGDHDRFEQTyfstFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFS 540
Cdd:PRK08316 368 GEIVHRS--PQLMLGYWDDPEKTAEA----FRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHP 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 541 KIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK08316 442 AVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
5.54e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 164.60 E-value: 5.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 139 MPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEAltnpevkNISKVM 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA-------APAKAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 219 VLKRTGGNVAWH-EHRDIWWHE--ATAKVSDQC-----QPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDflGVAAAQGSVggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 291 YVfDYQPGEVFWCTADVGWITGhSYLVYGPLSNGAKTILFEGVpnyPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDE 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA---PLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 371 AIKGTSRDSLRIMGSVGEPINPEAWEW------YYRtigneksPIVDTWWQTETGG--ILITPL-PGAtalkPGSATRPF 441
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWlssvrgYYK-------PVIEYCGGTELASgyISSTLLqPQA----PGAFSTAS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 442 FGVQPALVDNMGEI--VEGATEGNLVLLDSWPG-QMRTVYGDHDrfeQTYF-----STFKGMYFT--GDGARRDEDGYYW 511
Cdd:PLN03051 298 LGTRFVLLNDNGVPypDDQPCVGEVALAPPMLGaSDRLLNADHD---KVYYkgmpmYGSKGMPLRrhGDIMKRTPGGYFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 512 ITGRVDDVLNVSGHRMGTAEIESALV-AFSKIAEAAVVGVPhDIKGQAIYAYITLNDGV----YPSAE---LHKEVKDWV 583
Cdd:PLN03051 375 VQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEekkgFDQARpeaLQKKFQEAI 453
|
490 500 510
....*....|....*....|....*....|...
gi 258583962 584 RKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PLN03051 454 QTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-624 |
1.57e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 164.46 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIWEGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:PRK13295 31 DACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVItadegvrggraVP-LKKNVD-EALTN---PEVKNISKVMVLKRTGGN--------VAW 229
Cdd:PRK13295 111 MPIFRERELSFMLKHAESKVLV-----------VPkTFRGFDhAAMARrlrPELPALRHVVVVGGDGADsfeallitPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 230 HEHRDIwwheatAKVSDQCQPEemkAEDPLFILYTSGSTGKPKGVLHTT----GGYLVYATMtfkyvFDYQPGEVFWCTA 305
Cdd:PRK13295 180 EQEPDA------PAILARLRPG---PDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 306 DVGWITGHSYLVYGPLSNGAKTILFEGVPNypttARMSEVVDKHKVNilYT-APTAIRALMAKGDEAiKGTSRDSLRIMG 384
Cdd:PRK13295 246 PMAHQTGFMYGLMMPVMLGATAVLQDIWDP----ARAAELIRTEGVT--FTmASTPFLTDLTRAVKE-SGRPVSSLRTFL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 385 SVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNL 464
Cdd:PRK13295 319 CAGAPIPGALVERARAALG---AKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 465 vlldswpgQMR--TVYGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKI 542
Cdd:PRK13295 396 --------QVRgcSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 543 AEAAVVGVPHDIKGQAIYAYITLNdgvyPSAELHKE-VKDWVRKEIGAIA-TPDVLHWTDALPKTRSDKIMRRILRKIAT 620
Cdd:PRK13295 468 AQVAIVAYPDERLGERACAFVVPR----PGQSLDFEeMVEFLKAQKVAKQyIPERLVVRDALPRTPSGKIQKFRLREMLR 543
|
....
gi 258583962 621 GDTS 624
Cdd:PRK13295 544 GEDA 547
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-617 |
3.88e-43 |
|
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: 162.64 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 104 QDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLV 183
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEgvrggravPLKKNVDEALTNPEVKNISKVMVLKRTGGNVAWHEHRDiwWhEATAKVSDQCQPEEMKAEDPLFILY 263
Cdd:TIGR03098 102 VTSSE--------RLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPAS--W-PKLLALGDADPPHPVIDSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVL--HTTggyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGpLSNGAKTILFegvpNYPTTAR 341
Cdd:TIGR03098 171 TSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLH----DYLLPRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 MSEVVDKHKVnilyTAPTAIRALMAK-GDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKspIVDTWWQTETGG 420
Cdd:TIGR03098 243 VLKALEKHGI----TGLAAVPPLWAQlAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMYGLTEAFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 421 ILITPlPGATALKPGSATR--PFFGVQ-------PALVDNMGEIVEgatEGNLVLLDSWPGQMRTVygdhDRFE----QT 487
Cdd:TIGR03098 317 STYLP-PEEVDRRPDSIGKaiPNAEVLvlredgsECAPGEEGELVH---RGALVAMGYWNDPEKTA----ERFRplppFP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 488 YFSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLN 566
Cdd:TIGR03098 389 GELHLPELaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPP 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 258583962 567 DGVypsaELHKEV-KDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:TIGR03098 469 GGE----ELDRAAlLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-616 |
1.22e-40 |
|
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: 155.19 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:cd17651 1 FERQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITADEgvrggravplkknvDEALTNPEVKNISKVMVLKRTGGNVAwhehrdiwwhEAT 241
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLTHPA--------------LAGELAVELVAVTLLDQPGAAAGADA----------EPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 AKVSdqcqpeemkAEDPLFILYTSGSTGKPKGVL--HTTGGYLVY------------ATMTFKYV-FDYQPGEVFwctad 306
Cdd:cd17651 131 PALD---------ADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAwqarasslgpgaRTLQFAGLgFDVSVQEIF----- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 307 vgwitghSYLVYGplsngaKTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSV 386
Cdd:cd17651 197 -------STLCAG------ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 387 GEP--INPEAWEWY----YRTIGNEKSPivdtwwqTETGGILITPLPGATALKPGSAT--RPFFGVQPALVDNMGEIVEG 458
Cdd:cd17651 262 GEQlvLTEDLREFCaglpGLRLHNHYGP-------TETHVVTALSLPGDPAAWPAPPPigRPIDNTRVYVLDAALRPVPP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 459 ATEGNLVLldSWPGQMRTVYGD----HDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:cd17651 335 GVPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 535 ALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRI 614
Cdd:cd17651 413 ALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRA 489
|
..
gi 258583962 615 LR 616
Cdd:cd17651 490 LP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
1.64e-40 |
|
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: 152.80 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHtIVFGGFSPEALAGRII-DSNAKLVITA 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAY-VPLDPAYPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 187 DEGvrggravplkkNVDEALTNPEVKNISKVMVLKRTGGNVAwhEHRDIwwheatakvsdqcqpeEMKAEDPLFILYTSG 266
Cdd:TIGR01733 80 SAL-----------ASRLAGLVLPVILLDPLELAALDDAPAP--PPPDA----------------PSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 267 STGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTA----DVgwitghSYL-VYGPLSNGAKTILFEGVPNYPTTAR 341
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFAslsfDA------SVEeIFGALLAGATLVVPPEDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 MSEVVDKHKVNILYTAPTAIRALMAKGDEAIkgtsrDSLRIMGSVGEPINPEAWEWYYRTIGNekSPIVDTWWQTETG-- 419
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALLAAALPPAL-----ASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTETTvw 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 420 -GILITPLPGATALKPGSATRPFFGVQPALVDNMGEIV-EGATeGNLVLldSWPGQMRtvyGDHDRFEQT---------Y 488
Cdd:TIGR01733 277 sTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVpVGVV-GELYI--GGPGVAR---GYLNRPELTaerfvpdpfA 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 489 FSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAV 547
Cdd:TIGR01733 351 GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
1.91e-40 |
|
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: 153.56 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 86 LATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 166 FSPEALAgRIIDSNAKLVITADEGvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvs 245
Cdd:cd05945 75 SPAERIR-EILDAAKPALLIADGD-------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 246 dqcqpeemkaeDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYvFDYQPGEVFWCTAD------VgwitghsYLVYG 319
Cdd:cd05945 98 -----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPfsfdlsV-------MDLYP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 320 PLSNGAKTILfegVPNYPTT--ARMSEVVDKHKVNILYTAPTAIRalMAKGDEAIKGTSRDSLRIMGSVGEPI-NPEAWE 396
Cdd:cd05945 159 ALASGATLVP---VPRDATAdpKQLFRFLAEHGITVWVSTPSFAA--MCLLSPTFTPESLPSLRHFLFCGEVLpHKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 397 WYYRTignEKSPIVDTWWQTET----GGILITPLPgATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPG 472
Cdd:cd05945 234 LQQRF---PDARIYNTYGPTEAtvavTYIEVTPEV-LDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVI--SGPS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 473 QMRTVYGDHDRFEQTYFSTFK-GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVP 551
Cdd:cd05945 308 VSKGYLNNPEKTAAAFFPDEGqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKY 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258583962 552 HDIKGQAIYAYITLNDGVypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd05945 388 KGEKVTELIAFVVPKPGA--EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
9.29e-40 |
|
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: 152.43 E-value: 9.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDealtnpevkniskvmvlkrtggnvawhehrdiwwHEAT 241
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLG----------------------------------DEAL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 AKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTA----DV-GWitghsyL 316
Cdd:cd17646 124 AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTplsfDVsVW------E 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 VYGPLSNGAKTILFE----GVPNYpttarMSEVVDKHKVNILYTAPTAIRALMAKGDeaikGTSRDSLRIMGSVGEPINP 392
Cdd:cd17646 197 LFWPLVAGARLVVARpgghRDPAY-----LAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 393 EAWEWYYRTIG----NEKSP---IVD-TWWQTeTGGILITPLP-GatalkpgsatRPFFGVQPALVDNMGEIVEGATEGN 463
Cdd:cd17646 268 ELAARFLALPGaelhNLYGPteaAIDvTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 464 LVLldswpGQMRTVYGDHDRFEQTY-------FSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:cd17646 337 LYL-----GGVQLARGYLGRPALTAerfvpdpFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 537 VAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYP--SAELHKEVKDWVRkeigAIATPDVLHWTDALPKTRSDKIMRRI 614
Cdd:cd17646 412 AAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpdTAALRAHLAERLP----EYMVPAAFVVLDALPLTANGKLDRAA 487
|
.
gi 258583962 615 L 615
Cdd:cd17646 488 L 488
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
2.32e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 152.88 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 AD---------------EGV---RGGRAVPLKKNvdeaLTNPEVKNISKVMVLKrtggnVAWHEHRDIW---WHEATAKV 244
Cdd:PRK06710 128 LDlvfprvtnvqsatkiEHVivtRIADFLPFPKN----LLYPFVQKKQSNLVVK-----VSESETIHLWnsvEKEVNTGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 245 SDQCQPEEmkaeDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGE-VFWCTADVGWITGHSYLVYGPLSN 323
Cdd:PRK06710 199 EVPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEeVVLGVLPFFHVYGMTAVMNLSIMQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 324 GAKTILfegVPNYPTTArMSEVVDKHKVNILYTAPTAIRALMakGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIG 403
Cdd:PRK06710 275 GYKMVL---IPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 404 ---------NEKSPIVDT--WWQTETGGILITPLPGATA----LKPGSATRPffgvqpalvdnmGEIVEGATEGNLVLLD 468
Cdd:PRK06710 349 gklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTEAmimsLETGEALPP------------GEIGEIVVKGPQIMKG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 469 SWpgqmrtvygdhDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVV 548
Cdd:PRK06710 417 YW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 549 GVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK06710 486 GVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-616 |
3.52e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 151.29 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 73 GTLNISAncidrhLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLAC 152
Cdd:PRK06188 15 GHLLVSA------LKRYPDRPALVLG------DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 153 TRIGAVHTIVFGGFSPEALAGRIIDSNAKLVItADEGVRGGRAVPLKKNVDealtnpevkNISKVMVLKRTGGNVawheh 232
Cdd:PRK06188 83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVPDGV----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 233 rDIWwhEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYlvyATMTFkyvfdyqpgevfWCTADVGWITG 312
Cdd:PRK06188 148 -DLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI---ATMAQ------------IQLAEWEWPAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 313 HSYLVYGPLSNGAktilfeGVPNYPTTARMSEV--------------VDKHKVNILYTAPTAIRALMAKGDEAikgtSRD 378
Cdd:PRK06188 210 PRFLMCTPLSHAG------GAFFLPTLLRGGTVivlakfdpaevlraIEEQRITATFLVPTMIYALLDHPDLR----TRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 --SLRIMGSVGEPINP----EAWEwyyrTIGneksPI-VDTWWQTETGgILITPLP-----GATALKPGSATRPFFGVQP 446
Cdd:PRK06188 280 lsSLETVYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGLRV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 447 ALVDNMGEIVEGATEGNLVLldSWPGQMRtvyGDHDRFEQTYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK06188 351 ALLDEDGREVAQGEVGEICV--RGPLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGF 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 526 RMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKT 605
Cdd:PRK06188 425 NVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLT 501
|
570
....*....|.
gi 258583962 606 RSDKIMRRILR 616
Cdd:PRK06188 502 ALGKPDKKALR 512
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
1.30e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 151.26 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIW--EGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLActriGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 160 TIVF---GGFSPEALAGRIIDSNAKLVITAdeGVRGGRAVPLKknVDEALTN-PEVKNISKVMVLKRTGGNVAW------ 229
Cdd:PRK07529 107 GIANpinPLLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQK--VAEVLAAlPELRTVVEVDLARYLPGPKRLavplir 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 230 --HEHRDIWWHEATAKVSDQC--QPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWC-- 303
Cdd:PRK07529 183 rkAHARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCgl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 304 ----------TADVGWITGHSYLVYGPLsnGAKTilfEGVpnyptTARMSEVVDKHKVNILYTAPTAIRALMakgDEAIK 373
Cdd:PRK07529 262 plfhvnallvTGLAPLARGAHVVLATPQ--GYRG---PGV-----IANFWKIVERYRINFLSGVPTVYAALL---QVPVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 374 GTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTE-TGGILITPLPGatALKPGSATRPFFG--VQPALVD 450
Cdd:PRK07529 329 GHDISSLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 451 NMGEIVEGATEGNL-VLLDSWPGqmrtVYGDHDRFEQTYFSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMG 528
Cdd:PRK07529 404 DAGRYLRDCAVDEVgVLCIAGPN----VFSGYLEAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNID 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 529 TAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGA-IATPDVLHWTDALPKTRS 607
Cdd:PRK07529 480 PAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAErAAVPKHVRILDALPKTAV 556
|
570
....*....|...
gi 258583962 608 DKIMRRILRKIAT 620
Cdd:PRK07529 557 GKIFKPALRRDAI 569
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-615 |
1.93e-38 |
|
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: 148.50 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVIT--ADEGVRGGRAVPLkknvdealtnpevkniskvmvlkrtggnvawhEHRDIWWHEA 240
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTdrSLAGRAGGLEVAV--------------------------------VIDEALDAGP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 TAKVSDQCQPEemkaeDPLFILYTSGSTGKPKGVLHTTGGY--LVYATmtfKYVfDYQPGEVFWCTADVGWiTGHSYLVY 318
Cdd:cd12117 126 AGNPAVPVSPD-----DLAYVMYTSGSTGRPKGVAVTHRGVvrLVKNT---NYV-TLGPDDRVLQTSPLAF-DASTFEIW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 GPLSNGAKTILFE-GVPNYPTtaRMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGtsrdsLRIMGSVGEPINPEAwew 397
Cdd:cd12117 196 GALLNGARLVLAPkGTLLDPD--ALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPPH--- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 398 yYRTIGNEKSP--IVDTWWQTETGGI----LITPL-PGATALKPGsatRPFFGVQPALVDNMGEIVEGATEGNLVLldSW 470
Cdd:cd12117 266 -VRRVLAACPGlrLVNGYGPTENTTFttshVVTELdEVAGSIPIG---RPIANTRVYVLDEDGRPVPPGVPGELYV--GG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 PGQMRTVYGDHD----RFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAA 546
Cdd:cd12117 340 DGLALGYLNRPAltaeRFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAV 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 547 VVGVPHDIKGQAIYAYITLNDGVYPSaelhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd12117 420 VVVREDAGGDKRLVAYVVAEGALDAA-----ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
5.99e-38 |
|
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: 146.68 E-value: 5.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 eemKAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYATmtfKYVFDYQPGEVfwctadvgWITGHSYL-------VYGPL 321
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVvsHANVLALFAAT---QRWFGFNEDDV--------WTLFHSYAfdfsvweIWGAL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTILfegVPNYptTARMSE----VVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLR--IMGsvGEPINPEAW 395
Cdd:cd17643 157 LHGGRLVV---VPYE--VARSPEdfarLLRDEGVTVLNQTPSAFYQLVEAADRD--GRDPLALRyvIFG--GEALEAAML 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 396 EWYYRTIGNEKSPIVDTWWQTET----GGILITP--LPGATALKPGsatRPFFGVQPALVDNMGEIVEGATEGNLVLldS 469
Cdd:cd17643 228 RPWAGRFGLDRPQLVNMYGITETtvhvTFRPLDAadLPAAAASPIG---RPLPGLRVYVLDADGRPVPPGVVGELYV--S 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 470 WPGQMRtvyGDHDRFEQT--YF--STFKG----MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSK 541
Cdd:cd17643 303 GAGVAR---GYLGRPELTaeRFvaNPFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPS 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 542 IAEAAVVgVPHDIKG-QAIYAYITLNDGvypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17643 380 VRDAAVI-VREDEPGdTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
105-616 |
3.17e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.43 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGVRGGRAVPlkknvdEALTNPevkniskVMVLKRTGGNVAWHEHrdiwWHEATAKVSDQCQPEEMKAEDplfILYT 264
Cdd:PRK08276 89 VSAALADTAAELA------AELPAG-------VPLLLVVAGPVPGFRS----YEEALAAQPDTPIADETAGAD---MLYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYLVYAT---MTFKYVFDYQPGEvfwctadvgwitGHSYLVYGPL-----SNGAKTILFEGVpny 336
Cdd:PRK08276 149 SGTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYGGP------------DSVYLSPAPLyhtapLRFGMSALALGG--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 337 pTTARMS--------EVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEA----WEWYyrtign 404
Cdd:PRK08276 214 -TVVVMEkfdaeealALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVkramIDWW------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 405 ekSPIVD-TWWQTETGGI-LITPlpgATAL-KPGSATRPFFGVQPALVDNMGEIVegategnlvlldswPGQMRTVYGD- 480
Cdd:PRK08276 287 --GPIIHeYYASSEGGGVtVITS---EDWLaHPGSVGKAVLGEVRILDEDGNELP--------------PGEIGTVYFEm 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 -------HDRFEQTYFSTFKGMYFT-GDGARRDEDGYYWITGRVDDVLnVSGhrmGT----AEIESALVAFSKIAEAAVV 548
Cdd:PRK08276 348 dgypfeyHNDPEKTAAARNPHGWVTvGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAVF 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 549 GVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK08276 424 GVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
5.57e-37 |
|
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: 143.58 E-value: 5.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQG-VRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtivfggfspe 169
Cdd:cd05941 1 DRIAIV------DDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 alagriidsnaklvitadegvrggrAVPLKKNVDEA-----LTNPEVKniskvMVLkrtggnvawhehrdiwwheatakv 244
Cdd:cd05941 64 -------------------------AVPLNPSYPLAeleyvITDSEPS-----LVL------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 245 sdqcqpeemkaeDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYvFDYQPGEVF--------------------WCT 304
Cdd:cd05941 90 ------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLlhvlplhhvhglvnallcplFAG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 305 ADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTtaRMSEVVDKHkvnilYTAPTAIRALMAKGdeaikgtsrdsLRIM- 383
Cdd:cd05941 157 ASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYT--RLLQYYEAH-----FTDPQFARAAAAER-----------LRLMv 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 384 -GSVGEPInPEAWEWYYRTiGNeksPIVDTWWQTETGGILITPLPGATalKPGSATRPFFGVQPALVD-NMGEIVEGATE 461
Cdd:cd05941 219 sGSAALPV-PTLEEWEAIT-GH---TLLERYGMTEIGMALSNPLDGER--RPGTVGMPLPGVQARIVDeETGEPLPRGEV 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 462 GNL------VLLDSWPGQMRTVygdhDRFeqtyfsTFKGMYFTGDGARRDEDGYYWITGRV-DDVLNVSGHRMGTAEIES 534
Cdd:cd05941 292 GEIqvrgpsVFKEYWNKPEATK----EEF------TDDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIER 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 535 ALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRI 614
Cdd:cd05941 362 VLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE--ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKE 439
|
...
gi 258583962 615 LRK 617
Cdd:cd05941 440 LRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
2.62e-36 |
|
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: 141.46 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITAD 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EgvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkAEDPLFILYTSGS 267
Cdd:cd05935 82 E------------------------------------------------------------------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAkTILFEGVPNYPTTArmsEVVD 347
Cdd:cd05935 96 TGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG-TYVLMARWDRETAL---ELIE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 348 KHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEkspIVDTWWQTETGGILITPLP 427
Cdd:cd05935 171 KYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQTHTNPP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 428 GAtaLKPGSATRPFFGVQPALVD-NMGEIVEGATEGNLVLldSWPGQMRTvYGDHDRFEQTYFSTFKGMYF--TGDGARR 504
Cdd:cd05935 246 LR--PKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVV--RGPQIFKG-YWNRPEETEESFIEIKGRRFfrTGDLGYM 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 505 DEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGvYPSAELHKEVKDWVR 584
Cdd:cd05935 321 DEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE-YRGKVTEEDIIEWAR 399
|
490 500 510
....*....|....*....|....*....|.
gi 258583962 585 KEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd05935 400 EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
91-615 |
5.22e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 142.79 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:PRK08314 25 DKTAIVFYG------RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVITADEGVrgGRAVPLKKNV-----------DEALTNPEVKnISKVMVLKRTGGNVAwhEHRDIWWH 238
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELA--PKVAPAVGNLrlrhvivaqysDYLPAEPEIA-VPAWLRAEPPLQALA--PGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 239 EATAKvsdQCQPEEMKA--EDPLFILYTSGSTGKPKGVLHTTGGylVYATMTFKYV-FDYQPGEVFWCTADVGWITGHSY 315
Cdd:PRK08314 174 EALAA---GLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRT--VMANAVGSVLwSNSTPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 316 LVYGPLSNGAKTILfegVPNYP-TTARmsEVVDKHKVNILYTAPTAIRALMAKGDEAikgtSRD--SLRIMGSVGEPInP 392
Cdd:PRK08314 249 SMNAPIYAGATVVL---MPRWDrEAAA--RLIERYRVTHWTNIPTMVVDFLASPGLA----ERDlsSLRYIGGGGAAM-P 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 393 EA-WEWYYRTIGnekSPIVDTWWQTETGGILITPLPGATalKPGSATRPFFGVQPALVD-NMGEIVEGATEGNLVLldSW 470
Cdd:PRK08314 319 EAvAERLKELTG---LDYVEGYGLTETMAQTHSNPPDRP--KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVV--HG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 PGQMRTVYGDHDRFEQTyFSTFKGMYF--TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVV 548
Cdd:PRK08314 392 PQVFKGYWNRPEATAEA-FIEIDGKRFfrTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 549 GVPHDIKGQAIYAYITLNDGvYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK08314 471 ATPDPRRGETVKAVVVLRPE-ARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
84-615 |
5.44e-36 |
|
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: 141.88 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLATRG-DQVAIIwegdDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:cd05923 8 RRAASRApDACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVITAD-----EGVRGGRAVPLKKNVDEALTNPEVkniskvmvlkrtggnvawhehrdiww 237
Cdd:cd05923 84 NPRLKAAELAELIERGEMTAAVIAVdaqvmDAIFQSGVRVLALSDLVGLGEPES-------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 238 heatakVSDQCQPEEMKAEDPLFILYTSGSTGKPKGV-------------LHTTGGYL------------VYATMTFKYV 292
Cdd:cd05923 138 ------AGPLIEDPPREPEQPAFVFYTSGTTGLPKGAvipqraaesrvlfMSTQAGLRhgrhnvvlglmpLYHVIGFFAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 293 FdyqpgevfwctadVGWITGHSYLVygplsngaktilfegVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKgdEAI 372
Cdd:cd05923 212 L-------------VAALALDGTYV---------------VVEEFDPADALKLIEQERVTSLFATPTHLDALAAA--AEF 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 373 KGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKspiVDTWWQTETGGILITPLPgatalKPGSATRPFFGVQPALVDNM 452
Cdd:cd05923 262 AGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK---VNIYGTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 453 GEIVEGAT---EGNLVLLDS----WPGQMRtvygdhdRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:cd05923 334 GSPDEALAngeEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGE 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 526 RMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDwvrKEIGAIATPDVLHWTDALPKT 605
Cdd:cd05923 407 NIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKN 483
|
570
....*....|
gi 258583962 606 RSDKIMRRIL 615
Cdd:cd05923 484 AMNKVLRRQL 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
8.97e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 141.84 E-value: 8.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 79 ANCIDRHLATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGN------TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 159 HTIVFGGFSPEALAGRIIDSNAKLVITadEGVrggrAVPLKKNVDEAltnpeVKNISKVMVL-KRTGGNVAWHEhrdiww 237
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAA----LAPVATAVRDI-----VPLLSTVVVAgGSSDDSVLGYE------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 238 hEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYATMTFKYVFDYQ-PGEVFWCTADVGWITGHS 314
Cdd:PRK07786 157 -DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 YLVYGpLSNGAKTILfegvpnYPTTA----RMSEVVDKHKVNILYTAPTAIRALMAkgdeAIKGTSRD-SLRIMGSVGEP 389
Cdd:PRK07786 233 SMLPG-LLLGAPTVI------YPLGAfdpgQLLDVLEAEKVTGIFLVPAQWQAVCA----EQQARPRDlALRVLSWGAAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 390 INPEAWEWYYRTIgnEKSPIVDTWWQTETGGILITpLPGATAL-KPGSATRPFFGVQPALVD-NM-----GEIVEGATEG 462
Cdd:PRK07786 302 ASDTLLRQMAATF--PEAQILAAFGQTEMSPVTCM-LLGEDAIrKLGSVGKVIPTVAARVVDeNMndvpvGEVGEIVYRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 463 NLVLLDSWPGQMRTVygdhDRFEQTYFSTfkgmyftGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKI 542
Cdd:PRK07786 379 PTLMSGYWNNPEATA----EAFAGGWFHS-------GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 543 AEAAVVGVPHDIKGQAIYAYITLNDGvypSAELH-KEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK-IAT 620
Cdd:PRK07786 448 VEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErYGA 524
|
570
....*....|.
gi 258583962 621 GDTSNLGDTST 631
Cdd:PRK07786 525 CVNVERRSASA 535
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
1.63e-35 |
|
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: 139.37 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLATRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 164 GGFSPEALAGRIIDSNAKLVITadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatak 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 244 vsdqcqpeemKAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYATMTF------------KYVFDYQPGEVFwctadvg 308
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSICFDLSVFELF------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 309 witghsylvyGPLSNGAKTILFEGVPNYPTTARMSEVvdkhkvNILYTAPTAIRALMAKGdeAIKGtsrdSLRIMGSVGE 388
Cdd:cd12115 166 ----------GPLATGGKVVLADNVLALPDLPAAAEV------TLINTVPSAAAELLRHD--ALPA----SVRVVNLAGE 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 PINPEAWEWYYRTIGNEKspIVDTWWQTETggiliTPLPGATALKPGSAT-----RPFFGVQPALVDNMGEIVEGATEGN 463
Cdd:cd12115 224 PLPRDLVQRLYARLQVER--VVNLYGPSED-----TTYSTVAPVPPGASGevsigRPLANTQAYVLDRALQPVPLGVPGE 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 464 LVLldSWPGQMRTVYGD----HDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:cd12115 297 LYI--GGAGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 540 SKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd12115 375 PGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
2.25e-34 |
|
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: 136.34 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd17649 2 DAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADegvrggravplkknvdealtnpevkniskvmvlkrtGGNVAWhehrdiwwheatakvsdqcqp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLTHH------------------------------------PRQLAY--------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 eemkaedplfILYTSGSTGKPKGVLHTTGGYLVYATMTFKYvFDYQPGEVFWCTADVGWITGHSYLvYGPLSNGAkTILF 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 331 EGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMakgDEAIKGTSRD--SLRIMGSVGEPINPEAWEwyyRTIGNEKSp 408
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLA---EEADRTGDGRppSLRLYIFGGEALSPELLR---RWLKAPVR- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 409 IVDTWWQTETggiLITPL-----PGATALKPGSAT-RPFFGVQPALVDN-MGEIVEGATeGNLVLldSWPGQMRtvyGDH 481
Cdd:cd17649 239 LFNAYGPTEA---TVTPLvwkceAGAARAGASMPIgRPLGGRSAYILDAdLNPVPVGVT-GELYI--GGEGLAR---GYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 482 DRFEQT--------YFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHD 553
Cdd:cd17649 310 GRPELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 554 IkGQAIYAYITLNDGVyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd17649 390 G-GKQLVAYVVLRAAA-AQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
72-617 |
2.83e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 137.82 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 72 DGTLnisANCIDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLA 151
Cdd:PRK05605 31 DTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 152 CTRIGAV---HTIVFggfSPEALAGRIIDSNAKLVITAD------EGVRggRAVPLKKNVDEALTN--PEVKNISKVMVL 220
Cdd:PRK05605 102 VLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWDkvaptvERLR--RTTPLETIVSVNMIAamPLLQRLALRLPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 221 KR--------TG---GNVAWHEHRDiwwhEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTF 289
Cdd:PRK05605 177 PAlrkaraalTGpapGTVPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 290 KYVFDYQPG-EVFWCTADVGwitgHSY-----LVYGPlSNGAKTILFegvpnyPTtARMSEVVD---KHKVNILYTAPTA 360
Cdd:PRK05605 253 AWVPGLGDGpERVLAALPMF----HAYgltlcLTLAV-SIGGELVLL------PA-PDIDLILDamkKHPPTWLPGVPPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 361 IRALMAKGDEaiKGTSRDSLRIMGSVGEPINPEAWE-WYYRTIGNekspIVDTWWQTETGGILITPlPGATALKPGSATR 439
Cdd:PRK05605 321 YEKIAEAAEE--RGVDLSGVRNAFSGAMALPVSTVElWEKLTGGL----LVEGYGLTETSPIIVGN-PMSDDRRPGYVGV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 440 PFFGVQPALVD--NMGEIVEGATEGNLVLldSWPgqmRTVYGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVD 517
Cdd:PRK05605 394 PFPDTEVRIVDpeDPDETMPDGEEGELLV--RGP---QVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 518 DVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGvypsAELHKE-VKDWVRKEIGAIATPDVL 596
Cdd:PRK05605 469 ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG----AALDPEgLRAYCREHLTRYKVPRRF 544
|
570 580
....*....|....*....|.
gi 258583962 597 HWTDALPKTRSDKIMRRILRK 617
Cdd:PRK05605 545 YHVDELPRDQLGKVRRREVRE 565
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
109-612 |
3.78e-34 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 135.27 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADe 188
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 189 gvrggravPLKKNVDEALTNPEVkniskvmvlkrtggnvawhehrdiwWHEATAKVSDQCQpeeMKAEDPLFILYTSGST 268
Cdd:TIGR01923 80 --------LLEEKDFQADSLDRI-------------------------EAAGRYETSLSAS---FNMDQIATLMFTSGTT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 269 GKPKGVLHTTGGYLVYAtMTFKYVFDYQPGEVFWCTADVGWITGHSyLVYGPLSNGAKTILFEGvpnyptTARMSEVVDK 348
Cdd:TIGR01923 124 GKPKAVPHTFRNHYASA-VGSKENLGFTEDDNWLLSLPLYHISGLS-ILFRWLIEGATLRIVDK------FNQLLEMIAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 349 HKVNILYTAPTAIRALMakgDEAIKGTSRDSLRIMGS-VGEPINPEAWEwyyrtignEKSPIVDTWWQTETGGILITPLP 427
Cdd:TIGR01923 196 ERVTHISLVPTQLNRLL---DEGGHNENLRKILLGGSaIPAPLIEEAQQ--------YGLPIYLSYGMTETCSQVTTATP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 428 GATALKPGSAtRPFFGVQPAL-VDNM---GEI-VEGATegnlVLLDSW-PGQMRTVygdhdRFEQTYFSTfkgmyftGDG 501
Cdd:TIGR01923 265 EMLHARPDVG-RPLAGREIKIkVDNKeghGEImVKGAN----LMKGYLyQGELTPA-----FEQQGWFNT-------GDI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 502 ARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGvyPSAElhkEVKD 581
Cdd:TIGR01923 328 GELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD--ISQA---KLIA 402
|
490 500 510
....*....|....*....|....*....|.
gi 258583962 582 WVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:TIGR01923 403 YLTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
105-615 |
3.37e-33 |
|
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: 133.19 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGV----RGGRAVPLKknvdealtnpevkniskvmvlkrtggnvawhehrdiwwhEATAKVSDQCQPEEMKAEDPLF 260
Cdd:cd12116 90 TDDALPdrlpAGLPVLLLA---------------------------------------LAAAAAAPAAPRTPVSPDDLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGV----------LHTTGGYL-------VYATMTfkYVFDYQPGEVFWctadvgwitghsylvygPLSN 323
Cdd:cd12116 131 VIYTSGSTGRPKGVvvshrnlvnfLHSMRERLglgpgdrLLAVTT--YAFDISLLELLL-----------------PLLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 324 GAKTILFEgvpnyPTTAR----MSEVVDKHKVNILYTAPTAIRALMAKGDEAikgtsRDSLRIM-GsvGEPINPEAWEWY 398
Cdd:cd12116 192 GARVVIAP-----RETQRdpeaLARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG--GEALPPDLAARL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 YRTIG---NEKSPIVDTWWQTetggilitplpgATALKPGSAT----RPFFGVQPALVDNMGEIVEGATEGNLVLldSWP 471
Cdd:cd12116 260 LSRVGslwNLYGPTETTIWST------------AARVTAAAGPipigRPLANTQVYVLDAALRPVPPGVPGELYI--GGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 GQMRTVYGDHD----RFEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAA 546
Cdd:cd12116 326 GVAQGYLGRPAltaeRFVPDPFAGPGSrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 547 VVGVPHDIKGQaIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd12116 406 VVVREDGGDRR-LVAYVVLKAGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
3.45e-33 |
|
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: 133.91 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDDPtqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV-HT 160
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGE--VHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 161 I---VFggfsPEALAGRIIDSNAKLVITADEgvrggrAVPLKKNVDealtnPEVKNISKVMVLKRTGGNVAWHEHRDIWW 237
Cdd:cd12119 80 InprLF----PEQIAYIINHAEDRVVFVDRD------FLPLLEAIA-----PRLPTVEHVVVMTDDAAMPEPAGVGVLAY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 238 HEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGV--------LHTtggylvYATMTFKyVFDYQPGEVF-------- 301
Cdd:cd12119 145 EELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHA------MAALLTD-GLGLSESDVVlpvvpmfh 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 302 ---WCTADVGWITGHSYLVYGPlsngaktilfegvpnYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEaiKGTSRD 378
Cdd:cd12119 218 vnaWGLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 SLR---IMGSVGEPINPEAWEwyYRTIgneksPIVDTWWQTETG--GILITPLPGATALKPG-------SATRPFFGVQP 446
Cdd:cd12119 281 SLRrvvIGGSAVPRSLIEAFE--ERGV-----RVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVEL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 447 ALVDNMGEIVE--GATEGNLVLLDSWPGQmrTVYGDHDRfeqTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:cd12119 354 RIVDDDGRELPwdGKAVGELQVRGPWVTK--SYYKNDEE---SEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 525 HRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPK 604
Cdd:cd12119 429 EWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPK 505
|
570
....*....|...
gi 258583962 605 TRSDKIMRRILRK 617
Cdd:cd12119 506 TSTGKIDKKALRE 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
4.43e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 130.08 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtIVF--GGFSP 168
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLlnTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 169 EALAGRIIDSNAKLVITADEGVRggravplKKNVDEALTNPEVKNiskvmvlkrtggnvawhehrdiwwhEATAKVSDQc 248
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDFEA-------KLIPGISVKFAELMN-------------------------GPKEEAEIQ- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 249 qpEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATmtfkyvfdyqpGEV--FWCTADVGW--------ITGHSylvy 318
Cdd:PRK03640 136 --EEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAV-----------GSAlnLGLTEDDCWlaavpifhISGLS---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 gplsngaktILFEGVPnYPTTARMSEVVDKHKVN---------ILYTAPTAIRALMAKGDEaikGTSRDSLRIMGSVGEP 389
Cdd:PRK03640 199 ---------ILMRSVI-YGMRVVLVEKFDAEKINkllqtggvtIISVVSTMLQRLLERLGE---GTYPSSFRCMLLGGGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 390 INPEAWEwyyrtIGNEKS-PIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNmGEIVEGATEGNLVLld 468
Cdd:PRK03640 266 APKPLLE-----QCKEKGiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV-- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 469 swPGQMRTVyGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVV 548
Cdd:PRK03640 338 --KGPNVTK-GYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 549 GVPHDIKGQAIYAYITLNDGVyPSAELhkevKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKI 618
Cdd:PRK03640 415 GVPDDKWGQVPVAFVVKSGEV-TEEEL----RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
6.65e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 129.81 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIWEGDDptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTG----EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVITAdegvrggRAvplKKNVDEALTNpEVKNISKVMVLKRTGGNVAWHEhrdiwWHEATA 242
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITS-------AA---KLDVARALLK-QCPGVRHRLVLDGDGELEGFVG-----YAEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 243 KVSDQCQPEEMKAEDplfILYTSGSTGKPKGVLH--------TTGGYlvyaTMTFKYVFDYQPGEVFWCTADVgWITGHS 314
Cdd:PRK13391 144 GLPATPIADESLGTD---MLYSSGTTGRPKGIKRplpeqppdTPLPL----TAFLQRLWGFRSDMVYLSPAPL-YHSAPQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 YLVYGPLSNGAKTILFEGVpnypTTARMSEVVDKHKVNILYTAPTA-IRalMAKGDEAIKGT-SRDSLRIMGSVGEPINP 392
Cdd:PRK13391 216 RAVMLVIRLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMfSR--MLKLPEEVRDKyDLSSLEVAIHAAAPCPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 393 EAWE----WYyrtignekSPIVDTWWQTeTGGILITPLPGATAL-KPGSATRPFFGVQPALVDNMGEIVegategnlvll 467
Cdd:PRK13391 290 QVKEqmidWW--------GPIIHEYYAA-TEGLGFTACDSEEWLaHPGTVGRAMFGDLHILDDDGAELP----------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 468 dswPGQMRTVYGDHDR-FEqtYF----------STFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL 536
Cdd:PRK13391 350 ---PGEPGTIWFEGGRpFE--YLndpaktaearHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 537 VAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK13391 425 ITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
90-617 |
5.11e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 127.46 E-value: 5.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIWegddptQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:PRK07470 21 PDRIALVW------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVITADEGVRGGRAVplkknvdeALTNPEVKNiskVMVLkrtGGNVAWHEHRDIWWHEATAKVSDQcq 249
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFPEHAAAV--------RAASPDLTH---VVAI---GGARAGLDYEALVARHLGARVANA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 peEMKAEDPLFILYTSGSTGKPKGVLHTTGgylvyaTMTF---KYVFDYQPGevfwctadvgwITGHS-YLVYGPLSNGA 325
Cdd:PRK07470 159 --AVDHDDPCWFFFTSGTTGRPKAAVLTHG------QMAFvitNHLADLMPG-----------TTEQDaSLVVAPLSHGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 326 ------------KTILfegvpnyPTTARM--SEV---VDKHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSVGE 388
Cdd:PRK07470 220 gihqlcqvargaATVL-------LPSERFdpAEVwalVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 PINPEAWEWYYRTIGNEkspIVDTWWQTETGGIlITPLPGA-------TALKPGSATRPFFGVQPALVDNMGEIVEGATE 461
Cdd:PRK07470 291 PMYRADQKRALAKLGKV---LVQYFGLGEVTGN-ITVLPPAlhdaedgPDARIGTCGFERTGMEVQIQDDEGRELPPGET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 462 GNLVLLDSwpgqmrTVY-GDHDRFEQTYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:PRK07470 367 GEICVIGP------AVFaGYYNNPEANA-KAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTH 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 540 SKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK07470 440 PAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
83-620 |
6.63e-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: 127.18 E-value: 6.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHtiV 162
Cdd:COG1021 32 RRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FggfspeALAG-RIID-------SNAKLVITADEgVRGGRAVPLKKNVDEAltNPEVKNiskVMVLKRTGGNVAWhehrD 234
Cdd:COG1021 104 F------ALPAhRRAEishfaeqSEAVAYIIPDR-HRGFDYRALARELQAE--VPSLRH---VLVVGDAGEFTSL----D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 235 IWWHEATAKVSDQCQPEemkaeDPLFILYTSGSTGKPKGVLHTTGGYLvyatmtfkyvfdYQpgevFWCTADVGWITGHS 314
Cdd:COG1021 168 ALLAAPADLSEPRPDPD-----DVAFFQLSGGTTGLPKLIPRTHDDYL------------YS----VRASAEICGLDADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 -YLV---------------YGPLSNGAKTILfegVPNyPTTARMSEVVDKHKVNILYTAPTAIRALMakgdEAIKGTSRD 378
Cdd:COG1021 227 vYLAalpaahnfplsspgvLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWL----DAAERSRYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 --SLRIMGSVGEPINPEAwewyYRTIGneksPIVDTWWQ-----TEtGGILITPL--PGATALkpGSATRPffgVQPA-- 447
Cdd:COG1021 299 lsSLRVLQVGGAKLSPEL----ARRVR----PALGCTLQqvfgmAE-GLVNYTRLddPEEVIL--TTQGRP---ISPDde 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 448 --LVDNMGEIVEGATEGNLvlLDSWPGQMRTVYGD--HDrfeQTYFsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:COG1021 365 vrIVDEDGNPVPPGEVGEL--LTRGPYTIRGYYRApeHN---ARAF-TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 524 GHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLnDGVYPSAelhKEVKDWVRkEIGaIAT---PDVLHWTD 600
Cdd:COG1021 439 GEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTL---AELRRFLR-ERG-LAAfklPDRLEFVD 512
|
570 580
....*....|....*....|
gi 258583962 601 ALPKTRSDKIMRRILRKIAT 620
Cdd:COG1021 513 ALPLTAVGKIDKKALRAALA 532
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
7.49e-31 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 127.11 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIWEgdDPTQD-KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSP 168
Cdd:PRK08008 21 GHKTALIFE--SSGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 169 EALAGRIIDSNAKLVITADEgvrggrAVPLKKNVDEALTNPeVKNIskvmVLKRTGGnvawhehrdiwwhEATAKVSD-- 246
Cdd:PRK08008 99 EESAWILQNSQASLLVTSAQ------FYPMYRQIQQEDATP-LRHI----CLTRVAL-------------PADDGVSSft 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 ---QCQPEEMK------AEDPLFILYTSGSTGKPKGVLHTT-----GGYL-----------VYATMTFKYVFDYQpgevf 301
Cdd:PRK08008 155 qlkAQQPATLCyapplsTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYsawqcalrdddVYLTVMPAFHIDCQ----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 302 wCTAdvgwitghsylVYGPLSNGAKTILFEgvpNYPTTARMSEVVdKHKVNILYTAPTAIRALMAKGDEAikgTSRD-SL 380
Cdd:PRK08008 230 -CTA-----------AMAAFSAGATFVLLE---KYSARAFWGQVC-KYRATITECIPMMIRTLMVQPPSA---NDRQhCL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 381 RIMgsvgepinpeaweWYYRTIGNE---------KSPIVDTWWQTETGGILITPLPGATALKPgSATRPFFGVQPALVDN 451
Cdd:PRK08008 291 REV-------------MFYLNLSDQekdafeerfGVRLLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 452 MGEIVEGATEGNLVLlDSWPGQ--MRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGT 529
Cdd:PRK08008 357 HNRPLPAGEIGEICI-KGVPGKtiFKEYYLDPKATAKVL--EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 530 AEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDK 609
Cdd:PRK08008 434 VELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
|
....*..
gi 258583962 610 IMRRILR 616
Cdd:PRK08008 511 IIKKNLK 517
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
7.65e-31 |
|
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: 126.02 E-value: 7.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 117 VCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEalagrIIDSNAKLVITadegVRGGRAV 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 197 PLKKNVDEALTNPEVKNISKVMVLkrtGGNVAWHEHRDIWWHEatakVSDqcqpeemkaEDPLFILYTSGSTGKPKGVL- 275
Cdd:cd05922 74 LADAGAADRLRDALPASPDPGTVL---DADGIRAARASAPAHE----VSH---------EDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 276 -HTTggyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSyLVYGPLSNGAKTILFEGvpnYPTTARMSEVVDKHKVNIL 354
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVLTND---GVLDDAFWEDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 355 YTAPTaIRALMAKGDeaIKGTSRDSLRIMGSVGEPINPEawewyyrTIG--NEKSP---IVDTWWQTETGGILITPLPGA 429
Cdd:cd05922 211 AGVPS-TYAMLTRLG--FDPAKLPSLRYLTQAGGRLPQE-------TIArlRELLPgaqVYVMYGQTEATRRMTYLPPER 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 430 TALKPGSATRPFFGVQPALVDNMG------EIVEGATEGNLVLLDSWpgqmrtvygdHDRFEQTYFSTFKGMYFTGDGAR 503
Cdd:cd05922 281 ILEKPGSIGLAIPGGEFEILDDDGtptppgEPGEIVHRGPNVMKGYW----------NDPPYRRKEGRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 504 RDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPhDIKGQAIYAYITLNDGVYPsaelhKEVKDWV 583
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDP-----KDVLRSL 424
|
490 500 510
....*....|....*....|....*....|...
gi 258583962 584 RKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-575 |
9.75e-31 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 129.21 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhti 161
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA--- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 vfggFSP-------EALAGRIIDSNAKLVITADEgvrggravplkknVDEALTNPEVknisKVMVLkrtggnvawhehrD 234
Cdd:COG1020 553 ----YVPldpaypaERLAYMLEDAGARLVLTQSA-------------LAARLPELGV----PVLAL-------------D 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 235 iwwHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVF-WCTA---DVgwi 310
Cdd:COG1020 599 ---ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDRVlQFASlsfDA--- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 311 tghSYL-VYGPLSNGAKTILF--EGVPNyptTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikgtsRDSLRIMGSVG 387
Cdd:COG1020 672 ---SVWeIFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPEA-----LPSLRLVLVGG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 388 EPINPEAWEWYYRTIGN----------EKSpiVD-TWWQTETGGILITPLP-GatalkpgsatRPFFGVQPALVDNMGEI 455
Cdd:COG1020 741 EALPPELVRRWRARLPGarlvnlygptETT--VDsTYYEVTPPDADGGSVPiG----------RPIANTRVYVLDAHLQP 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 456 V-EGAtegnlvlldswPGQMrtvY--GD------HDRFEQT--YF----STFKG--MYFTGDGARRDEDG---YywiTGR 515
Cdd:COG1020 809 VpVGV-----------PGEL---YigGAglargyLNRPELTaeRFvadpFGFPGarLYRTGDLARWLPDGnleF---LGR 871
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 516 VDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAEL 575
Cdd:COG1020 872 ADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
105-615 |
2.01e-30 |
|
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: 124.50 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcQPEemkaeDPLFILYT 264
Cdd:cd17650 90 T---------------------------------------------------------------QPE-----DLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYL-VYATMTFKYVFDYQPGEVFwctadvgWITGHSYLVYGplSNGAKTILFEG----VPN--YP 337
Cdd:cd17650 102 SGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLL-------QMASFSFDVFA--GDFARSLLNGGtlviCPDevKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 338 TTARMSEVVDKHKVNILYTAPTAIRALMAKGDEaiKGTSRDSLR--IMGSVGEPINPEAWEwyYRTIGnEKSPIVDTWWQ 415
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRllIVGSDGCKAQDFKTL--AARFG-QGMRIINSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 416 TETgGILITPLPGATALKPGSAT----RPFFGVQPALVDNMGEIVEGATEGNLvlldsWPGQMRTVYGDHDRFEQTY--- 488
Cdd:cd17650 248 TEA-TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQPVGVAGEL-----YIGGAGVARGYLNRPELTAerf 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 489 ----FSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVgVPHDIKGQA-IYAYI 563
Cdd:cd17650 322 venpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 258583962 564 TlndgvyPSAELH-KEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17650 401 V------AAATLNtAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
2.94e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 125.98 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDDPTQDktLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITADEGVrggravpLKKnVDEALtnPEVKNISKVMVLKRTGGnvaWHEHRDIWWHEAT 241
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVR--DELPSLRHIVVLDPRGL---RDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 AKVSDQCQPEEM-------KAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVF-----WCtadvgW 309
Cdd:COG1022 162 ALGREVADPAELearraavKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 310 ITGHSYLVYGpLSNGAKTILFEGVPNYPTTarMSEVvdkhKVNILYTAP-------TAIRALMAKG--------DEAIK- 373
Cdd:COG1022 236 VFERTVSYYA-LAAGATVAFAESPDTLAED--LREV----KPTFMLAVPrvwekvyAGIQAKAEEAgglkrklfRWALAv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 374 ----GTSRDS------------------------------LRIMGSVGEPINPEAWEWyYRTIGnekSPIVDTWWQTETG 419
Cdd:COG1022 309 grryARARLAgkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARF-FRALG---IPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 420 GILITPLPGATalKPGSATRPFFGVQPALVDNmGEI-VEGategnlvlldswPGQMRtvyGDHDRFEQTyFSTFK--GMY 496
Cdd:COG1022 385 PVITVNRPGDN--RIGTVGPPLPGVEVKIAED-GEIlVRG------------PNVMK---GYYKNPEAT-AEAFDadGWL 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 497 FTGDGARRDEDGYYWITGRVDDVLNVSGhrmGT----AEIESALVAFSKIAEAAVVG 549
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
87-618 |
6.85e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 124.27 E-value: 6.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 87 ATRGDQVAIIwegDDptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCI----YMPMVpeaaVAMLACTRIGAVHTIV 162
Cdd:PRK07788 60 RRAPDRAALI---DE---RGTLTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVITADEGVRGGRAVPlkknvdealtnPEVkniSKVMVLKRTGGNVAWHEHRDIWWHEATA 242
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDL---GRLRAWGGNPDDDEPSGSTDETLDDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 243 KVSDQCQPeemKAEDP-LFILYTSGSTGKPKGVLHTTggylVYATMTFKYVFDYQP---GEVFWCTADVGWITGHSYLVY 318
Cdd:PRK07788 196 GSSTAPLP---KPPKPgGIVILTSGTTGTPKGAPRPE----PSPLAPLAGLLSRVPfraGETTLLPAPMFHATGWAHLTL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 GpLSNGAKTIL---FEgvpnyPTTARmsEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAW 395
Cdd:PRK07788 269 A-MALGSTVVLrrrFD-----PEATL--EDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 396 EWYYRTIGneksPIV-DTWWQTETGGILITPlPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQM 474
Cdd:PRK07788 341 TRALEAFG----PVLyNLYGSTEVAFATIAT-PEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 475 RTvygdHDRFEQTyfstFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDI 554
Cdd:PRK07788 416 YT----DGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258583962 555 KGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKI 618
Cdd:PRK07788 488 FGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
107-617 |
1.57e-29 |
|
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: 121.30 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 107 TLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLvita 186
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 187 degvrggravplkknvDEALTnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaedplfILYTSG 266
Cdd:cd05912 77 ----------------DDIAT-----------------------------------------------------IMYTSG 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 267 STGKPKGVLHTTGGYLVYATMTfkyvfdyqpGEVFWCTADVGW--------ITGHSYLVYGpLSNGAKTILFEGVpnypT 338
Cdd:cd05912 88 TTGKPKGVQQTFGNHWWSAIGS---------ALNLGLTEDDNWlcalplfhISGLSILMRS-VIYGMTVYLVDKF----D 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 339 TARMSEVVDKHKVNILYTAPTAIRALMAKGDEaikgTSRDSLRIMGSVGEPINPEAWEwyyrtIGNEKS-PIVDTWWQTE 417
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQRLLEILGE----GYPNNLRCILLGGGPAPKPLLE-----QCKEKGiPVYQSYGMTE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 418 TGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIvegATEGNLVLldSWPGQMRTVYGDHDR----FEQTYFSTfk 493
Cdd:cd05912 225 TCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILL--KGPNVTKGYLNRPDAteesFENGWFKT-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 494 gmyftGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVypSA 573
Cdd:cd05912 298 -----GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI--SE 370
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 258583962 574 ElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05912 371 E---ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
105-616 |
1.57e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 122.88 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK-LV 183
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARvLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITAD--EGVRGgrAVPLKKNVDEALTNPEVKNISKVMVLKRT--GGNVAWHEhrdiWwheatakVSDQCQPEEMKAEDPL 259
Cdd:PRK12406 89 AHADllHGLAS--ALPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG----W-------LAQQEPYDGPPVPQPQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 260 FILYTSGSTGKPKGVLH---TTGGYLVYATMTfKYVFDYQPGEVFWCTADVGWITGHSY-LVYGPLsnGAKTIL---FEg 332
Cdd:PRK12406 156 SMIYTSGTTGHPKGVRRaapTPEQAAAAEQMR-ALIYGLKPGIRALLTGPLYHSAPNAYgLRAGRL--GGVLVLqprFD- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 333 vpnyptTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAwewyyrtigneKSPIVDt 412
Cdd:PRK12406 232 ------PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV-----------KRAMIE- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 413 WW---------QTETGgiLITPLPGATAL-KPGSATRPFFGVQPALVDNMGEIVEGATEGNLVlldswpgqMRT-VYGD- 480
Cdd:PRK12406 294 WWgpviyeyygSTESG--AVTFATSEDALsHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIY--------SRIaGNPDf 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 --HDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQA 558
Cdd:PRK12406 364 tyHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 559 IYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK12406 444 LMAVVEPQPGATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-622 |
2.17e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.45 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADegvRGGRAVPLKKNVDealtnpevkniskVMVLKRTGGNVAWHehrdiwwheatakvSDQCQPEEMKAEDPLFILYT 264
Cdd:PRK12316 614 SQS---HLGRKLPLAAGVQ-------------VLDLDRPAAWLEGY--------------SEENPGTELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTG-------------GYLVYATMTFK--YVFDYQPGEVFWctadvgwitghsylvygPLSNGAKTIL 329
Cdd:PRK12316 664 SGSTGKPKGAGNRHRalsnrlcwmqqayGLGVGDTVLQKtpFSFDVSVWEFFW-----------------PLMSGARLVV 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 330 F-EGVPNYPttARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikgtSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKsp 408
Cdd:PRK12316 727 AaPGDHRDP--AKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAG-- 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 409 IVDTWWQTETgGILITplpGATALKPGSAT----RPFFGVQPALVDNMGEIVEGATEGNLVLLDSwpGQMRTVYG----D 480
Cdd:PRK12316 799 LYNLYGPTEA-AIDVT---HWTCVEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglT 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 HDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVphdiKGQAIY 560
Cdd:PRK12316 873 AERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLV 948
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 561 AYITLNDgvyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATGD 622
Cdd:PRK12316 949 GYVVLES---EGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
6.29e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 121.15 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIWegddptQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC------GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVITADEgvRGGRAVPLKknvdealtnPEVKNISKVMVLKRTGGNVAWHEHRDiwWHEATAKVSDQCQ 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPRVAEVL---------PRLPKLRTLVVVEDGSGNDLLPGAVD--YEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 PEEMKAEDpLFILYTSGSTGKPKGVL-------HTTGGYLVYATMTFkyVFDYQpgEVfwcTADVGWITGHSYLVYGPLS 322
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMwrqedifRVLLGGRDFATGEP--IEDEE--EL---AKRAAAGPGMRRFPAPPLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 NGAKTI-----LFEG--VPNYPTT----ARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPIN 391
Cdd:PRK07798 230 HGAGQWaafaaLFSGqtVVLLPDVrfdaDEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 PEAWEWYYRTIGNekSPIVDTWWQTETGGILItplpGATALKPGSATRPFFGVQP--ALVDNMGEIVEGATEGnlvllDS 469
Cdd:PRK07798 310 PSVKEALLELLPN--VVLTDSIGSSETGFGGS----GTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVEPGSGE-----IG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 470 WPGQMRTV----YGDHDRFEQTYFsTFKGM-Y-FTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIA 543
Cdd:PRK07798 379 WIARRGHIplgyYKDPEKTAETFP-TIDGVrYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 544 EAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDK 609
Cdd:PRK07798 458 DALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
104-619 |
6.74e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 121.42 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 104 QDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLV 183
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADE-------GVRGGRAVPLKKNVDEALTNPEVKNISKVMVL--KRTGGNVAWHEhrdiwWHEATAKVSDQCQPE--- 251
Cdd:PRK12583 122 ICADAfktsdyhAMLQELLPGLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHE-----LQARGETVSREALAErqa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 252 EMKAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYATMTF----KYVFdyqPGEVFWCTADVgwitghsYLVYGPLS 322
Cdd:PRK12583 197 SLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---PVPLYHCFGMV-------LANLGCMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 NGAKTILfegvPN--YPTTARMsEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSrdSLR--IMGsvGEPINPEAWEwy 398
Cdd:PRK12583 267 VGACLVY----PNeaFDPLATL-QAVEEERCTALYGVPTMFIAELDHPQRGNFDLS--SLRtgIMA--GAPCPIEVMR-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 yRTIGNEKSP-IVDTWWQTETGGI-LITPLPGATALKPGSATRPFFGVQPALVDN------MGEIVEGATEGNLVLLDSW 470
Cdd:PRK12583 336 -RVMDEMHMAeVQIAYGMTETSPVsLQTTAADDLERRVETVGRTQPHLEVKVVDPdgatvpRGEIGELCTRGYSVMKGYW 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 PGQMRTVYG-DHDrfeqtyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:PRK12583 415 NNPEATAESiDED-----------GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 550 VPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK12583 484 VPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
82-620 |
9.43e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 120.35 E-value: 9.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALK-EQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHT 160
Cdd:PRK06839 8 IEKRAYLHPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 161 IVFGGFSPEALAGRIIDSNAKLVitadegvrggravplkknvdeaLTNPEVKNiskvMVLKRTGgnVAWHEHrdIWWHEA 240
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVL----------------------FVEKTFQN----MALSMQK--VSYVQR--VISITS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 TAKVSDQ--CQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVY 318
Cdd:PRK06839 132 LKEIEDRkiDNFVEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 GPLSNGAKTIlfegVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIkgTSRDSLRIMGSVGEPINPEawewY 398
Cdd:PRK06839 211 PTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFET--TNLQSVRWFYNGGAPCPEE----L 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 YRTIGNEKSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRTVY 478
Cdd:PRK06839 281 MREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI--RGPNVMKEYW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 479 gdhDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQA 558
Cdd:PRK06839 359 ---NRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEI 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 559 IYAYITLNDGvypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIAT 620
Cdd:PRK06839 436 PIAFIVKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
106-549 |
1.22e-28 |
|
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: 119.24 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 ADegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkAEDPLFILYTS 265
Cdd:cd05907 84 ED-------------------------------------------------------------------PDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 266 GSTGKPKGVLHTTGGYLVYATMTFKYVfDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTarMSE- 344
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDD--LSEv 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 345 ----------VVDKHKVNILYTAPTAIRALMAkgDEAIKGtsrdSLRIMGSVGEPINPEAWEWyYRTIGnekSPIVDTWW 414
Cdd:cd05907 174 rptvflavprVWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHF-FRALG---IPVYEGYG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 QTETGGILITPLPGatALKPGSATRPFFGVQPALVDNmGEIVegaTEGNLVLLdswpgqmrtvyGDHDRFEQTYFSTFK- 493
Cdd:cd05907 244 LTETSAVVTLNPPG--DNRIGTVGKPLPGVEVRIADD-GEIL---VRGPNVML-----------GYYKNPEATAEALDAd 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 494 GMYFTGDGARRDEDGYYWITGRVDDVL-NVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
107-616 |
7.07e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 118.32 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 107 TLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITA 186
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 187 DEgvrggravpLKKNVDEALTN-PEVKNIskvmvlkrtggnVAWHEHRDIWWHEA--TAKVSDQCQPEEMKAEdplFILY 263
Cdd:PRK13382 148 EE---------FSATVDRALADcPQATRI------------VAWTDEDHDLTVEVliAAHAGQRPEPTGRKGR---VILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVLHT-TGGYlvyatMTFKYVFDYQP---GEVFWCTADVGWITGHSYLVYGPLSngAKTILfegvpnypTT 339
Cdd:PRK13382 204 TSGTTGTPKGARRSgPGGI-----GTLKAILDRTPwraEEPTVIVAPMFHAWGFSQLVLAASL--ACTIV--------TR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 340 ARMS-----EVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNeksPIVDTWW 414
Cdd:PRK13382 269 RRFDpeatlDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 QTETGGILI-TPLPGATAlkPGSATRPFFGVQPALVD-NMGEIVEGATEG----NLVLLDSW-PGQMRTVygdHDrfeqt 487
Cdd:PRK13382 346 ATEAGMIATaTPADLRAA--PDTAGRPAEGTEIRILDqDFREVPTGEVGTifvrNDTQFDGYtSGSTKDF---HD----- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 488 yfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLND 567
Cdd:PRK13382 416 ------GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 258583962 568 GvypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK13382 490 G---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-618 |
7.81e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.27 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITadegvrggravplKKNVDEALtnPEVKNISKVMVlkrtggnvawheHRDIWWHEat 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLEQL--PAPAGDTALTL------------DRLDLNGY-- 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvSDQCQPEEMKAEDPLFILYTSGSTGKPKGV--------LHT---------TGGYLVYATMTFKyvFDYQPGEVFWct 304
Cdd:PRK12467 3226 ---SENNPSTRVMGENLAYVIYTSGSTGKPKGVgvrhgalaNHLcwiaeayelDANDRVLLFMSFS--FDGAQERFLW-- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 305 advgwitghsylvygPLSNGAKTILFEGvpNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDeaikGTSRDSLRIMG 384
Cdd:PRK12467 3299 ---------------TLICGGCLVVRDN--DLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYV 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 385 SVGEPINPEAWEWYYRTIgnEKSPIVDTWWQTETggiLITPL---------PGATALKPGsatRPFFGVQPALVDNMGEI 455
Cdd:PRK12467 3358 FGGEAVPPAAFEQVKRKL--KPRGLTNGYGPTEA---VVTVTlwkcggdavCEAPYAPIG---RPVAGRSIYVLDGQLNP 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 456 VEGATEGNLVLldswpGQMRTVYGDH-------DRFEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRM 527
Cdd:PRK12467 3430 VPVGVAGELYI-----GGVGLARGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 528 GTAEIESALVAFSKIAEAAVVGVPHDiKGQAIYAYITLNDgvyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRS 607
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPAD---PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPN 3580
|
570
....*....|.
gi 258583962 608 DKIMRRILRKI 618
Cdd:PRK12467 3581 GKVDRKALPDP 3591
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
75-616 |
9.95e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 117.29 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 75 LNISANcIDRHLATRGDQVAIIWegddptQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTR 154
Cdd:PRK06145 2 FNLSAS-IAFHARRTPDRAALVY------RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 155 IGAVHTIVFGGFSPEALAGRIIDSNAKLVItadegvrggravplkknVDEALTNPEVKNISKVMVlkrtgGNVAWHEHRD 234
Cdd:PRK06145 75 LGAVFLPINYRLAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETPKIVI-----DAAAQADSRR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 235 IwwheatAKVSDQCQPEEMKAEDPLF-ILYTSGSTGKPKGVLHTTGgylvyatmtfkyvfdyqpgEVFWCTAD----VGW 309
Cdd:PRK06145 133 L------AQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 310 ITGHSYLVYGPLSN-GA-----KTILFEG-----VPNYPTTARMsEVVDKHKVNILYTAPTAIRALMAKGDEaiKGTSRD 378
Cdd:PRK06145 188 TASERLLVVGPLYHvGAfdlpgIAVLWVGgtlriHREFDPEAVL-AAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 SLRIMGSVGEPiNPE----AWEWYYRtigneKSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGE 454
Cdd:PRK06145 265 SLAWCIGGGEK-TPEsrirDFTRVFT-----RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 455 IVEGATEGNLVLLDswPGQMRTVYGDHdrfEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK06145 339 WLPPNMKGEICMRG--PKVTKGYWKDP---EKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 535 ALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVypSAELhKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRI 614
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA--TLTL-EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRV 490
|
..
gi 258583962 615 LR 616
Cdd:PRK06145 491 LR 492
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
2.69e-27 |
|
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: 115.83 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd12114 2 DATAVI------CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEGVRGGRAVPlkknvdealtnpevkniskvmvlkrtggnvawhehRDIWWHEATAKVSDQCQP 250
Cdd:cd12114 76 REAILADAGARLVLTDGPDAQLDVAVF-----------------------------------DVLILDLDALAAPAPPPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYATMTFKYVFDyqpgevfwcTADVgwITGHS--------YLVYGPL 321
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG---------PDDR--VLALSslsfdlsvYDIFGAL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAkTILFEGVPNYPTTARMSEVVDKHKVNILYTAPtAIRALMAKGDEAIKGTSRdSLR-IMGSvGEPINPEawewyyr 400
Cdd:cd12114 190 SAGA-TLVLPDEARRRDPAHWAELIERHGVTLWNSVP-ALLEMLLDVLEAAQALLP-SLRlVLLS-GDWIPLD------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 401 tignekspIVDTWWQTETGGILITpLPGAT----------------ALKPGSATRPFFGVQPALVDNMGEIVEGATEGNL 464
Cdd:cd12114 259 --------LPARLRALAPDARLIS-LGGATeasiwsiyhpidevppDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGEL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 465 VLldSWPGQMRTVYGDHDRFEQTYFSTFKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKI 542
Cdd:cd12114 330 WI--GGRGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 543 AEAAVVGVPhDIKGQAIYAYITLNDGVYPSAELhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd12114 408 ARAVVVVLG-DPGGKRLAAFVVPDNDGTPIAPD--ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-616 |
2.80e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 115.67 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 189 GVRGGRAVPLkknvdealtnpevkniskvmvlkrtggnvawhehrDIWWHEATAKVSDQCQPEEMKAEDPLFILYTSGST 268
Cdd:PRK09088 103 AVAAGRTDVE-----------------------------------DLAAFIASADALEPADTPSIPPERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 269 GKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPNYPTTARMSEVvdK 348
Cdd:PRK09088 148 GQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDP--A 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 349 HKVNILYTAPTAIRALMAKGDeaIKGTSRDSLRIMGSVGEPINPEAWEWYYrtigNEKSPIVDTWWQTETGGILITPL-P 427
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQPG--FDAAALRHLTALFTGGAPHAAEDILGWL----DDGIPMVDGFGMSEAGTVFGMSVdC 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 428 GATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLL--DSWPGQMRTVYGDHDRFeqtyfsTFKGMYFTGDGARRD 505
Cdd:PRK09088 299 DVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAF------TGDGWFRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 506 EDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRK 585
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE---RIRSHLST 449
|
490 500 510
....*....|....*....|....*....|.
gi 258583962 586 EIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
91-615 |
4.64e-27 |
|
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: 115.12 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVfggfSPEA 170
Cdd:cd17655 12 DHTAVVFE------DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRII----DSNAKLVITADEgvrggraVPLKKNVDEALTNPEVKNISkvmvlkrtggnvawHEHRdiwwhEATAKVSd 246
Cdd:cd17655 82 PEERIQyileDSGADILLTQSH-------LQPPIAFIGLIDLLDEDTIY--------------HEES-----ENLEPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 qcqpeemKAEDPLFILYTSGSTGKPKGVLHTTGG---YLVYATMTF------------KYVFDYQPGEVFwctadVGWIT 311
Cdd:cd17655 135 -------KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnLVEWANKVIyqgehlrvalfaSISFDASVTEIF-----ASLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 312 GHSYLVYGplsngaKTILFEGVPnypttarMSEVVDKHKVNILYTAPTAIRALmakgdEAIKGTSRDSLRIMGSVGEPIN 391
Cdd:cd17655 203 GNTLYIVR------KETVLDGQA-------LTQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 PE-AWEWYY-----RTIGNEKSPivdtwwqTETG-GILITPLPGATALKPG-SATRPFFGVQPALVDNMGEIVEGATEGN 463
Cdd:cd17655 265 TElAKKIIElfgtnPTITNAYGP-------TETTvDASIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQPVGVAGE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 464 LVLldSWPGQMRTvYGDH-----DRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVA 538
Cdd:cd17655 338 LYI--GGEGVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQ 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 539 FSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSaelhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17655 415 HPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA-----QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
9.63e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 112.19 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 263 YTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKtILFEGVPNYPTTARM 342
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 343 SE---VVDKHKVNILYTAPTAIRALMAKGDEAIKGtsrdSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETG 419
Cdd:cd05944 87 DNfwkLVERYRITSLSTVPTVYAALLQVPVNADIS----SLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 420 gILITPLPGATALKPGSATR--PFFGVQPALVDNMGEIVE---GATEGNLVLldswpgQMRTVYGDHDRFEQTYFSTFKG 494
Cdd:cd05944 160 -CLVAVNPPDGPKRPGSVGLrlPYARVRIKVLDGVGRLLRdcaPDEVGEICV------AGPGVFGGYLYTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 495 MYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSA 573
Cdd:cd05944 233 GWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 258583962 574 ElhkEVKDWVRKEIGA-IATPDVLHWTDALPKTRSDKIMRRILRKIAT 620
Cdd:cd05944 313 E---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
9.77e-27 |
|
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: 103.39 E-value: 9.77e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 531 EIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
84-623 |
1.10e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 114.75 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLA-TRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:PRK06178 40 RAWArERPQRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVITAD------EGVRGGRAV------------------PLKKNVDEALTNPEvkniskvm 218
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDqlapvvEQVRAETSLrhvivtsladvlpaeptlPLPDSLRAPRLAAA-------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 219 vlkrtggnvAWHehrDIWWHEATAKVSDQCQPEEMkaEDPLFILYTSGSTGKPKGVLHTTgGYLVYATMTFKYV-FDYQP 297
Cdd:PRK06178 186 ---------GAI---DLLPALRACTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQ-RDMVYTAAAAYAVaVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 298 GEVFWCTADVGWITGHSYLVYGPLSNGAKTILfegVPNYPTTARMsEVVDKHKVNILYTAPTAIRALMAKGDEAikgtSR 377
Cdd:PRK06178 251 DSVFLSFLPEFWIAGENFGLLFPLFSGATLVL---LARWDAVAFM-AAVERYRVTRTVMLVDNAVELMDHPRFA----EY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 378 D--SLRIMGSVG--EPINPEawewyYRtignekspivdTWWQTETGGILITPLPGATA-----------------LKpgs 436
Cdd:PRK06178 323 DlsSLRQVRVVSfvKKLNPD-----YR-----------QRWRALTGSVLAEAAWGMTEthtcdtftagfqdddfdLL--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 437 aTRPFF------GVQPALVD-NMGEIVEGATEGNLVLldSWPGQMRTVYGdhdRFEQTYFSTFKGMYFTGDGARRDEDGY 509
Cdd:PRK06178 384 -SQPVFvglpvpGTEFKICDfETGELLPLGAEGEIVV--RTPSLLKGYWN---KPEATAEALRDGWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 510 YWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGA 589
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAV 534
|
570 580 590
....*....|....*....|....*....|....
gi 258583962 590 IATPDVlHWTDALPKTRSDKIMRRILRKIATGDT 623
Cdd:PRK06178 535 YKVPEI-RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
1.49e-26 |
|
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: 102.17 E-value: 1.49e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 24 YQAMYQQSITDPEGFWGEQGKIVDWIKPFTKVKNTSFDPghiDIRWFEDGTLNISANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGP---FAKWFVGGKLNVCYNC 55
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
1.80e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 114.07 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 79 ANCIDRHLATRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALI------DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 159 HTIVFGGFSPEALAGRIIDSNAKLVITADegvrGGRAVPLKKNVDEAlTNPEVKNISKVMVLKRTGGNVAWHehrdiwWH 238
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAV-PPDALPPLRAIAVVDDAADATPAP------AP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 239 EATAKVSDQCQPEEMKA-------EDPLFILYT-SGSTGKPKGVLHTTGGYLVYATMTFKyVFDYQPGEVFWCTADVGWI 310
Cdd:PRK06164 156 GARVQLFALPDPAPPAAageraadPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 311 TGHSYLVyGPLSNGAkTILFEGVPNYPTTARMsevVDKHKVNILYTAPTAIRALMAKGDEaikgtSRD--SLRIMGSVGe 388
Cdd:PRK06164 235 FGFSTLL-GALAGGA-PLVCEPVFDAARTARA---LRRHRVTHTFGNDEMLRRILDTAGE-----RADfpSARLFGFAS- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 pINPeAWEWYYRTIGNEKSPIVDTWWQTE-----TGGILITP-----LPGATALKPGSATRpffgvqpaLVDNM-GEIVE 457
Cdd:PRK06164 304 -FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVR--------ARDPQdGALLP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 458 GATEGNLVLldSWPGQMRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:PRK06164 374 DGESGEIEI--RAPSLMRGYLDNPDATARAL--TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 538 AFSKIAEAAVVGVPHDIKGQAiYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSD---KIMRRI 614
Cdd:PRK06164 450 ALPGVAAAQVVGATRDGKTVP-VAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHR 525
|
....*
gi 258583962 615 LRKIA 619
Cdd:PRK06164 526 LREMA 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
84-615 |
2.30e-26 |
|
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: 112.81 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLATRGDQVAIIwegDDPTQdktLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVF 163
Cdd:cd05920 23 RSAARHPDRIAVV---DGDRR---LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 164 GGFSPEALAGRIIDSNAKLVITADEgvrggravplkknvdealtnpevkniskvmvlkrtggnvawHEHRDiwwHEATAK 243
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDR-----------------------------------------HAGFD---HRALAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 244 VSDQCQPeemkaeDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTfkyvfdyqpGEVFWCTADVGWIT----GHSYL--- 316
Cdd:cd05920 133 ELAESIP------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRAS---------AEVCGLDQDTVYLAvlpaAHNFPlac 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 --VYGPLSNGAKTILfeGVPNYPTTArmSEVVDKHKVNILYTAPTAIRALMakgDEAIKGTSRD-SLRIMGSVGEPINPE 393
Cdd:cd05920 198 pgVLGTLLAGGRVVL--APDPSPDAA--FPLIEREGVTVTALVPALVSLWL---DAAASRRADLsSLRLLQVGGARLSPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 394 AwewyYRTIGNEKSPIVDTWWQTETGGILITPLPGATALKPGSATRPffgVQP----ALVDNMGEIVEGATEGNLvlLDS 469
Cdd:cd05920 271 L----ARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEEGEL--LTR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 470 WPGQMRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:cd05920 342 GPYTIRGYYRAPEHNARAF--TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 550 VPHDIKGQAIYAYITLNDGVYPSAELHKEVKdwvRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd05920 420 MPDELLGERSCAFVVLRDPPPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
4.77e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 109.34 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYV-FDyqPGEVFWCTADVGWITGHSYLVYGplsngaktiLFEGVPN 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRS---------LLAGAEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 YPTTARMSEVVDKHKVNILYTA--PTAIRALMAKGDEAikgTSRDSLRIMGSVGEPINPEAWEwyyrTIGNEKSPIVDTW 413
Cdd:cd17630 70 VLLERNQALAEDLAPPGVTHVSlvPTQLQRLLDSGQGP---AALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 414 WQTETGGILITPLPGATALkpGSATRPFFGVQPALVDNmGEI-VEGATegnlVLLDSWPGQMRTvygdhDRFEQtyfstf 492
Cdd:cd17630 143 GMTETASQVATKRPDGFGR--GGVGVLLPGRELRIVED-GEIwVGGAS----LAMGYLRGQLVP-----EFNED------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 493 kGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPS 572
Cdd:cd17630 205 -GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 258583962 573 aelhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:cd17630 284 -----ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-621 |
4.79e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 109.68 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 81 CIDRhLATRGDQVAIIwegDDPTqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHT 160
Cdd:PLN02246 29 CFER-LSEFSDRPCLI---DGAT-GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 161 IVFGGFSPEALAGRIIDSNAKLVITADEGVrggravplkknvdEALTNPEVKNISKVMVLKrtggnvawhEHRDIWWH-- 238
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKLIITQSCYV-------------DKLKGLAEDDGVTVVTID---------DPPEGCLHfs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 239 EATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVyaTMTFKYV------FDYQPGEVFWCTADVGWITG 312
Cdd:PLN02246 162 ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKG-LV--TSVAQQVdgenpnLYFHSDDVILCVLPMFHIYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 313 -HSYLVYGpLSNGAkTIL----FEgvpnyptTARMSEVVDKHKVNILYTAPTAIRALmAKGDEAikgTSRD--SLRIMGS 385
Cdd:PLN02246 239 lNSVLLCG-LRVGA-AILimpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AKSPVV---EKYDlsSIRMVLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 386 VGEPINPEAWEWYYRTIGNEKspIVDTWWQTETGGILITPLPGA---TALKPGSAtrpffgvqpalvdnmGEIVEGA--- 459
Cdd:PLN02246 306 GAAPLGKELEDAFRAKLPNAV--LGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC---------------GTVVRNAelk 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 460 ---TEGNLVLLDSWPGQ--------MRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMG 528
Cdd:PLN02246 369 ivdPETGASLPRNQPGEicirgpqiMKGYLNDPEATANTI--DKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 529 TAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSD 608
Cdd:PLN02246 447 PAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSG 523
|
570
....*....|....
gi 258583962 609 KIMRRILR-KIATG 621
Cdd:PLN02246 524 KILRKDLRaKLAAG 537
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
1.22e-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: 107.56 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEgvrggRAVPLKKNvdEALTNPEVKNISKVmvlkrtggnvawhehrdiwwheatakvSDQCQP 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----LKSKLSFN--KSTILLEDPSISQE---------------------------DTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPLFILYTSGSTGKPKGV-------------------LHTTGGYLVYATMTFKYVfdYQpgEVF--WCTAdvgw 309
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVqlehknmvnllhferektnINFSDKVLQFATCSFDVC--YQ--EIFstLLSG---- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 310 itGHSYLVygplSNGAKTILFEgvpnypttarMSEVVDKHKVNILYTaPTAIRALMAKGDEAIKGTSrDSLRIMGSVGEP 389
Cdd:cd17656 195 --GTLYII----REETKRDVEQ----------LFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFP-TCVKHIITAGEQ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 390 --INPEAWEWYYR---TIGNEKSP----IVDTWwqTETGGILITPLPGATalKPGSATRPF-----FGVQPALVdnMGEI 455
Cdd:cd17656 257 lvITNEFKEMLHEhnvHLHNHYGPsethVVTTY--TINPEAEIPELPPIG--KPISNTWIYildqeQQLQPQGI--VGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 456 -VEGATEGNlvlldswpGQMRTVYGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:cd17656 331 yISGASVAR--------GYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEA 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 535 ALVAFSKIAEAAVVGVPHDIKGQAIYAYI----TLNDgvypsaelhKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKI 610
Cdd:cd17656 403 QLLNHPGVSEAVVLDKADDKGEKYLCAYFvmeqELNI---------SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
....*
gi 258583962 611 MRRIL 615
Cdd:cd17656 474 DRKAL 478
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-619 |
1.51e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.56 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGvRKGDVVCIYMPMVPE-----AAVAMLACTRIGavhtiVFGG 165
Cdd:PRK07638 16 NKIAIK------ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEflqlfAGAAMAGWTCVP-----LDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 166 FSPEALAGRIIDSNAKLVITADegvrggravpLKKNvdeALTNPEVKNISkvmvlkrtggnvaWHEhrdiwWHEATAKVS 245
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTER----------YKLN---DLPDEEGRVIE-------------IDE-----WKRMIEKYL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 246 DQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLvyatmtfkyvfdyqpgEVFWCTADVGWITG-----------HS 314
Cdd:PRK07638 133 PTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL----------------HSFDCNVHDFHMKRedsvliagtlvHS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 YLVYGPLS----NGAKTILFEGVPNypttaRMSEVVDKHKVNILYTAPTAIRALMAkgdeaIKGTSRDSLRIMGSVGE-- 388
Cdd:PRK07638 197 LFLYGAIStlyvGQTVHLMRKFIPN-----QVLDKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISSGAKwe 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 --------PINPEA--WEWYYrtiGNEKSpivdtwwqtetggiLITPL-PGATALKPGSATRPFFGVQPALVDNMGEIVE 457
Cdd:PRK07638 267 aeakekikNIFPYAklYEFYG---ASELS--------------FVTALvDEESERRPNSVGRPFHNVQVRICNEAGEEVQ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 458 gategnlvlldswPGQMRTVYGDHDRFEQTYFS--------TFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGT 529
Cdd:PRK07638 330 -------------KGEIGTVYVKSPQFFMGYIIggvlarelNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 530 AEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNdgvypsaELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDK 609
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGS-------ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGK 469
|
570
....*....|
gi 258583962 610 IMRRILRKIA 619
Cdd:PRK07638 470 IARMEAKSWI 479
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
3.61e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 106.76 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegDDptQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DN--HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITadegvrggravPLKknvdEALTNPEVKNISKVMVLKRTGGNVAWH----EHRDIWWHEATAKVSD 246
Cdd:PRK06087 113 LVWVLNKCQAKMFFA-----------PTL----FKQTRPVDLILPLQNQLPQLQQIVGVDklapATSSLSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 QCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAK 326
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 TILFEGVPnyPTTArmSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEPInPE--AWEWYYRTIgn 404
Cdd:PRK06087 257 SVLLDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PKkvARECQQRGI-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 405 eksPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDN------MGEIVEGATEGNLVLLDSWPGQMRTVY 478
Cdd:PRK06087 328 ---KLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlpPGCEGEEASRGPNVFMGYLDEPELTAR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 479 G-DHDrfeqtyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQ 557
Cdd:PRK06087 405 AlDEE-----------GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 558 AIYAYITLNDGVY-PSAElhkEVKDWV-RKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK06087 474 RSCAYVVLKAPHHsLTLE---EVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
82-617 |
5.03e-24 |
|
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: 105.47 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIiwegDDPTQdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:cd17653 3 FERIAAAHPDAVAV----ESLGG--SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGfSPEALAGRIID-SNAKLVITADegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwhea 240
Cdd:cd17653 77 LDAK-LPSARIQAILRtSGATLLLTTD----------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 takvsdqcqpeemKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTfKYVFDYQPGE--------VFWCTADVgwitg 312
Cdd:cd17653 103 -------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQP-PARLDVGPGSrvaqvlsiAFDACIGE----- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 313 hsylVYGPLSNGAKTILFEGVPNYPTTARmsevvdkhKVNILYTAPTAIRALmakgdeaiKGTSRDSLRIMGSVGEPINP 392
Cdd:cd17653 164 ----IFSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL--------SPQDFPNLKTIFLGGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 393 ---EAWeWYYRTIGNEKSPivdtwwqTETGgILITplpgATALKPGSAT---RPFFGV---------QPALVDNMGEI-V 456
Cdd:cd17653 224 sllDRW-SPGRRLYNAYGP-------TECT-ISST----MTELLPGQPVtigKPIPNStcyildadlQPVPEGVVGEIcI 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 457 EGategnlvlldswPGQMRTVYGDH----DRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:cd17653 291 SG------------VQVARGYLGNPaltaSKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 533 ESALVAFSKIAEAAVVGVphdiKGQAIYAYITlndgvyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17653 359 EEVVLQSQPEVTQAAAIV----VNGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDR 428
|
....*
gi 258583962 613 RILRK 617
Cdd:cd17653 429 KALRE 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
108-621 |
1.17e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 105.48 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALA--GRIIDSNAKLVit 185
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIErfCQITDPAAALV-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 adegVRGGRAvplkknvdEALTNPEVKNISKVMVLKRTGGNVAWHEHRDIWWHEAtakvsdqcQPEeMKAEDPLFILYTS 265
Cdd:PRK05857 120 ----APGSKM--------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG--------NAD-QGSEDPLAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 266 GSTGKPKGVLhttggylvYATMTFKYVFDYQPGE-VFWctadVGWITGHSylVYGPLSngAKTI---------LFEG--- 332
Cdd:PRK05857 179 GTTGEPKAVL--------LANRTFFAVPDILQKEgLNW----VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 333 VPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLRIMGSVGEpinpEAWEWYYRTIGNEKSPIVDT 412
Cdd:PRK05857 243 VTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSLRLVGYGGS----RAIAADVRFIEATGVRTAQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 413 WWQTETGGI---LITPLPGATALKPGSATRPFFGVQPALVD------NMGEIVEGATEGNLvlldsW---PGQMRTVYGD 480
Cdd:PRK05857 317 YGLSETGCTalcLPTDDGSIVKIEAGAVGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTL-----WiksPANMLGYWNN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 HDRFEQTYfstFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHD----IKG 556
Cdd:PRK05857 392 PERTAEVL---IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEefgaLVG 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 557 QAIYAYITLNDGVypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATG 621
Cdd:PRK05857 469 LAVVASAELDESA--ARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
105-615 |
1.30e-23 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 104.26 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemKAEDPLFILYT 264
Cdd:cd17652 90 T--------------------------------------------------------------------TPDNLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVL--HTTGGYLVYATMTFkyvFDYQPGEVFWCTADVGWITGHSYLVYGPLSnGAKTILfegVPNYPTTA-- 340
Cdd:cd17652 102 SGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVL---APAEELLPge 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 341 RMSEVVDKHKVNILYTAPTAIRALMAKGDEAikgtsrdsLRIMGSVGEPINPE-AWEWYY-RTIGNEKSPIVDTWWQTET 418
Cdd:cd17652 175 PLADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAElVDRWAPgRRMINAYGPTETTVCATMA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 419 GgilitPLPGATALKPGsatRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRtvyGDHDRFEQTY-------FST 491
Cdd:cd17652 247 G-----PLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYI--AGAGLAR---GYLNRPGLTAerfvadpFGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 492 FKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVY 570
Cdd:cd17652 314 PGSrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 258583962 571 PSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17652 394 PTAA---ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
91-617 |
1.44e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.06 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegdDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtivFGGFSPEA 170
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIID----SNAKLVITADegvrggravplkknvdeaLTNPEVKNIS-KVMVLKRT--GGNVAWHEHRDiwwheATAK 243
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTND------------------TNYGKVKGLGlPVIVLGEEkiEGAVNWKELLE-----AADR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 244 VSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVfwctADVGWITG-HSYLVYG--- 319
Cdd:PLN02330 172 AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIPFfHIYGITGicc 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 320 -PLSNGAKTILfegVPNYPTTARMSEVVdKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWY 398
Cdd:PLN02330 248 aTLRNKGKVVV---MSRFELRTFLNALI-TQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 YRTIGNEKspIVDTWWQTETGGILIT---PLPGATALKPGSATRPFFGVQPALVD-NMGEIVEGATEGNLVLLDSWpgQM 474
Cdd:PLN02330 324 EAKFPGVQ--VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQC--VM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 475 RTVYGDHDRFEQTYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDI 554
Cdd:PLN02330 400 QGYYNNKEETDRTIDE--DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258583962 555 KGQAIYAYITLNdgvyPSA-ELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PLN02330 478 AGEIPAACVVIN----PKAkESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
261-616 |
3.37e-23 |
|
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: 103.23 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGVLHTTGGYLVYATMtfkyvfdyqpgeVFWCTADVGWITGHSYLVYGPLSNGAK-----TILFEGVpn 335
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDT------------LMAAALGFGPGADSVYLSPAPLYHAAPfrwsmTALFMGG-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 ypTTARMS--------EVVDKHKVNILYTAPTaIRALMAKGDEAIKGtSRD--SLRIMGSVGEPINP---EAW-EWYyrt 401
Cdd:cd05929 196 --TLVLMEkfdpeeflRLIERYRVTFAQFVPT-MFVRLLKLPEAVRN-AYDlsSLKRVIHAAAPCPPwvkEQWiDWG--- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 402 ignekSPIVDTWWqTETGGILITPLPGATALK-PGSATRPFFGVQPALVDNMGEIVEGaTEGNLVLLDSWPgqmrtvYGD 480
Cdd:cd05929 269 -----GPIIWEYY-GGTEGQGLTIINGEEWLThPGSVGRAVLGKVHILDEDGNEVPPG-EIGEVYFANGPG------FEY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 481 HDRFEQTYFSTFKGMYFT-GDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAI 559
Cdd:cd05929 336 TNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRV 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 560 YAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05929 416 HAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
3.79e-23 |
|
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: 100.81 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSyLVYGPLSNGAKTILFEGVpny 336
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 337 pTTARMSEVVDKHKVNILYTAPTAIRALMakgDEAIK-GTSRDSLRIMGSVGEPINPEAWEwyyrtignEKSPivDTWW- 414
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSFPPILSNLL---DAAEKsGVDLSSLRHVLGLDAPETIQRFE--------ETTG--ATFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 ---QTETGGiLITPLPGATalKPGSATRPFFGVQPALVDN---------MGEIVegaTEGNLVLLDSWPGQMRTVYgdhd 482
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDndrpvpageTGEIV---VRGPLVFQGYWNLPELTAY---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 483 rfeqtyfsTFK-GMYFTGDGARRDEDGYYWITGRV--DDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPhDIK-GQA 558
Cdd:cd17637 212 --------TFRnGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-DPKwGEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 258583962 559 IYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17637 283 IKAVCVLKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
105-623 |
3.81e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 103.68 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGVRGGRAVPLKknvDEALtnPEVKNIskvmvlkrtGGNVAWHEHRDiwWHEATAKVSDQCQP-EEMKAEDPLFILY 263
Cdd:PRK06155 124 VEAALLAALEAADPG---DLPL--PAVWLL---------DAPASVSVPAG--WSTAPLPPLDAPAPaAAVQPGDTAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVLHTTGGYLVYATMTfkyvfdyqpgevfwcTADVGWITGHSYLVYGPL-SNGAKTILFEGVPN---YPTT 339
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLPLfHTNALNAFFQALLAgatYVLE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 340 ARMS-----EVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRdsLRIMGSVGEPinPEAWEWYYRTIGnekSPIVDTWW 414
Cdd:PRK06155 253 PRFSasgfwPAVRRHGATVTYLLGAMVSILLSQPARESDRAHR--VRVALGPGVP--AALHAAFRERFG---VDLLDGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 QTETGGILITPLPGAtalKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRTVYgdhDRFEQTYFSTFKG 494
Cdd:PRK06155 326 STETNFVIAVTHGSQ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGY---FGMPEKTVEAWRN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 495 MYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVypSA 573
Cdd:PRK06155 400 LWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGT--AL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 258583962 574 ELhKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKI-ATGDT 623
Cdd:PRK06155 478 EP-VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQgVTADT 527
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
4.11e-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: 101.20 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYATMTFKyVFDYQ--PGEVFWCtadVGWITGhsylVYGPLSNGAKTI 328
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT-EQDRLciPVPLFHC---FGSVLG----VLACLTHGATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 329 L----FEGVPNYpttarmsEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSrdSLR--IMGsvGEPINPEAWEWYYRTI 402
Cdd:cd05917 74 FpspsFDPLAVL-------EAIEKEKCTALHGVPTMFIAELEHPDFDKFDLS--SLRtgIMA--GAPCPPELMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 403 GNEKSPIVdtWWQTETGGILITPLPGATA-LKPGSATRPFFGVQPALVDNMGEIV-------EGATEGNLVlldswpgqM 474
Cdd:cd05917 143 NMKDVTIA--YGMTETSPVSTQTRTDDSIeKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpgELCIRGYSV--------M 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 475 RTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDI 554
Cdd:cd05917 213 KGYWNDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDER 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 555 KGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:cd05917 291 YGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-617 |
4.27e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplKKNVDEALTNPEvknisKVMVLKRTggnvawhehRDIWWHEatakvSDQCQPEEMKAEDPL-FILY 263
Cdd:PRK12316 2106 T-------------QRHLLERLPLPA-----GVARLPLD---------RDAEWAD-----YPDTAPAVQLAGENLaYVIY 2153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVLHTTGGYLVYATMTFKYvFDYQPGEVFWCTADVGWITGHSYLvYGPLSNGAKTILFEGVPNYPttARMS 343
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQW-FHPLLNGARVLIRDDELWDP--EQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 344 EVVDKHKVNILYTAPTAIRALmakGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEKspIVDTWWQTETggiLI 423
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQL---AEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VV 2301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 424 TPL--------PGATALKP-GSA--TRPFF----GVQPALVDNMGEIVEGATEGNLVLLDSwPGQMRtvygdhDRFEQTY 488
Cdd:PRK12316 2302 TPLlwkcrpqdPCGAAYVPiGRAlgNRRAYildaDLNLLAPGMAGELYLGGEGLARGYLNR-PGLTA------ERFVPDP 2374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 489 FSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVpHDIKGQAIYAYITLND 567
Cdd:PRK12316 2375 FSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDD 2453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 258583962 568 gvyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK12316 2454 ---AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
108-616 |
1.55e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 102.42 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITAd 187
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 eGVRGGRAVPlkKNVDEAltnpevkniskvmvlkrtggnvawhehRDIWWHEATAKVSDQcqpEEMKAEDPLFILYTSGS 267
Cdd:PRK06060 110 -DALRDRFQP--SRVAEA---------------------------AELMSEAARVAPGGY---EPMGGDALAYATYTSGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 268 TGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTIlfegVPNYPTTARMSEVVD 347
Cdd:PRK06060 157 TGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV----INSAPVTPEAAAILS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 348 -KHKVNILYTAPTairaLMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNekSPIVDTWWQTETGGILITPl 426
Cdd:PRK06060 233 aRFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 427 pGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLvlldsWpgqmrtVYGDhdRFEQTYFS------TFKGMYFTGD 500
Cdd:PRK06060 306 -RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDL-----W------VRGP--AIAKGYWNrpdspvANEGWLDTRD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 501 GARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVK 580
Cdd:PRK06060 372 RVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLH 451
|
490 500 510
....*....|....*....|....*....|....*.
gi 258583962 581 DWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK06060 452 RGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-643 |
1.71e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplkknvDEALTNPEVKNISKVMVlKRTGGNVAWHEhrdiwwheatakvsdqcQPEEMKAEDPLFILYT 264
Cdd:PRK12316 3160 S-----------------QSHLRLPLAQGVQVLDL-DRGDENYAEAN-----------------PAIRTMPENLAYVIYT 3204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVgwITGHSYLVYGPLSNGAkTILFEGVPNYPTTARMSE 344
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS--FDVFVEELFWPLMSGA-RVVLAGPEDWRDPALLVE 3281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 345 VVDKHKVNILYTAPTAIRALMAKGDEAikgtSRDSLRIMGSVGEPINPE------AWEWYYRTIGNEKSPIVDTWWQTET 418
Cdd:PRK12316 3282 LINSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADlqqqvfAGLPLYNLYGPTEATITVTHWQCVE 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 419 GGIliTPLPGATALKPGSATRPFFGVQPALVDNMGEIVEGAtEGNLVLLDSWPGQMRtvygdhDRFEQTYFSTFKGMYFT 498
Cdd:PRK12316 3358 EGK--DAVPIGRPIANRACYILDGSLEPVPVGALGELYLGG-EGLARGYHNRPGLTA------ERFVPDPFVPGERLYRT 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 499 GDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVgvphDIKGQAIYAYITLNDgvyPSAELHKE 578
Cdd:PRK12316 3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPED---EAGDLREA 3501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 579 VKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIatgdTSNLGDTSTLADPSVVDRLIA 643
Cdd:PRK12316 3502 LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP----DAALLQQDYVAPVNELERRLA 3562
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
106-616 |
2.67e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 100.85 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPeALAGRII-DSNAKLVI 184
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA-PEADYIVgDSGARVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 T--ADEGVRGGRAVPLKKNVDealtnpevkniskvmvlkrTGGNVAWHEHRDIWWHEATAKVSDQ-CQPeemkaedplFI 261
Cdd:PRK13390 102 AsaALDGLAAKVGADLPLRLS-------------------FGGEIDGFGSFEAALAGAGPRLTEQpCGA---------VM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 262 LYTSGSTGKPKGV--------LHTTGGYLVYATMTFkyvFDYQPGEVFWCTADVGwitgHSylvyGPL-------SNGAK 326
Cdd:PRK13390 154 LYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 TILFEGVPNYPTTARmsevVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEP------------INPEA 394
Cdd:PRK13390 223 VVLAKRFDAQATLGH----VERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdvkhamidwLGPIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 395 WEWYYrtignekspivdtwwQTETGGILITPLPGATAlKPGSATRPFFGVQPALVDnmgeivegatEGNlvllDSWPGQM 474
Cdd:PRK13390 299 YEYYS---------------STEAHGMTFIDSPDWLA-HPGSVGRSVLGDLHICDD----------DGN----ELPAGRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 475 RTVYGDHDRF--------EQTYFSTFKGMYF---TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIA 543
Cdd:PRK13390 349 GTVYFERDRLpfrylndpEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVH 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 544 EAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK13390 429 DVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-617 |
4.55e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 100.72 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFE------DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITADEgvrggravpLKKNVDEALtnPEVKNISKVMVLkrtGGNVAWHEHRDIWWHEAT 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEE---------LVEAFEEAR--ADLARPPRLWVA---GGDTLDDPEGYEDLAAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 AKVSDQCQPE--EMKAEDPLFILYTSGSTGKPKGVLHT----TGGYLVYATMTfkyvfDYQPGEVFWCT--------ADV 307
Cdd:PRK08279 183 AGAPTTNPASrsGVTAKDTAFYIYTSGTTGLPKAAVMShmrwLKAMGGFGGLL-----RLTPDDVLYCClplyhntgGTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 308 GWITGhsylvygpLSNGAKTILFEgvpNYPTTARMSEVVdKHKVnilyTAPTAI----RALMakgDEAIKGTSRD-SLRI 382
Cdd:PRK08279 258 AWSSV--------LAAGATLALRR---KFSASRFWDDVR-RYRA----TAFQYIgelcRYLL---NQPPKPTDRDhRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 383 MgsVGEPINPEAWEWYYRTIGNEKspIVDTWWQTEtggilitplpGATAL-----KPGSATR-PFFGVQP-ALV----DN 451
Cdd:PRK08279 319 M--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASE----------GNVGFinvfnFDGTVGRvPLWLAHPyAIVkydvDT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 452 mGEIVEGAtEGNLV--------LL-----DSWP--GqmrtvYGD---------HDRFEqtyfstfKG-MYF-TGDGARRD 505
Cdd:PRK08279 385 -GEPVRDA-DGRCIkvkpgevgLLigritDRGPfdG-----YTDpeasekkilRDVFK-------KGdAWFnTGDLMRDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 506 EDGYYWITGRVDDVL-----NVSghrmgTAEIESALVAFSKIAEAAVVGVP---HDikGQAIYAYITLNDGV-YPSAELH 576
Cdd:PRK08279 451 GFGHAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAAIVLADGAeFDLAALA 523
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 258583962 577 KEVKDwvrkEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK08279 524 AHLYE----RLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-617 |
5.30e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.96 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:PRK12316 4566 DAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEGVRGgraVPLKKNVDEaltnpevkniskvMVLKRTGGNVAWHEHrdiwwheatakvsdqcQP 250
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQR---LPIPDGLAS-------------LALDRDEDWEGFPAH----------------DP 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYATMTfkyvfdyqpGEVFWCTAD--VGWITGHSYLV-----YGPLS 322
Cdd:PRK12316 4688 AVRLHPDNLaYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDdrVLQFMSFSFDGsheglYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 NGAKTILFEgvPNYPTTARMSEVVDKHKVNILYTAPTAIRALmAKGDEAIKGTSrdSLRIMGSVGEPINPEAWEWYYRTI 402
Cdd:PRK12316 4759 NGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAERDGEPP--SLRVYCFGGEAVAQASYDLAWRAL 4833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 403 GNEKspIVDTWWQTETggiLITPLPGATA--LKPGSATRPFFGVQPA----LVDNMGEIVEGATEGNLVLldswpGQMRT 476
Cdd:PRK12316 4834 KPVY--LFNGYGPTET---TVTVLLWKARdgDACGAAYMPIGTPLGNrsgyVLDGQLNPLPVGVAGELYL-----GGEGV 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 477 VYGDH-------DRFEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVV 548
Cdd:PRK12316 4904 ARGYLerpaltaERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 549 GVPHDIkGQAIYAYITLND-GVYPSAELHKEVKDWVRKEIGAiATPDVL---HWT--DALPKTRSDKIMRRILRK 617
Cdd:PRK12316 4984 AQEGAV-GKQLVGYVVPQDpALADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLTPNGKLDRKALPQ 5056
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
6.05e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.96 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 79 ANCIDRHLATRGDQVAIIWegddpTQDKT-LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGA 157
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV-----TADRIaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 158 VHTIVFGGFSPEALAGRIIDSNAKLVITADEGVrGGRAVPLKKNVDEALTNPEVKNISKVMVLKrtggnvawheHRDIww 237
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIDADGP-HDRAEPTTRWWPLTVNVGGDSGPSGGTLSV----------HLDA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 238 heATAKVSDQCQPEEMKAEDPLfILYTSGSTGKPKGVLHTTGGylvYATMTFKYVFDYQPGEVFWCTADVGWITGHSYL- 316
Cdd:PRK05852 161 --ATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHAN---IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIa 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 -VYGPLSNGAKTILfegvpnyPTTARMSEVV---DKHKVN-ILYTA-PTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPI 390
Cdd:PRK05852 235 aLLATLASGGAVLL-------PARGRFSAHTfwdDIKAVGaTWYTAvPTIHQILLERAATEPSGRKPAALRFIRSCSAPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 391 NPEAWEWYYRTIGnekSPIVDTWWQTET---------GGILITPLPGATALKPGSATrpffGVQPALVDNMGEIVEGATE 461
Cdd:PRK05852 308 TAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 462 GNLVLldSWPGQMRTVYGDHdrfEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSK 541
Cdd:PRK05852 381 GEVWL--RGTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 542 IAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRR 613
Cdd:PRK05852 456 VMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
8.12e-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: 96.71 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 257 DPLFILYTSGSTGKPKGVLHTTGGYLvyatmtfkyvfdyqpgEVFWCTADVGWITGHS-YLVYGPLS-----NGAKTILF 330
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI----------------ESFVCNEDLFNISGEDaILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 331 EG----VPNYPTTARMSEVVDKHKVNILYTAPTAIRALmakgdeAIKGTSRDSLRIMGSVGEPINPEAwewyYRTIGNE- 405
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 406 -KSPIVDTWWQTETGgiLITPLPGATALKPGSATRPFFGVQPALVDNMGE-----------IVEGATEGNLVLLDSWpgq 473
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGeigkifvksemVFSGYVRGGFSNPDGW--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 474 mrtvygdhdrfeqtyfstfkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHD 553
Cdd:cd17633 210 ----------------------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 554 IKGQAIYAYITLNDGVYpsaelhKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17633 268 RFGEIAVALYSGDKLTY------KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
106-617 |
1.41e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.62 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 ADEGVR------GGRAVPLkknvDEALtnpevkniskvmvlkrtggnvawhehrDIWWHEATAKVSDQCQPEEMKaedpl 259
Cdd:PRK12467 616 QSHLLAqlpvpaGLRSLCL----DEPA---------------------------DLLCGYSGHNPEVALDPDNLA----- 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 260 FILYTSGSTGKPKGVLHTTGGYLVYATMTFKYvfdyqpgevFWCTADVGWITGHSY-------LVYGPLSNGAKTILFEg 332
Cdd:PRK12467 660 YVIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLLP- 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 333 vpnyPTTARMSE----VVDKHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSvgepinpEAWEWYYRTIGNEKSP 408
Cdd:PRK12467 730 ----PDCARDAEafaaLMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCGG-------EALQVDLLARVRALGP 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 409 ---IVDTWWQTETG-GILITPLPGATALKPGSAT-RPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRTVYG---- 479
Cdd:PRK12467 797 garLINHYGPTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYI--GGAGLARGYHRrpal 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 480 DHDRFEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQA 558
Cdd:PRK12467 875 TAERFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL 954
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 559 IyAYITLNDGvyPSAELHKEVKDWVRKEIGAI----ATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK12467 955 V-AYLVPAAV--ADGAEHQATRDELKAQLRQVlpdyMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
107-619 |
2.08e-21 |
|
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: 97.79 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 107 TLTYKQLHQEVCRFSNALKEqGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITA 186
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 187 DEGVRGGRAVPLkknvdealtnPEVKNISKVMVLKRTGGNVAWHEH---------RDIWWHEATAKVSDQcqpeemkAED 257
Cdd:cd05909 86 KQFIEKLKLHHL----------FDVEYDARIVYLEDLRAKISKADKckaflagkfPPKWLLRIFGVAPVQ-------PDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 258 PLFILYTSGSTGKPKGVLHTTGGYL--VYATMTfkyVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFegvPN 335
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH---PN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 yPTTAR-MSEVVDKHKVNILYTAPTAIRALMakgdEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWW 414
Cdd:cd05909 223 -PLDYKkIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG---IRILEGYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 415 QTETGGILITPLPgATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSwPGQMRTVYGDHdrfEQTYFSTFKG 494
Cdd:cd05909 295 TTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEP---ELTSFAFGDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 495 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAL-VAFSKIAEAAVVGVPHDIKGQAIYAYITLNDgvyPSA 573
Cdd:cd05909 370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVLLTTTTD---TDP 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 258583962 574 ElhkEVKDWVRK-EIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:cd05909 447 S---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
250-622 |
2.66e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 97.83 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 PEEMKAEDPLFILYTSGSTGKPKGVLhTTGGYLVYATMTFKYVFDYQPGEVFWCTAD--------VGWITGhsylvygpL 321
Cdd:PRK07867 146 FRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA--------L 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTIL---------FEGVPNYPTTarMSEVVDKHKVNILYTAPtairalmaKGDEAikgtsRDSLRIM-GSVGEPIN 391
Cdd:PRK07867 217 AAGASIALrrkfsasgfLPDVRRYGAT--YANYVGKPLSYVLATPE--------RPDDA-----DNPLRIVyGNEGAPGD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 PEAWEWYYRTIgnekspIVDTWWQTEtGGILITPLPGAtalKPGSATRPFFGVQ-----------PALVDNMGEIVEGAT 460
Cdd:PRK07867 282 IARFARRFGCV------VVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgtecpPAEDADGRLLNADEA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 461 EGNLVLLDSwPGQMRTVYGDHDRFEQtyfSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFS 540
Cdd:PRK07867 352 IGELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 541 KIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDwVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK--I 618
Cdd:PRK07867 428 DATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAegV 506
|
....
gi 258583962 619 ATGD 622
Cdd:PRK07867 507 DCAD 510
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
249-616 |
3.19e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 97.37 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 249 QPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGylVYATMtfkyvfDYQPGEVFWCTADV-----------GWITGhsylV 317
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRA--IAADL------DALAEAWQWTADDVlvhglplfhvhGLVLG----V 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 318 YGPLSNGAkTILFEGvpnYPTTARMSEVVDKhKVNILYTAPTAIRALMAKGDEAiKGTSRDSLRIMGSVGEPInPEawew 397
Cdd:PRK07787 189 LGPLRIGN-RFVHTG---RPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAA-RALRGARLLVSGSAALPV-PV---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 398 YYRTIGNEKSPIVDTWWQTETggiLITPLPGATA-LKPGSATRPFFGVQPALVDNMGEIV--EGATEGNLvlldswpgQM 474
Cdd:PRK07787 258 FDRLAALTGHRPVERYGMTET---LITLSTRADGeRRPGWVGLPLAGVETRLVDEDGGPVphDGETVGEL--------QV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 475 R--TVY-GDHDRFEQTYFS-TFKGMYFTGDGARRDEDGYYWITGRVD-DVLNVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:PRK07787 327 RgpTLFdGYLNRPDATAAAfTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258583962 550 VPHDIKGQAIYAYITLNDGVYPSaelhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK07787 407 VPDDDLGQRIVAYVVGADDVAAD-----ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
3.62e-21 |
|
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: 96.98 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVItadegvrggravplkknVDEALTNPEVkniskvmvLKRTGGNVAWHEHRDIWwheat 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-----------------VDREFEYEDL--------LAEGDPDFEWIPPADEW----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvsdqcqpeemkaeDPLFILYTSGSTGKPKGVLHT-TGGYLvyATMTFKYVFDYQPGEVFWCTADV----GWItghsyL 316
Cdd:cd12118 134 ---------------DPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 VYGPLSNGAKTILFEGVpNYPTTARMsevVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRdslRIMGSVGEPINPEAwe 396
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV-DAKAIYDL---IEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVHVMTAGAPPPAA-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 397 wyyrTIGNEKS---PIVDTWWQTETGGilitplPGAT-ALKPGSATRP--------------FFGVQPALVDN------- 451
Cdd:cd12118 263 ----VLAKMEElgfDVTHVYGLTETYG------PATVcAWKPEWDELPteerarlkarqgvrYVGLEEVDVLDpetmkpv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 452 ------MGEIVegaTEGNLVlldswpgqMRTVYGDHdrfEQTYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:cd12118 333 prdgktIGEIV---FRGNIV--------MKGYLKNP---EATA-EAFRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 525 HRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDaLPK 604
Cdd:cd12118 398 ENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPK 473
|
570
....*....|...
gi 258583962 605 TRSDKIMRRILRK 617
Cdd:cd12118 474 TSTGKIQKFVLRD 486
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
5.03e-21 |
|
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: 95.02 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEgvpn 335
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 YPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTsrDSLRIMGSVGE-PINPEA--WEWyyrtigNEKSPIVDT 412
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATV--PSLRLIGYGGSrAIAADVrfIEA------TGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 413 WWQTETGGILITPLpGATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWpgQMRTVYGDHDRFEQTYFStf 492
Cdd:cd17635 149 YGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLID-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 493 kGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLndgvypS 572
Cdd:cd17635 224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA------S 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 258583962 573 AELHKEV----KDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17635 297 AELDENAiralKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-619 |
7.20e-21 |
|
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: 96.07 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 81 CIDRHLATRGDQVAI-IWEGDdptqdktLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVH 159
Cdd:cd05918 4 LIEERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 160 TIVfggfSPEALAGR----IIDSNAKLVITADegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdi 235
Cdd:cd05918 77 VPL----DPSHPLQRlqeiLQDTGAKVVLTSS------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 236 wwheatakvsdqcqpeemkAEDPLFILYTSGSTGKPKGVL--HTTggyLVYATMTFKYVFDYQPGE-VFWCTA---DVgw 309
Cdd:cd05918 105 -------------------PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSESrVLQFASytfDV-- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 310 itgHSYLVYGPLSNGAkTILfegVPnyPTTARMS---EVVDKHKVNILYTAPTAIRALMAKGDEaikgtsrdSLRIMGSV 386
Cdd:cd05918 161 ---SILEIFTTLAAGG-CLC---IP--SEEDRLNdlaGFINRLRVTWAFLTPSVARLLDPEDVP--------SLRTLVLG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 387 GEPINPEawewyyrtignekspIVDTWWQ----------TET--GGILITPLPGATALKPGSAtrpfFGVQPALVD--NM 452
Cdd:cd05918 224 GEALTQS---------------DVDTWADrvrlinaygpAECtiAATVSPVVPSTDPRNIGRP----LGATCWVVDpdNH 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 453 GEIV-EGAT-----EGNLV----LLDswPGQMRTVYGDHDRFEQTYFSTFKG-MYFTGDGARRDEDG--YYwiTGRVDDV 519
Cdd:cd05918 285 DRLVpIGAVgelliEGPILargyLND--PEKTAAAFIEDPAWLKQEGSGRGRrLYRTGDLVRYNPDGslEY--VGRKDTQ 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 520 LNVSGHRMGTAEIESALVAFSKIAEAAVVGV--PHDIKGQAIY-AYITLN-------DGVYPSAELH-------KEVKDW 582
Cdd:cd05918 361 VKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLvAFVVLDgsssgsgDGDSLFLEPSdefralvAELRSK 440
|
570 580 590
....*....|....*....|....*....|....*..
gi 258583962 583 VRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:cd05918 441 LRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-618 |
4.77e-20 |
|
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: 93.89 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 87 ATRGDQVAIIWEGDDPTQDkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVfggf 166
Cdd:cd05906 20 AERGPTKGITYIDADGSEE-FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 167 sPEALAGRIIDSNAK------------LVITADEGVRGGRAVplkknvdEALTNPEVKNISKVMVLKRTGGNVAWHehrd 234
Cdd:cd05906 95 -TVPPTYDEPNARLRklrhiwqllgspVVLTDAELVAEFAGL-------ETLSGLPGIRVLSIEELLDTAADHDLP---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 235 iwwheatakvsdQCQPEemkaeDPLFILYTSGSTGKPKGVLHTTGGYLVY--ATMTfkyVFDYQPGEVF--WCTAD-VGW 309
Cdd:cd05906 163 ------------QSRPD-----DLALLMLTSGSTGFPKAVPLTHRNILARsaGKIQ---HNGLTPQDVFlnWVPLDhVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 310 ITgHSYLVygPLSNGAKTIlfegvpNYPTTARMSEV------VDKHKVNILYtAPTAIRALMAKGDEAIKGTSRD--SLR 381
Cdd:cd05906 223 LV-ELHLR--AVYLGCQQV------HVPTEEILADPlrwldlIDRYRVTITW-APNFAFALLNDLLEEIEDGTWDlsSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 382 IMGSVGEPINPEAWEWYYRTIGNEKSP---IVDTWWQTETG-GI---LITPLPGAT-ALKPGSATRPFFGVQPALVDNMG 453
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCsGViysRSFPTYDHSqALEFVSLGRPIPGVSMRIVDDEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 454 EIVEGATEGNLVLldswPGQMRTV-YGDHDRFEQTYFsTFKGMYFTGDGARRDeDGYYWITGRVDDVLNVSGHRMGTAEI 532
Cdd:cd05906 373 QLLPEGEVGRLQV----RGPVVTKgYYNNPEANAEAF-TEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 533 ESAL-----VAFSKIAEAAVVGVPHDIKGQAIYaYITLNDGVYPSAELHKEVKDWVRKEIGaiATPDVL--HWTDALPKT 605
Cdd:cd05906 447 EAAVeevpgVEPSFTAAFAVRDPGAETEELAIF-FVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLipLPKEEIPKT 523
|
570
....*....|...
gi 258583962 606 RSDKIMRRILRKI 618
Cdd:cd05906 524 SLGKIQRSKLKAA 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-625 |
6.68e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.75 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 48 WIKPFTKVKNTSFDPGHIDIrwfeDGTLNISANCIDRHlaTRGDQVAIIwegdDPTQDKTLTYKQLHQEVCRFSNALKEQ 127
Cdd:PLN02574 17 WYSPETGIYSSKHPPVPLPS----DPNLDAVSFIFSHH--NHNGDTALI----DSSTGFSISYSELQPLVKSMAAGLYHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 128 -GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADEGVrgGRAVPLKKNVdeaL 206
Cdd:PLN02574 87 mGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPV---I 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 207 TNPEVKNISKVMVLKRTggnvawhehrdiwWHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAT 286
Cdd:PLN02574 162 GVPENYDFDSKRIEFPK-------------FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 287 MTFKY---VFDYQPGE-VFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVpnypTTARMSEVVDKHKVNILYTAPTAIR 362
Cdd:PLN02574 229 LFVRFeasQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 363 ALMaKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIgneksPIVD---TWWQTETGGILITPLPGATALKPGSATR 439
Cdd:PLN02574 305 ALT-KKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDfiqGYGMTESTAVGTRGFNTEKLSKYSSVGL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 440 PFFGVQPALVD-NMGEIVEGATEGNLVLldSWPGQMRTVYGDHdrfEQTYFSTFK-GMYFTGDGARRDEDGYYWITGRVD 517
Cdd:PLN02574 379 LAPNMQAKVVDwSTGCLLPPGNCGELWI--QGPGVMKGYLNNP---KATQSTIDKdGWLRTGDIAYFDEDGYLYIVDRLK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 518 DVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLH 597
Cdd:PLN02574 454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPYKKVRKVV 530
|
570 580
....*....|....*....|....*...
gi 258583962 598 WTDALPKTRSDKIMRRILRKIATGDTSN 625
Cdd:PLN02574 531 FVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-619 |
9.62e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 93.40 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRF-SNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK08751 49 KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGVRGGRAV----PLKKNV-----------DEALTNPEVKNISKVMVlkrtggnvAWHEHRDIWWHEATAKVSDQCQ 249
Cdd:PRK08751 129 VIDNFGTTVQQViadtPVKQVIttglgdmlgfpKAALVNFVVKYVKKLVP--------EYRINGAIRFREALALGRKHSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 PE-EMKAEDPLFILYTSGSTGKPKGVLHTTGGYLvyATMTfkyvfdyQPGEvfWCTADVGWITGHS--------YLVYGP 320
Cdd:PRK08751 201 PTlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV--ANMQ-------QAHQ--WLAGTGKLEEGCEvvitalplYHIFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 321 LSNGAKTILFEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAK--GDEAIKGTSRDSLRIMGSVGEPINPEAWEWY 398
Cdd:PRK08751 270 TANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMAVQRSVAERW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 YRTIGnekSPIVDTWWQTETG-GILITPLpgatALKP--GSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMR 475
Cdd:PRK08751 350 KQVTG---LTLVEAYGLTETSpAACINPL----TLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCI--KGPQVMK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 476 tvyGDHDRFEQT-YFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDI 554
Cdd:PRK08751 421 ---GYWKRPEETaKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 555 KGQAIYAYITLNDGVYpSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK08751 498 SGEIVKVVIVKKDPAL-TAE---DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
109-618 |
4.96e-19 |
|
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: 90.66 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITADE 188
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 189 GvrggravpLKKNVDEALTNPEVKNI----SKVMVLKRTGGNVAWHEHRDIWWHEatakvSDQCQPEEMKAEDPLFILYT 264
Cdd:cd17642 126 G--------LQKVLNVQKKLKIIKTIiildSKEDYKGYQCLYTFITQNLPPGFNE-----YDFKPPSFDRDEQVALIMNS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYL-VYGPLSNGAKTILfegVPNYPTTARMS 343
Cdd:cd17642 193 SGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFtTLGYLICGFRVVL---MYKFEEELFLR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 344 EVVDkHKVNILYTAPTaIRALMAKgDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIgneKSPIV-DTWWQTE-TGGI 421
Cdd:cd17642 270 SLQD-YKVQSALLVPT-LFAFFAK-STLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRF---KLPGIrQGYGLTEtTSAI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 422 LITPlpgATALKPGSATR--PFFGVQpaLVD-NMGEIVEGATEGNLVLldSWPGQMRTVYGDHdrfEQTYFSTFK-GMYF 497
Cdd:cd17642 344 LITP---EGDDKPGAVGKvvPFFYAK--VVDlDTGKTLGPNERGELCV--KGPMIMKGYVNNP---EATKALIDKdGWLH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 498 TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSaelHK 577
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT---EK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 258583962 578 EVKDWVRkeiGAIATPDVLH----WTDALPKTRSDKIMRRILRKI 618
Cdd:cd17642 491 EVMDYVA---SQVSTAKRLRggvkFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
83-619 |
1.30e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.48 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 83 DRHLATRGDQVAIIwegdDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:PRK08315 23 DRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFSPEALAGRIIDSNAKLVITADeGVRGGR-------AVP-LKKNVDEALTNPEVKNISKVMVL--KRTGGNVAWHEh 232
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAAD-GFKDSDyvamlyeLAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLNFDE- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 233 rdiWWHEATAKVSDQCQP--EEMKAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYATMTFkyvfdyQPGE------ 299
Cdd:PRK08315 177 ---LLALGRAVDDAELAArqATLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKL------TEEDrlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 300 -VFWCtadVGWITGhsylVYGPLSNGAkTILFEGvPNYPTTARMsEVVDKHKVNILYTAPTAIRALMAKGDEAikgtSRD 378
Cdd:PRK08315 248 pLYHC---FGMVLG----NLACVTHGA-TMVYPG-EGFDPLATL-AAVEEERCTALYGVPTMFIAELDHPDFA----RFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 379 --SLR--IM-GSVGePInpeawEWYYR----------TIG---NEKSPiVDTwwQTETGgiliTPLpgatALKPGSATRP 440
Cdd:PRK08315 314 lsSLRtgIMaGSPC-PI-----EVMKRvidkmhmsevTIAygmTETSP-VST--QTRTD----DPL----EKRVTTVGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 441 FFGVQPALVD-NMGEIV------EGATEGNLVLLDSW--PGQMRTVYgDHDRFeqtyfstfkgMYfTGDGARRDEDGYYW 511
Cdd:PRK08315 377 LPHLEVKIVDpETGETVprgeqgELCTRGYSVMKGYWndPEKTAEAI-DADGW----------MH-TGDLAVMDEEGYVN 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 512 ITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIA 591
Cdd:PRK08315 445 IVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---DVRDFCRGKIAHYK 521
|
570 580
....*....|....*....|....*...
gi 258583962 592 TPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK08315 522 IPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
104-612 |
1.50e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 89.04 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 104 QDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLV 183
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEgvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaEDPLFILY 263
Cdd:cd05914 84 FVSDE-------------------------------------------------------------------DDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVLHTTGGYLVYATMTFKYVFdYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEGVPN-------- 335
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSakiialaf 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 336 YPTTARMS-----EVVDKHKVNILYTAPTA--IRALMAK-GDEAIKGTSRDSL--------RIMGSVGEPINPEAwEWYY 399
Cdd:cd05914 176 AQVTPTLGvpvplVIEKIFKMDIIPKLTLKkfKFKLAKKiNNRKIRKLAFKKVheafggniKEFVIGGAKINPDV-EEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 400 RTIGnekSPIVDTWWQTETGGILITPLPGATALkpGSATRPFFGVQPALVDNMGEIVEGAtegnlvLLDSWPGQMRTVYG 479
Cdd:cd05914 255 RTIG---FPYTIGYGMTETAPIISYSPPNRIRL--GSAGKVIDGVEVRIDSPDPATGEGE------IIVRGPNVMKGYYK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 480 DHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDV-LNVSGHRMGTAEIESALVAFSKIAEAAVVgVPHDiKGQA 558
Cdd:cd05914 324 NPEATAEAF--DKDGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVV-VQEK-KLVA 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 559 IyAYItlndgvYPSAELHKE---------VKDWVRKEIGAiATP------DVLHWTDALPKTRSDKIMR 612
Cdd:cd05914 400 L-AYI------DPDFLDVKAlkqrniidaIKWEVRDKVNQ-KVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
237-621 |
1.69e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 237 WHEATAKVSDQCQPEEMKAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYATMTFKYVfDYQPGEVFWCTADVGW-ITGHS 314
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTASQSFdISVWQ 3927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 YLVyGPLSnGAKTilfEGVPN---YPTTARMSEVVDKhKVNILYTAPTAIRALMAKGDEAIkgtsrDSLRIMGSVGEPIN 391
Cdd:PRK05691 3928 FLA-APLF-GARV---EIVPNaiaHDPQGLLAHVQAQ-GITVLESVPSLIQGMLAEDRQAL-----DGLRWMLPTGEAMP 3996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 PE-AWEWY--YRTIG--NEKSPI----------VDtwwQTETGGiliTPLPGATalkPGSATRPFfgvqpaLVDNMGEIV 456
Cdd:PRK05691 3997 PElARQWLqrYPQIGlvNAYGPAecsddvaffrVD---LASTRG---SYLPIGS---PTDNNRLY------LLDEALELV 4061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 457 EGATEGNLVLLDSWPGqmRTVYGDHDRFEQTYFSTFKG-----MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAE 531
Cdd:PRK05691 4062 PLGAVGELCVAGTGVG--RGYVGDPLRTALAFVPHPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGE 4139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 532 IESALVAFSKIAEAAvVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIM 611
Cdd:PRK05691 4140 IEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
410
....*....|
gi 258583962 612 RRILRKIATG 621
Cdd:PRK05691 4219 RKALPALDIG 4228
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
3.43e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITAdegvrggRAVPlkknvdEALtnPEVKNISKVMVLKRtggnvawheHRDIWwheat 241
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQ-------SHLL------ERL--PQAEGVSAIALDSL---------HLDSW----- 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGY---LVYATMTFKY------------VFDYQPGEVFWctad 306
Cdd:PRK05691 1262 ---PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQATYALddsdvlmqkapiSFDVSVWECFW---- 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 307 vgwitghsylvygPLSNGAKTILfEGVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMakgDEAIKGTSRdSLRIMGSV 386
Cdd:PRK05691 1335 -------------PLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI---DEPLAAACT-SLRRLFSG 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 387 GEPINPE----------AWEWYYRtIGNEKSPIVDTWWQTETGGILITPLpgatalkpgsaTRPFFGVQPALVDNMGEIV 456
Cdd:PRK05691 1397 GEALPAElrnrvlqrlpQVQLHNR-YGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLL 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 457 EGATEGNLVLldSWPGQMRTVYG----DHDRF-EQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAE 531
Cdd:PRK05691 1465 PPGVAGELCI--GGAGLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 532 IESALVAFSKIAEAAVVgVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIM 611
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618
|
....
gi 258583962 612 RRIL 615
Cdd:PRK05691 1619 RRAL 1622
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
91-617 |
4.57e-18 |
|
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: 87.87 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWeGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd05915 9 GRKEVVS-RLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEGVR-GGRAVPLKKNVDEaltNPEVKNISKVMVLKRTGGNVAWHEHRDIwwheatakvsDQCq 249
Cdd:cd05915 88 IAYILNHAEDKVLLFDPNLLPlVEAIRGELKTVQH---FVVMDEKAPEGYLAYEEALGEEADPVRV----------PER- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 peemkaeDPLFILYTSGSTGKPKGVLHT-TGGYLVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYlVYGPLSNGAKTI 328
Cdd:cd05915 154 -------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCL-PYAATLVGAKQV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 329 LFEGVPNYPTtarMSEVVDKHKVNILYTAPTAIRaLMAKGDEAIKGTSRDSLRIMGSVGEPinPEAWeWYYRTIGNEKsp 408
Cdd:cd05915 226 LPGPRLDPAS---LVELFDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVE-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 409 IVDTWWQTETGGI----LITP----LPGATALK------------------PGSATRPFFGVQPALVdnmgeivegATEG 462
Cdd:cd05915 297 VRQGYGLTETSPVvvqnFVKShlesLSEEEKLTlkaktglpiplvrlrvadEEGRPVPKDGKALGEV---------QLKG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 463 NLVlldswpgqMRTVYGDHDRFEQTYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKI 542
Cdd:cd05915 368 PWI--------TGGYYGNEEATRSALTP--DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 543 AEAAVVGVPHDIKGQAIYAYITLNDgvypSAELHKEVKDWVRKEIGAIAT-PDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05915 438 KEAAVVAIPHPKWQERPLAVVVPRG----EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-615 |
8.26e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.29 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTI 161
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGE------QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 162 VFGGFSPEALAGRIIDSNAKLVITadegvrggravplkknvdEALTNPEVKNISKVMVLKRTGGNvAWHEHRDiwwheat 241
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLT------------------QSHLQARLPLPDGLRSLVLDQED-DWLEGYS------- 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 242 akvsdQCQPEEMKAEDPL-FILYTSGSTGKPKGVL--HTTGGYLVYATmtfkyvfdyqpGEVFWCTADVGWITGHSYL-- 316
Cdd:PRK12467 1708 -----DSNPAVNLAPQNLaYVIYTSGSTGRPKGAGnrHGALVNRLCAT-----------QEAYQLSAADVVLQFTSFAfd 1771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 -----VYGPLSNGAKTILfegVPnyPTTARMSE----VVDKHKVNILYTAPTAIRALMaKGDEAIKGTSrdSLRIMGSVG 387
Cdd:PRK12467 1772 vsvweLFWPLINGARLVI---AP--PGAHRDPEqliqLIERQQVTTLHFVPSMLQQLL-QMDEQVEHPL--SLRRVVCGG 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 388 EPINPEAWEWYYRTIGNekSPIVDTWWQTETgGILITPLPGATALKPGSATRPfFGVQPA-----LVDNMGEIVEGATEG 462
Cdd:PRK12467 1844 EALEVEALRPWLERLPD--TGLFNLYGPTET-AVDVTHWTCRRKDLEGRDSVP-IGQPIAnlstyILDASLNPVPIGVAG 1919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 463 NLVLldswpGQMRTVYGDH-------DRFEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIES 534
Cdd:PRK12467 1920 ELYL-----GGVGLARGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA 1994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 535 ALVAFSKIAEAAVvgVPHD-IKGQAIYAYITLNDGVYPSAE-----LHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSD 608
Cdd:PRK12467 1995 RLREQGGVREAVV--IAQDgANGKQLVAYVVPTDPGLVDDDeaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072
|
....*..
gi 258583962 609 KIMRRIL 615
Cdd:PRK12467 2073 KLDRKAL 2079
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
9.54e-18 |
|
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: 85.51 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 256 EDPLFILYTSGSTGKPKGVLHTTGGYLV-----YATMTFKYVFDYQPGEVFWCTADVGW------ITGHSYLVYGPLSNG 324
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRmlmggADFGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 325 AKTILFEGVPNYPTTArmSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGN 404
Cdd:cd05924 83 GQTVVLPDDRFDPEEV--WRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 405 ekSPIVDTWWQTETGGilitplpGATALKPGSA--TRPFFGVQP--ALVDNMGEIVEGATEGnlvllDSWPGQMRTV--- 477
Cdd:cd05924 161 --ITLVDAFGSSETGF-------TGSGHSAGSGpeTGPFTRANPdtVVLDDDGRVVPPGSGG-----VGWIARRGHIplg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 478 -YGDHDRFEQTYFSTFKGMY-FTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIK 555
Cdd:cd05924 227 yYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 258583962 556 GQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDK 609
Cdd:cd05924 307 GQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
1.72e-17 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 86.14 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLATRGDQVAIIWEGDDPTQDKTLTYKQLHQEVCRFSNALKEQGvRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 164 GGFSPEA---LAGRIIDSNAKLVITADEgvrggravplkknVDEALtnpevkniskvmvlKRTGGNVAWHEHRDIWWHEA 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAA-------------ALAAV--------------RAFAASRPAAGTPRLLVVDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 TA-KVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKyVFDYQPGEVFwctadVGWI-TGHSY-LV 317
Cdd:cd05931 133 LPdTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVV-----VSWLpLYHDMgLI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 318 YG---PLSNGAKTILFEgvpnyPTT-----ARMSEVVDKHKVNILYtAPT-----AIRALMAKGDEAIkgtsrD--SLRI 382
Cdd:cd05931 207 GGlltPLYSGGPSVLMS-----PAAflrrpLRWLRLISRYRATISA-APNfaydlCVRRVRDEDLEGL-----DlsSWRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 383 MGSVGEPINPEAWEWYYR--------------------------TIGNEKSPIVDTW-WQTETGGILITPLPGATALKPG 435
Cdd:cd05931 276 ALNGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVdRDALAGRAVAVAADDPAARELV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 436 SATRPFFGVQPALVD-NMGEIVEGATEGNLVLldSWPGQMRTVYGDHDRFEQTYF---STFKGMYF-TGD-GARRdeDGY 509
Cdd:cd05931 356 SCGRPLPDQEVRIVDpETGRELPDGEVGEIWV--RGPSVASGYWGRPEATAETFGalaATDEGGWLrTGDlGFLH--DGE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 510 YWITGRVDDVLNVSGHRMGTAEIESALVAFSK---IAEAAVVGVPHDIKGQ-AIYAYITLNDGVYPSAELHKEVKDWVRK 585
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIRAAVAR 511
|
570 580 590
....*....|....*....|....*....|..
gi 258583962 586 EIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05931 512 EHGVAPADVVLVRPGSIPRTSSGKIQRRACRA 543
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
105-615 |
1.78e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.02 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK10252 481 RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEgvrggravplkknvdealtnpevkniskvmVLKR-TGGNVAWHEHRDIWWHEATAKVSDQCQPeemkaEDPLFILY 263
Cdd:PRK10252 561 TTAD------------------------------QLPRfADVPDLTSLCYNAPLAPQGAAPLQLSQP-----HHTAYIIF 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 264 TSGSTGKPKGVL--HTT-GGYLVYatMTFKY--------------VFDYQPGEVFWctadvgwitghsylvygPLSNGAK 326
Cdd:PRK10252 606 TSGSTGRPKGVMvgQTAiVNRLLW--MQNHYpltaddvvlqktpcSFDVSVWEFFW-----------------PFIAGAK 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 TILFEgvpnyPTTAR----MSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTI 402
Cdd:PRK10252 667 LVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLT 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 403 G----NEKSPI---VD-TWWQTEtggilitplPGATALKPGSAT---RPFFGVQPALVDNMGEIVEGATEGNLVLldswP 471
Cdd:PRK10252 742 GaplhNLYGPTeaaVDvSWYPAF---------GEELAAVRGSSVpigYPVWNTGLRILDARMRPVPPGVAGDLYL----T 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 G-QMRTVY-GDHD----RFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEA 545
Cdd:PRK10252 809 GiQLAQGYlGRPDltasRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 546 AVV------GVPHDIKGQAIYAYITLNDGVYPSAELhkeVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK10252 889 VTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
2.05e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 85.96 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV-HTIVFGGFsPEALAGRIIDSNAKLVITaD 187
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLF-PEQIAWIINHAEDRVVIT-D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EGVrggraVPLKKNVDEALtnPEVKNI-----SKVMVLKRTGGNVAWHEhrdiWWHEATAKVSDQCQPEEMKAEdplfIL 262
Cdd:PRK06018 119 LTF-----VPILEKIADKL--PSVERYvvltdAAHMPQTTLKNAVAYEE----WIAEADGDFAWKTFDENTAAG----MC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 263 YTSGSTGKPKGVLHTTGGYLVYATMTFkyvfdyQPGEVFWCTADV-----------GWITGHSylvyGPlSNGAKTIL-- 329
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADTmlpvvplfhanSWGIAFS----AP-SMGTKLVMpg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 330 --FEGVPNYpttarmsEVVDKHKVNILYTAPTAIRAL---MAKgdEAIKGTSRDSLRIMGSVgepiNPEAWEWYYRTIGN 404
Cdd:PRK06018 253 akLDGASVY-------ELLDTEKVTFTAGVPTVWLMLlqyMEK--EGLKLPHLKMVVCGGSA----MPRSMIKAFEDMGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 405 EkspIVDTWWQTETggiliTPLPGATALKPGSAT--------------RPFFGVQPALVDNMGEIV--EGATEGNLVLld 468
Cdd:PRK06018 320 E---VRHAWGMTEM-----SPLGTLAALKPPFSKlpgdarldvlqkqgYPPFGVEMKITDDAGKELpwDGKTFGRLKV-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 469 SWPGQMRTVYgdhdRFEQTYFSTfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVV 548
Cdd:PRK06018 390 RGPAVAAAYY----RVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 549 GVPHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK06018 465 GVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
8.25e-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: 82.16 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGVLHTtggylvyatmtfkyvfDYQPGEVFWCTADVGWIT-GHSYLVYGP--------------LSNGA 325
Cdd:cd17638 5 IMFTSGTTGRSKGVMCA----------------HRQTLRAAAAWADCADLTeDDRYLIINPffhtfgykagivacLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 326 kTILFEGVPNYPTTARMsevVDKHKVNILYTAPTAIRALMakGDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNE 405
Cdd:cd17638 69 -TVVPVAVFDVDAILEA---IERERITVLPGPPTLFQSLL--DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 406 KspIVDTWWQTETG-GILITPLPGATALKPGSAtRPFFGVQPALVDNmGEIVEGATEGNLVLLDSWPGQMRTVYGDhdrf 484
Cdd:cd17638 143 T--VLTAYGLTEAGvATMCRPGDDAETVATTCG-RACPGFEVRIADD-GEVLVRGYNVMQGYLDDPEATAEAIDAD---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 485 eqtyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYIT 564
Cdd:cd17638 215 ---------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVV 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 258583962 565 LNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMR 612
Cdd:cd17638 286 ARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
8.75e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 83.92 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 237 WHEATAKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-TMTFKYvfDYQPGEVFWCTADVGwitgHSY 315
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 316 LVY---GP-LSNGAKTILfegVPNYPTTARMSEVVDKHKVNILYTApTAIRALMA---KGDEAikgtsRDSLRImgSVGE 388
Cdd:PRK13388 205 AVMagwAPaVASGAAVAL---PAKFSASGFLDDVRRYGATYFNYVG-KPLAYILAtpeRPDDA-----DNPLRV--AFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 PINPEAWEWYYRTIGNEkspIVDTWWQTETGGIlITPLPGAtalKPGSATRPFFGVQ-----------PALVDNMGEIVE 457
Cdd:PRK13388 274 EASPRDIAEFSRRFGCQ---VEDGYGSSEGAVI-VVREPGT---PPGSIGRGAPGVAiynpetltecaVARFDAHGALLN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 458 GATE-GNLVllDSWPGQMRTVY-----GDHDRFEQtyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAE 531
Cdd:PRK13388 347 ADEAiGELV--NTAGAGFFEGYynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAP 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 532 IESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGV-YPSAELHKEVKDwvRKEIGAIATPDVLHWTDALPKTRSDKI 610
Cdd:PRK13388 418 IERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAtFDPDAFAAFLAA--QPDLGTKAWPRYVRIAADLPSTATNKV 495
|
....*.
gi 258583962 611 MRRILR 616
Cdd:PRK13388 496 LKRELI 501
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
247-549 |
2.41e-16 |
|
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: 82.13 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 247 QCQPEEMK----AEDPLFILYTSGSTGKPKGVLHTTGGYlVYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLS 322
Cdd:cd05932 124 QHPPLEERptrfPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 NG------------------AKTILFEGVPNYPTTARMSeVVDK---HKVNILYTAPTaIRALMAKgdEAIKGTSRDSLR 381
Cdd:cd05932 203 GGvlvafaesldtfvedvqrARPTLFFSVPRLWTKFQQG-VQDKipqQKLNLLLKIPV-VNSLVKR--KVLKGLGLDQCR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 382 IMGSVGEPINPEAWEWYyRTIGnekSPIVDTWWQTETGGILITPLPGATalKPGSATRPFFGVQPALVDNmGEIvegate 461
Cdd:cd05932 279 LAGCGSAPVPPALLEWY-RSLG---LNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRISED-GEI------ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 462 gnlvLLDSwPGQMRTVYGDHDRFEQTYfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVS-GHRMGTAEIESALVAFS 540
Cdd:cd05932 346 ----LVRS-PALMMGYYKDPEATAEAF--TADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHD 418
|
....*....
gi 258583962 541 KIAEAAVVG 549
Cdd:cd05932 419 RVEMVCVIG 427
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
106-616 |
3.54e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.12 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNAL-KEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK-LV 183
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITAD-----EGV---RGGRAV----------PLKKnvdeALTNPEVKNISKvMVlkrtggnVAWHEHRDIWWHEATAKVS 245
Cdd:PRK05677 128 CLANmahlaEKVlpkTGVKHVivtevadmlpPLKR----LLINAVVKHVKK-MV-------PAYHLPQAVKFNDALAKGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 246 DQ-CQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPG---EVFWCTADVGWITGHSYLVYGPL 321
Cdd:PRK05677 196 GQpVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRN-LVANMLQCRALMGSNLNegcEILIAPLPLYHIYAFTFHCMAMM 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTILfegVPNYPTTARMSEVVDKHKvnilYTAPTAIRALMAK--GDEAIKGTSRDSLRIMGSVGEPINPEAWEWYY 399
Cdd:PRK05677 275 LIGNHNIL---ISNPRDLPAMVKELGKWK----FSGFVGLNTLFVAlcNNEAFRKLDFSALKLTLSGGMALQLATAERWK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 400 RTIGnekSPIVDTWWQTETGGIL-ITPlpgATALKPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLldSWPGQMRTVY 478
Cdd:PRK05677 348 EVTG---CAICEGYGMTETSPVVsVNP---SQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV--KGPQVMKGYW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 479 GDHDRFEQTYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQA 558
Cdd:PRK05677 420 QRPEATDEILDS--DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 559 IYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK05677 498 IKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
91-616 |
7.14e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 80.87 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALK-EQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPE 169
Cdd:PRK08974 38 DQPAFINMG------EVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 170 ALAGRIIDSNAKLVItadegVRGGRAVPLKKNVDEA--------------------LTNPEVKNISKvMVLKrtggnvaW 229
Cdd:PRK08974 112 ELEHQLNDSGAKAIV-----IVSNFAHTLEKVVFKTpvkhviltrmgdqlstakgtLVNFVVKYIKR-LVPK-------Y 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 230 HEHRDIWWHEATAKVSD-QCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVyatmtfkyvfdyqpgEVFWCTAdvg 308
Cdd:PRK08974 179 HLPDAISFRSALHKGRRmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLA---------------NLEQAKA--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 309 witghsylVYGPLSNGAKTILFEGVPNYPTTARMSE---VVDKHKVNILYTAPTAIRALmakgdeaIKGTSRDSLRIMGS 385
Cdd:PRK08974 241 --------AYGPLLHPGKELVVTALPLYHIFALTVNcllFIELGGQNLLITNPRDIPGF-------VKELKKYPFTAITG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 386 VGEPINpeAWewyyrtIGNEKSPIVD-------------------TWWQTETGGILI--------TPL----PGATALKP 434
Cdd:PRK08974 306 VNTLFN--AL------LNNEEFQELDfsslklsvgggmavqqavaERWVKLTGQYLLegygltecSPLvsvnPYDLDYYS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 435 GSATRPFFGVQPALVDNMGEIVEGATEGNLvlldsW---PGQMRtvyGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYW 511
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGEL-----WvkgPQVML---GYWQRPEATDEVIKDGWLATGDIAVMDEEGFLR 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 512 ITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDgvypsAELHK-EVKDWVRKEIGAI 590
Cdd:PRK08974 450 IVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----PSLTEeELITHCRRHLTGY 524
|
570 580
....*....|....*....|....*.
gi 258583962 591 ATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK08974 525 KVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
103-617 |
7.53e-16 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 80.55 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 103 TQDKTLTYKQLHQEVCRFSNALK-EQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK 181
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 182 LVItadegvrggravplkknVDEaltnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaEDPLFI 261
Cdd:cd05937 81 FVI-----------------VDP---------------------------------------------------DDPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 262 LYTSGSTGKPKGVLHTTGGYLVYATMtFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILfegVPNYPTTAR 341
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLVTSNL-LSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL---SRKFSASQF 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 MSEVVDKHKVNILYTAPTaIRALMAKGDEaiKGTSRDSLRIMgsVGEPINPEAW-------------EWYYRTIGneksp 408
Cdd:cd05937 169 WKDVRDSGATIIQYVGEL-CRYLLSTPPS--PYDRDHKVRVA--WGNGLRPDIWerfrerfnvpeigEFYAATEG----- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 409 iVDTWWQTETGGILItplpGATALKpGSATRPFFGVQPALV------------DNMGEIVEGA--TEGNLVL------LD 468
Cdd:cd05937 239 -VFALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVkmdpetddpirdPKTGFCVRAPvgEPGEMLGrvpfknRE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 469 SWPGQMRTVYGDHDRFEQTYFStfKG-MYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAA 546
Cdd:cd05937 313 AFQGYLHNEDATESKLVRDVFR--KGdIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAN 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 547 VVGVP---HDikGQAIYAYITLNDGVYPSAELHK-EVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05937 391 VYGVKvpgHD--GRAGCAAITLEESSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
89-616 |
2.13e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 79.15 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 89 RGDQVAIiwEGDDPTqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSP 168
Cdd:PRK07514 15 DRDAPFI--ETPDGL---RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 169 EALAGRIIDSNAKLVITADEGVRGGRAVPLKKNVDEALTnpevkniskvMVLKRTGGNVawhehrdiwwhEATAKVSDQC 248
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVET----------LDADGTGSLL-----------EAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 249 QPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAtMTFKYVFDYQPGEVFWctadvgwitgHSYLVY---------- 318
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNA-LTLVDYWRFTPDDVLI----------HALPIFhthglfvatn 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 GPLSNGAKTILF---------EGVPNypTTARMSevvdkhkVNILYTaptaiRALMAKG--DEAikgTSRDSLRIMGSVg 387
Cdd:PRK07514 218 VALLAGASMIFLpkfdpdavlALMPR--ATVMMG-------VPTFYT-----RLLQEPRltREA---AAHMRLFISGSA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 388 ePINPEAW-EWYYRTiGNeksPIVDTWWQTETGGILITPLPGATalKPGSATRPFFGVQPALVDN-------MGEIveGA 459
Cdd:PRK07514 280 -PLLAETHrEFQERT-GH---AILERYGMTETNMNTSNPYDGER--RAGTVGFPLPGVSLRVTDPetgaelpPGEI--GM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 460 TE--GNLVLLDSWpgQMRtvygdhdrfEQTY--FsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESA 535
Cdd:PRK07514 351 IEvkGPNVFKGYW--RMP---------EKTAeeF-RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGE 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 536 LVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPS-AELHKEVKDwvrkEIGAIATPDVLHWTDALPKTRSDKIMRRI 614
Cdd:PRK07514 419 IDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDeAAILAALKG----RLARFKQPKRVFFVDELPRNTMGKVQKNL 494
|
..
gi 258583962 615 LR 616
Cdd:PRK07514 495 LR 496
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
7.82e-15 |
|
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: 77.21 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG------QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 eemKAEDPLFILYTSGSTGKPKGVL--HTTggyLVYATMTFKYVFDYQPGEVFWCTADVGWiTGHSYLVYGPLSNGAKTI 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 329 LFEGVPNYpTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEaikgtsrdSLRIMGSVGEPINPEAWEWY--YRTIGNEK 406
Cdd:cd17645 175 VVPSERRL-DLDALNDYFNQEGITISFLPTGAAEQFMQLDNQ--------SLRVLLTGGDKLKKIERKGYklVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 407 SPIVDTWWQT--ETGGILITplpgatalKPGSATRPFF-----GVQPALVdnMGEIV---EGATEGNLvlldSWPGQMRt 476
Cdd:cd17645 246 NTVVATSFEIdkPYANIPIG--------KPIDNTRVYIldealQLQPIGV--AGELCiagEGLARGYL----NRPELTA- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 477 vygdhDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKG 556
Cdd:cd17645 311 -----EKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 557 QAIYAYITLndgvyPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17645 386 KYLVAYVTA-----PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-622 |
1.96e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.36 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 90 GDQVAIIWEGDDPTQdktLTYKQLHQEVCRFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtivfggFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAV-------FNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 169 --EALAG----RIIDSNAKLVITADEGvrggravpLKKNVDEALTN-PEVKNISKVMVLKRTGGNVAWHEHRDIWWHEA- 240
Cdd:PRK05620 94 lnKQLMNdqivHIINHAEDEVIVADPR--------LAEQLGEILKEcPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEAl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 241 ---TAKVSDQCQPEEmkaEDPLFILYTSGSTGKPKGVLHTTGG-YLVYATMTFKYVFDYQPGEVFWCTADVgwitgHSYL 316
Cdd:PRK05620 166 ldgRSTVYDWPELDE---TTAAAICYSTGTTGAPKGVVYSHRSlYLQSLSLRTTDSLAVTHGESFLCCVPI-----YHVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 317 VYG-PLS---NGAKTILfegvPNYPTTA-RMSEVVDKHKVNILYTAPTAIRALMAKgdEAIKGTSRDSLRIMGSVGEPIN 391
Cdd:PRK05620 238 SWGvPLAafmSGTPLVF----PGPDLSApTLAKIIATAMPRVAHGVPTLWIQLMVH--YLKNPPERMSLQEIYVGGSAVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 P---EAWEWYYRTigneksPIVDTWWQTETG--GILITPLPGATalkpGSATRPFFGVQ---PA----LVDNMGEIVEGA 459
Cdd:PRK05620 312 PiliKAWEERYGV------DVVHVWGMTETSpvGTVARPPSGVS----GEARWAYRVSQgrfPAsleyRIVNDGQVMEST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 460 --TEGNLVLLDSW------------PGQMRTVYGDHDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK05620 382 drNEGEIQVRGNWvtasyyhspteeGGGAASTFRGEDVEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 526 RMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKT 605
Cdd:PRK05620 462 WIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKT 541
|
570
....*....|....*...
gi 258583962 606 RSDKIMRRILRK-IATGD 622
Cdd:PRK05620 542 SVGKFDKKDLRQhLADGD 559
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-555 |
2.13e-14 |
|
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: 75.86 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtivfggfspealagriidsNAklvit 185
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV--------------------DV----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 adegVRGGRAvplkkNVDEA---LTNPEvkniSKVMVLKRTGGNVAwhehrdiwwheatakvsdqcqpeemkaedplFIL 262
Cdd:cd17640 59 ----VRGSDS-----SVEELlyiLNHSE----SVALVVENDSDDLA-------------------------------TII 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 263 YTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVFWCTADVgWitgHSYlvygplSNGAKTILF-EGVPNYPTTAR 341
Cdd:cd17640 95 YTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSY------ERSAEYFIFaCGCSQAYTSIR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 342 -MSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMG---SVGE---PIN-----PEAWEWYYRTIGnekSPI 409
Cdd:cd17640 164 tLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 410 VDTWWQTETGGILITPLPGATALkpGSATRPFFGVQPALVD-NMGEIVEGATEGnlVLLDSWPGQMRTVYGDHDRFEQTY 488
Cdd:cd17640 241 LNGYGLTETSPVVSARRLKCNVR--GSVGRPLPGTEIKIVDpEGNVVLPPGEKG--IVWVRGPQVMKGYYKNPEATSKVL 316
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 489 FStfKGMYFTGDGARRDEDGYYWITGRVDD--VLNvSGHRMGTAEIESALVAFSKIAEAAVVGvpHDIK 555
Cdd:cd17640 317 DS--DGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG--QDQK 380
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
91-615 |
2.15e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.19 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 91 DQVAIIwegDDptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEA 170
Cdd:PRK13383 50 GRTAII---DD---DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 171 LAGRIIDSNAKLVITADEGVRGGRAVplkknvDEAltnpevkniskVMVLKrtggnvawhehrdiwwhEATAKVSDqCQP 250
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAERIAGA------DDA-----------VAVID-----------------PATAGAEE-SGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 251 EEMKAEDPLFILYTSGSTGKPKGVLHT---TGGYLVYATMTFKYVFDyqpgevfwctadvgwiTGHSYLVYGPLSNGAK- 326
Cdd:PRK13383 169 RPAVAAPGRIVLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLR----------------TGSRISVAMPMFHGLGl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 -----TILFEGV----PNYPTTARMSEVvDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMGSVGEPINPEAWEW 397
Cdd:PRK13383 233 gmlmlTIALGGTvlthRHFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 398 YYRTIGNeksPIVDTWWQTETG-GILITPLPGATAlkPGSATRPFFGVQPALVDNMGEIVEGATEGNLVLLDSWPGQMRT 476
Cdd:PRK13383 312 FMDTYGD---ILYNGYGSTEVGiGALATPADLRDA--PETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 477 VYGDHdrfeqtyfSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKG 556
Cdd:PRK13383 387 DGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 557 QAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK13383 459 HRLAAFVVLHPGSGVDAA---QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
2.50e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.14 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 70 FEDGTLNISANC--------IDRHLATRGDQVAIIWEgddptqDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 142 VPEAAVAMLACTRIGAV-HTIVFGgFSPEALAGRIIDSNAKLVITADEGVRGGRAV--------PLKKNVD--EALTNPE 210
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVlNTLNTR-LDAASIAFMLRHGEAKVLIVDTEFAEVAREAlallpgpkPLVIDVDdpEYPGGRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 211 VKNISKVMVLKRTGGNVAWHEHRDIWwheatakvsdqcqpeemkaeDPLFILYTSGSTGKPKGVL-HTTGGYL------V 283
Cdd:PRK08162 157 IGALDYEAFLASGDPDFAWTLPADEW--------------------DAIALNYTSGTTGNPKGVVyHHRGAYLnalsniL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 284 YATMTFKYVFDYQ-PgeVFWCTadvGWitGHSYLVygpLSNGAKTILFEGVpnypTTARMSEVVDKHKVNILYTAPTAIR 362
Cdd:PRK08162 217 AWGMPKHPVYLWTlP--MFHCN---GW--CFPWTV---AARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 363 ALmAKGDEAIKGTSRDSLRIMGSVGEPinPEAWEWYYRTIGNEKS----------PIVDTWWQTETG------------- 419
Cdd:PRK08162 283 AL-INAPAEWRAGIDHPVHAMVAGAAP--PAAVIAKMEEIGFDLThvygltetygPATVCAWQPEWDalplderaqlkar 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 420 -GILITPLPGATALKPGSatrpffgVQPALVDN--MGEIVegaTEGNLVlldswpgqMRTVYGDHDRFEQTyfstFKGMY 496
Cdd:PRK08162 360 qGVRYPLQEGVTVLDPDT-------MQPVPADGetIGEIM---FRGNIV--------MKGYLKNPKATEEA----FAGGW 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 497 F-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAEl 575
Cdd:PRK08162 418 FhTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE- 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 258583962 576 hkEVKDWVRKEIGAIATPDVLHWTdALPKTRSDKIMRRILRKIA 619
Cdd:PRK08162 497 --EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
105-616 |
2.66e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 75.83 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGVRGGRAVPLKKNVDE--------------ALTNPEVKNISKvMVlkrtggnVAWHEHRDIWWHEATAKVSDQC-Q 249
Cdd:PRK07059 126 VLENFATTVQQVLAKTAVKHvvvasmgdllgfkgHIVNFVVRRVKK-MV-------PAWSLPGHVRFNDALAEGARQTfK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 250 PEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLV-----YATMTFKYVFDYQPGEVFWCTA----DVGWITGHSYLvygP 320
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmEAWLQPAFEKKPRPDQLNFVCAlplyHIFALTVCGLL---G 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 321 LSNGAKTILfegVPNYPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSRDSLRIMG--SVGEPInpeAWEWY 398
Cdd:PRK07059 275 MRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGgmAVQRPV---AERWL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 399 YRTigneKSPIVDTWWQTETGGILITPLPGATALKpGSATRPFFGVQPALVDN------MGEIVEGATEGNLVLLDSWpg 472
Cdd:PRK07059 349 EMT----GCPITEGYGLSETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRDDdgndlpLGEPGEICIRGPQVMAGYW-- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 473 qmrtvygdhDRFEQTYFSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVP 551
Cdd:PRK07059 422 ---------NRPDETAKVMTADGFFrTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 552 HDIKGQAIYAYITLNDgvypSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK07059 493 DEHSGEAVKLFVVKKD----PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-549 |
4.32e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 75.54 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 ADEgvrggravplkKNVDEALT-NPEVKNISKVMVLKRTGgnvaWHEHRD---IWWHEATAK--VSDQCQPE-------E 252
Cdd:cd17641 90 EDE-----------EQVDKLLEiADRIPSVRYVIYCDPRG----MRKYDDprlISFEDVVALgrALDRRDPGlyerevaA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 253 MKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKyvFDYQ-PGEVFWCTADVGWITGHSYLVYGPLSNG------- 324
Cdd:cd17641 155 GKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPLgPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 325 -AKTI---LFEGVPNY----PTT---------ARMSEV------VDKHKVNILYTA----------PTAIRALMAKGDEA 371
Cdd:cd17641 233 ePETMmedLREIGPTFvllpPRVwegiaadvrARMMDAtpfkrfMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 372 IKGTSRDSL-----RIMGSVGEPINPEAWEwYYRTIGnekSPIVDTWWQTETGGIlITPLPGATAlKPGSATRPFFGVQp 446
Cdd:cd17641 313 LFRPLRDRLgfsrlRSAATGGAALGPDTFR-FFHAIG---VPLKQLYGQTELAGA-YTVHRDGDV-DPDTVGVPFPGTE- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 447 ALVDNMGEIVEGAtegnlvlldswPGQMRTVYGDhdrfEQTYFSTFK--GMYFTGDGARRDEDGYYWITGRVDDVLNVS- 523
Cdd:cd17641 386 VRIDEVGEILVRS-----------PGVFVGYYKN----PEATAEDFDedGWLHTGDAGYFKENGHLVVIDRAKDVGTTSd 450
|
490 500
....*....|....*....|....*.
gi 258583962 524 GHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
109-619 |
4.94e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.27 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT--- 185
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVdqe 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 ----ADEGVR-------GGRAVPLKKNVDEALTNPEVKN-------ISKVMVLKRTGGNVAWHEHRDIWwheatakvsdq 247
Cdd:PLN02479 127 fftlAEEALKilaekkkSSFKPPLLIVIGDPTCDPKSLQyalgkgaIEYEKFLETGDPEFAWKPPADEW----------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 248 cqpeemkaeDPLFILYTSGSTGKPKGV-LHTTGGYLvyATMTFKYVFDYQPGEVF-----------WC-TADVGWITGHS 314
Cdd:PLN02479 196 ---------QSIALGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMNEGAVYlwtlpmfhcngWCfTWTLAALCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 315 YLvygpLSNGAKTILFEGVPNYPTTARMSEVVdkhKVNILYTAPTAIRAL--------MAKG----DEAIKGTSRDSLRI 382
Cdd:PLN02479 265 IC----LRQVTAKAIYSAIANYGVTHFCAAPV---VLNTIVNAPKSETILplprvvhvMTAGaappPSVLFAMSEKGFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 383 MGSVG--EPINPE---AW--EWyyrtignEKSPIVDTWWQTETGGILITPLPGATALKPGSaTRPFfgvqPALVDNMGEI 455
Cdd:PLN02479 338 THTYGlsETYGPStvcAWkpEW-------DSLPPEEQARLNARQGVRYIGLEGLDVVDTKT-MKPV----PADGKTMGEI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 456 VegaTEGNLVLldswPGQMRTVYGDHDRFEQtyfstfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESA 535
Cdd:PLN02479 406 V---MRGNMVM----KGYLKNPKANEEAFAN-------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 536 LVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAE--LHKEVKDWVRKEIGAIATPDVLHWtDALPKTRSDKIMRR 613
Cdd:PLN02479 472 VYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKH 550
|
....*.
gi 258583962 614 ILRKIA 619
Cdd:PLN02479 551 VLRAKA 556
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-605 |
7.50e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 73.10 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYATMTfkyvfdyqpgevfwctADVGWITGHS-YLVYGPL------SNGAKTIL 329
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVL----------------AVLQAIDEGTvFLNSGPLfhigtlMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 330 FEGVPNY-PTT--ARMSEVVDKHKVNILYTAPTAIRALMakgdEAIKGTSRD--SLRIMgsvgepinPEAWEWyyrtigN 404
Cdd:cd17636 65 AGGTNVFvRRVdaEEVLELIEAERCTHAFLLPPTIDQIV----ELNADGLYDlsSLRSS--------PAAPEW------N 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 405 EKSPIVDTWW--------QTETGGILITPLPGATALkpGSATRPFFGVQPALVDNMGEIV------EGATEGNLVLLDSW 470
Cdd:cd17636 127 DMATVDTSPWgrkpggygQTEVMGLATFAALGGGAI--GGAGRPSPLVQVRILDEDGREVpdgevgEIVARGPTVMAGYW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 471 pgqmrtvygdhDRFEQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGV 550
Cdd:cd17636 205 -----------NRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 258583962 551 PHDIKGQAIYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKT 605
Cdd:cd17636 274 PDPRWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRT 325
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
107-619 |
1.35e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 73.70 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 107 TLTYKQLHQEVCRFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAK-LV- 183
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARaLVy 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ----------ITADEG------VRGGRAVPLKKNvdeALTNPEVKNISKvMVlkrtggnVAWHEHRDIWWHEATAKVSDQ 247
Cdd:PRK12492 129 lnmfgklvqeVLPDTGieylieAKMGDLLPAAKG---WLVNTVVDKVKK-MV-------PAYHLPQAVPFKQALRQGRGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 248 -CQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGyLVyATMTfkyvfdyqpgEVFWCTADVGwITGHsylvygPLSNGAK 326
Cdd:PRK12492 198 sLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN-LV-ANML----------QVRACLSQLG-PDGQ------PLMKEGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 TILFEGVPNYPTTARMSE-----VVDKHkvNILYTAP----------------------TAIRALMAKGDeaIKGTSRDS 379
Cdd:PRK12492 259 EVMIAPLPLYHIYAFTANcmcmmVSGNH--NVLITNPrdipgfikelgkwrfsallglnTLFVALMDHPG--FKDLDFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 380 LRIMGSVGEPINPEAWEWYYRTIGnekSPIVDTWWQTETGGILITPlPGATALKPGSATRPFFGVQPALVDNMGEIVEGA 459
Cdd:PRK12492 335 LKLTNSGGTALVKATAERWEQLTG---CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDGNELPLG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 460 TEGNLVLldSWPGQMRTVYGDHDRFEQTYFStfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAF 539
Cdd:PRK12492 411 ERGELCI--KGPQVMKGYWQQPEATAEALDA--EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAH 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 540 SKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELhkevKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK12492 487 PKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEEL----KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
108-621 |
1.50e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.51 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITAD 187
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EGVRGGRAVPLKKNVDEALTNPEVKNISKVMVLKRtggnvAWHEHRD----IWWHEATAKVSDQ--CQPEEmkaEDPLFI 261
Cdd:PLN03102 120 SFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKR-----PSSEELDyeclIQRGEPTPSLVARmfRIQDE---HDPISL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 262 LYTSGSTGKPKGVLHT-TGGYLVyatmTFKYVFDYQPG---------EVFWCTadvGWItghsyLVYGPLSNGAKTILFE 331
Cdd:PLN03102 192 NYTSGTTADPKGVVIShRGAYLS----TLSAIIGWEMGtcpvylwtlPMFHCN---GWT-----FTWGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 332 GVpnypTTARMSEVVDKHKVNILYTAPTAIRALMaKGDEAIKGTSRDSLRIMGSVGEPinPEAWEWYYRTIG-------- 403
Cdd:PLN03102 260 HV----TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGfqvmhayg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 404 --NEKSPIVDTWWQTETGGIlitPLPGATALKPGSATRpFFGVQPALVDNMGEIV----EGATEGNLVLLDSwpgqmrTV 477
Cdd:PLN03102 333 ltEATGPVLFCEWQDEWNRL---PENQQMELKARQGVS-ILGLADVDVKNKETQEsvprDGKTMGEIVIKGS------SI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 478 YGDHDRFEQTYFSTFK-GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKG 556
Cdd:PLN03102 403 MKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258583962 557 QAIYAYITLNDGVYPSAEL-------HKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIATG 621
Cdd:PLN03102 483 ETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-615 |
2.06e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.01 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 82 IDRHLATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIG----- 156
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGE------KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 157 -AVHtivfggfSPEALAGRIID-SNAKLVITADEgvrggravplkknvdealTNPEVKNISKVmvlkrTGGNVAwhehrD 234
Cdd:PRK04813 82 vDVS-------SPAERIEMIIEvAKPSLIIATEE------------------LPLEILGIPVI-----TLDELK-----D 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 235 IWWHEATAKVSDQcqpeeMKAEDPLFILYTSGSTGKPKGV--LHTTggyLVyatmTFkyvfdyqpgeVFWCTADVGWITG 312
Cdd:PRK04813 127 IFATGNPYDFDHA-----VKGDDNYYIIFTSGTTGKPKGVqiSHDN---LV----SF----------TNWMLEDFALPEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 313 HSYLVYGPLSngaktilFE-GVPN-YPTTARMSE--VVDKHKVN---ILYTAPTAIR----------ALMAKGDEAIKGT 375
Cdd:PRK04813 185 PQFLNQAPYS-------FDlSVMDlYPTLASGGTlvALPKDMTAnfkQLFETLPQLPinvwvstpsfADMCLLDPSFNEE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 376 SRDSLRIMGSVGEPI-NPEAWEWYYRTignEKSPIVDTWWQTET----GGILIT--------PLP-GATalKPGSATrpf 441
Cdd:PRK04813 258 HLPNLTHFLFCGEELpHKTAKKLLERF---PSATIYNTYGPTEAtvavTSIEITdemldqykRLPiGYA--KPDSPL--- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 442 fgvqpALVDNMGEIVEGATEGNLVLldSWPGQMRTVYGDHDRFEQTYFsTFKGM--YFTGDGARRDeDGYYWITGRVDDV 519
Cdd:PRK04813 330 -----LIIDEEGTKLPDGEQGEIVI--SGPSVSKGYLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQ 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 520 LNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPS-AELHKEVKDWVRKEIGAIATPDVLHW 598
Cdd:PRK04813 401 IKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEReFELTKAIKKELKERLMEYMIPRKFIY 480
|
570
....*....|....*..
gi 258583962 599 TDALPKTRSDKIMRRIL 615
Cdd:PRK04813 481 RDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
260-615 |
3.55e-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: 72.05 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 260 FILYTSGSTGKPKGVLHTTGGYL----------------VYATMTF-KYVFDYqpgevFWCTADVGWITGHSYLVYGPls 322
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGSVVnlrtslseryfgrdngDEAVLFFsNYVFDF-----FVEQMTLALLNGQKLVVPPD-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 323 ngaktilfEGVPNYPttaRMSEVVDKHKVNILYTAPTAIralmakgdEAIKGTSRDSLRIMGSVGEPINPEAWEwyyRTI 402
Cdd:cd17648 171 --------EMRFDPD---RFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFE---KLR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 403 GNEKSPIVDTWWQTETG-GILITPLPGATALKpGSATRPFFGVQP-ALVDNMGEIVEGATeGNLVL--LDSWPGQMRTVY 478
Cdd:cd17648 229 SRFAGLIINAYGPTETTvTNHKRFFPGDQRFD-KSLGRPVRNTKCyVLNDAMKRVPVGAV-GELYLggDGVARGYLNRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 479 GDHDRFEQTYFST--------FKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGV 550
Cdd:cd17648 307 LTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 551 PHDIKGQA-----IYAYITLNDGVYPSAELhkevKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17648 387 EDASQAQSriqkyLVGYYLPEPGHVPESDL----LSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
249-615 |
1.28e-12 |
|
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: 70.54 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 249 QPEEMkaedpLFILYTSGSTGKPKGVL--------HTTGGYLVYATMTFKYV-------FDYQPGEVFwctadVGWITGH 313
Cdd:cd17644 104 QPENL-----AYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 314 SYLVygplsngaktilfegVPN--YPTTARMSEVVDKHKVNILYTAPTAIRALMAKGDEAiKGTSRDSLRIMGSVGEPIN 391
Cdd:cd17644 174 TLVL---------------RPEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLS-TIDLPSSLRLVIVGGEAVQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 392 PEAWEWYYRTIGNeKSPIVDTWWQTE----TGGILITPLPGATALKPgSATRPFFGVQPALVDNMGEIVEGATEGNLVLl 467
Cdd:cd17644 238 PELVRQWQKNVGN-FIQLINVYGPTEatiaATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHI- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 468 dswpGQMRTVYGDHDRFEQT---------YFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVA 538
Cdd:cd17644 315 ----GGVGLARGYLNRPELTaekfishpfNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQ 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 539 FSKIAEAAVVgVPHDIKGQA-IYAYITlndGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:cd17644 391 HNDVKTAVVI-VREDQPGNKrLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
106-619 |
5.03e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.18 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKeQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVhtIVFGGF--SPEALAGRIIDSNAKLV 183
Cdd:PRK08633 640 GELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGKV--PVNLNYtaSEAALKSAIEQAQIKTV 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEGVRggrAVPLKKNVDEALTNPEV-------KNISKVmvlkrtggnvawhehrDIWWHEATAKVSDQC-----QPE 251
Cdd:PRK08633 717 ITSRKFLE---KLKNKGFDLELPENVKViyledlkAKISKV----------------DKLTALLAARLLPARllkrlYGP 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 252 EMKAEDPLFILYTSGSTGKPKGVLHTtgGYLVYATMTfkyvfdyQPGEVFWCTA-DVgwITG-----HS--YLV--YGPL 321
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLS--HHNILSNIE-------QISDVFNLRNdDV--ILSslpffHSfgLTVtlWLPL 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 322 SNGAKTILfegVPNyPTTARMS-EVVDKHKVNILYTAPTAIRALMAkgDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYR 400
Cdd:PRK08633 847 LEGIKVVY---HPD-PTDALGIaKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 401 TIGNEkspIVDTWWQTETGGILITPLPGA--------TALKPGSATRPFFGVQPALVD-NMGEIVEGATEGnLVLLdSWP 471
Cdd:PRK08633 921 KFGIR---ILEGYGATETSPVASVNLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDG-LILI-GGP 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 GQMRTVYGDHDRF-EQTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEA--AVV 548
Cdd:PRK08633 996 QVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVvfAVT 1075
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258583962 549 GVPHDIKGQAIYAYITLNDGvyPSAELHKEVKDwvrKEIGAIATPDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK08633 1076 AVPDEKKGEKLVVLHTCGAE--DVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
87-277 |
3.83e-11 |
|
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: 65.94 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 87 ATRGDQVAIIWEGDdptqdkTLTYKQLHQEVCRFSNALK-EQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGG 165
Cdd:cd17632 53 ATGRTTLRLLPRFE------TITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 166 FSPEALAG-------RIIDSNAKLVITADEGVRGGRAVPLKKNVDEAltnPEVKNISKVMVLKRT---GGNVAWHEHRDI 235
Cdd:cd17632 127 ASAAQLAPilaetepRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDHR---PEVDAHRAALESARErlaAVGIPVTTLTLI 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 258583962 236 WWHEATAKVSDQCQPEEmkAEDPL-FILYTSGSTGKPKGVLHT 277
Cdd:cd17632 204 AVRGRDLPPAPLFRPEP--DDDPLaLLIYTSGSTGTPKGAMYT 244
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
480-617 |
8.30e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.91 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 480 DHDRF-EQTYFSTfkgmyftgDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQA 558
Cdd:PRK07824 226 DPDPFaEPGWFRT--------DDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQR 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 258583962 559 IYAYITLNDGVYPSAElhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:PRK07824 298 VVAAVVGDGGPAPTLE---ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
494-619 |
1.23e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.24 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 494 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSA 573
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ 488
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 258583962 574 elhkeVKDWVRkEIGaIAT---PDVLHWTDALPKTRSDKIMRRILRKIA 619
Cdd:PRK10946 489 -----LRRFLR-EQG-IAEfklPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
87-615 |
1.28e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 87 ATRGDQVAIIWEGddptqdKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGF 166
Cdd:PRK05691 2199 ARTPQAPALTFAG------QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 167 SPEALAGRIIDSNAKLVITadegvrggravplkknvDEALTNpevkniskvmVLKRTGGNVA-WHEHRDIwwhEATAKVS 245
Cdd:PRK05691 2273 PLERLHYMIEDSGIGLLLS-----------------DRALFE----------ALGELPAGVArWCLEDDA---AALAAYS 2322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 246 DQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYLVYATMTFKyVFDYQPGEvfwCTADVGWIT--GHSYLVYGPLSN 323
Cdd:PRK05691 2323 DAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASERLLVPLLC 2398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 324 GAKTIL-FEGVPNyptTARMSEVVDKHKVNILYTAPTAIRAL---MAKGDEAIkgtsrdSLRIMGSVGEPINPEAWEWYY 399
Cdd:PRK05691 2399 GARVVLrAQGQWG---AEEICQLIREQQVSILGFTPSYGSQLaqwLAGQGEQL------PVRMCITGGEALTGEHLQRIR 2469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 400 RTIgnEKSPIVDTWWQTETggiLITPL--PGATALKPGSATRPFFGVQPALV-----DNMGEIVEGATeGNLVLldswpG 472
Cdd:PRK05691 2470 QAF--APQLFFNAYGPTET---VVMPLacLAPEQLEEGAASVPIGRVVGARVayildADLALVPQGAT-GELYV-----G 2538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 473 QMRTVYGDHDR-------FEQTYFSTFKG-MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAE 544
Cdd:PRK05691 2539 GAGLAQGYHDRpgltaerFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE 2618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258583962 545 AAVVGVPHDiKGQAIYAYI---TLNDGVYPSAELHKEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK05691 2619 AVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
78-551 |
2.49e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.38 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 78 SANcIDRHL----ATRGDQVAII----WEGDDPTQDKTLTYKQLHQEVCRFSNALKEQGVRKGD-VVCiympMV---PEA 145
Cdd:PRK09274 5 MAN-IARHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMrAVL----MVtpsLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 146 AVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITadegvrggravplkknvdealtnpevknISKVMVLKRT-G 224
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG----------------------------IPKAHLARRLfG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 225 GNVAWHEH-----RDIWWHEAT------AKVSDQCQPEEMKAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAtmtFKY 291
Cdd:PRK09274 132 WGKPSVRRlvtvgGRLLWGGTTlatllrDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEA---LRE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 292 VFDYQPGEVFWCTADVgwitghsYLVYGPlSNGAKTILFEGVPNYPTTA---RMSEVVDKHKVNILYTAPTAIRALmakG 368
Cdd:PRK09274 209 DYGIEPGEIDLPTFPL-------FALFGP-ALGMTSVIPDMDPTRPATVdpaKLFAAIERYGVTNLFGSPALLERL---G 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 369 DEAI-KGTSRDSLRIMGSVGEPINPEAWEwYYRTIGNEKSPIV---------------------DTWWQTETG-GILI-T 424
Cdd:PRK09274 278 RYGEaNGIKLPSLRRVISAGAPVPIAVIE-RFRAMLPPDAEILtpygatealpissiesreilfATRAATDNGaGICVgR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 425 PLPGAT----AL--KPGSAtrpFFGVQPALVDNMGEIVegaTEGNLVLldswpgqmrTVYgdHDRFEQTYFSTFK---GM 495
Cdd:PRK09274 357 PVDGVEvriiAIsdAPIPE---WDDALRLATGEIGEIV---VAGPMVT---------RSY--YNRPEATRLAKIPdgqGD 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 496 YF--TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVP 551
Cdd:PRK09274 420 VWhrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
105-568 |
8.42e-10 |
|
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: 61.22 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhehrdiwwheatakvsdqcqpeemkaeDPLFILYT 264
Cdd:cd05940 81 V-----------------------------------------------------------------------DAALYIYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYLvYATMTFKYVFDYQPGEVFWCTADVGWITGHSYLVYGPLSNGAKTILFEgvpNYPTTARMSE 344
Cdd:cd05940 90 SGTTGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRK---KFSASNFWDD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 345 VVdKHKVNILYTAPTAIRALMAKGDeaiKGTSRD-SLRIMgsVGEPINPEAWEWYYRTIGNEKspIVDTWWQTE--TGGI 421
Cdd:cd05940 166 IR-KYQATIFQYIGELCRYLLNQPP---KPTERKhKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFI 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 422 LITPLPGATALKPgSATRPFFGVQPALVD-NMGEIVEGAT-------EGNLVLLDSWPGQMRTVYGDHDRFEQT---YFS 490
Cdd:cd05940 238 NFFGKPGAIGRNP-SLLRKVAPLALVKYDlESGEPIRDAEgrcikvpRGEPGLLISRINPLEPFDGYTDPAATEkkiLRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 491 TFK--GMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVP---HDikGQAIYAYIT 564
Cdd:cd05940 317 VFKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GRAGMAAIV 394
|
....
gi 258583962 565 LNDG 568
Cdd:cd05940 395 LQPN 398
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-581 |
9.67e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 61.32 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 254 KAEDPLFILYTSGSTGKPKGVLHTTgGYLVYATMTFKYVFDYQPGEVFWCTADVgwitghsYLVYGPLSnGAKTILFEGV 333
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRH-GTFAAQIDALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 334 PNYPTTARMSEVVD---KHKVNILYTAPTAIRALMAKGdeAIKGTSRDSLRIMGSVGEPINPEAWEWYYRTIGNEkSPIV 410
Cdd:cd05910 154 PTRPARADPQKLVGairQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDE-AEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 411 DTWWQTETGGI-------LITPLPGATAlkPGSAT---RPFFGVQPALVdnmgEIVEG--ATEGNLVLLDSW-------P 471
Cdd:cd05910 231 TPYGATEALPVssigsreLLATTTAATS--GGAGTcvgRPIPGVRVRII----EIDDEpiAEWDDTLELPRGeigeitvT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 472 GQMRT-VYgdHDRFEQTYFSTFKG-----MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEA 545
Cdd:cd05910 305 GPTVTpTY--VNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 258583962 546 AVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVKD 581
Cdd:cd05910 383 ALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRA 418
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
79-568 |
2.12e-09 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 60.58 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 79 ANCIDRHLATRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAV 158
Cdd:PLN02860 10 CQCLTRLATLRGNAVVTI------SGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 159 HTIVFGGFSPEALAGRIIDSNAKLVITaDEGVR-------GGRAVPLKKNV--DEALTNPEVKNISKV---MVLKRTGG- 225
Cdd:PLN02860 84 VAPLNYRWSFEEAKSAMLLVRPVMLVT-DETCSswyeelqNDRLPSLMWQVflESPSSSVFIFLNSFLtteMLKQRALGt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 226 ---NVAWhehrdiwwheatakvsdqcqpeemKAEDPLFILYTSGSTGKPKGVL--HTTggyLVYATMTFKYVFDYQPGEV 300
Cdd:PLN02860 163 telDYAW------------------------APDDAVLICFTSGTTGRPKGVTisHSA---LIVQSLAKIAIVGYGEDDV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 301 FWCTADVGWITGHSylvygplsnGAKTILFEG-----VPNYPTTARMsEVVDKHKVNILYTAPTAIRALMAKGDEAIKGT 375
Cdd:PLN02860 216 YLHTAPLCHIGGLS---------SALAMLMVGachvlLPKFDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 376 SRDSLRIM----GSVGEPINPEAWEWYYR----------------TIGNEKSPIVDTWWQTETGGILI----TPLPGATA 431
Cdd:PLN02860 286 VFPSVRKIlnggGSLSSRLLPDAKKLFPNaklfsaygmteacsslTFMTLHDPTLESPKQTLQTVNQTksssVHQPQGVC 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 432 L-KPgsATRPFFGVQPALVDNMGEIVegaTEGNLVLLDSWpGQMRTVYGDhdrfeqtyfSTFKGMYFTGDGARRDEDGYY 510
Cdd:PLN02860 366 VgKP--APHVELKIGLDESSRVGRIL---TRGPHVMLGYW-GQNSETASV---------LSNDGWLDTGDIGWIDKAGNL 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 511 WITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDG 568
Cdd:PLN02860 431 WLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDG 488
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
106-279 |
2.42e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.38 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVIT 185
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 adegvrGGRAVPlkkNVDEALTNPEVKNiSKVMVLKRTGGNVAWHEHRDIWWHEATAKvsdqcqPEEMKAEDPL------ 259
Cdd:PTZ00216 200 ------NGKNVP---NLLRLMKSGGMPN-TTIIYLDSLPASVDTEGCRLVAWTDVVAK------GHSAGSHHPLnipenn 263
|
170 180
....*....|....*....|....
gi 258583962 260 ----FILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 264 ddlaLIMYTSGTTGDPKGVMHTHG 287
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
105-617 |
3.15e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 59.75 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVI 184
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TadegvrggravplkknvdealtnpevkniskvmvlkrtggnvawhEHRDIwWHEATAKVSDQCQPEEMKaeDPLFILYT 264
Cdd:cd05939 81 F---------------------------------------------NLLDP-LLTQSSTEPPSQDDVNFR--DKLFYIYT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 265 SGSTGKPKGVLHTTGGYLVYATMTFkYVFDYQPGEVFWCTAdvgwitghsylvygPLSNGAKTILfeGVPNypTTARMSE 344
Cdd:cd05939 113 SGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVVYDCL--------------PLYHSAGGIM--GVGQ--ALLHGST 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 345 VV--------------DKHKVNILYTAPTAIRALMA---KGDEaikgtSRDSLRIMgsVGEPINPEAWEWYYRTIGNEKs 407
Cdd:cd05939 174 VVirkkfsasnfwddcVKYNCTIVQYIGEICRYLLAqppSEEE-----QKHNVRLA--VGNGLRPQIWEQFVRRFGIPQ- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 408 pIVDTWWQTETGGIL--ITPLPGATALKP--GSATRPffgVQPALVD-NMGEIVEGaTEGNLVLLD-SWPGQMRTVYGDH 481
Cdd:cd05939 246 -IGEFYGATEGNSSLvnIDNHVGACGFNSriLPSVYP---IRLIKVDeDTGELIRD-SDGLCIPCQpGEPGLLVGKIIQN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 482 D---RFE----------QTYFSTFKG---MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEA 545
Cdd:cd05939 321 DplrRFDgyvnegatnkKIARDVFKKgdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 546 AVVGV--PHdIKGQAIYAYItlndgVYPSAE--LHKEVKDwVRKEIGAIATPDVLHWTDALPKTRSDKIMRRILRK 617
Cdd:cd05939 401 VVYGVevPG-VEGRAGMAAI-----VDPERKvdLDRFSAV-LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
490-625 |
1.38e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.70 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 490 STFKGMY----------FTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPHDIKGQAI 559
Cdd:PRK07445 310 SLALGYYpqildsqgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVV 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 560 YAYITLNDGVyPSAElhkEVKDWVRKEIGAIATPDvlHW--TDALPKTRSDKIMRRILRKIATGDTSN 625
Cdd:PRK07445 390 TAIYVPKDPS-ISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
263-616 |
6.25e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.48 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 263 YTSGSTGKPKG--------VLHTTGGYL--VYATMTFKYVFDYQPgeVFWCTAdvgWITGHSylvyGPLsNGAKTIL--- 329
Cdd:PRK07008 183 YTSGTTGNPKGalyshrstVLHAYGAALpdAMGLSARDAVLPVVP--MFHVNA---WGLPYS----APL-TGAKLVLpgp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 330 -FEGvpnypttARMSEVVDKHKVNILYTAPTAIRALMAKGDEAikGTSRDSLR---IMGSVGEPINPEAWEWYYrtiGNE 405
Cdd:PRK07008 253 dLDG-------KSLYELIEAERVTFSAGVPTVWLGLLNHMREA--GLRFSTLRrtvIGGSACPPAMIRTFEDEY---GVE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 406 kspIVDTWWQTEtggilITPLPGATALK------PGSAT--------RPFFGVQPALVDNMGEIV--EGATEGNLVLLDS 469
Cdd:PRK07008 321 ---VIHAWGMTE-----MSPLGTLCKLKwkhsqlPLDEQrkllekqgRVIYGVDMKIVGDDGRELpwDGKAFGDLQVRGP 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 470 WPGQmRTVYGDHDRFEQTYFSTfkgmyftGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVG 549
Cdd:PRK07008 393 WVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 550 VPHDIKGQAIYAYITLNdgvyPSAELHKEvkDWVRKEIGAIA---TPDVLHWTDALPKTRSDKIMRRILR 616
Cdd:PRK07008 465 CAHPKWDERPLLVVVKR----PGAEVTRE--ELLAFYEGKVAkwwIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
109-277 |
6.35e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 55.98 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 109 TYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACtrigAVHTIV----FGGFSPEALaGRIID-SNAKLV 183
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEAC----AAHSLIcvplYDTLGPGAV-DYIVDhAEIDFV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEGVRG------GRAVPLKKNVdeALTNP--EVKNISKVMVLKrtggNVAWHEhrdiWWHEATAKVSDQCQPeemKA 255
Cdd:PLN02430 153 FVQDKKIKEllepdcKSAKRLKAIV--SFTSVteEESDKASQIGVK----TYSWID----FLHMGKENPSETNPP---KP 219
|
170 180
....*....|....*....|..
gi 258583962 256 EDPLFILYTSGSTGKPKGVLHT 277
Cdd:PLN02430 220 LDICTIMYTSGTSGDPKGVVLT 241
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
84-289 |
1.96e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 53.72 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 84 RHLA-TRGDQVAIIwegddpTQDKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIV 162
Cdd:PRK09029 10 RHWAqVRPQAIALR------LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 163 FGGFsPEALAGRIIDSNaklvitadegvrggravplkkNVDEALTNPEVKNISKVMVL----KRTGGNVAWHEHRDiwwh 238
Cdd:PRK09029 84 NPQL-PQPLLEELLPSL---------------------TLDFALVLEGENTFSALTSLhlqlVEGAHAVAWQPQRL---- 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 258583962 239 eATakvsdqcqpeemkaedplFILyTSGSTGKPKGVLHTTGGYL-----VYATMTF 289
Cdd:PRK09029 138 -AT------------------MTL-TSGSTGLPKAAVHTAQAHLasaegVLSLMPF 173
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
108-283 |
3.58e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 53.31 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITAD 187
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EGVRGGRAVpLKKNVDEALTNPEVKNISKVMVLKRTGGNVAWHEhrdiwWHEATAKVSDQCQPEEMKAEDPLFILYTSGS 267
Cdd:PLN02861 158 SKISSILSC-LPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFS-----WEEFSLMGSLDCELPPKQKTDICTIMYTSGT 231
|
170
....*....|....*.
gi 258583962 268 TGKPKGVLHTTGGYLV 283
Cdd:PLN02861 232 TGEPKGVILTNRAIIA 247
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-288 |
1.07e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.04 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLVITAD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 188 EgvrggravPLKKNVDEALTNPEVKNI-------SKVMVLKRTGGNVAWHEHRDIwwhEATAKVSdQCQPEEMKAEDPLF 260
Cdd:PLN02387 187 K--------QLKKLIDISSQLETVKRViymddegVDSDSSLSGSSNWTVSSFSEV---EKLGKEN-PVDPDLPSPNDIAV 254
|
170 180 190
....*....|....*....|....*....|
gi 258583962 261 ILYTSGSTGKPKGVLHTTGGYL--VYATMT 288
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTHGNIVatVAGVMT 284
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-277 |
1.26e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 51.45 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 108 LTYKQLHQEVCRFSNALKEQGVR--KGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALagRIIDSNAKL-VI 184
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAI--EYILNHAEIsIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADEGVrggravplkknvdealtnpEVKNISKVMVLKRtggnvawhehrdiwwheatakvSDQCQPEEMKAEDPLFILYT 264
Cdd:cd05927 84 FCDAGV-------------------KVYSLEEFEKLGK----------------------KNKVPPPPPKPEDLATICYT 122
|
170
....*....|...
gi 258583962 265 SGSTGKPKGVLHT 277
Cdd:cd05927 123 SGTTGNPKGVMLT 135
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
106-288 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 106 KTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAgriidsnaklvit 185
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALI------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 186 adegvrggravplkknvdEALTNPEVKNISkvmvlkrtggnvawhehrdiwwheatakvsdqCQPeemKAEDPLFILYTS 265
Cdd:cd17639 71 ------------------HSLNETECSAIF--------------------------------TDG---KPDDLACIMYTS 97
|
170 180
....*....|....*....|...
gi 258583962 266 GSTGKPKGVLHTTGGylVYATMT 288
Cdd:cd17639 98 GSTGNPKGVMLTHGN--LVAGIA 118
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
255-615 |
4.58e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 49.26 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 255 AEDPLFILYTSGSTGKPKGVLHTtggYLVYATMTFKYVfdyqpgEVFWCTADVGWITG----HSY-LVYGPLS---NGAK 326
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRS---WTEIDREIEAYN------EALNCEQDETPIVAcpvtHSYgLICGVLAaltRGSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 -TILFEGVPNYpTTARMSEvvdkHKVNILYTAPTAIRAL--MAKGDEAIKgtsrdslRIMGSvGEPInPEAWewyYRTIG 403
Cdd:PRK08308 171 pVIITNKNPKF-ALNILRN----TPQHILYAVPLMLHILgrLLPGTFQFH-------AVMTS-GTPL-PEAW---FYKLR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 404 NEKSPIVDTWWQTETGGILIT-----------PLPGATaLKPGSATrpffgvqpalvDNMGEIVegategnlvlldSWPG 472
Cdd:PRK08308 234 ERTTYMMQQYGCSEAGCVSICpdmkshldlgnPLPHVS-VSAGSDE-----------NAPEEIV------------VKMG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 473 QmRTVYgdhdrfeqtyfstfkgmyfTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALVAFSKIAEAAVVGVPH 552
Cdd:PRK08308 290 D-KEIF-------------------TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 553 DIKGQAIYAYITLNDGVYPSaelhkEVKDWVRKEIGAIATPDVLHWTDALPKTRSDKIMRRIL 615
Cdd:PRK08308 350 PVAGERVKAKVISHEEIDPV-----QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
255-617 |
2.39e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 47.48 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 255 AEDPLFILYTSGSTGKPKGVLHTTGGyLVYATMTFKYVFDYQPGEVF--W--CTADVGWITGHsylvYGPLSNGAK---- 326
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNqylm 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 327 -TILFEGVPnyptTARMSEvVDKHKVNILYTAPTAIRALMAK-GDEAIKGTSRDSLRIMGSVGEPINPEAWEWYYR---- 400
Cdd:cd05908 180 pTRLFIRRP----ILWLKK-ASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmsk 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 401 -----------------TIG--------NEKSPIVDTWWQTETGGILITPLPGATALKPGSATRPFFGVQPALVDNMGEI 455
Cdd:cd05908 255 yglkrnailpvyglaeaSVGaslpkaqsPFKTITLGRRHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 456 VEGATEGNLVL--LDSWPGqmrtVYGDHDRFEQTYfsTFKGMYFTGD-GARRDEDGYywITGRVDDVLNVSGHRMGTAEI 532
Cdd:cd05908 335 LPDGYIGHIQIrgKNVTPG----YYNNPEATAKVF--TDDGWLKTGDlGFIRNGRLV--ITGREKDIIFVNGQNVYPHDI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 533 ESalVAFSKIAE----AAVVGVpHD--IKGQAIYAYITLNDGVYPSAELHKEVKD-------WVRKEIGAIATpdvlhwt 599
Cdd:cd05908 407 ER--IAEELEGVelgrVVACGV-NNsnTRNEEIFCFIEHRKSEDDFYPLGKKIKKhlnkrggWQINEVLPIRR------- 476
|
410
....*....|....*...
gi 258583962 600 daLPKTRSDKIMRRILRK 617
Cdd:cd05908 477 --IPKTTSGKVKRYELAQ 492
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
100-610 |
3.32e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 47.27 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 100 DDPTQdKTLTYKQLHQEVCRFSNALKEqGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVfgGFSpeALAGRIIDS- 178
Cdd:PRK06814 652 EDPVN-GPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSAc 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 179 ---NAKLVITADEGVRGGRAVPLKKNVDEALtnpevknisKVMVLKRTGGNVAWHEHRDIWWHEATAKVSdQCQPeemKA 255
Cdd:PRK06814 726 kaaQVKTVLTSRAFIEKARLGPLIEALEFGI---------RIIYLEDVRAQIGLADKIKGLLAGRFPLVY-FCNR---DP 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 256 EDPLFILYTSGSTGKPKGVL--HT---TGGYLVYATMTFK---YVFDYQPgeVFwctadvgwitgHSY-LVYG---PLSN 323
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVlsHRnllANRAQVAARIDFSpedKVFNALP--VF-----------HSFgLTGGlvlPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 324 GAKTILFEGVPNYPTtarMSEVVDKHKVNILYTAptairalmakgDEAIKGTSR-----D--SLRIMGSVGEPINPEAWE 396
Cdd:PRK06814 860 GVKVFLYPSPLHYRI---IPELIYDTNATILFGT-----------DTFLNGYARyahpyDfrSLRYVFAGAEKVKEETRQ 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 397 WYYRTIGNEkspIVDTWWQTETGGILI--TPLpgatALKPGSATRPFFGVQPALvdnmgEIVEGATEG--------NLVL 466
Cdd:PRK06814 926 TWMEKFGIR---ILEGYGVTETAPVIAlnTPM----HNKAGTVGRLLPGIEYRL-----EPVPGIDEGgrlfvrgpNVML 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 467 ldswpGQMRT----VY-----GDHDrfeqtyfstfkgmyfTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESALV 537
Cdd:PRK06814 994 -----GYLRAenpgVLeppadGWYD---------------TGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAA 1053
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 258583962 538 AFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVypSAELHKEVKdwvRKEIGAIATPDVLHWTDALPKTRSDKI 610
Cdd:PRK06814 1054 ELWPDALHAAVSIPDARKGERIILLTTASDAT--RAAFLAHAK---AAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
105-272 |
7.61e-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: 45.75 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQ-GVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVFGGFSPEALAGRIIDSNAKLV 183
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 184 ITADEgvrggravpLKKNVDEALtnPEVK-NISKVMVLKRTGgnvawHEHRDIWWHEATAKVSDQCQPEEMKAE----DP 258
Cdd:cd05938 83 VVAPE---------LQEAVEEVL--PALRaDGVSVWYLSHTS-----NTEGVISLLDKVDAASDEPVPASLRAHvtikSP 146
|
170
....*....|....
gi 258583962 259 LFILYTSGSTGKPK 272
Cdd:cd05938 147 ALYIYTSGTTGLPK 160
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
105-607 |
1.52e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.09 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 105 DKTLTYKQLHQEVCRFSNALKEQGVRKGDVVCIYMPMVPEAAVAMLACTRIGAVHTIVfggfSPEALAGRIIDSNAKLVI 184
Cdd:PRK07868 470 GRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM----PPDTDLAAAVRLGGVTEI 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 185 TADegvrggravplKKNVDEALTNPEvknisKVMVLkrtGGNvawhEHRDIwwH-EATAKVSD--QCQPEEMK------- 254
Cdd:PRK07868 546 ITD-----------PTNLEAARQLPG-----RVLVL---GGG----ESRDL--DlPDDADVIDmeKIDPDAVElpgwyrp 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 255 ----AEDPLFILYTsgstgkpkgvlhTTGGYLVYatmtfKYVFDYQpgevfWCTADVGWIT----GHSYLVY-------- 318
Cdd:PRK07868 601 npglARDLAFIAFS------------TAGGELVA-----KQITNYR-----WALSAFGTASaaalDRRDTVYcltplhhe 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 319 --------GPLSNGAKTILFEGV-PNypttaRMSEVVDKHKVNILYTAPTAIRALMAKGDEAIKGTSrdSLRI-MGSvGE 388
Cdd:PRK07868 659 sgllvslgGAVVGGSRIALSRGLdPD-----RFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNH--PVRLfIGS-GM 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 389 PInpEAWEwyyRTIGNEKSPIVDTWWQTETGGILITPLPGAtalKPGSATRPFFG---VQPALVD-NMGEIVEG------ 458
Cdd:PRK07868 731 PT--GLWE---RVVEAFAPAHVVEFFATTDGQAVLANVSGA---KIGSKGRPLPGagrVELAAYDpEHDLILEDdrgfvr 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583962 459 -ATEGNLVLL--------DSWPGQMRTVYGDHDrfeqTYFSTfkGMYFtgdgaRRDEDGYYWITGRVDDVLNVSGHRMGT 529
Cdd:PRK07868 803 rAEVNEVGVLlarargpiDPTASVKRGVFAPAD----TWIST--EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYT 871
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258583962 530 AEIESALVAFSKIAEAAVVGVPHDIKGQAIYAYITLNDGVYPSAELHKEVkdwvrKEIGAIATPDVLHWTDALPKTRS 607
Cdd:PRK07868 872 EPVTDALGRIGGVDLAVTYGVEVGGRQLAVAAVTLRPGAAITAADLTEAL-----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| |
