|
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 446000384 6 KHTIPANIADRCLINPQQYEAMYQQSINVPDTFWGEQGKILDWIKPYqkvkNTSFAPGNVSIKWYEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 86 LQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 166 FSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNvtSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQAS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 246 DQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 406 KCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 486 QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 566 NHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTsNLGDTSTLADPGVVEKLLEEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
gi 446000384 646 QAIA 649
Cdd:PRK00174 634 QNRK 637
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
18-644 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1208.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 18 LINPQQYEAMYQQSINVPDTFWGEQGK-ILDWIKPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQENGDRTAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 97 WEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 177 DSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNvTSVEHVVVLKRTGGKID-WQEGRDLWWHDLVEQASDQHQAEEMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCP-VSVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 WPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 416 TETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATE-GSLVITDSWPGQARTLFGDHERFEQTYFSTFKN 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEgGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLEE 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: 1191.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 22 QQYEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSFapGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK--GPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 102 ASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSR 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 182 LVITSDEGVRAGRSIPLKKNVDDALKNpnVTSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQHQAEEMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 262 LYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 342 MAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGF 421
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 422 MITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDG 501
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRN 581
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdTSNLGDTSTLAD 634
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG-EEELGDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
24-611 |
0e+00 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 1058.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 24 YEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDAS 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 104 QSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 184 ITSDEGVRAGRSIPLKKNVDDALkNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQHQAEEMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 264 TSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMA 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 344 QVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGFMI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 424 TPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 446000384 584 RKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
68-643 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 949.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 68 KWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGED-GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 148 AMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNpnVTSVEHVVVLKRTGGKI 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEE--LPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 228 DWQEgrDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 308 GWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPGaTELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVIT 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 468 DSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 548 VGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
gi 446000384 628 DTSTLADPGVVEKLLE 643
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-643 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 839.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 20 NPQQYEAMYQQSINVPDTFWGEQGKILDWIKPY--QKV--KNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQE-NGDRTA 94
Cdd:PLN02654 28 SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegDEVcsENLDVRKGPISIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 95 IIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGR 174
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 175 IIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNP--NVTSV------EHVVVLKRTGGKidWQEGRDLWWHDLVEQASD 246
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESakNGVSVgicltyENQLAMKREDTK--WQEGRDVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 247 QHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 327 TLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEK 406
Cdd:PLN02654 346 VLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 407 CPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQ 486
Cdd:PLN02654 426 CPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYET 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 487 TYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLN 566
Cdd:PLN02654 506 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 567 HGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSNLGDTSTLADPGVVEKLLE 643
Cdd:PLN02654 586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-638 |
0e+00 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 652.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 24 YEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQE-NGDRTAIIWEGDDA 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPP---FTRWFVGGRLNTCYNALDRHVEAgRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 103 SQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 183 VITSDEGVRAGRSIPLKKNVDDALKNPNvTSVEHVVVLKRTGGKID-WQEGRDLWWHDLVEQASdQHQAEEMNAEDPLFI 261
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSG-HKPHHVLVLNRPQVPADlTKPGRDLDWSELLAKAE-PVDCVPVAATDPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 262 LYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVP-NWPTPA 340
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 341 RMAQVVDKHQVNILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTET 418
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQTET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 419 GGFMITPLPGATEL--KAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSW-PGQARTLFGDHERFEQTYFSTFKNM 495
Cdd:cd05967 393 GWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPE- 574
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEe 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446000384 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADPGVV 638
Cdd:cd05967 553 LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE--DYTIPSTIEDPSVL 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-649 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 620.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 22 QQYEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTS---FApgnvsiKWYEDGTLNLAANCLDRHLQENGDRTAIIWE 98
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSnppFA------RWFVGGRTNLCHNAVDRHLAKRPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 99 GDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDS 178
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 179 NSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSvEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQH-QAEEMNAED 257
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKP-RHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARvPVEWLESNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWP 337
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 338 TPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekcPVVDTWWQTE 417
Cdd:PRK10524 315 DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 418 TGGFMITPLPG--ATELKAGSATRPFFGVQPALVDNE-GNPLEGATEGSLVITDSW-PGQARTLFGDHERFEQTYFSTF- 492
Cdd:PRK10524 392 TGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG---- 568
Cdd:PRK10524 472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsla 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 569 -EEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG-DTsnlGDTSTLADPGVVEKLleeKQ 646
Cdd:PRK10524 552 dREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI---RQ 625
|
...
gi 446000384 647 AIA 649
Cdd:PRK10524 626 ALE 628
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-635 |
0e+00 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 555.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 22 QQYEAMYQQSINVPDTFWGEQGKILD--WIKPYQKVKNTSfaPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEG 99
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 100 DDASqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSN 179
Cdd:cd05968 85 EDGT-SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 180 SRLVITSDEGVRAGRSIPLKKNVDDALKNpnVTSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQhqAEEMNAEDPL 259
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACAQ--CPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDG--AERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 260 FILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGD-IYWCTaDVGWVTGhSYLLYGPLACGATTLMFEGVPNWPT 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 339 PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTET 418
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 419 GGFMITPLPgATELKAGSATRPFFGVQPALVDNEGNPLEGaTEGSLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFS 498
Cdd:cd05968 398 SGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 499 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAE 578
Cdd:cd05968 476 GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEE 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 579 VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADP 635
Cdd:cd05968 556 LMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-628 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 525.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 69 WYEDGTLNLAANCLDRHLQEN-GDRTAIIWEGDDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGrKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 148 AMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRagrsiplKKNVDDalknpnVTSVEHVVVLKRTGGki 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD------LPSLKHVLLVGEDVE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 228 dwQEGRDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAlTFKYVFDYHPGDIYWCTADV 307
Cdd:PRK04319 179 --EGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ-TGKYVLDLHEDDVYWCTADP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 308 GWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK04319 256 GWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEAWEWYWKKIGNekcPVVDTWWQTETGGFMITPLPgATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVIT 467
Cdd:PRK04319 333 EPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 468 DSWPGQARTLFGDHERFEQtYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:PRK04319 409 KGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 548 VGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK----IAAGDT 623
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgLPEGDL 565
|
....*
gi 446000384 624 SNLGD 628
Cdd:PRK04319 566 STMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
109-619 |
8.60e-149 |
|
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: 438.47 E-value: 8.60e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 gvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhQAEEMNAEDPLFILYTSGST 268
Cdd:cd05969 82 ------------------------------------------------------------LYERTDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 269 GKPKGVLHTTGGYLVYAaLTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMAQVVDK 348
Cdd:cd05969 102 GTPKGVLHVHDAMIFYY-FTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 349 HQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPG 428
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 429 aTELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEqtyfSTFKN-MYFSGDGARRDED 507
Cdd:cd05969 255 -MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYK----NSFIDgWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEI 587
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
gi 446000384 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05969 410 GAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
109-617 |
4.45e-125 |
|
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: 377.06 E-value: 4.45e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITsde 188
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 gvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemNAEDPLFILYTSGST 268
Cdd:cd05972 79 -----------------------------------------------------------------DAEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 269 GKPKGVLHTTGgYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwpTPARMAQVVDK 348
Cdd:cd05972 94 GLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLER 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 349 HQVNILYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEWyWKKIGNEkcPVVDTWWQTETGgFMITPLPG 428
Cdd:cd05972 171 YGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEW-WRAATGL--PIRDGYGQTETG-LTVGNFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 429 aTELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDG 508
Cdd:cd05972 244 -MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDY---YLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 509 YYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIG 588
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
gi 446000384 589 PLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
1.96e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.61 E-value: 1.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAiiWEGDDasqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEgvragrsiPLKKNVDDALknPNVTSVEHVVVLKRTggkiDWQEGRDLWWHDLV 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEAL--GKLEVVKLVLVLDRD----PVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EqASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAALTFKYV----FDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 142 A-DVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 318 YGPLACGATTLMFEGVPNwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 398 YWKKIGnekCPVVDTWWQTETGGFMITPLPGATEL-KAGSATRPFFGVQPALVD-NEGNPLEGATEGSLVItdSWPGQAR 475
Cdd:pfam00501 297 FRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446000384 476 TLFGDHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:pfam00501 372 GYLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-623 |
4.13e-107 |
|
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: 331.39 E-value: 4.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlv 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeemnaedplFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 322 ACGATTLMfegVPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:COG0318 165 LAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 402 IGnekCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQARTLFGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 482 ERFEQTyfstFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRDgWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 561 AYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDT 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 |
8.00e-101 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 311.14 E-value: 8.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYvFDYHPGDIYWCTADVGWVtGHSYLLYGPLACGATTLMFEGvpnw 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 337 PTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 417 ETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQartlfGDHERFEQTYFSTFKNMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK-----GYWNNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPEly 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 446000384 577 aEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
24-639 |
1.04e-90 |
|
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: 294.18 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 24 YEAMYQQSINVPDTFWGEqgkILDWI-----KPYQKV-KNTSFAPGNvsiKWYEDGTLNLAANCLDRHlqeNGDRTAIIW 97
Cdd:cd05943 19 YAALHRWSVDDPGAFWAA---VWDFSgvrgsKPYDVVvVSGRIMPGA---RWFPGARLNYAENLLRHA---DADDPAAIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 98 EGDDASqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIID 177
Cdd:cd05943 90 AAEDGE-RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 178 SNSRLVITSDEGVRAGRSIPLKKNVDDALKnpNVTSVEHVVVLKRTG--GKIDWQE-GRDLWWHDLVEQASDQHQA-EEM 253
Cdd:cd05943 169 IEPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVaaGQPDLSKiAKALTLEDFLATGAAGELEfEPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 254 NAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSylLYGPLACGATTLMFEGV 333
Cdd:cd05943 247 PFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 334 PNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekcpvvDTW 413
Cdd:cd05943 325 PFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 414 WQTETGG------FMIT-PL----PGatELKAgsatrPFFGVQPALVDNEGNPLEGATeGSLVITDSWPGQARTLFGDHE 482
Cdd:cd05943 399 LASISGGtdiiscFVGGnPLlpvyRG--EIQC-----RGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPSMPVGFWNDPD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 483 --RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:cd05943 471 gsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVI 550
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 561 AYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdtSNLGDTSTLADPGVVE 639
Cdd:cd05943 551 LFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPESLD 627
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
6.57e-90 |
|
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: 286.34 E-value: 6.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITsd 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrsiplkkNVDDAlknpnvtsvehvvvlkrtgGKIDwqegrdlwwhdlveqasdqhqaeemnaEDPLFILYTSGS 267
Cdd:cd05973 79 -------------DAANR-------------------HKLD---------------------------SDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYLVYAALtFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARmaqVVD 347
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWR---VIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 348 KHQVNILYTAPTAIRALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLP 427
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 428 GATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVI-TDSWPgqaRTLFGDHERFEQTYFStfKNMYFSGDGARRDE 506
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSP---LMWFRGYQLPDTPAID--GGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKE 586
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
gi 446000384 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
24-639 |
5.18e-89 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 290.54 E-value: 5.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 24 YEAMYQQSINVPDTFWGEqgkILDWI-----KPYQKVKNTSFAPGNvsiKWYEDGTLNLAANCLdRHlqENGDRTAIIWE 98
Cdd:PRK03584 36 YAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLAGRRMPGA---RWFPGARLNYAENLL-RH--RRDDRPAIIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 99 GDDASQSKhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDS 178
Cdd:PRK03584 107 GEDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 179 NSRLVITSDeGVR-AGRSIPLKKNVD---DALKnpnvtSVEHVVVLKRTGGKIDWQEG-RDLWWHDLVEQASDQH-QAEE 252
Cdd:PRK03584 186 EPKVLIAVD-GYRyGGKAFDRRAKVAelrAALP-----SLEHVVVVPYLGPAAAAAALpGALLWEDFLAPAEAAElEFEP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 253 MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGD-IYWCTAdVGW------VTGhsyllygpLACGA 325
Cdd:PRK03584 260 VPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNe 405
Cdd:PRK03584 331 TLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 406 kcpvvDTWWQTETGG------FMI-TPL----PGatELKAgsatrPFFGVQPALVDNEGNPLEGATeGSLVITDSWPGQA 474
Cdd:PRK03584 410 -----DVWLASISGGtdicscFVGgNPLlpvyRG--EIQC-----RGLGMAVEAWDEDGRPVVGEV-GELVCTKPFPSMP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 475 RTLFGD--HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPH 552
Cdd:PRK03584 477 LGFWNDpdGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEW 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 553 NIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM----RRILRKIAAGDTSNLGd 628
Cdd:PRK03584 557 PDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAVNRD- 635
|
650
....*....|.
gi 446000384 629 tsTLADPGVVE 639
Cdd:PRK03584 636 --ALANPEALD 644
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-616 |
5.65e-82 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 268.59 E-value: 5.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 64 NVSIKWYEdgTLNLAANCLDRHLQENGDRTAIIWeGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVP 143
Cdd:cd05970 7 NFSINVPE--NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 144 EAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVragrsipLKKNVDDALKN-PNVTsvehvvVLKR 222
Cdd:cd05970 84 EFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAAPEcPSKP------KLVW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 223 TGGKIdwqegRDLW--WHDLVEQASDQHQAEEMNA----EDPLFILYTSGSTGKPKGVLHTTGgYLVYAALTFKYVFDYH 296
Cdd:cd05970 151 VGDPV-----PEGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 297 PGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGvpNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGdkaIEGTD 376
Cdd:cd05970 225 EGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED---LSRYD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 377 RSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGgFMITPLPGaTELKAGSATRPFFGVQPALVDNEGNPL 456
Cdd:cd05970 300 LSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 457 EGATEGSLVITDSwPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:cd05970 375 EAGEEGEIVIRTS-KGKPVGLFGGYYKDAEKTAEVWHDgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 536 LVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05970 454 LIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
.
gi 446000384 616 R 616
Cdd:cd05970 534 R 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-616 |
3.70e-81 |
|
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: 265.77 E-value: 3.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 78 AANCLDRHLQEN-GDRTAIIwegDDASqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEGrGDKTAFI---DDAG---SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 157 AVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEgvragrsipLKKNVDDALKNpnvtSVEHVVVLKRTGGKIdwQEGRDLW 236
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTK----SEHTLVVLIVSGGAG--PEAGALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 237 WHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05959 144 LAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPLACGATTLMFegvPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 397 WYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGNPLEGATEGSLVIT-DSwpgqar 475
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRgPS------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 476 TLFGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNI 554
Cdd:cd05959 368 SATMYWNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 555 KGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
18-617 |
3.76e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 261.60 E-value: 3.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 18 LINPQQYEAMYQQSINVPDTFWGEQG-KILDWIKPYQKVkntsFAPGNVSIKWYEDGTLNLAANCLDRHLQ--ENGDRTA 94
Cdd:PTZ00237 4 LSDPFDYENDSNYANSNPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVKnpLKRDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 95 IIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGR 174
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 175 IIDSNSRLVITSDEGVRAGRSIPLKKNVDDALK----NPNvtsveHVVVLKRTggkiDWQEGRD-------------LWW 237
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIElstfKPS-----NVITLFRN----DITSESDlkkietiptipntLSW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 238 HDLVEQASDQHQA---EEMNAED--PLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTG 312
Cdd:PTZ00237 231 YDEIKKIKENNQSpfyEYVPVESshPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 313 HSYLlYGPLACGATTLMFEG--VPNWPTPARMAQVVDKHQVNILYTAPTAIRALMA---EGDKAIEGTDRSSLRILGSVG 387
Cdd:PTZ00237 311 HGFL-YGSLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpEATIIRSKYDLSNLKEIWCGG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEAWEWYWKKIgneKCPVVDTWWQTETGgfmITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPLEGATEGSLV 465
Cdd:PTZ00237 390 EVIEESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCYGHINIPYNAtgVPSIFIKPSILSEDGKELNVNEIGEVA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 466 ITDSWP-GQARTLFGDHERFEQTyFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:PTZ00237 464 FKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPSP----ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 543 CCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-616 |
1.33e-75 |
|
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: 248.89 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 105 SKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 185 TsDEgvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 265 SGSTGKPKGVLHTTG---GYLVYAALTFKyvFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM-----FEgvpnw 336
Cdd:cd05971 97 SGTTGPPKGALHAHRvllGHLPGVQFPFN--LFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrmtkFD----- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 337 ptPARMAQVVDKHQVNILYTAPTAIRaLMAEGDKAIEGTDRSsLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQT 416
Cdd:cd05971 170 --PKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVE---VNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 417 EtGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQARTLFGDHERFEQTYFSTFknmY 496
Cdd:cd05971 243 E-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDW---L 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELY 576
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446000384 577 AEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 399 REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
2.56e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 247.79 E-value: 2.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 72 DGTLNLAaNCLDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 152 CARIGAV-HSV-IFggFSPEAVAGRIIDSNSRLVITSDEGVragrsiPLKKNVDDALknpnvTSVEHVVVLK---RTGGK 226
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQL-----PTVRTVIVEGdgpAAPLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 227 IDWQEgrdlwWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTtggY--LVYAALTFKYVFDYHPGDIYWCT 304
Cdd:PRK06187 143 PEVGE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS---HrnLFLHSLAVCAWLKLSRDDVYLVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 305 ADV----GWVTGhsyllYGPLACGATTLM---FEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALMAEgdKAIEGTDR 377
Cdd:PRK06187 215 VPMfhvhAWGLP-----YLALMAGAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQMLLKA--PRAYFVDF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 378 SSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFM-ITPLP---GATELKAGSATRPFFGVQPALVDNEG 453
Cdd:PRK06187 281 SSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPEdqlPGQWTKRRSAGRPLPGVEARIVDDDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 454 NPLE--GATEGSLVITDSWPGQArtLFGDHERFEqtyfSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK06187 358 DELPpdGGEVGEIIVRGPWLMQG--YWNRPEATA----ETIDGgWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 531 EIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKI 610
Cdd:PRK06187 432 ELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKI 508
|
570
....*....|...
gi 446000384 611 MRRILR-KIAAGD 622
Cdd:PRK06187 509 LKRVLReQYAEGK 521
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-617 |
2.55e-73 |
|
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: 245.45 E-value: 2.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 76 NLAANCLDR--HLQENGDRTA--IIWEGDDASQSKHISYKELHRDVCRFANTLLEL-GIKKGDVVAIYMPMVPEAAVAML 150
Cdd:cd05928 6 NFASDVLDQwaDKEKAGKRPPnpALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 151 ACARIGAVhsVIFGGFSPEA--VAGRIIDSNSRLVITSDEGVRAGRSIplkknvddALKNPNVtSVEHVVVLKRTGGKID 228
Cdd:cd05928 86 ACIRTGLV--FIPGTIQLTAkdILYRLQASKAKCIVTSDELAPEVDSV--------ASECPSL-KTKLLVSEKSRDGWLN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 229 WQEgrdlwwhdLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVG 308
Cdd:cd05928 155 FKE--------LLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 WVTGHSYLLYGPLACGATTLMFEgVPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEgtdRSSLRILGSVGE 388
Cdd:cd05928 227 WIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYK---FPSLQHCVTGGE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 389 PINPEAWEWYWKKIGNEkcpVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITD 468
Cdd:cd05928 302 PLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 SwPGQARTLFGDHERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd05928 377 K-PIRPFGLFSGYVDNPEKTAATIRgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAV 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 548 VGIPHNIKGQAIYAYVTLN-----HGEEpspELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 456 VSSPDPIRGEVVKAFVVLApqflsHDPE---QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
2.38e-71 |
|
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: 237.51 E-value: 2.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IfggfspeavagriidsNSRLvitsdegvragrsiplkknvddalknpnvTSVEHVVVLKRTGGKIdwqegrdlwwhdLV 241
Cdd:cd17631 75 L----------------NFRL-----------------------------TPPEVAYILADSGAKV------------LF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EqasdqhqaeemnaeDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:cd17631 98 D--------------DLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 322 ACGATTLMFEGvpnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPInPEAWEWYWKK 401
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 402 IGnekCPVVDTWWQTETGGfMITPL-PGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQARtlfGD 480
Cdd:cd17631 236 RG---VKFVQGYGMTETSP-GVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA---GY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 481 HERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17631 307 WNRPEATA-AAFRDGWFhTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 386 VAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
92-616 |
2.84e-71 |
|
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: 237.36 E-value: 2.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 92 RTAIIwegdDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV 171
Cdd:cd05919 1 KTAFY----AADRS--VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 172 AGRIIDSNSRLVITSdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqae 251
Cdd:cd05919 75 AYIARDCEARLVVTS----------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 252 emnAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADV--GWVTGHSylLYGPLACGATTLM 329
Cdd:cd05919 90 ---ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 330 FegvPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEwYWKKIGNekCPV 409
Cdd:cd05919 165 N---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFG--GPI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 410 VDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDswPGQARTLFGDHERFEQTYF 489
Cdd:cd05919 237 LDGIGATEVGHIFLSNRPGAWRL--GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 490 STFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE 569
Cdd:cd05919 313 GGW---YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446000384 570 EPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 390 APQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-616 |
1.38e-67 |
|
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: 228.22 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 159 HSVIFGgfsPEAVAGRIIDSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrDLWWH 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIV------------------------------------------------AVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 239 DLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFK-YVFDYHPGD-----------IYWCTAd 306
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN-LVANALQIKaWLEDLLEGDdvvlaalplfhVFGLTV- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 307 vgwvtghSYLLygPLACGATTLMfegVPNwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSV 386
Cdd:cd05936 186 -------ALLL--PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 387 GEPINPEAWEWYWKKIGnekCPVVDTWWQTETG-GFMITPLPGATelKAGSATRPFFGVQPALVDNEGNPLEGATEGSLV 465
Cdd:cd05936 251 GAPLPVEVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELW 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 466 ITdswpGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:cd05936 326 VR----GPQVMK-GYWNRPEETA-EAFVDGWLrTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAE 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 400 AAVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-624 |
9.69e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 219.80 E-value: 9.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEgvragrsipLKKNVDDALKNPNVTSVEHVVVLKRTGGkidwqEGRDLWWHDLVEQASDQHQA 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREA-----PGGWLDFADWAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 EEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaALTFKYV-----FDYHPGDI-------YWCTAdvgwvtGHSYLly 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVscivaGDMSADDIplhalplYHCAQ------LDVFL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 319 GP-LACGATTLMFEGvpnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRiLGSVGEPINPEAwew 397
Cdd:PRK08316 232 GPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR-KGYYGASIMPVE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 398 YWKKIgNEKCPVVDTW---WQTEtggfmITPL-----PGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVitds 469
Cdd:PRK08316 302 VLKEL-RERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 wpgqART------LFGDHERFEQtyfsTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK08316 372 ----HRSpqlmlgYWDDPEKTAE----AFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK08316 444 AEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
..
gi 446000384 623 TS 624
Cdd:PRK08316 521 FT 522
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
24-617 |
8.69e-63 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 221.49 E-value: 8.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 24 YEAMYQQSINVPDTFWG---EQGKILDWIKPYQKVKNTSFA-PGNvsiKWYEDGTLNLAANCLDRHLQENGDRTAIIW-- 97
Cdd:PLN03052 122 FSEFQRFSVENPEVYWSivlDELSLVFSVPPRCILDTSDESnPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrd 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 98 EGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIID 177
Cdd:PLN03052 199 EGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 178 SNSRLVITSDEGVRAGRSIPLKKNVDDAlKNPNvtsvehVVVLKRTGGKIDWQ-EGRDLWWHDLVEQAS-----DQHQAE 251
Cdd:PLN03052 279 SKAKAIFTQDVIVRGGKSIPLYSRVVEA-KAPK------AIVLPADGKSVRVKlREGDMSWDDFLARANglrrpDEYKAV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 252 EMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVfDYHPGDIY-WCTaDVGWVTGHsYLLYGPLACGATTLMF 330
Cdd:PLN03052 352 EQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALY 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 331 EGVPNWPTPARMAQvvdKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcPVV 410
Cdd:PLN03052 429 NGSPLGRGFAKFVQ---DAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PII 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 411 DTWWQTETGG-FMITPLPGATELKAGSAtrPFFGVQPALVDNEGNPL--EGATEGSLVITDSWPGQARTLF-GDHerfEQ 486
Cdd:PLN03052 502 EYCGGTELGGgFVTGSLLQPQAFAAFST--PAMGCKLFILDDSGNPYpdDAPCTGELALFPLMFGASSTLLnADH---YK 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 487 TYfstFKNM-YFSGDGARRDED-------GYYWITGRVDDVLNVSGHRLGTAEIESAL-VAHPKIAEAAVVGIPHNIKGQ 557
Cdd:PLN03052 577 VY---FKGMpVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGP 653
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446000384 558 ---AIYAYVTLNHGEEPSPELYAEVRN-WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 654 eqlVIAAVLKDPPGSNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
108-617 |
1.59e-62 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 215.64 E-value: 1.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 EGVRagrsiplkknvdDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWH--DLVEQASDQHqaeeMNAEDPLFILYTS 265
Cdd:cd05926 95 GELG------------PASRAASKLGLAILELALDVGVLIRAPSAESLSNLlaDKKNAKSEGV----PLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtparm 342
Cdd:cd05926 159 GTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFSASTFWP----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 343 aQVVDkHQVNiLYTA-PTAIRAL--MAEGDKAIEgtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETG 419
Cdd:cd05926 233 -DVRD-YNAT-WYTAvPTIHQILlnRPEPNPESP---PPKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 420 GFMIT-PLPGATElKAGSATRPFfGVQPALVDNEGNPLEGATEGSLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF- 497
Cdd:cd05926 304 HQMTSnPLPPGPR-KPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNPE---ANAEAAFKDGWFr 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLnhgEEPSPELYA 577
Cdd:cd05926 377 TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL---REGASVTEE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446000384 578 EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
3.92e-62 |
|
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: 214.70 E-value: 3.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 73 GTLNLAANCLDRHLQE-NGDRTAIIwegDDASQskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI---DDISS---LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 152 CARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEgvragrSIPLKKNVddALKNPNVtsvEHVVVLKRT-GGKIDWQ 230
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA------LLPVIKAA--LGKSPHL---EHRVVVGRPeAGEVQLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 231 EgrdlwwhdLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWV 310
Cdd:TIGR02262 144 E--------LLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 311 TGHSYLLYGPLACGATTLMFegvPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRssLRILGSVGEPI 390
Cdd:TIGR02262 216 YGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVR--LRLCTSAGEAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 nPEAWEWYWK-KIGNEkcpVVDTWWQTETGGFMITPLPGAteLKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdS 469
Cdd:TIGR02262 291 -PAEVGQRWQaRFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLI--S 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 WPGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:TIGR02262 363 GPSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVG 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 550 IP---HNIKGQaiyAYVTLNHGEEpspELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 440 VAdedGLIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-616 |
9.51e-62 |
|
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: 211.38 E-value: 9.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 107 HISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITs 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 187 degvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 267 STGKPKGVLhTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMAQVV 346
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 347 DKHQVNILYTAPTAIRALMAEGDKAiegTDRSS-LRILGsvGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITP 425
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSP---DDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 426 LPGATelKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITdSWPGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARR 504
Cdd:cd05934 239 RDEPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR-GLRGWGFFK-GYYNMPEATA-EAMRNGWFhTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVR 584
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCE 390
|
490 500 510
....*....|....*....|....*....|..
gi 446000384 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 391 GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-611 |
2.54e-60 |
|
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: 209.38 E-value: 2.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 101 DASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 181 RLVITSDEGVragrsiplkKNVDDALKNpnVTSVEHVVVLkrtGGKIDWQEGR-DLWWHDLVEQASDQHQAEEMNAEDPL 259
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAKE--LGPKDKIIVL---DDKPDGVLSIeDLLSPTLGEEDEDLPPPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 260 FILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFD-YHPGDIYWCTADVGWVTGHSYLLYGPLaCGATTLMFegvpNWPT 338
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM----PKFD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 339 PARMAQVVDKHQVNILYTAPtAIRALMAEgDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTET 418
Cdd:cd05911 225 SELFLDLIEKYKITFLYLVP-PIAAALAK-SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPN--ATIKQGYGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 419 GGfMITPLPGaTELKAGSATRPFFGVQPALVDNEGNPLEGATE-GSLVItdsWPGQArtLFGDHERFEQTYFSTFKNMYF 497
Cdd:cd05911 301 GG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEpGEICV---RGPQV--MKGYYNNPEATKETFDEDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 498 -SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPEly 576
Cdd:cd05911 374 hTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEK-- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446000384 577 aEVRNWVRKEIgplatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 452 -EVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
5.04e-60 |
|
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: 207.38 E-value: 5.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRII----DSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasd 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 247 qhqaeemNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPLA 322
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE-----IFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATTLMfegVPN--WPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEwYWK 400
Cdd:cd05930 158 AGATLVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVR-RWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNeKCPVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPL-EGATeGSLVITDswPGQARTL 477
Cdd:cd05930 230 ELLP-GARLVNLYGPTEATVDATYYRVPPDDEEDGRVPigRPIPNTRVYVLDENLRPVpPGVP-GELYIGG--AGLARGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 478 FGDHE----RFEQTYFSTFKNMYFSGDGARRDEDG--YYwiTGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:cd05930 306 LNRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARE 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 552 HNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 384 DGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-617 |
2.32e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.75 E-value: 2.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEgvragrSIPLKKNVDDALknPNvtsVEHVVVLkrTGGKIDWQEGRDLWWHDLV 241
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGL------FLGVDYSATTRL--PA---LEHVVIC--ETEEDDPHTEKMKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAALTFKYVFDYHPGDIYWCTA--------DVGWVTgh 313
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANpffhvfgyKAGVNA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 314 syllygPLACGATTLMfegVPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEgtDRSSLRILGSVGEPINPE 393
Cdd:PRK07656 229 ------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE--DLSSLRLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 AWEWYWKKIGnekCPVVDTWWQ-TETGGFM-ITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDswP 471
Cdd:PRK07656 297 LLERFESELG---VDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG--P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 472 GQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:PRK07656 372 NVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 552 HNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
255-616 |
2.68e-58 |
|
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: 202.71 E-value: 2.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 255 AEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVp 334
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 335 nwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWW 414
Cdd:cd05958 175 ---TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 415 QTETGGFMITPLPGatELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDswPGQARTLFgdhERFEQTYFSTFKN 494
Cdd:cd05958 247 STEMFHIFISARPG--DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCRYLA---DKRQRTYVQGGWN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 495 myFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPE 574
Cdd:cd05958 320 --ITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPV 397
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446000384 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 398 LARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-624 |
5.15e-57 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 201.82 E-value: 5.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVItsdegvragrsIP-LKKNVDDA-----LKnPNVTSVEHVVVLkrtGGkidwqEGRDL 235
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLV-----------VPkTFRGFDHAamarrLR-PELPALRHVVVV---GG-----DGADS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 236 WWHDLV----EQASDQHQ---AEEMNAEDPLFILYTSGSTGKPKGVLHTT----GGYLVYAALtfkyvFDYHPGDIYWCT 304
Cdd:PRK13295 170 FEALLItpawEQEPDAPAilaRLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 305 ADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMAQVVDKHQVNilYT-APTAIRALMAEGDKAiEGTDRSSLRIL 383
Cdd:PRK13295 245 SPMAHQTGFMYGLMMPVMLGATAVLQD---IW-DPARAAELIRTEGVT--FTmASTPFLTDLTRAVKE-SGRPVSSLRTF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 384 GSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGS 463
Cdd:PRK13295 318 LCAGAPIPGALVERARAALGAK---IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 464 LVITdswpgqARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIA 543
Cdd:PRK13295 395 LQVR------GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPSpelYAEVRNWVR-KEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK13295 469 QVAIVAYPDERLGERACAFVVPRPGQSLD---FEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
..
gi 446000384 623 TS 624
Cdd:PRK13295 546 DA 547
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
1.39e-55 |
|
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: 195.09 E-value: 1.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspeavagrIIDSNSRLviTSD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------VIPATTLL--TPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 EgvragrsipLKKNVDdalknpnvtsvehvvvlkRTGGKIDWQEgrdlwwhdlveqasdqhqaEEMNAEDPLFILYTSGS 267
Cdd:cd05974 63 D---------LRDRVD------------------RGGAVYAAVD-------------------ENTHADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYLVyAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFegvpNWP--TPARMAQV 345
Cdd:cd05974 97 TSKPKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 346 VDKHQVNILYTAPTAIRALMAEGDKAIegtdRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTETGGfMITP 425
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETTA-LVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 426 LPGATeLKAGSATRPFFGVQPALVDNEGNPlegATEG--SLVITDSWP-GQARTLFGDHERfeqTYFSTFKNMYFSGDGA 502
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGAP---ATEGevALDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNW 582
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 446000384 583 VRKEIGPLATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
9.46e-53 |
|
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: 189.38 E-value: 9.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDasQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEG--EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEGVragrsiPLKKNVDDALKNpnvtsVEHVVVLKRTGGKIDWQEGRDLWWHDLV 241
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFL------PLLEAIAPRLPT-----VEHVVVMTDDAAMPEPAGVGVLAYEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EQASDQHQAEEMNAEDPLFILYTSGSTGKPKGV--------LHTtggylvYAALTFKyVFDYHPGDIY-----------W 302
Cdd:cd12119 149 AAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHA------MAALLTD-GLGLSESDVVlpvvpmfhvnaW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 303 CTADVGWVTGHSYLLYGPlacgattlmfegvpnWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRI 382
Cdd:cd12119 222 GLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 383 LGSVGEPINPEAWEWyWKKIGnekCPVVDTWWQTETG--GFMITPLPGATELKAG-------SATRPFFGVQPALVDNEG 453
Cdd:cd12119 285 VVIGGSAVPRSLIEA-FEERG---VRVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 454 NPLE--GATEGSLVITDSWpgQARTLFGDHER----FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:cd12119 361 RELPwdGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLRT-------GDVATIDEDGYLTITDRSKDVIKSGGEWI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 528 GTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:cd12119 432 SSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTST 508
|
570
....*....|
gi 446000384 608 GKIMRRILRK 617
Cdd:cd12119 509 GKIDKKALRE 518
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
1.23e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 188.63 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIW--EGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 160 SvIFGGFSPEAVAGRIIDSNSRLVITSdeGVRAGRSIPLKknVDDALknPNVTSVEHVVVL---KRTGGKIDWQ------ 230
Cdd:PRK07529 111 P-INPLLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQK--VAEVL--AALPELRTVVEVdlaRYLPGPKRLAvplirr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 231 --EGRDLWWHDLVEQASDQH--QAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTAD 306
Cdd:PRK07529 184 kaHARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 307 VGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA---------RMAQVVDKHQVNILYTAPTAIRALMaegDKAIEGTDR 377
Cdd:PRK07529 263 LFHVNALLVTGLAPLARGAHVV-------LATPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 378 SSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTWWQTE-TGGFMITPLPGatELKAGSATRPFFG--VQPALVDNEGN 454
Cdd:PRK07529 333 SSLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 455 PLEGATEGSL-VITDSWPGQART-LFGDHER---FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK07529 408 YLRDCAVDEVgVLCIAGPNVFSGyLEAAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 530 AEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIG-PLATPDVLHWTDSLPKTRSG 608
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELLAFARDHIAeRAAVPKHVRILDALPKTAVG 557
|
570
....*....|..
gi 446000384 609 KIMRRILRKIAA 620
Cdd:PRK07529 558 KIFKPALRRDAI 569
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
109-617 |
2.02e-51 |
|
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: 183.74 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDE 188
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 gvragrsiplkknvddalknpnvtsvehvvvlkrtggkidWQegrdlwwhdlveqasdQHQAEEMNAeDPLFILYTSGST 268
Cdd:cd05903 83 ----------------------------------------FR----------------QFDPAAMPD-AVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 269 GKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMAQVVDK 348
Cdd:cd05903 106 GEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IW-DPDKALALMRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 349 HQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVvdtWWQTETGGFMITPLPG 428
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGAVTSITPA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 429 ATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDED 507
Cdd:cd05903 256 PEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS------RGPSVFLGYLDRPDLTADAAPEGWFrTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVrnWVRKEI 587
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY--LDRQGV 407
|
490 500 510
....*....|....*....|....*....|
gi 446000384 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 408 AKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
2.24e-51 |
|
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: 184.05 E-value: 2.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqa 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 eemNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTfKYVFDYHPGDIywctadvgWVTGHSYL-------LYGPLAC 323
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT-QRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 GATTLMfegVPNWP--TPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLR--ILGsvGEPINPEAWEWYW 399
Cdd:cd17643 159 GGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPWA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 400 KKIGNEKCPVVDTWWQTETGGFM-ITPLpGATELKAGSAT---RPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQAR 475
Cdd:cd17643 232 GRFGLDRPQLVNMYGITETTVHVtFRPL-DAADLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAGVAR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 476 TLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI 550
Cdd:cd17643 309 GYLGrpelTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVR 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 551 PHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 389 EDEPGDTRLVAYVVADDGAAADI---AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
1.85e-49 |
|
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: 180.12 E-value: 1.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 87 QENGDRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 167 SPEAVAGRIIDSNSRLVITSDEGVragrsiplKKNVDDALKnpnvtsvehVVVLKRTggkidwQEGRDLWWHDLVEQASD 246
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELA--------EKLASLALP---------VVLLDSA------EFDSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 247 QHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFD--YHPGDIYWCTADVGWVTGHSYLLYGPLACG 324
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 325 ATTL---MFEGvpnwptpARMAQVVDKHQVNILYTAPTAIRAlMAEGDKAiEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:cd05904 228 ATVVvmpRFDL-------EELLAAIERYKVTHLPVVPPIVLA-LVKSPIV-DKYDLSSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 402 IGNekCPVVDTWWQTE-TGGFMITPLPGATELKAGSATRPFFGVQPALVD-NEGNPLEGATEGSLVITDswPGQARTLFG 479
Cdd:cd05904 299 FPN--VDLGQGYGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG--PSIMKGYLN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 480 DHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd05904 375 NPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 453 MAFVVRKPGSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-617 |
7.98e-49 |
|
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: 178.82 E-value: 7.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 104 QSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLV 183
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 184 ITSDEgvragrsiPLKKNVDDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDlwWHDLvEQASDQHQAEEMNAEDPLFILY 263
Cdd:TIGR03098 102 VTSSE--------RLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPAS--WPKL-LALGDADPPHPVIDSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 264 TSGSTGKPKGVL--HTTggyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegvpNWPTPAR 341
Cdd:TIGR03098 171 TSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH-----DYLLPRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 342 MAQVVDKHQVNILYTAPtAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTEtgGF 421
Cdd:TIGR03098 243 VLKALEKHGITGLAAVP-PLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMYGLTE--AF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 422 MITPL-PGATELKAGSATR--PFFGVQPALVDNE----GNPLEGATEGSLVITDSWPGQARTlfgdHERFE-----QTYF 489
Cdd:TIGR03098 316 RSTYLpPEEVDRRPDSIGKaiPNAEVLVLREDGSecapGEEGELVHRGALVAMGYWNDPEKT----AERFRplppfPGEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 490 STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE 569
Cdd:TIGR03098 392 HLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446000384 570 EPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 472 ELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
2.32e-48 |
|
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: 176.02 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17649 2 DAVALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwQEGRDLWWhdlveqasdqhqa 250
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQLAY------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 eemnaedplfILYTSGSTGKPKGVLHTTGGYLVYAALTFKYvFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMf 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 331 EGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGtDRSSLRILGSVGEPINPEAWeWYWKKIGnekCPVV 410
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELL-RRWLKAP---VRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 411 DTWWQTETggfMITPL--PGATELKAGSAT----RPFFGVQPALVDNEGNPLEGATEGSLVITDswPGQARtlfGDHERF 484
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASmpigRPLGGRSAYILDADLNPVPVGVTGELYIGG--EGLAR---GYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 485 EQT--------YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIkG 556
Cdd:cd17649 313 ELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 557 QAIYAYVTLNHGEEpSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 392 KQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-620 |
7.29e-48 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 176.49 E-value: 7.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIwEGDdasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 159 ------HSVI--FGGFSpEAVAgriidsnsrlVITSD-----------EGVRAGrsiplkknvddalknpnVTSVEHVVV 219
Cdd:COG1021 105 alpahrRAEIshFAEQS-EAVA----------YIIPDrhrgfdyralaRELQAE-----------------VPSLRHVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 220 LKRTGGKIDWQegrdlwwhDLVEQASDQHQAEeMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAALTFKYVFDYHPGD 299
Cdd:COG1021 157 VGDAGEFTSLD--------ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 300 IYWCTADVGwvtgHSYllygPLAC---------GATTLMfegVPNwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDK 370
Cdd:COG1021 227 VYLAALPAA----HNF----PLSSpgvlgvlyaGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWLDAAER 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 371 aiEGTDRSSLRILGSVGEPINPEAWewywKKIGnekcPVVDTWWQ-----TEtGGFMITPLPGATELKAGSATRPffgVQ 445
Cdd:COG1021 295 --SRYDLSSLRVLQVGGAKLSPELA----RRVR----PALGCTLQqvfgmAE-GLVNYTRLDDPEEVILTTQGRP---IS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 446 PA----LVDNEGNPLEGATEGSLV------IT---DSwPGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWI 512
Cdd:COG1021 361 PDdevrIVDEDGNPVPPGEVGELLtrgpytIRgyyRA-PEHNARAF-TPDGF-----------YRTGDLVRRTPDGYLVV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 513 TGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNhGEEPSPelyAEVRNWVRkEIGpLAT 592
Cdd:COG1021 428 EGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTL---AELRRFLR-ERG-LAA 501
|
570 580 590
....*....|....*....|....*....|.
gi 446000384 593 ---PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:COG1021 502 fklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-616 |
1.24e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 172.86 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 73 GTLNLAAncLDRHlqenGDRTAIIWegDDASqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLAC 152
Cdd:PRK06188 15 GHLLVSA--LKRY----PDRPALVL--GDTR----LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 153 ARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVItSDEGVRAGRSIPLKKNVDdalknpnvtSVEHVVVLKRTGGkidwqeG 232
Cdd:PRK06188 83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVPD------G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 233 RDLWwhDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAltfkyvfdyhpgdiyWCTADVGWVTG 312
Cdd:PRK06188 147 VDLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 313 HSYLLYGPL--ACGAT---TLM----------FEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDR 377
Cdd:PRK06188 210 PRFLMCTPLshAGGAFflpTLLrggtvivlakFD-------PAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 378 SSLRILGSVGEPINP----EAWEwywkKIGnekcPV-VDTWWQTETGGFmITPLP-----GATELKAGSATRPFFGVQPA 447
Cdd:PRK06188 281 SSLETVYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 448 LVDNEGNPLEGATEGSLVItdSWPGQARtlfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK06188 352 LLDEDGREVAQGEVGEICV--RGPLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGFN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 527 LGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK06188 426 VFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTA 502
|
570
....*....|
gi 446000384 607 SGKIMRRILR 616
Cdd:PRK06188 503 LGKPDKKALR 512
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-616 |
1.41e-46 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 171.76 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHLQENGDRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 164 GGFSPEAVAGRIIDSNSRLVITSDE--GVRAGRSIPLKKnvDDALKNPNVTSVEHVVvlkrtggkidwqegrdlwwhdlv 241
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlaGELAVELVAVTL--LDQPGAAAGADAEPDP----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAAltfKYVFDYHPGDIYWCTADVGW-VTGHSylLY 318
Cdd:cd17651 132 ----------ALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQ---ARASSLGPGARTLQFAGLGFdVSVQE--IF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 319 GPLACGATtLMFEGvPNW-PTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEP--INPEAW 395
Cdd:cd17651 197 STLCAGAT-LVLPP-EEVrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQ 473
Cdd:cd17651 273 EFCAGLPGLR---LHNHYGPTETHVVTALSLPGDPAAWPAPPPigRPIDNTRVYVLDAALRPVPPGVPGELYI--GGAGL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 474 ARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd17651 348 ARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 550 IPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17651 428 REDRPGEKRLVAYVVGDPEAPVDA---AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
91-615 |
1.22e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 170.53 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08314 25 DKTAIVFYG------RAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSDEgvRAGRSIPLKKNvddalknpnvTSVEHVVVLKRTG-----GKI---DW----------QE 231
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSE--LAPKVAPAVGN----------LRLRHVIVAQYSDylpaePEIavpAWlraepplqalAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 232 GRDLWWHDLVEQasdQHQAEEMNA--EDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGW 309
Cdd:PRK08314 167 GGVVAWKEALAA---GLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRT-VMANAVGSVLWSNSTPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 310 VTGHSYLLYGPLACGATTLMfegVPNWPTPArMAQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEP 389
Cdd:PRK08314 243 VTGMVHSMNAPIYAGATVVL---MPRWDREA-AARLIERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 390 InPEA-WEWYWKKIGnekCPVVDTWWQTETGGFMITPLPGATELK-AGSatrPFFGVQPALVDNE-GNPLEGATEGSLVI 466
Cdd:PRK08314 317 M-PEAvAERLKELTG---LDYVEGYGLTETMAQTHSNPPDRPKLQcLGI---PTFGVDARVIDPEtLEELPPGEVGEIVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 tdSWPGQARTLFGDHERFEQTyFSTF--KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:PRK08314 390 --HGPQVFKGYWNRPEATAEA-FIEIdgKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 545 AAVVGIPHNIKGQAIYAYVTLN--HGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08314 467 ACVIATPDPRRGETVKAVVVLRpeARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
1.64e-45 |
|
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: 168.61 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEgvRAGRSIPLkknvddalknPNVTSVEHVVVLKRTGGKIDWQEGRDlwwhdlv 241
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTAD--LAARLPAG----------GDVALLGDEALAAPPATPPLVPPRPD------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeemnaeDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGW-VTGhsYLLYGP 320
Cdd:cd17646 139 ---------------NLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFWP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 LACGATTLMFEgvPNWPT-PARMAQVVDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLRILGSVGEPINPEAWEWYW 399
Cdd:cd17646 201 LVAGARLVVAR--PGGHRdPAYLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARFL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 400 KKIG----NEKCP---VVD-TWWQTeTGGFMITPLP-GatelkagsatRPFFGVQPALVDNEGNPLEGATEGSLVITDsw 470
Cdd:cd17646 275 ALPGaelhNLYGPteaAIDvTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGELYLGG-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 471 PGQARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAA 546
Cdd:cd17646 342 VQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 547 VVGIPHNIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17646 422 VVARAAPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
4.24e-45 |
|
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: 165.90 E-value: 4.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLEL-GIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGfSPEAVAGRII-DSNSRLVITS 186
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-YPAERLAFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 187 DEGVRAGRSIPLkknvddalknpnvtsvEHVVVlkrtggkidwqegRDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSG 266
Cdd:TIGR01733 80 SALASRLAGLVL----------------PVILL-------------DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 267 STGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTA----DVgwvtghSYL-LYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFAslsfDA------SVEeIFGALLAGATLVVPPEDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 342 MAQVVDKHQVNILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTE-TGG 420
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTEtTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 421 FMITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPL-EGATeGSLVItdSWPGQARTLFGD----HERF-EQTYF-ST 491
Cdd:TIGR01733 277 STATLVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVpVGVV-GELYI--GGPGVARGYLNRpeltAERFvPDPFAgGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 492 FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:TIGR01733 354 GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
92-616 |
4.41e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 165.08 E-value: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 92 RTAIIWEGDdasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV 171
Cdd:PRK08276 1 PAVIMAPSG-----EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 172 AGRIIDSNSRLVITSDEGVRAGRSIPlkknvdDALKNpnvtsveHVVVLKRTGGKID-WQEgrdlwWHDLVEQASDQHQA 250
Cdd:PRK08276 76 AYIVDDSGAKVLIVSAALADTAAELA------AELPA-------GVPLLLVVAGPVPgFRS-----YEEALAAQPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 EEMNAEDplfILYTSGSTGKPKGVLHTTGGYLVYAAL---TFKYVFDYH--PGDIYWCTADvgwvtghsylLY--GPLAC 323
Cdd:PRK08276 138 DETAGAD---MLYSSGTTGRPKGIKRPLPGLDPDEAPgmmLALLGFGMYggPDSVYLSPAP----------LYhtAPLRF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 GATTLMFEGV----PNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA----W 395
Cdd:PRK08276 205 GMSALALGGTvvvmEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVkramI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWyWKKIGNEkcpvvdTWWQTETGGF-MITPLPGATelKAGSATRPFFGVQpALVDNEGNPLEGATEGslVITDSWPGQA 474
Cdd:PRK08276 284 DW-WGPIIHE------YYASSEGGGVtVITSEDWLA--HPGSVGKAVLGEV-RILDEDGNELPPGEIG--TVYFEMDGYP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 475 RTLFGDHERFEQTY----FSTFknmyfsGDGARRDEDGYYWITGRVDDVLnVSGhrlGT----AEIESALVAHPKIAEAA 546
Cdd:PRK08276 352 FEYHNDPEKTAAARnphgWVTV------GDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 547 VVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 422 VFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
1.19e-43 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 163.83 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 139 MPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDAlkNPNVtsvehVV 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA--APAK-----AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 219 VLKRTGGKIDWQ-EGRDLWWHDLVEQASDQHQAEE-------MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFLGVAAAQGSVGGneyspvyAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 291 YVfDYHPGDIYWCTADVGWVTGhSYLLYGPLACGATTLMFEGVpnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDK 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA---PLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 371 AIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcPVVDTWWQTETGGFMI--TPL-PGAtelkAGSATRPFFGVQPA 447
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLqPQA----PGAFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 448 LVDNEGNPL--EGATEGSLVITDSWPGQA-RTLFGDHerfEQTYFSTFKnMYFS--------GDGARRDEDGYYWITGRV 516
Cdd:PLN03051 304 LLNDNGVPYpdDQPCVGEVALAPPMLGASdRLLNADH---DKVYYKGMP-MYGSkgmplrrhGDIMKRTPGGYFCVQGRA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 517 DDVLNVSGHRLGTAEIESALV-AHPKIAEAAVVGIPhNIKGQAIYAYVTLNHGEEPS-------PELYAEVRNWVRKEIG 588
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTNLN 458
|
490 500
....*....|....*....|....*...
gi 446000384 589 PLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 459 PLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
1.38e-43 |
|
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: 162.46 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwegddASQSKHiSYKELHRDVCRFANTLLELG-IKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspe 169
Cdd:cd05941 1 DRIAIV-----DDGDSI-TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVagriidsnsrlvitsdegvragrsiPLkknvddalkNPNVTSVEHVVVLKRTGGKIdwqegrdlwwhdlveqasdqhq 249
Cdd:cd05941 64 AV-------------------------PL---------NPSYPLAELEYVITDSEPSL---------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 aeemnAEDPLFILYTSGSTGKPKGVLHTtggylvYAALTF--KYVFDYHPgdiyWCTADV-----------GWVTGhsyl 316
Cdd:cd05941 88 -----VLDPALILYTSGTTGRPKGVVLT------HANLAAnvRALVDAWR----WTEDDVllhvlplhhvhGLVNA---- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPLACGATTLMfegVPNwPTPARMAQVVDKHQVNILYTAPT-------AIRALMAEGDKAIEGTDRSsLRILGSVGEP 389
Cdd:cd05941 149 LLCPLFAGASVEF---LPK-FDPKEVAISRLMPSITVFMGVPTiytrllqYYEAHFTDPQFARAAAAER-LRLMVSGSAA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 390 INPEAWEwYWKKIGNEkcPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVDNEGN-PLEGATEGSL---- 464
Cdd:cd05941 224 LPVPTLE-EWEAITGH--TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIqvrg 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 465 --VITDSWPGQARTlfgdHERF-EQTYFSTfknmyfsGDGARRDEDGYYWITGRV-DDVLNVSGHRLGTAEIESALVAHP 540
Cdd:cd05941 299 psVFKEYWNKPEAT----KEEFtDDGWFKT-------GDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHP 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05941 368 GVSECAVIGVPDPDWGERVVAVVVLRAGAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
2.44e-43 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 163.31 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIIWEgDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNvddalknpnvTSVEHVVVLKRTGGKIDwqeGRDLWWHDLVEQASDQHQ 249
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQEDA----------TPLRHICLTRVALPADD---GVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 AEEMNAEDPLFILYTSGSTGKPKGVLHTT-----GGYlvYAALTFKYVFDyhpgDIYW-----------CTAdvgwvtgh 313
Cdd:PRK08008 167 APPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLtvmpafhidcqCTA-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 314 sylLYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTD--RSSLRILgsvgePIN 391
Cdd:PRK08008 233 ---AMAAFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclREVMFYL-----NLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 392 PEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLPGAtELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwP 471
Cdd:PRK08008 301 DQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV-P 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 472 GqaRTLFgdherfeQTYF----STFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK08008 376 G--KTIF-------KEYYldpkATAKVLeadgwLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08008 447 QDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
88-615 |
5.98e-43 |
|
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: 161.60 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 88 ENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:cd12117 9 RTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 168 PEAVAGRIIDSNSRLVIT--SDEGVRAGRSIPLkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdLVEQAS 245
Cdd:cd12117 83 AERLAFMLADAGAKVLLTdrSLAGRAGGLEVAV-----------------------------------------VIDEAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 246 DQHQAEEMN----AEDPLFILYTSGSTGKPKGVLHTTGGY--LV----YAALTfkyvfdyhPGDIYWCTADVGWvTGHSY 315
Cdd:cd12117 122 DAGPAGNPAvpvsPDDLAYVMYTSGSTGRPKGVAVTHRGVvrLVkntnYVTLG--------PDDRVLQTSPLAF-DASTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 316 LLYGPLACGAT-TLMFEGVPnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEPINPEa 394
Cdd:cd12117 193 EIWGALLNGARlVLAPKGTL--LDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPP- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 wewyWKKIGNEKCP---VVDTWWQTETGGF----MITPL-PGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVI 466
Cdd:cd12117 265 ----HVRRVLAACPglrLVNGYGPTENTTFttshVVTELdEVAGSIPIG---RPIANTRVYVLDEDGRPVPPGVPGELYV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 tdSWPGQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:cd12117 338 --GGDGLALGYLNRpaltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPspelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 416 REAVVVVREDAGGDKRLVAYVVAEGALDA-----AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
4.84e-42 |
|
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: 158.25 E-value: 4.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHLQENGDRTAIIwegddaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 164 GGFSPEAVAGRIIDSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveq 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 244 asdqhqaeemNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAALTFkyvfdyhPGDiYWctADVGWVTG-----HSY 315
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAF-------SAE-EL--AGVLASTSicfdlSVF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 316 LLYGPLACGATTLMFEGVPNWPT-PARMaqvvdkhQVNILYTAPTAIRALMAEGDKAiegtdrSSLRILGSVGEPINPEA 394
Cdd:cd12115 163 ELFGPLATGGKVVLADNVLALPDlPAAA-------EVTLINTVPSAAAELLRHDALP------ASVRVVNLAGEPLPRDL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 WEWYWKKIGNEKcpVVDTWWQTETGGF-MITPLPGATElKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQ 473
Cdd:cd12115 230 VQRLYARLQVER--VVNLYGPSEDTTYsTVAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYI--GGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 474 ARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd12115 305 ARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 550 IPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 385 IGDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
1.93e-41 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 156.64 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 86 LQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:cd05945 1 AAANPDRPAVVEGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 166 FSPEAVAgRIIDSnsrlvitsdegvragrSIPlkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhDLVEQAS 245
Cdd:cd05945 75 SPAERIR-EILDA----------------AKP-----------------------------------------ALLIADG 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 246 DqhqaeemnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYvFDYHPGDIYWCTADVGW---VTGhsylLYGPLA 322
Cdd:cd05945 97 D----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFdlsVMD----LYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATTlmfegvpnWPTP-------ARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGEPI-NPEA 394
Cdd:cd05945 162 SGATL--------VPVPrdatadpKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLpHKTA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 WEWywkKIGNEKCPVVDTWWQTET----GGFMITPLP--GATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVITD 468
Cdd:cd05945 232 RAL---QQRFPDARIYNTYGPTEAtvavTYIEVTPEVldGYDRLPIG---YAKPGAKLVILDEDGRPVPPGEKGELVISG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 swPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd05945 306 --PSVSKGYLNNPEKTAAAFFPDEGQrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 548 VGIPHNIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 384 VPKYKGEKVTELIAFVVPKPGAEAGLT--KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
2.93e-41 |
|
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: 155.71 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspeavagriidsnsrlvitsd 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrSIPLkknvddalkNPNVTSVEHVVVLKRTGGKIdwqegrdlwwhdLVEQASdqhqaeemnAEDPLFILYTSGS 267
Cdd:cd05935 53 -------VVPI---------NPMLKERELEYILNDSGAKV------------AVVGSE---------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegVPNWPTPArMAQVVD 347
Cdd:cd05935 96 TGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL---MARWDRET-ALELIE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 348 KHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGFMITPLP 427
Cdd:cd05935 171 KYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQTHTNPP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 428 GAteLKAGSATRPFFGVQPALVDNE-GNPLEGATEGSLVItdSWPGQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRD 505
Cdd:cd05935 246 LR--PKLQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIEIKGRRFFrTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 506 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgeepsPELYAEVR----- 580
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR------PEYRGKVTeedii 395
|
490 500 510
....*....|....*....|....*....|....*
gi 446000384 581 NWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 396 EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-649 |
3.05e-41 |
|
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: 161.56 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IfggfSPEAVAGRII----DSNSRLVITSDEgvragrsiplkknVDDALKNPNVTSVEhvvvlkrtggkIDWQEgrdlww 237
Cdd:COG1020 556 L----DPAYPAERLAymleDAGARLVLTQSA-------------LAARLPELGVPVLA-----------LDALA------ 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 238 hdlVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIywctadVGWVTGHS--- 314
Cdd:COG1020 602 ---LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfda 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 315 --YLLYGPLACGATTLMF--EGVPNwptPARMAQVVDKHQVNILYTAPTAIRALMAEGdkaieGTDRSSLRILGSVGEPI 390
Cdd:COG1020 672 svWEIFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVGGEAL 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 NPEAWEWYWKKIGNekCPVVDTWWQTETGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPL-EGATeGSLVIt 467
Cdd:COG1020 744 PPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYEVTPPDADGGSVPigRPIANTRVYVLDAHLQPVpVGVP-GELYI- 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 468 dSWPGQARtlfGDHERFEQT--YF--STFKN----MYFSGDGARRDEDG---YywiTGRVDDVLNVSGHR--LGtaEIES 534
Cdd:COG1020 820 -GGAGLAR---GYLNRPELTaeRFvaDPFGFpgarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRieLG--EIEA 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 535 ALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRnwvRKEIGPLATPDVLHWTDSLPKTRSGKimrrI 614
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAAVVLLLPLPLTGNGK----L 963
|
570 580 590
....*....|....*....|....*....|....*
gi 446000384 615 LRKIAAGDTSNLGDTSTLADPGVVEKLLEEKQAIA 649
Cdd:COG1020 964 DRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLL 998
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-617 |
3.92e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 154.43 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 75 LNLAaNCLDRHLQENGDRTAIIWeGDdasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 155 IGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD---EGVRAGRSIPLkknvddalknpnvtSVEHVVVLKRTGGKIDWQe 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASP--------------DLTHVVAIGGARAGLDYE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 232 grdlwwhDLV-EQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaalTFKYVFDYHPGDIYWCT--ADVG 308
Cdd:PRK07470 145 -------ALVaRHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG--------QMAFVITNHLADLMPGTteQDAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 WVT-------GHSYLLygPLACGATTLMFEGVPNwpTPARMAQVVDKHQVNILYTAPTaIRALMAEgDKAIEGTDRSSLR 381
Cdd:PRK07470 210 LVVaplshgaGIHQLC--QVARGAATVLLPSERF--DPAEVWALVERHRVTNLFTVPT-ILKMLVE-HPAVDRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 382 ILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGfMITPLPGA-------TELKAGSATRPFFGVQPALVDNEGN 454
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTG-NITVLPPAlhdaedgPDARIGTCGFERTGMEVQIQDDEGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 455 PLEGATEGSL-VItdswpGQArtLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK07470 360 ELPPGETGEIcVI-----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 533 ESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
....*
gi 446000384 613 RILRK 617
Cdd:PRK07470 510 KMVRE 514
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-615 |
1.08e-39 |
|
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: 152.28 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfspea 170
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 vagriidsNSRLviTSDEgvragrsiplkknVDDALKNPNVTSVEHVVVLKRTGGKIDwQEGRDLWWHDLV-----EQAS 245
Cdd:cd05923 84 --------NPRL--KAAE-------------LAELIERGEMTAAVIAVDAQVMDAIFQ-SGVRVLALSDLVglgepESAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 246 DQHQAEEMNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLvYAA--LTFKYVFDYHpgdiywctadvgwV 310
Cdd:cd05923 140 PLIEDPPREPEQPAFVFYTSGTTGLPKGAvipqraaesrvlfMSTQAGLR-HGRhnVVLGLMPLYH-------------V 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 311 TGHSYLLYGPLACGATTLmfegVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPI 390
Cdd:cd05923 206 IGFFAVLVAALALDGTYV----VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGATM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 NPEAWEWYWKKIGNEKcpvVDTWWQTETGGFMITPLPgatelKAGSATRPFFGVQPALVDNEGNPLEGAT---EGSLVIT 467
Cdd:cd05923 280 PDAVLERVNQHLPGEK---VNIYGTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEALAngeEGELIVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 468 DS----WPGQARtlfgdheRFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIA 543
Cdd:cd05923 352 AAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVT 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNwvrKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05923 425 EVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
87-618 |
3.87e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 151.62 E-value: 3.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 87 QENGDRTAIIwegDDASQskhISYKELHRDVCRFANTLLELGIKKGDVVAI----YMPMVpeaaVAMLACARIGAVHSVI 162
Cdd:PRK07788 60 RRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 163 FGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPlkknvddalknPNVTSVeHVVVLKRTGGKIDWQEGRDLwwHDLVE 242
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRL-RAWGGNPDDDEPSGSTDETL--DDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 243 QASDQhqaeemnaedPL--------FILYTSGSTGKPKGVLH-TTGGYLVYAALtfkyvFDYHP---GDIYWCTADVGWV 310
Cdd:PRK07788 196 GSSTA----------PLpkppkpggIVILTSGTTGTPKGAPRpEPSPLAPLAGL-----LSRVPfraGETTLLPAPMFHA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 311 TGHSYLLYGpLACGATTLM---FEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK07788 261 TGWAHLTLA-MALGSTVVLrrrFD-------PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEAWEWYWKKIGnekcPVV-DTWWQTETGGFMI-TPlpgaTELKAGSAT--RPFFGVQPALVDNEGNPLEGATEGS 463
Cdd:PRK07788 333 SALSPELATRALEAFG----PVLyNLYGSTEVAFATIaTP----EDLAEAPGTvgRPPKGVTVKILDENGNEVPRGVVGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 464 LVITDSWPGQARTLFGDHERFeqtyfstfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIA 543
Cdd:PRK07788 405 IFVGNGFPFEGYTDGRDKQII--------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVV 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK07788 477 EAAVIGVDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-615 |
1.53e-38 |
|
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: 148.59 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIiwEGDDASqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd12116 1 PDATAV--RDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSDEGVRAGRsiplkknvddalknpnvtsvehvvvlkrtggkidwqeGRDLWWHDLVEQASDQH- 248
Cdd:cd12116 75 RLRYILEDAEPALVLTDDALPDRLP-------------------------------------AGLPVLLLALAAAAAAPa 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 249 -QAEEMNAEDPLFILYTSGSTGKPKGVlHTTGGYLVYAALTFKYVFDYHPGD----IYWCTADVgwvtghSYL-LYGPLA 322
Cdd:cd12116 118 aPRTPVSPDDLAYVIYTSGSTGRPKGV-VVSHRNLVNFLHSMRERLGLGPGDrllaVTTYAFDI------SLLeLLLPLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATTLMFEGVPNwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGdkaieGTDRSSLRIL-GsvGEPINPEawewywkk 401
Cdd:cd12116 191 AGARVVIAPRETQ-RDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAGLTALcG--GEALPPD-------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 402 IGNEKCPVVDTWWQ----TETggfmiTPLPGATELKAGSAT----RPFFGVQPALVDNEGNPLEGATEGSLVITDswPGQ 473
Cdd:cd12116 255 LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPipigRPLANTQVYVLDAALRPVPPGVPGELYIGG--DGV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 474 ARTLFGD----HERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd12116 328 AQGYLGRpaltAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 549 GIPHNIKGQaIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12116 408 VREDGGDRR-LVAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
1.02e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 147.34 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIIWeGDDAsqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSDEgvRAGRsiplkknVDDALknPNVTSVEHVVVLKRTGGKIDWQEGRDlwWHDLVEQASDQHQ 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPR-------VAEVL--PRLPKLRTLVVVEDGSGNDLLPGAVD--YEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 AEEMNAEDpLFILYTSGSTGKPKGVL-------HTTGGYLVYAALTFkyvfdyhPGDIYWCTADVGWVTGHSYLLYGPLA 322
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMwrqedifRVLLGGRDFATGEP-------IEDEEELAKRAAAGPGMRRFPAPPLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATTL-----MFEG----VPNWPT--PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPIN 391
Cdd:PRK07798 230 HGAGQWaafaaLFSGqtvvLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 392 PEAWEWYWKKIGNekCPVVDTWWQTETGgFMITplpGATELKAGSATRPFFGVQP--ALVDNEGNPLEGATEGSLVItds 469
Cdd:PRK07798 310 PSVKEALLELLPN--VVLTDSIGSSETG-FGGS---GTVAKGAVHTGGPRFTIGPrtVVLDEDGNPVEPGSGEIGWI--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 wpgqART------LFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK07798 381 ----ARRghiplgYYKDPEKTAETFPTIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK07798 457 ADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
2.69e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 146.46 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 79 ANCLDRHLQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 159 HSVIFGGFSPEAVAGRIIDSNSRLVITsdEGVRAgrsiPLKKNVDDAlknpnVTSVEHVVVLkrtGGKIDwqeGRDLWWH 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALA----PVATAVRDI-----VPLLSTVVVA---GGSSD---DSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 239 DLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAALTFKYVFDYH-PGDIYWCTADVGWVTGHSY 315
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 316 LLYGpLACGATTLMFegvpnwPT----PARMAQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRsSLRILGSVGEPIN 391
Cdd:PRK07786 234 MLPG-LLLGAPTVIY------PLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDL-ALRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 392 PEAWEWYwkkigNEKCP---VVDTWWQTEtggfmITP----LPGATEL-KAGSATRPFFGVQPALVDNEGNPLEGATEGS 463
Cdd:PRK07786 304 DTLLRQM-----AATFPeaqILAAFGQTE-----MSPvtcmLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 464 LVItdswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK07786 374 IVY------RAPTLMSGYWNNPEATAEAFAGGWFhSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEpSPELyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK-IAAG 621
Cdd:PRK07786 448 VEVAVIGRADEKWGEVPVAVAAVRNDDA-ALTL-EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErYGAC 525
|
570
....*....|
gi 446000384 622 DTSNLGDTST 631
Cdd:PRK07786 526 VNVERRSASA 535
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
82-620 |
1.70e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 144.15 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEgddaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12583 24 FDATVARFPDREALVVR----HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVI------TSDEGVRAGRSIP-LKKNVDDALKNPNVTSVEHVVVL--KRTGGKidwqeg 232
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVIcadafkTSDYHAMLQELLPgLAEGQPGALACERLPELRGVVSLapAPPPGF------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 233 rdLWWHDLV---EQASDQHQAE---EMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAALTF----KYVFdyhP 297
Cdd:PRK12583 174 --LAWHELQargETVSREALAErqaSLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---P 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 298 GDIYWC----TADVGWVTGHSYLLY-----GPLAcgatTLmfegvpnwptparmaQVVDKHQVNILYTAPTAIRALMAEG 368
Cdd:PRK12583 249 VPLYHCfgmvLANLGCMTVGACLVYpneafDPLA----TL---------------QAVEEERCTALYGVPTMFIAELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 369 DKAieGTDRSSLRILGSVGEPINPEAWEwywKKIGNEKCP-VVDTWWQTETGGfmITPLPGAT---ELKAGSATRPFFGV 444
Cdd:PRK12583 310 QRG--NFDLSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAAddlERRVETVGRTQPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 445 QPALVDNEGNPL------EGATEGSLVITDSWpgqartlfGDHERfeqTYFSTFKN--MYfSGDGARRDEDGYYWITGRV 516
Cdd:PRK12583 383 EVKVVDPDGATVprgeigELCTRGYSVMKGYW--------NNPEA---TAESIDEDgwMH-TGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 517 DDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVL 596
Cdd:PRK12583 451 KDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYF 527
|
570 580
....*....|....*....|....
gi 446000384 597 HWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12583 528 RFVDEFPMTVTGKVQKFRMREISI 551
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
2.69e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 144.09 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEGVragrsipLKKnVDDALKnpNVTSVEHVVVLKRTGGK-----IDWQE----G 232
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRD--ELPSLRHIVVLDPRGLRddprlLSLDEllalG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 233 RDLWWHDLVEQASDQHQaeemnAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIY-----WCtadv 307
Cdd:COG1022 165 REVADPAELEARRAAVK-----PDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 308 gWVTGHSyLLYGPLACGAT-------------------TLMFeGVP-------------------------NW--PTPAR 341
Cdd:COG1022 235 -HVFERT-VSYYALAAGATvafaespdtlaedlrevkpTFML-AVPrvwekvyagiqakaeeagglkrklfRWalAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 342 MAQVVDKHQvnilyTAPTAIRALMAEGDKAIegtdRSSLR-ILG-------SVGEPINPEAWEWYWkKIGnekCPVVDTW 413
Cdd:COG1022 312 YARARLAGK-----SPSLLLRLKHALADKLV----FSKLReALGgrlrfavSGGAALGPELARFFR-ALG---IPVLEGY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 414 WQTETGGFMITPLPGATelKAGSATRPFFGVQpalV----DNE-------------GNPleGATegslvitdswpgqART 476
Cdd:COG1022 379 GLTETSPVITVNRPGDN--RIGTVGPPLPGVE---VkiaeDGEilvrgpnvmkgyyKNP--EAT-------------AEA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 477 LFGDHerfeqtYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGhrlGT----AEIESALVAHPKIAEAAVVG 549
Cdd:COG1022 439 FDADG------WLHT-------GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
70-617 |
2.96e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 143.60 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 70 YEDGTLnlaANCLDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAM 149
Cdd:PRK05605 29 YGDTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 150 LACARIGAV---HSVIFggfSPEAVAGRIIDSNSRLVITSDegvragrsiplkKNVDDALKNPNVTSVEHVV-------- 218
Cdd:PRK05605 100 YAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWD------------KVAPTVERLRRTTPLETIVsvnmiaam 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 219 -VLKRTGGKI---DWQEGRD---------LWWHDLVEQA----SDQHQAEEMNAEDPLFILYTSGSTGKPKGvlhttggy 281
Cdd:PRK05605 165 pLLQRLALRLpipALRKARAaltgpapgtVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKG-------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 282 lvyAALTFKYVFdyhpgdiywCTADVG--WVTG---------------HSY-----LLYGPLaCGATTLMFegvpnwPTP 339
Cdd:PRK05605 237 ---AQLTHRNLF---------ANAAQGkaWVPGlgdgpervlaalpmfHAYgltlcLTLAVS-IGGELVLL------PAP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 340 aRMAQVVD---KHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEawewywkkignekcpVVDTWwQT 416
Cdd:PRK05605 298 -DIDLILDamkKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMALPVS---------------TVELW-EK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 417 ETGGFMI--------TPL----PGATELKAGSATRPFFGVQPALVDNEgNPLEG---ATEGSLVItdswpgQARTLF-GD 480
Cdd:PRK05605 359 LTGGLLVegygltetSPIivgnPMSDDRRPGYVGVPFPDTEVRIVDPE-DPDETmpdGEEGELLV------RGPQVFkGY 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 481 HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIY 560
Cdd:PRK05605 432 WNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVV 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 561 AYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 512 AAVVLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
2.11e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 141.32 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 106 KHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 186 SDegvragRSIPLKKNVDDAlknpnvTSVEHVVVL-------------------KRTGGKIDWQEGRDLWWHDLVEQASD 246
Cdd:PRK06710 128 LD------LVFPRVTNVQSA------TKIEHVIVTriadflpfpknllypfvqkKQSNLVVKVSESETIHLWNSVEKEVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 247 QHQAEEMNAEDPLFIL-YTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDiywctaDVGWVTGHSYLLYGPLACGA 325
Cdd:PRK06710 196 TGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TTLMfEGVPNWPTPA---RMA-QVVDKHQVNILYTAPTAIRALMaeGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:PRK06710 270 LSIM-QGYKMVLIPKfdmKMVfEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 402 IG---------NEKCPVVDT--WWQTETGGFMITPLPGA----TELKAGSATRPffgvqpalvdneGNPLEGATEGSLVI 466
Cdd:PRK06710 347 TGgklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKGPQIM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 TDSWpgqartlfgdhERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAA 546
Cdd:PRK06710 415 KGYW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 547 VVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-623 |
2.16e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 139.94 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLvITSDE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 GVRAGRSIPLkknvddalknpnvtsvehvvvlkrtggkidwqegrDLwwhDLVEQASDQHQ---AEEMNAEDPLFILYTS 265
Cdd:PRK09088 103 AVAAGRTDVE-----------------------------------DL---AAFIASADALEpadTPSIPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQV 345
Cdd:PRK09088 145 GTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 346 vdKHQVNILYTAPTAIRALMAEgdkaiEGTDRSSLRILGSV---GEPiNPEAWEWYWKKIGnekCPVVDTWWQTETGGFM 422
Cdd:PRK09088 224 --ALGITHYFCVPQMAQAFRAQ-----PGFDAAALRHLTALftgGAP-HAAEDILGWLDDG---IPMVDGFGMSEAGTVF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 423 ITPL-PGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVIT--DSWPGQARTLFGDHERF-EQTYFSTfknmyfs 498
Cdd:PRK09088 293 GMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAFtGDGWFRT------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 499 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGeepSPELYAE 578
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLER 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446000384 579 VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR-KIAAGDT 623
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRdALAAGRK 488
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
3.40e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 140.27 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwegDDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DNHGAS--YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVI--TSDEGVR-AGRSIPLKKNVDdalknpnvtSVEHVVVLKRTGGKIDwqegrDLWWHDLVEQASDQ 247
Cdd:PRK06087 113 LVWVLNKCQAKMFFapTLFKQTRpVDLILPLQNQLP---------QLQQIVGVDKLAPATS-----SLSLSQIIADYEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 248 HQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATT 327
Cdd:PRK06087 179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 328 LMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPInP-----EAWEWYWKki 402
Cdd:PRK06087 258 VLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PkkvarECQQRGIK-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 403 gnekcpVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVitDSWPGQARTLFGDHE 482
Cdd:PRK06087 329 ------LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA--SRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 483 RfeqtyfsTFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQ 557
Cdd:PRK06087 401 L-------TARALdeegwYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 558 AIYAYVTLNhGEEPSPELyAEVRNWV-RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 474 RSCAYVVLK-APHHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
88-621 |
1.08e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.02 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 88 ENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:PRK12316 4563 MTPDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 168 PEAVAGRIIDSNSRLVITSDegvRAGRSIPLKKNVddalknpnvtsveHVVVLKRTGgkiDWqEGRdlwwhdlveqaSDQ 247
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQS---HLLQRLPIPDGL-------------ASLALDRDE---DW-EGF-----------PAH 4685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 248 HQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTfkyvfdyhpGDIYWCTADVGWVTGHSYL-------LYGP 320
Cdd:PRK12316 4686 DPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYHP 4756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 LACGATTLMFEgvPNWPTPARMAQVVDKHQVNILYTAPTAIRALmAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:PRK12316 4757 LINGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAWR 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNEKcpVVDTWWQTETggfMITPL---------PGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVITDSwp 471
Cdd:PRK12316 4832 ALKPVY--LFNGYGPTET---TVTVLlwkardgdaCGAAYMPIG---TPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-- 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 472 GQARTLFG----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAA 546
Cdd:PRK12316 4902 GVARGYLErpalTAERFVPDPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 547 VVGIPHNIkGQAIYAYVTLNHGE-EPSPELYAEVRNWVRKEIGPlATPDVL---HWT--DSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12316 4982 VIAQEGAV-GKQLVGYVVPQDPAlADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLTPNGKLDRKALPQPDA 5059
|
.
gi 446000384 621 G 621
Cdd:PRK12316 5060 S 5060
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-622 |
2.13e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.25 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvRAGRSIPLKKNVDdalknpnvtsvehVVVLKRTGgkidwqegrdLWwhdlVEQASDQHQAEEMNAEDPLFILYTSGS 267
Cdd:PRK12316 617 ---HLGRKLPLAAGVQ-------------VLDLDRPA----------AW----LEGYSEENPGTELNPENLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHsYLLYGPLACGATtLMFEGVPNWPTPARMAQVVD 347
Cdd:PRK12316 667 TGKPKGAGNRHRA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGAR-LVVAAPGDHRDPAKLVELIN 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 348 KHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTETGgfmiTPLP 427
Cdd:PRK12316 744 REGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQ--AGLYNLYGPTEAA----IDVT 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 428 GATELKAGSAT----RPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQARTLFG----DHERFEQTYFSTFKNMYFSG 499
Cdd:PRK12316 814 HWTCVEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAGERMYRTG 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 500 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEEPSPELYAEV 579
Cdd:PRK12316 892 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL---ESEGGDWREAL 964
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446000384 580 RNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 965 KAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
2.86e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 137.13 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 83 DRHLQENGDRTAIIWEGDDASqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGEV----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 163 FGGFSPEAVAGRIIDSNSRLVITSdegvRAGRSIplkknVDDALKNpnVTSVEHVVVLKRTGGKIDWQEgrdlwWHDLVE 242
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITS----AAKLDV-----ARALLKQ--CPGVRHRLVLDGDGELEGFVG-----YAEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 243 QASDQHQAEEMNAEDplfILYTSGSTGKPKGVL---------HTTGgylvYAALtFKYVFDYHPGDIYWCTADVGwvtgH 313
Cdd:PRK13391 144 GLPATPIADESLGTD---MLYSSGTTGRPKGIKrplpeqppdTPLP----LTAF-LQRLWGFRSDMVYLSPAPLY----H 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 314 SyllyGPLA-------CGATTLMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSV 386
Cdd:PRK13391 212 S----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 387 GEPINPEAWE----WyWKkignekcPVVDTWW-QTETGGFMITPLPGATElKAGSATRPFFGVqPALVDNEGNPLEGATE 461
Cdd:PRK13391 284 AAPCPPQVKEqmidW-WG-------PIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDDGAELPPGEP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 462 GSLvitdsWPGQARTL--FGDHE-----RFEQTYFSTfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK13391 354 GTI-----WFEGGRPFeyLNDPAktaeaRHPDGTWST------VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAEN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 535 ALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK13391 423 LLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRL 502
|
..
gi 446000384 615 LR 616
Cdd:PRK13391 503 LR 504
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-623 |
3.97e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 137.48 E-value: 3.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 87 QENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggf 166
Cdd:PRK06178 44 RERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 167 SPEAVAGRII----DSNSRLVITSDegvragRSIPLKKNVDDAlknpnvTSVEHVVVLKRTG-----------GKIDWQE 231
Cdd:PRK06178 114 SPLFREHELSyelnDAGAEVLLALD------QLAPVVEQVRAE------TSLRHVIVTSLADvlpaeptlplpDSLRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 232 GRDLWWHDL---VEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGgYLVYAALTFKYVfdYHPGDiywcTADVG 308
Cdd:PRK06178 182 LAAAGAIDLlpaLRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR-DMVYTAAAAYAV--AVVGG----EDSVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 -------WVTGHSYLLYGPLACGATTLMfegVPNWPTPARMAqVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLR 381
Cdd:PRK06178 255 lsflpefWIAGENFGLLFPLFSGATLVL---LARWDAVAFMA-AVERYRVTRTVMLVDNAVELMDHPRFA--EYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 382 ILGSVG--EPINPEawewYWKKignekcpvvdtwWQTETGGFMITPLPGATE------LKAGSAT-------RPFF---- 442
Cdd:PRK06178 329 QVRVVSfvKKLNPD----YRQR------------WRALTGSVLAEAAWGMTEthtcdtFTAGFQDddfdllsQPVFvglp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 443 --GVQPALVDNE-GNPLEGATEGSLVItdswpgqaRT---LFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRV 516
Cdd:PRK06178 393 vpGTEFKICDFEtGELLPLGAEGEIVV--------RTpslLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 517 DDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVl 596
Cdd:PRK06178 465 KEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAVYKVPEI- 540
|
570 580
....*....|....*....|....*..
gi 446000384 597 HWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK06178 541 RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
5.60e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 135.26 E-value: 5.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 117 VCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEavagrIIDSNSRLVITsdegVRAGRSI 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 197 PLKKNVDDALKNPNVTSVEHVVVLkrtggkidwqeGRDLWWHdlveqASDQHQAEEMNAEDPLFILYTSGSTGKPKGVL- 275
Cdd:cd05922 74 LADAGAADRLRDALPASPDPGTVL-----------DADGIRA-----ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 276 -HTTggyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFE-GVPnwptPARMAQVVDKHQVNI 353
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNdGVL----DDAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 354 LYTAPTaIRALMAEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYwkkigNEKCP---VVDTWWQTETGGFMiTPLPGAT 430
Cdd:cd05922 210 LAGVPS-TYAMLTRLGFDPAKL--PSLRYLTQAGGRLPQETIARL-----RELLPgaqVYVMYGQTEATRRM-TYLPPER 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 431 EL-KAGSATRPFFGVQPALVDNEGNPL------EGATEGSLVITDSWPGQArtlfgdherfEQTYFSTFKNMYFSGDGAR 503
Cdd:cd05922 281 ILeKPGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYWNDPP----------YRRKEGRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIkGQAIYAYVTLNHGEEPSPelyaeVRNWV 583
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-----VLRSL 424
|
490 500 510
....*....|....*....|....*....|...
gi 446000384 584 RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
8.58e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 132.60 E-value: 8.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 263 YTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA-- 340
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV-------LAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 341 -------RMAQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGnekCPVVDTW 413
Cdd:cd05944 81 rnpglfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 414 WQTE-TGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLE---GATEGSLVItdswpgQARTLFGDHERFEQTYF 489
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRdcaPDEVGEICV------AGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 490 STFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:cd05944 228 AFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 569 EEPSPElyaEVRNWVRKEIGP-LATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05944 308 AVVEEE---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
91-615 |
1.38e-33 |
|
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: 134.76 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA 170
Cdd:cd17655 12 DHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI----DPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRII----DSNSRLVIT---SDEGVRAGRSIPLKKnvDDALKNPNVTSVEHVVvlkrtggkidwqegrdlwwhdlveq 243
Cdd:cd17655 82 PEERIQyileDSGADILLTqshLQPPIAFIGLIDLLD--EDTIYHEESENLEPVS------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 244 asdqhqaeemNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLVYAALTF----KYVFDYHPGDIYwctadvg 308
Cdd:cd17655 135 ----------KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankvIYQGEHLRValfaSISFDASVTEIF------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 wvtghsyllyGPLACGATTLMFEGVPNWPTPARMaQVVDKHQVNILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGE 388
Cdd:cd17655 198 ----------ASLLSGNTLYIVRKETVLDGQALT-QYIRQNRITIIDLTPAHLKLLDAADD-----SEGLSLKHLIVGGE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 389 PINPEAWEwYWKKIGNEKCPVVDTWWQTETG-GFMITPLPGATELKAG-SATRPFFGVQPALVDNEGNPLEGATEGSLVI 466
Cdd:cd17655 262 ALSTELAK-KIIELFGTNPTITNAYGPTETTvDASIYQYEPETDQQVSvPIGKPLGNTRIYILDQYGRPQPVGVAGELYI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 tdSWPGQARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:cd17655 341 --GGEGVARGYLNrpelTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDI 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTlnhGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17655 419 KEAVVIARKDEQGQNYLCAYIV---SEKELPV--AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
1.97e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 134.87 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 79 ANCLDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 159 HSVIFGGFSPEAVAGRIIDSNSRLVITSDegvrAGRSIPLKKNVDDALKNpNVTSVEHVVVLKRTGGKI-DWQEGRDLWW 237
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPD-ALPPLRAIAVVDDAADATpAPAPGARVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 238 HDLVEQASDQHQAEEMNAEDPLFILY-TSGSTGKPKGVLHTTGGYLVYAALTFKyVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:PRK06164 162 FALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LyGPLACGATTLM---FEGvpnwptpARMAQVVDKHQVNILYTAPTAIRALMAEGDkaiEGTDRSSLRILGSVG-EPINP 392
Cdd:PRK06164 241 L-GALAGGAPLVCepvFDA-------ARTARALRRHRVTHTFGNDEMLRRILDTAG---ERADFPSARLFGFASfAPALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 393 EAWEWywkkignekcpvvdtwwqTETGGFMITPLPGATELKAgsatrpFFGVQPALVDNE------GNPLEGATE----- 461
Cdd:PRK06164 310 ELAAL------------------ARARGVPLTGLYGSSEVQA------LVALQPATDPVSvrieggGRPASPEARvrard 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 462 ---GSLV-------ITDSWPGQARTLFGDHERFEQTYFStfkNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK06164 366 pqdGALLpdgesgeIEIRAPSLMRGYLDNPDATARALTD---DGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 531 EIESALVAHPKIAEAAVVGIPHniKGQAI-YAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG- 608
Cdd:PRK06164 443 EIEHALEALPGVAAAQVVGATR--DGKTVpVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAn 517
|
570
....*....|...
gi 446000384 609 --KIMRRILRKIA 619
Cdd:PRK06164 518 gaKIQKHRLREMA 530
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
3.80e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 133.16 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEGVRagrsiplkknvddalknpnvtsvEHVVvlkrtGGKIDWQEgrdlwwhdlVEQASDQHQA 250
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA-----------------------KLIP-----GISVKFAE---------LMNGPKEEAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 --EEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLL----YG-PLac 323
Cdd:PRK03640 134 iqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMrsviYGmRV-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 gatTLM--FEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaiEGTDRSSLR--ILGsvGEPINPEAWEwyw 399
Cdd:PRK03640 211 ---VLVekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLG---EGTYPSSFRcmLLG--GGPAPKPLLE--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 400 kkIGNEK-CPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNeGNPLEGATEGSLVItdswpgQARTLF 478
Cdd:PRK03640 273 --QCKEKgIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV------KGPNVT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 479 GDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQ 557
Cdd:PRK03640 344 KGYLNREDATRETFQDGWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 558 AIYAYVTlnHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 424 VPVAFVV--KSGEVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-617 |
4.77e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.83 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 83 DRHLQENGDRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK12467 519 EAQARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 163 FGGFSPEAVAGRIIDSNSRLVITSDEGVRagrsiplKKNVDDALKnpnvtsvehVVVLKRTGgkidwqegrdlwwhDLVE 242
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLA-------QLPVPAGLR---------SLCLDEPA--------------DLLC 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 243 QASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYvfdyhpgdiYWCTADVGWVTGHSY------- 315
Cdd:PRK12467 643 GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvt 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 316 LLYGPLACGATTLMFEGVPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIegtDRSSLRILgsVGEPINPEAW 395
Cdd:PRK12467 714 ELFGALASGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL---PRPQRALV--CGGEALQVDL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWYWKKIGNEkCPVVDTWWQTETG-GFMITPLPGATELKAGSAT-RPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQ 473
Cdd:PRK12467 788 LARVRALGPG-ARLINHYGPTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 474 ARTLFG----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:PRK12467 865 ARGYHRrpalTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 549 GIPhNIKGQAIYAYVTLNHGEEPS--PELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 945 AQP-GDAGLQLVAYLVPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-615 |
1.08e-32 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 131.22 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17652 2 DAPAVVFGDE------TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqa 250
Cdd:cd17652 76 IAYMLADARPALLLTT---------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 eemnAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAALTFkyvFDYHPGDIYWCTADVGWVTGHSYLLyGPLACGATTL 328
Cdd:cd17652 92 ----PDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSFDASVWELL-MALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 329 MFEGVPNWPTPArMAQVVDKHQVNILYTAPTAIRALMAEGDKAiegtdrssLRILGSVGEPINPEawewywkkignekcp 408
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAE--------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 409 VVDTWWQ----------TET--GGFMITPLPGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQARt 476
Cdd:cd17652 220 LVDRWAPgrrminaygpTETtvCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYI--AGAGLAR- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 477 lfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd17652 294 --GYLnrpgltaERFVADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 549 GIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 372 VRDDRPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-617 |
1.50e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.47 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITsDEGVRAGRSIPlkknvddalknpnvtsvEHVVVLKRTggkidwqegRDLWWHDLveqaSDQHQA 250
Cdd:PRK12316 2092 LAYMLEDSGAALLLT-QRHLLERLPLP-----------------AGVARLPLD---------RDAEWADY----PDTAPA 2140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 EEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYvFDYHPGDIYWCTADVGWVTGHSYLLYgPLACGATTLMF 330
Cdd:PRK12316 2141 VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFH-PLLNGARVLIR 2218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 331 EGvPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEgdKAIEGtDRSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVV 410
Cdd:PRK12316 2219 DD-ELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEH--AERDG-RPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LF 2291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 411 DTWWQTETggfMITPL---------PGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQARTLFG-- 479
Cdd:PRK12316 2292 NGYGPTEA---VVTPLlwkcrpqdpCGAAYVPIG---RALGNRRAYILDADLNLLAPGMAGELYLGGE--GLARGYLNrp 2363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 480 --DHERFEQTYFS-TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIpHNIKG 556
Cdd:PRK12316 2364 glTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASG 2442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 557 QAIYAYVTlnhGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 2443 KQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-616 |
3.82e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.39 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 85 HLQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 165 GFSPEAVAGRIIDSNSRLVITsDEGVRAGRSIPLKKNVDDALKNPNVTsvehvvVLKRTGgkidwqegrdlwwhdlvEQA 244
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLV-DEEFDAIVALETPKIVIDAAAQADSR------RLAQGG-----------------LEI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 245 SDQHQAEEmnaEDPLFILYTSGSTGKPKGVLHTTggylvyaaltfkyvfdyhpGDIYWCTAD----VGWVTGHSYLLYGP 320
Cdd:PRK06145 141 PPQAAVAP---TDLVRLMYTSGTTDRPKGVMHSY-------------------GNLHWKSIDhviaLGLTASERLLVVGP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 L----AC---GATTLMFEG---VPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRilgsvgepi 390
Cdd:PRK06145 199 LyhvgAFdlpGIAVLWVGGtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLA--------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 npeawewyWKKIGNEKCP---------------VVDTWWQTETGGfMITPLPGATEL-KAGSATRPFFGVQPALVDNEGN 454
Cdd:PRK06145 268 --------WCIGGGEKTPesrirdftrvftrarYIDAYGLTETCS-GDTLMEAGREIeKIGSTGRALAHVEIRIADGAGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 455 PLEGATEGSLVITDswPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK06145 339 WLPPNMKGEICMRG--PKVTKGYWKDPEKTAEAFYGDW---FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 535 ALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRV 490
|
..
gi 446000384 615 LR 616
Cdd:PRK06145 491 LR 492
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
108-617 |
4.16e-32 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 129.00 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspeavagrIIDSNSRLVItsd 187
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE----------------AVLLNTRLTP--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwHDLVEQASDQhqaeEMNAEDPLFILYTSGS 267
Cdd:cd05912 63 --------------------------------------------------NELAFQLKDS----DVKLDDIATIMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYLvYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnwptPARMAQV 345
Cdd:cd05912 89 TGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVdkFD-------AEQVLHL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 346 VDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLR--ILGsvGEPINPEAWEwywkkigneKC-----PVVDTWWQTET 418
Cdd:cd05912 161 INSGKVTIISVVPTMLQRLLEILG----EGYPNNLRciLLG--GGPAPKPLLE---------QCkekgiPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 419 GGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPlegATEGSLV-----ITDSWPGQARTlfgDHERFEQTYFSTfk 493
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILlkgpnVTKGYLNRPDA---TEESFENGWFKT-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 494 nmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgeepSP 573
Cdd:cd05912 298 -----GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-----RP 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446000384 574 ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 368 ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
103-616 |
5.62e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.20 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 103 SQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRL 182
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 183 VITSDEGVRAGRS-IPLKKNVDDALKNPNVTSVEHVVVLKRT--GGKIDWQEgrdlWWHDlvEQASDQHQAEEmnaedPL 259
Cdd:PRK12406 87 LIAHADLLHGLASaLPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG----WLAQ--QEPYDGPPVPQ-----PQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 260 FILYTSGSTGKPKGVLHT--TGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpn 335
Cdd:PRK12406 156 SMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQprFD---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 wptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA----WEWyWKKIGNEkcpvvd 411
Cdd:PRK12406 232 ---PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEW-WGPVIYE------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 TWWQTETGgfMITplpGATELKA----GSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwpgqARTLFGDHERFEQT 487
Cdd:PRK12406 302 YYGSTESG--AVT---FATSEDAlshpGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA----GNPDFTYHNKPEKR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 488 YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK12406 373 AEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446000384 568 GEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 453 GATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-549 |
7.81e-32 |
|
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: 128.87 E-value: 7.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemnAEDPLFILYTSGS 267
Cdd:cd05907 86 -------------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYL--VYAALTFkyvFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPT------P 339
Cdd:cd05907 99 TGRPKGVMLSHRNILsnALALAER---LPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDdlsevrP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 340 ARMAQV---VDKHQVNILYTAPTAIRALMAegDKAIEGtdrsSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQT 416
Cdd:cd05907 176 TVFLAVprvWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHFF-RALG---IPVYEGYGLT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 417 ETGGFMITPLPGAteLKAGSATRPFFGVQPALV-DNE-------------GNPLEGATEgslVITDSWpgqartlfgdhe 482
Cdd:cd05907 246 ETSAVVTLNPPGD--NRIGTVGKPLPGVEVRIAdDGEilvrgpnvmlgyyKNPEATAEA---LDADGW------------ 308
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 483 rfeqtyFSTfknmyfsGDGARRDEDGYYWITGRVDDVL-NVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd05907 309 ------LHT-------GDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
91-618 |
1.62e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.82 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwegddaSQSKHISYKELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSDEGVRAGRSIPlkknvddalknpNVTSVEHVVvlkrtggkidwqegrdlWWHDLVEqaSDQHQ 249
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSMQ------------KVSYVQRVI-----------------SITSLKE--IEDRK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 ---AEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PRK06839 140 idnFVEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 327 TLmfegVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPInPEAWEWYWKKIGnek 406
Cdd:PRK06839 219 II----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVRWFYNGGAPC-PEELMREFIDRG--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 407 CPVVDTWWQTETGG--FMITPLPGATelKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdswpgQARTLFGDHERF 484
Cdd:PRK06839 289 FLFGQGFGMTETSPtvFMLSEEDARR--KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI------RGPNVMKEYWNR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 485 EQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYV 563
Cdd:PRK06839 361 PDATEETIQDGWLcTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 564 TLNHGeepSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK06839 441 VKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
108-615 |
1.64e-31 |
|
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: 127.97 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITsd 187
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemNAEDPLFILYTSGS 267
Cdd:cd17650 91 ------------------------------------------------------------------QPEDLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYL-VYAALTFKYVFDYHPGDIYWctadvgwVTGHSY-LLYGPLAcgaTTLMFEG----VPN--WPTP 339
Cdd:cd17650 105 TGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFdVFAGDFA---RSLLNGGtlviCPDevKLDP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 340 ARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRIL--GSVGEPINPEAWEWywKKIGnEKCPVVDTWWQTE 417
Cdd:cd17650 175 AALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKAQDFKTLA--ARFG-QGMRIINSYGVTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 418 ----TGGFMIT--PLPGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQARTLFGD----HERFEQT 487
Cdd:cd17650 250 atidSTYYEEGrdPLGDSANVPIG---RPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpeltAERFVEN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 488 YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVgIPHNIKGQA-IYAYVTLN 566
Cdd:cd17650 325 PFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVVAA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446000384 567 HgeepSPELyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 404 A----TLNT-AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-615 |
2.74e-31 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 127.83 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIweGDDasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsV 161
Cdd:cd05920 21 LARSAARHPDRIAVV--DGD----RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAvagriidSNSRLVITSDEGVragrsiplkknvddalknpnvtsvehVVVLKRTGGKIDWQEgrdlwwhdlv 241
Cdd:cd05920 93 VLALPSHRR-------SELSAFCAHAEAV--------------------------AYIVPDRHAGFDHRA---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhQAEEMNAE--DPLFILYTSGSTGKPKGVLHTTGGYlVYAALTFKYVFDYHPGDIYWCTADVGwvtgHSYLLYG 319
Cdd:cd05920 130 -------LARELAESipEVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 320 P-----LACGATTLMfegVPNwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEA 394
Cdd:cd05920 198 PgvlgtLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPAL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 WEWYWKKIGnekcPVVDTWWQTETGGFMITPLPGATELKAGSATRPffgVQP----ALVDNEGNPLEGATEGSLVITDsw 470
Cdd:cd05920 272 ARRVPPVLG----CTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEEGELLTRG-- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 471 PGQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI 550
Cdd:cd05920 343 PYTIRGYYRAPEHNARAF--TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 551 PHNIKGQAIYAYVTLNhgeEPSPELyAEVRNWVRkEIGpLAT---PDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 421 PDELLGERSCAFVVLR---DPPPSA-AQLRRFLR-ERG-LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
3.20e-31 |
|
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: 127.39 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwegdDASQskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHsVIFGGFSPEA 170
Cdd:cd12114 2 DATAVI----CGDG--TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY-VPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRII-DSNSRLVITSDEgvragrsiPLKKNVDDAlknpnvtsvehvvvlkrtggkidwqegRDLWWHDLVEQASDQHQ 249
Cdd:cd12114 75 RREAILaDAGARLVLTDGP--------DAQLDVAVF---------------------------DVLILDLDALAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 AEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAALTFKYVFDyhPGDIYWCTADVGW---VtghsYLLYGPLACGA 325
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSSLSFdlsV----YDIFGALSAGA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TtLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLR-ILGSvGEPINPEawewywkkign 404
Cdd:cd12114 194 T-LVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL--EAAQALLPSLRlVLLS-GDWIPLD----------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 405 ekcpVVDTWWQTETGGFMITpLPGATELKAGSAT----------------RPFFGVQPALVDNEGNPLEGATEGSLVItd 468
Cdd:cd12114 259 ----LPARLRALAPDARLIS-LGGATEASIWSIYhpidevppdwrsipygRPLANQRYRVLDPRGRDCPDWVPGELWI-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 SWPGQARTLFGDHERFEQTYFS--TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAA 546
Cdd:cd12114 332 GGRGVALGYLGDPELTAARFVThpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 547 VVGIPhNIKGQAIYAYVTLnhGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 412 VVVLG-DPGGKRLAAFVVP--DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-622 |
9.35e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 106 KHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVIT 185
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 186 SDEgvragrsiplkknvddaLKNPNVTSVEHVVVLKRTggkidwqegrdlwwhdlvEQASDQHQAEEMNAEDPLFILYTS 265
Cdd:PRK12316 3161 QSH-----------------LRLPLAQGVQVLDLDRGD------------------ENYAEANPAIRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVLHTTGGYLVYAALTfkyvfdyhpGDIYWCTAD--VGWVTGHSY-----LLYGPLACGATTLMfEGVPNWPT 338
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWM---------QQAYGLGVGdrVLQFTTFSFdvfveELFWPLMSGARVVL-AGPEDWRD 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 339 PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYwkkigNEKCPVVDTWWQTET 418
Cdd:PRK12316 3276 PALLVELINSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEA 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 419 GGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQARTLFG----DHERFEQTYFSTFKN 494
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNrpglTAERFVPDPFVPGER 3424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGiphnIKGQAIYAYVTLnhgEEPSPE 574
Cdd:PRK12316 3425 LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP---EDEAGD 3497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446000384 575 LYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
1.60e-30 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 122.38 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvp 334
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 335 nwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEwywkkignEKCPVvdTWW 414
Cdd:cd17637 77 ----PAEALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLRHVLGLDAPETIQRFE--------ETTGA--TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 415 ----QTETGGFmITPLPgATElKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVItdswpgQARTLFGDHERFEQTYFS 490
Cdd:cd17637 141 slygQTETSGL-VTLSP-YRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV------RGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 491 TFKN-MYFSGDGARRDEDGYYWITGRV--DDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:cd17637 212 TFRNgWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446000384 568 GEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 292 GATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-628 |
3.35e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 125.26 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK06155 27 LARQAERYPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 I---FGGFSPEAVAGRiidSNSRLVITSDEGVRAGRSIPlkknvddalknPNVTSVEHVVVLkrtGGKIDWQEgrDLWWH 238
Cdd:PRK06155 101 IntaLRGPQLEHILRN---SGARLLVVEAALLAALEAAD-----------PGDLPLPAVWLL---DAPASVSV--PAGWS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 239 DLVEQASDQH-QAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKyVFDYHPGDIYWCTADVGWVTGHSyLL 317
Cdd:PRK06155 162 TAPLPPLDAPaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-AF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 318 YGPLACGATTLM---FEGVPNWPTPARmaqvvdkHQ----------VNILYTAPTAiralmaEGDKAiegtdrSSLRILG 384
Cdd:PRK06155 240 FQALLAGATYVLeprFSASGFWPAVRR-------HGatvtyllgamVSILLSQPAR------ESDRA------HRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 385 SVGEPinPEAWEWYWKKIGnekCPVVDTWWQTETGGFMITPLPgatELKAGSATRPFFGVQPALVDNEGNPLEGATEGSL 464
Cdd:PRK06155 301 GPGVP--AALHAAFRERFG---VDLLDGYGSTETNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 465 VITDSWPGQ-ARTLFGDHERFEQTYfstfKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK06155 373 LLRADEPFAfATGYFGMPEKTVEAW----RNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPE---LYAEVRnwvrkeIGPLATPDVLHWTDSLPKTRSGKIMRRILRkiA 619
Cdd:PRK06155 449 AAAAVFPVPSELGEDEVMAAVVLRDGTALEPValvRHCEPR------LAYFAVPRYVEFVAALPKTENGKVQKFVLR--E 520
|
....*....
gi 446000384 620 AGDTSNLGD 628
Cdd:PRK06155 521 QGVTADTWD 529
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
4.01e-30 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 113.02 E-value: 4.01e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 531 EIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-621 |
4.09e-30 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 125.09 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 75 LNLAANCLDRhLQENGDRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI----DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 155 IGAVHSVIFGGFSPEAVAGRIIDSNSRLVITsdegvragrsipLKKNVDdalKNPNVTSVEHVVVLKrtggkIDWQEGRD 234
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIIT------------QSCYVD---KLKGLAEDDGVTVVT-----IDDPPEGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 235 LWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAltfKYV------FDYHPGDIYWCTADVg 308
Cdd:PLN02246 158 LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPM- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 wvtGHSYLLYGPLACG-----ATTLM--FEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALmAEGDkAIEGTDRSSLR 381
Cdd:PLN02246 234 ---FHIYSLNSVLLCGlrvgaAILIMpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AKSP-VVEKYDLSSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 382 ILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTETG-------GFMITPLPgateLKAGSATRPFFGVQPALVDNE-G 453
Cdd:PLN02246 302 MVLSGAAPLGKELEDAFRAKLPNAV--LGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAELKIVDPEtG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 454 NPLEGATEGSLVITdswpGQ-------------ARTLfgDHERFEQTyfstfknmyfsGDGARRDEDGYYWITGRVDDVL 520
Cdd:PLN02246 376 ASLPRNQPGEICIR----GPqimkgylndpeatANTI--DKDGWLHT-----------GDIGYIDDDDELFIVDRLKELI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 521 NVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTD 600
Cdd:PLN02246 439 KYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIHKVFFVD 515
|
570 580
....*....|....*....|..
gi 446000384 601 SLPKTRSGKIMRRILR-KIAAG 621
Cdd:PLN02246 516 SIPKAPSGKILRKDLRaKLAAG 537
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-616 |
4.55e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 124.35 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 85 HLQENGDRTAIIWegddASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK13390 6 HAQIAPDRPAVIV----AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 165 GFSPeAVAGRII-DSNSRLVITSD--EGV--RAGRSIPLKKNVddalknpnvtsvehvvvlkrtGGKIDwqegrdlwwhD 239
Cdd:PRK13390 82 HLTA-PEADYIVgDSGARVLVASAalDGLaaKVGADLPLRLSF---------------------GGEID----------G 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 240 LVEQASDQHQAEEMNAEDPL--FILYTSGSTGKPKGV--------LHTTGGYLVYAALTFkyvFDYHPGDIYWCTADVgw 309
Cdd:PRK13390 130 FGSFEAALAGAGPRLTEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPI-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 310 vtGHSyllyGPL-------ACGATTLM---FEGvpnwptpARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSS 379
Cdd:PRK13390 205 --YHA----APLrwcsmvhALGGTVVLakrFDA-------QATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 380 LRILGSVGEP------------INPEAWEWYwkkignekcpvvdtwWQTETGGFMITPLPGATElKAGSATRPFFGVQpA 447
Cdd:PRK13390 272 LRAVIHAAAPcpvdvkhamidwLGPIVYEYY---------------SSTEAHGMTFIDSPDWLA-HPGSVGRSVLGDL-H 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 448 LVDNEGNPLEGATEGSLVIT-DSWPgqartlFGDHERFEQTYFSTFKNMYF---SGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK13390 335 ICDDDGNELPAGRIGTVYFErDRLP------FRYLNDPEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISG 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 524 GHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK13390 409 GVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELP 488
|
570
....*....|...
gi 446000384 604 KTRSGKIMRRILR 616
Cdd:PRK13390 489 RTPTGKLVKGLLR 501
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-620 |
7.33e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 124.54 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDegvrAGRS----------IP-LKKNVDDALKNPNVTSVEHVVVL--KRTGGKID 228
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD----GFKDsdyvamlyelAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 229 WQEgrdlwWHDLVEQASD---QHQAEEMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAALTFKyvfdyhPGD- 299
Cdd:PRK08315 174 FDE-----LLALGRAVDDaelAARQATLDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------EEDr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 300 ------IYWCtadVGWVTGHsyllygpLAC---GATTLM----FEgvpnwptPARMAQVVDKHQVNILYTAPTairalM- 365
Cdd:PRK08315 243 lcipvpLYHC---FGMVLGN-------LACvthGATMVYpgegFD-------PLATLAAVEEERCTALYGVPT-----Mf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 366 -AE-GDKAIEGTDRSSLR--IL-GSVgepinpeawewywkkignekCP------VVD---------TWWQTETGgfmitp 425
Cdd:PRK08315 301 iAElDHPDFARFDLSSLRtgIMaGSP--------------------CPievmkrVIDkmhmsevtiAYGMTETS------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 426 lPGAT--------ELKAGSATRPFFGVQPALVDNE-------GNPLEGATEGSLVITDSWPGQART---LfgDHERFeqt 487
Cdd:PRK08315 355 -PVSTqtrtddplEKRVTTVGRALPHLEVKIVDPEtgetvprGEQGELCTRGYSVMKGYWNDPEKTaeaI--DADGW--- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 488 yfstfknMYfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK08315 429 -------MH-TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 568 GEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08315 501 GATLTEE---DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-620 |
1.94e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 125.66 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITsdegvragrsiplKKNVDDALknPNVTSVeHVVVLkrtggkidwqEGRDLWWHdlv 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLEQL--PAPAGD-TALTL----------DRLDLNGY--- 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqaSDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL----VYAALtfkYVFDYHPGDIYWCTADVgwvTGHSYLL 317
Cdd:PRK12467 3226 ---SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALAnhlcWIAEA---YELDANDRVLLFMSFSF---DGAQERF 3296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 318 YGPLACGATtLMFEGVPNWpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:PRK12467 3297 LWTLICGGC-LVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFEQ 3370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 398 YWKKI---------GNEKCPVVDTWWQTETGGfmitpLPGATELKAGsatRPFFGVQPALVDNEGNPLEGATEGSLVITD 468
Cdd:PRK12467 3371 VKRKLkprgltngyGPTEAVVTVTLWKCGGDA-----VCEAPYAPIG---RPVAGRSIYVLDGQLNPVPVGVAGELYIGG 3442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 SwpGQARtlfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 540
Cdd:PRK12467 3443 V--GLAR---GYHqrpsltaERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHP 3517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 541 KIAEAAVVGIPhNIKGQAIYAYVTLNhgeEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12467 3518 SVREAVVLARD-GAGGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
2.94e-29 |
|
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: 118.59 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYV-FDyhPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFEgvPN 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 WPTPARMAQVVDKHqvniLYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEwywkKIGNEKCPVVDTWWQ 415
Cdd:cd17630 76 QALAEDLAPPGVTH----VSLVPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 416 TETGGfMITPLPgATELKAGSATRPFFGVQPALVDNEGNPLEGATegslVITDSWPGQARTLFgdherFEQTYFSTfknm 495
Cdd:cd17630 145 TETAS-QVATKR-PDGFGRGGVGVLLPGRELRIVEDGEIWVGGAS----LAMGYLRGQLVPEF-----NEDGWFTT---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 496 yfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPspel 575
Cdd:cd17630 210 ---KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP---- 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446000384 576 yAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 283 -AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
87-616 |
2.96e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 122.56 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 87 QENGDRTAIIwegDDASQskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAvHSVIFG-G 165
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 166 FSPEAVAGRIIDSNSRLVITSDEgvragrSIPLkknVDDALKN-PNVTSVEhvvvlkrtggkiDWQEGRDlwwHDLVEQA 244
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDEE------FSAT---VDRALADcPQATRIV------------AWTDEDH---DLTVEVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 245 SDQH--QAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGylvyAALTFKYVFDYHPgdiywctadvgWVTGHSYLLYGPL- 321
Cdd:PRK13382 183 IAAHagQRPEPTGRKGRVILLTSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 322 -ACGATTLMFEGVPNWP-------TPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPE 393
Cdd:PRK13382 248 hAWGFSQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 AWEWYWKKIGnekcPVV-DTWWQTETGgfMITPlpgAT--ELKAG--SATRPFFGVQPALVDNEGNPLEGATEGSLVITD 468
Cdd:PRK13382 328 VVIAFMDQFG----DVIyNNYNATEAG--MIAT---ATpaDLRAApdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 SwpgqarTLF-----GDHERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIA 543
Cdd:PRK13382 399 D------TQFdgytsGSTKDFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 544 EAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 466 EAAVIGVDDEQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
87-617 |
3.83e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.01 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 87 QENGDRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsviFGGF 166
Cdd:PLN02330 39 ELYADKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 167 SPEAVAGRIID----SNSRLVITSDEGVRAGRSIPLKknvddalknpnvtsvehVVVLKRT--GGKIDWQEgrdlwWHDL 240
Cdd:PLN02330 111 NPTALESEIKKqaeaAGAKLIVTNDTNYGKVKGLGLP-----------------VIVLGEEkiEGAVNWKE-----LLEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 241 VEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIywctADVGWVTghSYLLYGP 320
Cdd:PLN02330 169 ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIP--FFHIYGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 LACGATTLMFEG---VPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRI--LGSVGEPINPEAW 395
Cdd:PLN02330 243 TGICCATLRNKGkvvVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWYWKKIGNEKcpVVDTWWQTETGgfMITPLPGATELKAGSATRPFFG-VQPAL----VDNE-GNPLEGATEGSLVITDS 469
Cdd:PLN02330 321 TAFEAKFPGVQ--VQEAYGLTEHS--CITLTHGDPEKGHGIAKKNSVGfILPNLevkfIDPDtGRSLPKNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 WpgqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:PLN02330 397 C-----VMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 549 GIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 472 PLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
261-616 |
1.21e-28 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 119.79 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 261 ILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHP--GDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnw 336
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMekFD----- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 337 ptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINP---EAWEWYWKkignekcPVVDTW 413
Cdd:cd05929 205 --PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIDWGG-------PIIWEY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 414 WQ-TETGGFmiTPLPGATELK-AGSATRPFFGVQpALVDNEGNPLEGATEGSLVITDSWPgqartlFGDHERFEQTYFST 491
Cdd:cd05929 276 YGgTEGQGL--TIINGEEWLThPGSVGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 492 FKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEE 570
Cdd:cd05929 347 NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAD 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446000384 571 PSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 427 AGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
1.48e-28 |
|
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: 119.50 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEgddasqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEgvragrsiplkknvddaLKNPNVTSVEHVVvlkrtggkIDWqegrdlwwhDLVEQASDQHQA 250
Cdd:cd17656 77 RIYIMLDSGVRVVLTQRH-----------------LKSKLSFNKSTIL--------LED---------PSISQEDTSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 EEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVyaALTFKYVFDYHPGDIYW---CTADVGWVTGHSYLLYGP---LA 322
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSGGtlyII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATTLMFEgvpnwptpaRMAQVVDKHQVNILYTaPTAIRALMAEGDKAIEGTDRSSLRILgSVGEP--INPEAWEWYWK 400
Cdd:cd17656 201 REETKRDVE---------QLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFPTCVKHII-TAGEQlvITNEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KigneKCPVVDTWWQTET---GGFMITPLPGATELKAgsATRPFFGVQPALVDNEGNPLEGATEGSLVItdSWPGQARTL 477
Cdd:cd17656 270 H----NVHLHNHYGPSEThvvTTYTINPEAEIPELPP--IGKPISNTWIYILDQEQQLQPQGIVGELYI--SGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 478 FGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHN 553
Cdd:cd17656 342 LNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 554 IKGQAIYAYVTlnhgeePSPEL-YAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17656 422 KGEKYLCAYFV------MEQELnISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
3.06e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 116.22 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAALTFKyvfdyhPGDI-------YWCTADVGwvtghsyllyGPLAC 323
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT------EQDRlcipvplFHCFGSVL----------GVLAC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 ---GATTLMFEgvpnwPT--PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIegTDRSSLR--ILGsvGEPINPEAWE 396
Cdd:cd05917 66 lthGATMVFPS-----PSfdPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDK--FDLSSLRtgIMA--GAPCPPELMK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 397 WYWKKIGNEKCPVVdtWWQTETGGFMITPLPGAT-ELKAGSATRPFFGVQPALVDNEGNPL-------EGATEGSLVITD 468
Cdd:cd05917 137 RVIEVMNMKDVTIA--YGMTETSPVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpgELCIRGYSVMKG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 469 SWpgqartlfGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd05917 215 YW--------NDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVV 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 549 GIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 285 GVPDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
91-617 |
5.66e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 118.24 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDDASQSKHIsykelhRDVCRFANTLLELGIKKGDV-VAIYMPMVPEAAVAMLACARIGAVhsviFGGFSP- 168
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHI------RGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIV----PVGLNPt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 169 ---EAVAGRIIDSNSRLVITSDEgvragrSIPLkknVDDALKNpnvtsVEHVVVlkrtggkiDWQEgrdlWWHDLVEQAS 245
Cdd:PRK07867 88 rrgAALARDIAHADCQLVLTESA------HAEL---LDGLDPG-----VRVINV--------DSPA----WADELAAHRD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 246 DQHQAEEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAALTFKYVFDYHPGDIYWCTAD--------VGWVTGhsyll 317
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 318 ygpLACGATTLM---FEGVPNWPTPARM----AQVVDKHQVNILYTAPtairalmaegdkaiEGTDRS-SLRIL-GSVGE 388
Cdd:PRK07867 216 ---LAAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPE--------------RPDDADnPLRIVyGNEGA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 389 PINPEAWEwywKKIGnekCPVVDTWWQTEtGGFMITPLPGATElkaGSATRPFFGVQ-----------PALVDNEGNPLE 457
Cdd:PRK07867 279 PGDIARFA---RRFG---CVVVDGFGSTE-GGVAITRTPDTPP---GALGPLPPGVAivdpdtgtecpPAEDADGRLLNA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 458 GATEGSLVITDSwPGQARTLFGDHERFEQtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:PRK07867 349 DEAIGELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 538 AHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07867 425 RYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
84-619 |
1.01e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 117.19 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHLQENGDRTAIIWEgddasqSKHISYKELHRDVCRFANTLLELGiKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:PRK07638 9 KHASLQPNKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 164 GGFSPEAVAGRIIDSNSRLVITsdegvragrsiplkknvDDALKNPnVTSVEHVVvlkrtggkIDWQEgrdlwWHDLVEQ 243
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVT-----------------ERYKLND-LPDEEGRV--------IEIDE-----WKRMIEK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 244 ASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvyaaltfkYVFDYHPGDIYWCTADVGWVTG---HSYLLYGP 320
Cdd:PRK07638 131 YLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHSLFLYGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 ---LACGAT-TLMFEGVPNwptparmaQVVDK---HQVNILYTAPTAIRALMAEgdkaiEGTDRSSLRILGSVGEpinpe 393
Cdd:PRK07638 203 istLYVGQTvHLMRKFIPN--------QVLDKletENISVMYTVPTMLESLYKE-----NRVIENKMKIISSGAK----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 awewyWKKIGNEKcpVVDTW--------WQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSL- 464
Cdd:PRK07638 265 -----WEAEAKEK--IKNIFpyaklyefYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVy 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 465 ---------VITDSWPGQARTLFGdherfeqtyFSTFKNMYFSgdgarrDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK07638 338 vkspqffmgYIIGGVLARELNADG---------WMTVRDVGYE------DEEGFIYIVGREKNMILFGGINIFPEEIESV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 536 LVAHPKIAEAAVVGIPHNIKGQAIYAYVtlnHGEEPSPELyaevRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK07638 403 LHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQL----KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
....
gi 446000384 616 RKIA 619
Cdd:PRK07638 476 KSWI 479
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
91-621 |
5.19e-27 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 115.89 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWegddasQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PLN03102 29 NRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVEHVVVLKRTGGKidwqegrDLWWHDLVEQASDQHQA 250
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSE-------ELDYECLIQRGEPTPSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 EE-----MNAEDPLFILYTSGSTGKPKGVLHT-TGGYLVYAALTFKYVFDYHPgdIYWCTADV----GWVtghsyLLYGP 320
Cdd:PLN03102 176 VArmfriQDEHDPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMfhcnGWT-----FTWGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 LACGATTLMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMaEGDKAIEGTDRSSLRILGSVGEPinPEAwewYWK 400
Cdd:PLN03102 249 AARGGTSVCMRHV----TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAA---LVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNEKCPVVDTWWQTETGGFMI----------TPLPGATELKAGSATRpFFGVQPALVDN----EGNPLEGATEGSLVI 466
Cdd:PLN03102 319 KVQRLGFQVMHAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGVS-ILGLADVDVKNketqESVPRDGKTMGEIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 TDSwpgqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:PLN03102 398 KGS------SIMKGYLKNPKATSEAFKHGWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 546 AVVGIPHNIKGQAIYAYVTLNHGEEPSPE----LYAEVRN---WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PLN03102 472 AVVAMPHPTWGETPCAFVVLEKGETTKEDrvdkLVTRERDlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
...
gi 446000384 619 AAG 621
Cdd:PLN03102 552 AKG 554
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
248-616 |
1.37e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.55 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 248 HQAEEMNAEDPLFILYTSGSTGKPKGVLhttggyLVYAALTfkyvfdyhpGDI-------YWCTADV-----------GW 309
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVV------LSRRAIA---------ADLdalaeawQWTADDVlvhglplfhvhGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 310 VTGhsylLYGPLACGATtLMFEGVPnwpTPARMAQVVDKHQvNILYTAPTAIRALMAEGDKAiegtdR--SSLRILGSVG 387
Cdd:PRK07787 185 VLG----VLGPLRIGNR-FVHTGRP---TPEAYAQALSEGG-TLYFGVPTVWSRIAADPEAA-----RalRGARLLVSGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEAWEWYWKKIGNEkcpVVDTWWQTETggFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPL--EGATEGSLV 465
Cdd:PRK07787 251 AALPVPVFDRLAALTGHR---PVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVphDGETVGELQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 466 ItdswpgQARTLF-GDHERFEQT--------YFSTfknmyfsGDGARRDEDGYYWITGRVD-DVLNVSGHRLGTAEIESA 535
Cdd:PRK07787 326 V------RGPTLFdGYLNRPDATaaaftadgWFRT-------GDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 536 LVAHPKIAEAAVVGIPHNIKGQAIYAYVTlnHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK07787 393 LLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
.
gi 446000384 616 R 616
Cdd:PRK07787 468 L 468
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-615 |
1.72e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.03 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 105 SKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVI 184
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 185 TSDEgvrAGRSIPLKKNVddalknpnvtsveHVVVLKRTGgkiDWQEGRdlwwhdlveqaSDQHQAEEMNAEDPLFILYT 264
Cdd:PRK12467 1677 TQSH---LQARLPLPDGL-------------RSLVLDQED---DWLEGY-----------SDSNPAVNLAPQNLAYVIYT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 265 SGSTGKPKGVLHTTGGyLVYAALTFKYVFDYhpgdiywCTADVgWVTGHSYL-------LYGPLACGATTLMfegVPNWP 337
Cdd:PRK12467 1727 SGSTGRPKGAGNRHGA-LVNRLCATQEAYQL-------SAADV-VLQFTSFAfdvsvweLFWPLINGARLVI---APPGA 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 338 --TPARMAQVVDKHQVNILYTAPTAIRALMaEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYWKKIGNEKcpVVDTWWQ 415
Cdd:PRK12467 1795 hrDPEQLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYGP 1869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 416 TETggfMITPLPGATELK--AGSATRPfFGVQPA-----LVDNEGNPLEGATEGSLVITDSwpGQARtlfGDH------- 481
Cdd:PRK12467 1870 TET---AVDVTHWTCRRKdlEGRDSVP-IGQPIAnlstyILDASLNPVPIGVAGELYLGGV--GLAR---GYLnrpalta 1940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 482 ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVvgIPHN-IKGQAI 559
Cdd:PRK12467 1941 ERFVADPFGTVgSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgANGKQL 2018
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 560 YAYVT-----LNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK12467 2019 VAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
4.81e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 112.01 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEgddasqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVItsdegvragrsiplkknVDdalknpnvTSVEHVVVLKRTGGKIDWQEGRDLWwhdlv 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-----------------VD--------REFEYEDLLAEGDPDFEWIPPADEW----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeemnaeDPLFILYTSGSTGKPKGVLHT-TGGYLvyAALTFKYVFDYHPGDIYWCTADV----GWVtghsyL 316
Cdd:cd12118 134 ---------------DPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAwe 396
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVHVMTAGAPPPAA-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 397 wYWKKIGNEKCPVVDTWWQTETGGFMIT--------PLPgaTELKAGSATR---PFFGVQPALV-DNEGN---PLEGATE 461
Cdd:cd12118 263 -VLAKMEELGFDVTHVYGLTETYGPATVcawkpewdELP--TEERARLKARqgvRYVGLEEVDVlDPETMkpvPRDGKTI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 462 GSLVItdswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 540
Cdd:cd12118 340 GEIVF------RGNIVMKGYLKNPEATAEAFRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDsLPKTRSGKIMRRILRK 617
Cdd:cd12118 414 AVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
2.52e-25 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 110.61 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDE 188
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 gvragrSIPLKKNVDDALKnpnvtSVEHVVV-----------LKRTGGKIDWQEGRDlwwHDLVEQASDQHQAEEMnaed 257
Cdd:PRK06018 121 ------FVPILEKIADKLP-----SVERYVVltdaahmpqttLKNAVAYEEWIAEAD---GDFAWKTFDENTAAGM---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 258 plfiLYTSGSTGKPKGVLHTTGGYLVYAALTFkyvfdyHPGDIYWCTADV-----------GWVTGHSyllyGPlACGAT 326
Cdd:PRK06018 183 ----CYTSGTTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADTmlpvvplfhanSWGIAFS----AP-SMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 327 TLMfegvpnwPTP----ARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiegtDRSSLRILGSV--GEPINPEAWEWYWK 400
Cdd:PRK06018 248 LVM-------PGAkldgASVYELLDTEKVTFTAGVPTVWLMLLQYMEK-----EGLKLPHLKMVvcGGSAMPRSMIKAFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNEkcpVVDTWWQTETggfmiTPLPGATELKAGSAT--------------RPFFGVQPALVDNEGN--PLEGATEGSL 464
Cdd:PRK06018 316 DMGVE---VRHAWGMTEM-----SPLGTLAALKPPFSKlpgdarldvlqkqgYPPFGVEMKITDDAGKelPWDGKTFGRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 465 VItdSWPGQARTLF--GDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK06018 388 KV--RGPAVAAAYYrvDGEILDDDGFFDT-------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 459 AEAAVIGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
3.16e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.98 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 79 ANCLDRHLQENGDRTAIIWegddASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 159 hsvifggFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVehvvvlkrtgGKIDWQEGRDLWWH 238
Cdd:PRK05852 95 -------VVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNV----------GGDSGPSGGTLSVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 239 --DLVEQASDQHQAEEMNAEDPLfILYTSGSTGKPKGVLHTTGGYlvyAALTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:PRK05852 158 ldAATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGHGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 --LYGPLACGATTLMfegvpnwPTPARMAQVV---DKHQVN-ILYTA-PTAIRALMAEGDKAIEGTDRSSLRILGSVGEP 389
Cdd:PRK05852 234 aaLLATLASGGAVLL-------PARGRFSAHTfwdDIKAVGaTWYTAvPTIHQILLERAATEPSGRKPAALRFIRSCSAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 390 INPEAWEWYWKKIGnekCPVVDTWWQTET---------GGFMITPLPGATELKAGSATrpffGVQPALVDNEGNPLEGAT 460
Cdd:PRK05852 307 LTAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 461 EGSLVItdSWPGQARTLFGDHE----RFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:PRK05852 380 VGEVWL--RGTTVVRGYLGDPTitaaNFTDGWLRT-------GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 537 VAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK05852 451 ASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-618 |
8.04e-25 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 108.77 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIIwegdDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17642 31 PGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 170 AVAGRIIDSNSRLVITSdegvragrsiplKKNVDDALK-NPNVTSVEHVVVLKrtgGKIDWQEGRDLW----WHDLVEQA 244
Cdd:cd17642 107 ELDHSLNISKPTIVFCS------------KKGLQKVLNvQKKLKIIKTIIILD---SKEDYKGYQCLYtfitQNLPPGFN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 245 SDQHQAEEMNAEDPL-FILYTSGSTGKPKGVLHT--------------TGGYLVYAALTFKYVFDYHPGdiYWCTADVGW 309
Cdd:cd17642 172 EYDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFHHG--FGMFTTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 310 VTghsyllygplaCGATTLM---FEgvpnwptPARMAQVVDKHQVNILYTAPTairaLMAEGDKA--IEGTDRSSLRILG 384
Cdd:cd17642 250 LI-----------CGFRVVLmykFE-------EELFLRSLQDYKVQSALLVPT----LFAFFAKStlVDKYDLSNLHEIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 385 SVGEPINPEAWEWYWKKIgneKCPVV-DTWWQTE-TGGFMITPlpgATELKAGSATR--PFFGVQpaLVDNEGNPLEGAT 460
Cdd:cd17642 308 SGGAPLSKEVGEAVAKRF---KLPGIrQGYGLTEtTSAILITP---EGDDKPGAVGKvvPFFYAK--VVDLDTGKTLGPN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 461 E-GSLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 538
Cdd:cd17642 380 ErGELCVKG--PMIMKGYVNNPE---ATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 539 HPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLA-TPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd17642 455 HPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
.
gi 446000384 618 I 618
Cdd:cd17642 532 I 532
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
1.20e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 105.93 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDyHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 WPT----------PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNe 405
Cdd:cd05924 82 GGQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 406 kCPVVDTWWQTETGGFMItplpgATELKAGSATRPFFGVQP--ALVDNEGNPLEGATEGSLVItdswpgqART------L 477
Cdd:cd05924 161 -ITLVDAFGSSETGFTGS-----GHSAGSGPETGPFTRANPdtVVLDDDGRVVPPGSGGVGWI-------ARRghiplgY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 478 FGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKG 556
Cdd:cd05924 228 YGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 557 QAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 308 QEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-620 |
1.73e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 107.24 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHLQENGDRTAI-IWEGDdasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhSVI 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA-FVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 163 FGGFSPEA-VAGRIIDSNSRLVITSDegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlv 241
Cdd:cd05918 79 LDPSHPLQrLQEILQDTGAKVVLTSS------------------------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeemnAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAALTFKYVFDYHPG-----------DIywCTADVg 308
Cdd:cd05918 105 -------------PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSEsrvlqfasytfDV--SILEI- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 wvtghsyllYGPLACGATTLmfegVP-NWPTPARMAQVVDKHQVNILYTAPTAIRALMAEgdkaiegtDRSSLRILGSVG 387
Cdd:cd05918 166 ---------FTTLAAGGCLC----IPsEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 388 EPINPEawewywkkignekcpVVDTWWQ----------TETGGFMITPLPGATElKAGSATRPfFGVQPALVDNEGN--- 454
Cdd:cd05918 225 EALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVPST-DPRNIGRP-LGATCWVVDPDNHdrl 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 455 -PLeGATeGSLVItdSWPGQARtlfGDHERFEQTYFSTFKN--------------MYFSGDGARRDEDG--YYwiTGRVD 517
Cdd:cd05918 288 vPI-GAV-GELLI--EGPILAR---GYLNDPEKTAAAFIEDpawlkqegsgrgrrLYRTGDLVRYNPDGslEY--VGRKD 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 518 DVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI--PHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLAT--- 592
Cdd:cd05918 359 TQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAelr 438
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 446000384 593 ------------PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05918 439 sklrqrlpsymvPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
72-625 |
2.20e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 107.62 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 72 DGTLNLAANCLDRHlQENGDrTAIIwegdDASQSKHISYKELHRDVCRFANTLLE-LGIKKGDVVAIYMPMVPEAAVAML 150
Cdd:PLN02574 37 DPNLDAVSFIFSHH-NHNGD-TALI----DSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 151 ACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVraGRSIPLKKNVddalknpnvtsvehvvVLKRTGGKIDWQ 230
Cdd:PLN02574 111 AVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPV----------------IGVPENYDFDSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 231 EGRDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKY---VFDYHPGD-IYWCTAD 306
Cdd:PLN02574 173 RIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeasQYEYPGSDnVYLAALP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 307 VGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGdKAIEGTDRSSLRILGSV 386
Cdd:PLN02574 253 MFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTKKA-KGVCGEVLKSLKQVSCG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 387 GEPINPEAWEWYWKKIgnekcPVVDTwwqteTGGFmitplpGATElKAGSATRPFF---------------GVQPALVDN 451
Cdd:PLN02574 328 AAPLSGKFIQDFVQTL-----PHVDF-----IQGY------GMTE-STAVGTRGFNteklskyssvgllapNMQAKVVDW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 452 E-GNPLEGATEGSLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PLN02574 391 StGCLLPPGNCGELWIQG--PGVMKGYLNNPK---ATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 530 AEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PLN02574 466 ADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGK 542
|
570
....*....|....*.
gi 446000384 610 IMRRILRKIAAGDTSN 625
Cdd:PLN02574 543 ILRRELKRSLTNSVSS 558
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
82-620 |
9.47e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 105.46 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQenGDRTAIIwegddaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsV 161
Cdd:PRK10946 31 LTRHAA--SDAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPE-----AVAGRIidsNSRLVItsdegvrAGRSIPLKKNVD--DALKNpNVTSVEHVVVLKRTGGkidwqegRD 234
Cdd:PRK10946 101 VNALFSHQrselnAYASQI---EPALLI-------ADRQHALFSDDDflNTLVA-EHSSLRVVLLLNDDGE-------HS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 235 LwwHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAALTFKYVFDYHPGDIYWCTADvgwvTGHS 314
Cdd:PRK10946 163 L--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSVRRSVEICGFTPQTRYLCALP----AAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 315 YLLYGPLA-----CGATTLMfegVPNwPTPARMAQVVDKHQVNILYTAPTA----IRALMAEGDKAiegtDRSSLRILgS 385
Cdd:PRK10946 236 YPMSSPGAlgvflAGGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAvslwLQAIAEGGSRA----QLASLKLL-Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 386 VGEPINPEAWEwywKKIGNE-KCPVVDTWWQTEtGGFMITPLPGATELKAGSATRPffgVQPA----LVDNEGNPLEGAT 460
Cdd:PRK10946 307 VGGARLSETLA---RRIPAElGCQLQQVFGMAE-GLVNYTRLDDSDERIFTTQGRP---MSPDdevwVADADGNPLPQGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 461 EGSLVITDSW--------PGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK10946 380 VGRLMTRGPYtfrgyyksPQHNASAF-DANGF-----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 533 ESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPspelyAEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK10946 448 ENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA-----VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....*....
gi 446000384 612 RRILRKIAA 620
Cdd:PRK10946 523 KKQLRQWLA 531
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-619 |
1.00e-23 |
|
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: 105.11 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFAnTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:cd05909 8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 EGVRAGRSIPLKknvdDALKNPNVTSVEHVVvlkrtgGKIDWQEG---------RDLWWHDLVEQASDQhqaeemnAEDP 258
Cdd:cd05909 87 QFIEKLKLHHLF----DVEYDARIVYLEDLR------AKISKADKckaflagkfPPKWLLRIFGVAPVQ-------PDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 259 LFILYTSGSTGKPKGVLHTTGGYL--VYAALTfkyVFDYHPGDIywctadvgwVTG-----HSYLLYG----PLACGATT 327
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV---------VFGalpffHSFGLTGclwlPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 328 LMFegvPNwPTPAR-MAQVVDKHQVNILYTAPTAIRALMaegdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIG--- 403
Cdd:cd05909 218 VFH---PN-PLDYKkIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGiri 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 404 ------NEKCPVVDtwwqtetggfMITPLPGAtelKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwPGQARTL 477
Cdd:cd05909 290 legygtTECSPVIS----------VNTPQSPN---KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 478 FGDHerfEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH-PKIAEAAVVGIPHNIKG 556
Cdd:cd05909 356 LNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446000384 557 QAIYAYVTlnhGEEPSPElyaEVRNWVRK-EIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 433 EKIVLLTT---TTDTDPS---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
1.62e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 105.34 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPlkknvdDALKNPNVTSVEhvvvlkrTGGKIDWQEGrdlwWHDLV 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEAR------ADLARPPRLWVA-------GGDTLDDPEG----YEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EQASDQHQA-----EEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAlTFKYVFDYHPGDIYWCT--------ADVG 308
Cdd:PRK08279 180 AAAAGAPTTnpasrSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCClplyhntgGTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 WVTGhsyllygpLACGATTLM---FEGVPNWPTparmaqvVDKHQVnilyTAPTAI----RALMAEGDKAiegTDRS-SL 380
Cdd:PRK08279 259 WSSV--------LAAGATLALrrkFSASRFWDD-------VRRYRA----TAFQYIgelcRYLLNQPPKP---TDRDhRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 381 RILgsVGEPINPEAWEwywkkignekcpvvdtWWQTETGGFMITPLPGATEL---------KAGSATR-PFFGVQP-ALV 449
Cdd:PRK08279 317 RLM--IGNGLRPDIWD----------------EFQQRFGIPRILEFYAASEGnvgfinvfnFDGTVGRvPLWLAHPyAIV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 450 --DNE-GNPLEGAtEGSLV-------------ITDSWP--GQA----------RTLF--GDherfeqTYFSTfknmyfsG 499
Cdd:PRK08279 379 kyDVDtGEPVRDA-DGRCIkvkpgevglligrITDRGPfdGYTdpeasekkilRDVFkkGD------AWFNT-------G 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 500 DGARRDEDGYYWITGRVDDVL-----NVSghrlgTAEIESALVAHPKIAEAAVVGIP-HNIKGQAIYAYVTLNHGEEPSP 573
Cdd:PRK08279 445 DLMRDDGFGHAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDL 519
|
....*...
gi 446000384 574 -ELYAEVR 580
Cdd:PRK08279 520 aALAAHLY 527
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-621 |
1.73e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 104.71 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 76 NLAANCLDRHLQENGDR-TAIIWEGDDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQpEAIALRRCDGTSA--LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 155 IGAVhSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSiplkknvddalKNPNVTSVEHVVVLKRTGGKIDWQEGRD 234
Cdd:PRK05857 89 LGAI-AVMADGNLPIAAIERFCQITDPAAALVAPGSKMASS-----------AVPEALHSIPVIAVDIAAVTRESEHSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 235 lwwhdlveqaSDQHQAE-EMNAEDPLFILYTSGSTGKPKGVLhttggylvYAALTFKYVFD-YHPGDIYWctadVGWVTG 312
Cdd:PRK05857 157 ----------AASLAGNaDQGSEDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VTWVVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 313 HSylLYGPLACG--------ATTLMFEG--VPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRI 382
Cdd:PRK05857 215 ET--TYSPLPAThigglwwiLTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSLRL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 383 LGSVGEpinpEAWEWYWKKIGNEKCPVVDTWWQTETGGFMITpLPGATE----LKAGSATRPFFGVQPALVD-NEGNPL- 456
Cdd:PRK05857 291 VGYGGS----RAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPTDDGsivkIEAGAVGRPYPGVDVYLAAtDGIGPTa 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 457 ----EGATEGSLVITDswPGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK05857 366 pgagPSASFGTLWIKS--PANMLGYWNNPERTAEVLIDGWVN---TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 533 ESALVAHPKIAEAAVVGIPHN----IKGQAIYAYVTLNhgEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:PRK05857 441 DRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSG 518
|
570
....*....|...
gi 446000384 609 KIMRRILRKIAAG 621
Cdd:PRK05857 519 KVMRASLAAAATA 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
2.28e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.41 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSdeGVRAGRsiplkknvddalknpnVTSVEHVVVLKRTGGKID-Wqegrdlwwhdl 240
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQ--SHLLER----------------LPQAEGVSAIALDSLHLDsW----------- 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 241 veqaSDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTtggylvYAALTFK-------YVFDyhPGDIYWCTADVGWVTGh 313
Cdd:PRK05691 1262 ----PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNT------HAALAERlqwmqatYALD--DSDVLMQKAPISFDVS- 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 314 SYLLYGPLACGATtLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPE 393
Cdd:PRK05691 1329 VWECFWPLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAE 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 AWEWYWKKI---------GNEKCPVVDTWWQTETGGFMITPLpgatelkagsaTRPFFGVQPALVDNEGNPLEGATEGSL 464
Cdd:PRK05691 1404 LRNRVLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGEL 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 465 VITDSwpGQARTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH 539
Cdd:PRK05691 1473 CIGGA--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQ 1550
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 540 PKIAEAAVVgIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 1551 PGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
2.37e-23 |
|
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: 104.24 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLELGiKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 164 GGFSPEA---VAGRIIDSNSRLVITsDEGVRAGrsiplkknvddalknpnvtsvehvvvLKRTGGKIDWQEGRDLWWHDL 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLT-TAAALAA--------------------------VRAFAASRPAAGTPRLLVVDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 241 VEQAS-DQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKyVFDYHPGDIY--W--CTADVGWVTGhsy 315
Cdd:cd05931 133 LPDTSaADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 316 lLYGPLACGATTLMFEgvpnwPT-----PARMAQVVDKHQVNILYtAPT-----AIRALMAEGdkaIEGTDRSSLRILGS 385
Cdd:cd05931 209 -LLTPLYSGGPSVLMS-----PAaflrrPLRWLRLISRYRATISA-APNfaydlCVRRVRDED---LEGLDLSSWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 386 VGEPINPEAWEWYWKK--------------------------IGNEKCPVVDTW--WQTETGGFMITPL-PGATELKagS 436
Cdd:cd05931 279 GAEPVRPATLRRFAEAfapfgfrpeafrpsyglaeatlfvsgGPPGTGPVVLRVdrDALAGRAVAVAADdPAARELV--S 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 437 ATRPFFGVQPALVDNEGN-PLEGATEGSLVITDS------W--PGQARTLFG--DHERfEQTYFSTfknmyfsGD-GARR 504
Cdd:cd05931 357 CGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPsvasgyWgrPEATAETFGalAATD-EGGWLRT-------GDlGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 505 deDGYYWITGRVDDVLNVSGHRLGTAEIE-SALVAHPKIAE--AAVVGIPHNIKGQ-AIYAYVTLNHGEEPSPELYAEVR 580
Cdd:cd05931 429 --DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIR 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 446000384 581 NWVRKEIGpLATPDV-LHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 507 AAVAREHG-VAPADVvLVRPGSIPRTSSGKIQRRACRA 543
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
2.50e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 101.57 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDyhpgdiyWCTADVGWVTGHSYLLYGpLACGATTLMFEGV-- 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 334 --PNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGE-PINPEAWEWYWKKIGNekcpVV 410
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADVRFIEATGLTN----TA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 411 DTWWQTETGGFMITPLpGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSWpgqarTLFGDHERFEQTYFS 490
Cdd:cd17635 147 QVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 491 TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNhgEE 570
Cdd:cd17635 221 LIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446000384 571 PSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
3.65e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.95 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 237 WHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-ALTFKYvfDYHPGDIYWCTADVGwvtgHS- 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 315 --YLLYGP-LACGATTLMfegvPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRssLRIlgSVGEPIN 391
Cdd:PRK13388 205 avMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 392 PEAWEWYWKKIGnekCPVVDTWWQTETGGfMITPLPGATElkaGSATRPFFGVQ-----------PALVDNEG---NPLE 457
Cdd:PRK13388 277 PRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPGTPP---GSIGRGAPGVAiynpetltecaVARFDAHGallNADE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 458 GAteGSLVITdswpgQARTLF--------GDHERFEQtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK13388 350 AI--GELVNT-----AGAGFFegyynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 530 AEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK13388 416 APIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRIAADLPSTATNK 494
|
....*..
gi 446000384 610 IMRRILR 616
Cdd:PRK13388 495 VLKRELI 501
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
7.34e-23 |
|
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: 99.79 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYaaltfkyvFDYHPGDIYWCTADVGWVTG---HSYLLYGPL--------ACGA 325
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGAIsalylggtFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TTLmfegvpnwpTPARMAQVVDKHQVNILYTAPTAIRALmaegdkAIEGTDRSSLRILGSVGEPINPEAwewyWKKIGNE 405
Cdd:cd17633 73 RKF---------NPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFEST----KKKLKNI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 406 --KCPVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNEGNPL-----------EGATEGSLVITDSWpg 472
Cdd:cd17633 134 fpKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIgkifvksemvfSGYVRGGFSNPDGW-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 473 qartlfgdherfeqtyFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPH 552
Cdd:cd17633 210 ----------------MSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 553 NIKGQ---AIYAYVTLNhgeepspelYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 267 ARFGEiavALYSGDKLT---------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
91-616 |
1.30e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 101.88 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDDASqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK07514 15 DRDAPFIETPDGL---RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVddalknpnvtsvEHVVVL--KRTGGKIDwqegrdlwwhdLVEQASDQH 248
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAGA------------PHVETLdaDGTGSLLE-----------AAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 249 QAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGD-------IYwctadvgwvtgHSYLLY--- 318
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 319 -GPLACGATtlMFegvpnWPTPARMAQVVDK-HQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVgePINPE--- 393
Cdd:PRK07514 217 nVALLAGAS--MI-----FLPKFDPDAVLALmPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSA--PLLAEthr 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 AWEwywKKIGNekcPVVDTWWQTETGgfMITPLPGATELKAGSATRPFFGVQPALVDNE-GNPLEGATEGSL------VI 466
Cdd:PRK07514 288 EFQ---ERTGH---AILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPEtGAELPPGEIGMIevkgpnVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 467 TDSW--PGQARTLFGdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:PRK07514 360 KGYWrmPEKTAEEFR-----ADGFFIT-------GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 545 AAVVGIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07514 428 SAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-620 |
2.88e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.11 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 106 KHISYKELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVI 184
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 185 TSD------EGVRAGrsIPLKKNVDD-----------ALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLwwhdlveqaSDQ 247
Cdd:PRK08751 129 VIDnfgttvQQVIAD--TPVKQVITTglgdmlgfpkaALVNFVVKYVKKLVPEYRINGAIRFREALAL---------GRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 248 HQ--AEEMNAEDPLFILYTSGSTGKPKGvlhttggylvyAALTFKYVFDYHPGDIYWCTADVGWVTGHSYL-----LYGP 320
Cdd:PRK08751 198 HSmpTLQIEPDDIAFLQYTGGTTGVAKG-----------AMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVitalpLYHI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 321 LACGATTLMFEGVPNW----PTPARMAQVVdKHQVNILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:PRK08751 267 FALTANGLVFMKIGGCnhliSNPRDMPGFV-KELKKTRFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMAVQRSV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 WEwYWKKIGNekCPVVDTWWQTETG-GFMITPLpgatELKA--GSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwp 471
Cdd:PRK08751 346 AE-RWKQVTG--LTLVEAYGLTETSpAACINPL----TLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP-- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 472 gqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI 550
Cdd:PRK08751 417 ---QVMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 551 PHNIKGQAIYAYVTlnhgeEPSPELYAE-VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08751 494 PDEKSGEIVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-615 |
3.28e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 102.04 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDdasqskHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK10252 464 VAQQAAKTPDAPALADARY------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEgvRAGRsiplkknVDDAlknPNVTSVEHVVVLKRTGGKidwqegrdlwwhdlV 241
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD--QLPR-------FADV---PDLTSLCYNAPLAPQGAA--------------P 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 EQASDQHqaeemnaeDPLFILYTSGSTGKPKGVL--HTTggyLVYAALTFKYVFDYHPGDIYW----CTADVG-WVtghs 314
Cdd:PRK10252 592 LQLSQPH--------HTAYIIFTSGSTGRPKGVMvgQTA---IVNRLLWMQNHYPLTADDVVLqktpCSFDVSvWE---- 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 315 ylLYGPLACGATTLMFEgvpnwPT----PARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPI 390
Cdd:PRK10252 657 --FFWPFIAGAKLVMAE-----PEahrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEAL 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 NPE---AWE-WYWKKIGNEKCPV---VD-TWWqtetggfmitPLPGATELKAGSAT----RPFFGVQPALVDNEGNPLEG 458
Cdd:PRK10252 730 PADlcrEWQqLTGAPLHNLYGPTeaaVDvSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILDARMRPVPP 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 459 ATEGSLVITdswpG-Q-ARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK10252 800 GVAGDLYLT----GiQlAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEI 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 533 ESALVAHPKIAEAAVV------GIPHNIKGQAIYAYVTLNHGEEPSPELyaeVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK10252 876 DRAMQALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQLDQLPLSA 952
|
....*....
gi 446000384 607 SGKIMRRIL 615
Cdd:PRK10252 953 NGKLDRKAL 961
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
3.72e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 100.79 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 70 YEDGTLNLAANC--------LDRHLQENGDRTAIIWEGddasqsKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 142 VPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGV--------RAGRSIPLKKNVDDAL--KNPNV 211
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAevarealaLLPGPKPLVIDVDDPEypGGRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 212 TSVEHVVVLKRTGGKIDWQEGRDLWwhdlveqasdqhQAEEMNaedplfilYTSGSTGKPKGVL-HTTGGYLVYAALTFK 290
Cdd:PRK08162 158 GALDYEAFLASGDPDFAWTLPADEW------------DAIALN--------YTSGTTGNPKGVVyHHRGAYLNALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 291 YVFDYHPgdIY-W------CTadvGWvtghsyllygplaCGATTLMFEGVPN----WPTPARMAQVVDKHQVNILYTAPT 359
Cdd:PRK08162 218 WGMPKHP--VYlWtlpmfhCN---GW-------------CFPWTVAARAGTNvclrKVDPKLIFDLIREHGVTHYCGAPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 360 AIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAwewywkkignekcpVVDtwwQTETGGFMITPLPGATEL------- 432
Cdd:PRK08162 280 VLSALINAPAEWRAGIDH---PVHAMVAGAAPPAA--------------VIA---KMEEIGFDLTHVYGLTETygpatvc 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 433 --KAGSATRPFfGVQPALVDNEGNP---LEGATEGSLVITDSWPGQARTLfGD-------------------HERFEQTY 488
Cdd:PRK08162 340 awQPEWDALPL-DERAQLKARQGVRyplQEGVTVLDPDTMQPVPADGETI-GEimfrgnivmkgylknpkatEEAFAGGW 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 489 FSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHG 568
Cdd:PRK08162 418 FHT-------GDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446000384 569 EEPSPElyaEVRNWVRKEIGPLATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 491 ASATEE---EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
4.51e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 100.48 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIwegddaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07059 29 LEESFRQYADRPAFI------CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDEgvragrsipLKKNVDDALKNpnvTSVEHVVV--------LK--------RTGG 225
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVLEN---------FATTVQQVLAK---TAVKHVVVasmgdllgFKghivnfvvRRVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 226 KI--DWQEGRDLWWHD-LVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL---------VYAALTFKYVF 293
Cdd:PRK07059 171 KMvpAWSLPGHVRFNDaLAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawLQPAFEKKPRP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 294 D----------YHpgdIYWCTAdvgwvtghSYLLygPLACGATTLMfegVPNWPTPARMAQVVDKHQVNILYTAPTAIRA 363
Cdd:PRK07059 251 DqlnfvcalplYH---IFALTV--------CGLL--GMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 364 LMAEGDkaIEGTDRSSLRI-LG---SVGEPInpeAWEWYwKKIGnekCPVVDTWWQTETGGFMITPLPGATELkAGSATR 439
Cdd:PRK07059 315 LLNNPD--FDKLDFSKLIVaNGggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSPVATCNPVDATEF-SGTIGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 440 PFFGVQPALVDNEGN--PLEGATE----GSLVITDSWpgqartlfgdhERFEQTYFSTFKNMYF-SGDGARRDEDGYYWI 512
Cdd:PRK07059 385 PLPSTEVSIRDDDGNdlPLGEPGEicirGPQVMAGYW-----------NRPDETAKVMTADGFFrTGDVGVMDERGYTKI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 513 TGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTlnhgeEPSPELY-AEVRNWVRKEIGPLA 591
Cdd:PRK07059 454 VDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-----KKDPALTeEDVKAFCKERLTNYK 528
|
570 580
....*....|....*....|....*
gi 446000384 592 TPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07059 529 RPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
254-615 |
6.73e-22 |
|
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: 99.05 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 254 NAEDPLFILYTSGSTGKPKGVL--------HTTGGYLVYAALTFKYV-------FDYHPGDIYwctadVGWVTGHSYLLy 318
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 319 gplacgATTLMFegvpnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKA-IEGTDRSSLRILGsvGEPINPEAWEw 397
Cdd:cd17644 178 ------RPEEMR------SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStIDLPSSLRLVIVG--GEAVQPELVR- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 398 YWKKIGNEKCPVVDTWWQTE-TGGFMITPLPGATELKAGSAT--RPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQA 474
Cdd:cd17644 243 QWQKNVGNFIQLINVYGPTEaTIAATVCRLTQLTERNITSVPigRPIANTQVYILDENLQPVPVGVPGELHIGGV--GLA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 475 RTLFG----DHERFEQTYF--STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd17644 321 RGYLNrpelTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVI 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 549 GIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17644 401 VREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-617 |
1.05e-21 |
|
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: 99.04 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 115 RDVC-RFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVR-A 192
Cdd:cd05915 31 YQRArRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPlV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 193 GRSIPLKKNVDDalkNPNvtsvehvvvlkrtggkidwQEGRDLWWHDLVEQASDQHQA-EEMNAEDPLFILYTSGSTGKP 271
Cdd:cd05915 111 EAIRGELKTVQH---FVV-------------------MDEKAPEGYLAYEEALGEEADpVRVPERAACGMAYTTGTTGLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 272 KGVLHT-TGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMFEGVPNwptPARMAQVVDKHQ 350
Cdd:cd05915 169 KGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLD---PASLVELFDGEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 351 VNILYTAPTAIRaLMAEGDKAIEGTDRSSLRILGSVGEPinPEAWeWYWKKIGNEK------CPVV-----DTWWQTEtg 419
Cdd:cd05915 245 VTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVEvrqgygLTETspvvvQNFVKSH-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 420 gFMITPLPGATELKAGSATRPFFGVQPAL------VDNEGNPLEG-ATEGSLVITDswpgqartLFGDHERFEQTYFStf 492
Cdd:cd05915 319 -LESLSEEEKLTLKAKTGLPIPLVRLRVAdeegrpVPKDGKALGEvQLKGPWITGG--------YYGNEEATRSALTP-- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPS 572
Cdd:cd05915 388 DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446000384 573 PELYaevrNWVRKEIGPLAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 468 EELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-636 |
1.14e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 99.47 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIIWEGDDASQskhISYKELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 169 EAVAgRIIDSNSRLVITSDEgVRAGRSIPLKKNVDdalknpnvtSVEHVVVLKRTGGKIDWQEGRD----LWWHDLVEQA 244
Cdd:PRK05620 101 DQIV-HIINHAEDEVIVADP-RLAEQLGEILKECP---------CVRAVVFIGPSDADSAAAHMPEgikvYSYEALLDGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 245 SDQHQAEEMNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLVYAALTFKY-VFDYHPgdIYWCTADVGWV 310
Cdd:PRK05620 170 STVYDWPELDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESFLCcVPIYHV--LSWGVPLAAFM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 311 TGhsyllygplacgaTTLMFEGVPnwPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPI 390
Cdd:PRK05620 248 SG-------------TPLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGSAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 391 NP---EAWEwywKKIGNEkcpVVDTWWQTETG--GFMITPLPGAtelkAGSATRPFFGVQ---PA----LVDNEGNPLEG 458
Cdd:PRK05620 311 PPiliKAWE---ERYGVD---VVHVWGMTETSpvGTVARPPSGV----SGEARWAYRVSQgrfPAsleyRIVNDGQVMES 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 459 A--TEGSLVITDSW-------------PGQARTLFGDHERFEQTYFsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK05620 381 TdrNEGEIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRF-TADGWLRTGDVGSVTRDGFLTIHDRARDVIRSG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 524 GHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK05620 460 GEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEID 539
|
570 580 590
....*....|....*....|....*....|....
gi 446000384 604 KTRSGKIMRRILRK-IAAGDTsnlgDTSTLADPG 636
Cdd:PRK05620 540 KTSVGKFDKKDLRQhLADGDF----EIIKLKGPG 569
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
1.34e-21 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 88.30 E-value: 1.34e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 24 YEAMYQQSINVPDTFWGEQGKILDWIKPYQKVKNTSFAPGnvsIKWYEDGTLNLAANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
126-616 |
7.50e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 96.66 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 126 ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSR-LVITSD-----EGVRAGRSIplk 199
Cdd:PRK08974 68 GLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVIVSNfahtlEKVVFKTPV--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 200 KNV-----DDALKNPNVTSVEHVV-VLKRTGGKIDW----------QEGRDLwwhdlveqasdQHQAEEMNAEDPLFILY 263
Cdd:PRK08974 145 KHViltrmGDQLSTAKGTLVNFVVkYIKRLVPKYHLpdaisfrsalHKGRRM-----------QYVKPELVPEDLAFLQY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 264 TSGSTGKPKGVLHTTGGYL--------VYAALtfkyvfdYHPGDIYWCTAdvgwvtghsYLLYGPLACGATTLMFegvpn 335
Cdd:PRK08974 214 TGGTTGVAKGAMLTHRNMLanleqakaAYGPL-------LHPGKELVVTA---------LPLYHIFALTVNCLLF----- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 wptparmaqvVDKHQVNILYTAPTAIRALMAEGDK----AIEGT----------------DRSSLRILGSVGEPINPEAW 395
Cdd:PRK08974 273 ----------IELGGQNLLITNPRDIPGFVKELKKypftAITGVntlfnallnneefqelDFSSLKLSVGGGMAVQQAVA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EwYWKKIgnEKCPVVDTWWQTETGGfMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLvitdsWPGQAR 475
Cdd:PRK08974 343 E-RWVKL--TGQYLLEGYGLTECSP-LVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGEL-----WVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 476 TLFGDHERFEQTYfSTFKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNI 554
Cdd:PRK08974 414 VMLGYWQRPEATD-EVIKDGWLAtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 555 KGQAIYAYVTLNhgeepSPELYA-EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08974 493 SGEAVKIFVVKK-----DPSLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-617 |
1.06e-20 |
|
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: 95.07 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 83 DRHLQENGDRTAIiwegDDASQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:cd17653 4 ERIAAAHPDAVAV----ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 163 FGGfSPEAVAGRIID-SNSRLVITSDegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlv 241
Cdd:cd17653 78 DAK-LPSARIQAILRtSGATLLLTTD------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 242 eqasdqhqaeemNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA---------------ALTFKYVFDYhpgdiywCTAD 306
Cdd:cd17653 103 ------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsqpparldvgpgsrvAQVLSIAFDA-------CIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 307 VgwvtghsyllYGPLACGATTLMFEGVPNWPTPARmaqvvdkhQVNILYTAPTAIRALmaegdkaiEGTDRSSLRILGSV 386
Cdd:cd17653 164 I----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL--------SPQDFPNLKTIFLG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 387 GEPINPeawewywkkignekcPVVDTWWQ----------TETggfmiTPLPGATELKAGSAT---RPFFGVQPALVDNEG 453
Cdd:cd17653 218 GEAVPP---------------SLLDRWSPgrrlynaygpTEC-----TISSTMTELLPGQPVtigKPIPNSTCYILDADL 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 454 NPLEGATEGSLVItdSWPGQARTLFGDHE----RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:cd17653 278 QPVPEGVVGEICI--SGVQVARGYLGNPAltasKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINL 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 530 AEIESALVAHPKIAEAAVVgIPHNikgQAIYAYVTlnhgeePSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd17653 356 EEIEEVVLQSQPEVTQAAA-IVVN---GRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 446000384 610 IMRRILRK 617
Cdd:cd17653 426 VDRKALRE 433
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
4.82e-20 |
|
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: 93.39 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGddasQSkhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG----QS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITsdegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqa 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 251 eemNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAALTFKYVFDYHPGDIYWCTADVGWvTGHSYLLYGPLACGATTL 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 329 MFEGVPNWPTpARMAQVVDKHQVNILYTAPTAIRALMAegdkaiegTDRSSLRILGSVGEPInpeawewywKKIGNEKCP 408
Cdd:cd17645 175 VVPSERRLDL-DALNDYFNQEGITISFLPTGAAEQFMQ--------LDNQSLRVLLTGGDKL---------KKIERKGYK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 409 VVDTWWQTETGgFMITPLPGATELKAGSATRPFFGVQpALVDNEGNPL--EGATeGSLVITDSwpGQARTLFG----DHE 482
Cdd:cd17645 237 LVNNYGPTENT-VVATSFEIDKPYANIPIGKPIDNTR-VYILDEALQLqpIGVA-GELCIAGE--GLARGYLNrpelTAE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 483 RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAY 562
Cdd:cd17645 312 KFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 563 VTLNhgEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 392 VTAP--EEIPHE---ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
108-616 |
1.33e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.17 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragrsiPLKknvdDALKNPNVTSVEhvvvlkrtggkidwqegrdlwwhDLVEQASDQHQA--EEMNAEDPLFILYTS 265
Cdd:PRK06060 111 ---------ALR----DRFQPSRVAEAA-----------------------ELMSEAARVAPGgyEPMGGDALAYATYTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegVPNWPTPARMAQV 345
Cdd:PRK06060 155 GTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV----INSAPVTPEAAAI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 346 VD-KHQVNILYTAPTairaLMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNekCPVVDTWWQTETGGFMIT 424
Cdd:PRK06060 231 LSaRFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 425 PlpGATELKAGSATR--PFFGVQPALVDnegnpleGATEGSLVITDSW---PGQArtlfgdherfeQTYFSTFKNMYFSG 499
Cdd:PRK06060 305 N--RVDEWRLGTLGRvlPPYEIRVVAPD-------GTTAGPGVEGDLWvrgPAIA-----------KGYWNRPDSPVANE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 500 ------DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSP 573
Cdd:PRK06060 365 gwldtrDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDG 444
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446000384 574 ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 445 SVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
104-617 |
1.40e-19 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 92.11 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 104 QSKHISYKELHRDVCRFANTLL-ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRL 182
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 183 VItsdegvragrsiplkknVDDalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemnaEDPLFIL 262
Cdd:cd05937 82 VI-----------------VDP---------------------------------------------------DDPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 263 YTSGSTGKPKGVLHTTGGYLVyAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtp 339
Cdd:cd05937 94 YTSGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsrkFSASQFWK-- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 340 armaQVVDKHQVNILYTAPTaIRALMAegdKAIEGTDRSSlRILGSVGEPINPEAWEWYWKKIGnekCPVVD-------- 411
Cdd:cd05937 171 ----DVRDSGATIIQYVGEL-CRYLLS---TPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFN---VPEIGefyaateg 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 --TWWQTETGGFMItplpGATELKaGSATRPFFGVQPALVD---NEGNPLEGATEG-SLVITDSWPGQA--RTLFGDHER 483
Cdd:cd05937 239 vfALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVKmdpETDDPIRDPKTGfCVRAPVGEPGEMlgRVPFKNREA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 484 FeQTYFSTFK--------------NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd05937 314 F-QGYLHNEDatesklvrdvfrkgDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 549 GI--PHNiKGQAIYAYVTL-NHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05937 393 GVkvPGH-DGRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
108-619 |
3.44e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 91.42 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLE-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSR-LV-- 183
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARaLVyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 184 ---------ITSDEG------VRAGRSIPLKKNvddALKNPNVTSVEHVV----VLKRTGGKIDWQEGRDLwwhdlveqa 244
Cdd:PRK12492 130 nmfgklvqeVLPDTGieylieAKMGDLLPAAKG---WLVNTVVDKVKKMVpayhLPQAVPFKQALRQGRGL--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 245 sdQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGD--------------------IYWCT 304
Cdd:PRK12492 198 --SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN-LVANMLQVRACLSQLGPDgqplmkegqevmiaplplyhIYAFT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 305 ADVG--WVTG-HSYLLYGPLACGAttlMFEGVPNWPTPARMAqvvdkhqVNILYTAptairaLMAEGDkaIEGTDRSSLR 381
Cdd:PRK12492 275 ANCMcmMVSGnHNVLITNPRDIPG---FIKELGKWRFSALLG-------LNTLFVA------LMDHPG--FKDLDFSALK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 382 ILGSVGEPINPEAWEwYWKKIGNekCPVVDTWWQTETGGFMITPlPGATELKAGSATRPFFGVQPALVDNEGNPLEGATE 461
Cdd:PRK12492 337 LTNSGGTALVKATAE-RWEQLTG--CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDGNELPLGER 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 462 GSLVITDSwpgqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 540
Cdd:PRK12492 413 GELCIKGP-----QVMKGYWQQPEATAEALDAEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 541 KIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAevrnWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-615 |
4.47e-19 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 91.33 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 EgvragrsiplkKNVDDALK-NPNVTSVEHVVVLKRTGGKiDWQEGRDLWWHDLVEQASDQHQAE---------EMNAED 257
Cdd:cd17641 92 E-----------EQVDKLLEiADRIPSVRYVIYCDPRGMR-KYDDPRLISFEDVVALGRALDRRDpglyerevaAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 258 PLFILYTSGSTGKPKGVLHTTGGYL----VYAALTFKyvfdyHPGDIYWCTADVGWVTGHSYLLYGPLACG--------A 325
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLghcaAYLAADPL-----GPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeeP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 326 TTLM-----------------FEGVPNwPTPARMA------QVVDKHQVNILYTA----------PTAIRALMAEGDKAI 372
Cdd:cd17641 235 ETMMedlreigptfvllpprvWEGIAA-DVRARMMdatpfkRFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADALL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 373 EGTDR-----SSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQTETGGFmitplpgATELKAGSAtrPFFGVQPA 447
Cdd:cd17641 314 FRPLRdrlgfSRLRSAATGGAALGPDTFRFF-HAIG---VPLKQLYGQTELAGA-------YTVHRDGDV--DPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 448 LVDNEgnpLEGATEGSLVITDswPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GH 525
Cdd:cd17641 381 FPGTE---VRIDEVGEILVRS--PG---VFVGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVGTTSdGT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 526 RLGTAEIESALVAHPKIAEAAVVGI------------PHNI------KGQAIYAYVTLNHgeepSPELYAEVRNWVRKEI 587
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLGAgrpyltaficidYAIVgkwaeqRGIAFTTYTDLAS----RPEVYELIRKEVEKVN 528
|
570 580 590
....*....|....*....|....*....|....*..
gi 446000384 588 GPLATPDVLHWTDSLPK---------TRSGKIMRRIL 615
Cdd:cd17641 529 ASLPEAQRIRRFLLLYKeldaddgelTRTRKVRRGVI 565
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-621 |
1.01e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.38 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 233 RDLWWHDLVEQASDQHQAEEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYL-------VYAALTfkyvfdyhPGDIYWCT 304
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLnnqlskvPYLALS--------EADVIAQT 3916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 305 ADVGWVTGHSYLLYGPLAcGATTlmfEGVPNW----PTpARMAQVVDKhQVNILYTAPTAIRALMAEGDKAIEGtdrssL 380
Cdd:PRK05691 3917 ASQSFDISVWQFLAAPLF-GARV---EIVPNAiahdPQ-GLLAHVQAQ-GITVLESVPSLIQGMLAEDRQALDG-----L 3985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 381 RILGSVGEPINPE-AWEWY--WKKIGnekcpVVDTWWQTETG---GFMITPLPG--ATELKAGSATRP----FFGVQPAL 448
Cdd:PRK05691 3986 RWMLPTGEAMPPElARQWLqrYPQIG-----LVNAYGPAECSddvAFFRVDLAStrGSYLPIGSPTDNnrlyLLDEALEL 4060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 449 VdnegnPLeGATeGSLVITDSwpGQARTLFGDHERFEQTYF-----STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK05691 4061 V-----PL-GAV-GELCVAGT--GVGRGYVGDPLRTALAFVphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR 4131
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 524 GHRLGTAEIESALVAHPKIAEAAvVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK05691 4132 GYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLP 4210
|
410
....*....|....*...
gi 446000384 604 KTRSGKIMRRILRKIAAG 621
Cdd:PRK05691 4211 LNANGKLDRKALPALDIG 4228
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
91-615 |
1.61e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 89.29 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIweGDDASqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK13383 50 GRTAII--DDDGA----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAGRIIDSNSRLVITSDEGVR----AGRSI----PLKKNVDDALKNPNVTSvehvvvlkrtGGKIdwqegrdlwwhdlve 242
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAEriagADDAVavidPATAGAEESGGRPAVAA----------PGRI--------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 243 qasdqhqaeemnaedplfILYTSGSTGKPKGVLHT---TGGYLVYAALTFKYVFdyHPGDIYWCTADVGWVTGHSYLLYg 319
Cdd:PRK13383 179 ------------------VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRL--RTGSRISVAMPMFHGLGLGMLML- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 320 PLACGATTLMFEgvpNWPTPARMAQVvDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYW 399
Cdd:PRK13383 238 TIALGGTVLTHR---HFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 400 KKIGNekcPVVDTWWQTETG-GFMITPlpgaTELKAGSAT--RPFFGVQPALVDNEGNPLEGATEGSLVITDSWPGQART 476
Cdd:PRK13383 314 DTYGD---ILYNGYGSTEVGiGALATP----ADLRDAPETvgKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 477 LFGDHerfeqtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKG 556
Cdd:PRK13383 387 DGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 557 QAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 459 HRLAAFVVLHPGSGVDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
1.65e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 87.17 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 261 ILYTSGSTGKPKGVL--HTTGgYLVYAAltfkyvfdyhpgdiyWCtaDVGWVT-GHSYLLYGP-----------LAC--- 323
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPffhtfgykagiVACllt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 GATTL---MFEgvpnwptPARMAQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:cd17638 67 GATVVpvaVFD-------VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNEKcpVVDTWWQTETG-GFMITPLPGATELkAGSATRPFFGVQPALVDnegnplegatEGSLVITDswPGQARTLFG 479
Cdd:cd17638 138 ELGFET--VLTAYGLTEAGvATMCRPGDDAETV-ATTCGRACPGFEVRIAD----------DGEVLVRG--YNVMQGYLD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 480 DHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17638 203 DPEATAEAIDA--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446000384 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 281 KAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
247-615 |
2.77e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.84 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 247 QHQAeemnaedplFILYTSGSTGKPKGVLHTTGGYLVYAALTFKyVFDYHPGD----IYWCTADVGwvtghSYLLYGPLA 322
Cdd:PRK05691 2333 QHQA---------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLLVPLL 2397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 323 CGATtLMFEGVPNWPTpARMAQVVDKHQVNILYTAPT----AIRALMAEGDkaiegtdRSSLRILGSVGEPINPEawewY 398
Cdd:PRK05691 2398 CGAR-VVLRAQGQWGA-EEICQLIREQQVSILGFTPSygsqLAQWLAGQGE-------QLPVRMCITGGEALTGE----H 2464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 399 WKKIGNEKCPVV--DTWWQTETggfMITPL--PGATELKAGSATRPFFGVQPALV----DNEGNPL-EGATeGSLVITDS 469
Cdd:PRK05691 2465 LQRIRQAFAPQLffNAYGPTET---VVMPLacLAPEQLEEGAASVPIGRVVGARVayilDADLALVpQGAT-GELYVGGA 2540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 wpGQARtlfGDH-------ERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPK 541
Cdd:PRK05691 2541 --GLAQ---GYHdrpgltaERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA 2615
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 542 IAEAAVVGIpHNIKGQAIYAYV---TLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 2616 VREAVVLAL-DTPSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
88-618 |
1.56e-17 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 86.18 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 88 ENGDRTAIIWEGDDASQSKhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACarigavhsvIFGGFS 167
Cdd:cd05906 21 ERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 168 PeavagriidsnsrlvitsdegvragrsIPLKKNVDDALKNPNVTSVEHV-------VVLKRTGGKIDWQEGRDLWWH-- 238
Cdd:cd05906 91 P---------------------------APLTVPPTYDEPNARLRKLRHIwqllgspVVLTDAELVAEFAGLETLSGLpg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 239 ---DLVEQASD---QHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKyVFDYHPGDIY--WCTAD--VG 308
Cdd:cd05906 144 irvLSIEELLDtaaDHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLDhvGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 309 WVTGHSYLLYgpLACG----ATTLMFEGVPNWptparmAQVVDKHQVNILYtAPTAIRALMAEGDKAIEGT--DRSSLRI 382
Cdd:cd05906 223 LVELHLRAVY--LGCQqvhvPTEEILADPLRW------LDLIDRYRVTITW-APNFAFALLNDLLEEIEDGtwDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 383 LGSVGEPINPEAWEWYWKKIgnEKCPVVDT-----WWQTETGGFMI----TPLPGAT-ELKAGSATRPFFGVQPALVDNE 452
Cdd:cd05906 294 LVNAGEAVVAKTIRRLLRLL--EPYGLPPDairpaFGMTETCSGVIysrsFPTYDHSqALEFVSLGRPIPGVSMRIVDDE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 453 GNPLEGATEGSLVItdswpgQARTLFGDHERFEQTYFSTFKN--MYFSGDGARRDeDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:cd05906 372 GQLLPEGEVGRLQV------RGPVVTKGYYNNPEANAEAFTEdgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 531 EIESAL-----VAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSpELYAEVRNWVRKEIG-------PLAtpdvlhw 598
Cdd:cd05906 445 EIEAAVeevpgVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALS-ETLRAIRSVVSREVGvspayliPLP------- 516
|
570 580
....*....|....*....|
gi 446000384 599 TDSLPKTRSGKIMRRILRKI 618
Cdd:cd05906 517 KEEIPKTSLGKIQRSKLKAA 536
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
104-612 |
7.36e-17 |
|
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: 83.65 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 104 QSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLV 183
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 184 ITSDEgvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemnaEDPLFILY 263
Cdd:cd05914 84 FVSDE-------------------------------------------------------------------DDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 264 TSGSTGKPKGVLHTTGGYLVYAALTFKYVFdYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwPTPARMA 343
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI---PSAKIIA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 344 QVVDKHQVNILYTAPTAI--RALMAE--------------------------GDKAIEGTDrSSLRILGSVGEPINPEAw 395
Cdd:cd05914 173 LAFAQVTPTLGVPVPLVIekIFKMDIipkltlkkfkfklakkinnrkirklaFKKVHEAFG-GNIKEFVIGGAKINPDV- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWYWKKIGnekCPVVDTWWQTETGGFMITPLPGatELKAGSATRPFFGVQPALVDnegnPLEGATEGSLVITDSwpgqaR 475
Cdd:cd05914 251 EEFLRTIG---FPYTIGYGMTETAPIISYSPPN--RIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGP-----N 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 476 TLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDV-LNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHN 553
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFhTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 554 IKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGpLATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 397 LVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-619 |
1.81e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.97 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEgddasqSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PLN02479 26 LERAAVVHPTRKSVVHG------SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 162 IFGGFSPEAVAGRIIDSNSRLVITSDE---------GVRAGRSI-----PL----------KKNVDDALKNpnvTSVEHV 217
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVDQEfftlaeealKILAEKKKssfkpPLlivigdptcdPKSLQYALGK---GAIEYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 218 VVLKRTGGKIDWQEGRDLWwhdlveqasdqhqaeemnaeDPLFILYTSGSTGKPKGV-LHTTGGYLvyAALTFKYVFDYH 296
Cdd:PLN02479 177 KFLETGDPEFAWKPPADEW--------------------QSIALGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 297 PGDIY-----------WC-TADVGWVTGHSYLL--------YGPLA-------CGATTL--MFEGVPNWPTPARMAQVVD 347
Cdd:PLN02479 235 EGAVYlwtlpmfhcngWCfTWTLAALCGTNICLrqvtakaiYSAIAnygvthfCAAPVVlnTIVNAPKSETILPLPRVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 348 khqVNILYTAPTAIrALMAEGDKAIEGTDRSSLrilgsvGEPINPE---AWEWYWKKIgnekcpvvdtwwqtetggfmit 424
Cdd:PLN02479 315 ---VMTAGAAPPPS-VLFAMSEKGFRVTHTYGL------SETYGPStvcAWKPEWDSL---------------------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 425 PLPGATELKAGSATRpFFGVQPA-LVDNEGN---PLEGATEGSLVITDS--WPGQARTLFGDHERFEQTYFStfknmyfS 498
Cdd:PLN02479 363 PPEEQARLNARQGVR-YIGLEGLdVVDTKTMkpvPADGKTMGEIVMRGNmvMKGYLKNPKANEEAFANGWFH-------S 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 499 GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPE--LY 576
Cdd:PLN02479 435 GDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLA 514
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 446000384 577 AEVRNWVRKEIGPLATPDVLHWtDSLPKTRSGKIMRRILRKIA 619
Cdd:PLN02479 515 EDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-580 |
1.88e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 82.64 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 84 RHL----QENGDRTAII----WEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 156 GAVHSVIFGGFSPEAVAGRIIDSNSRLVITsdegvragrsIPlKKNVDDALKNPNVTSVEHVVVlkrTGGKIDWqEGRDL 235
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIG----------IP-KAHLARRLFGWGKPSVRRLVT---VGGRLLW-GGTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 236 wwhDLVEQASDQHQAE--EMNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAltfKYVFDYHPGDIYWCTADVgwvt 311
Cdd:PRK09274 155 ---ATLLRDGAAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEIDLPTFPL---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 312 ghsYLLYGPlACGATTLmfegVPNW-PT------PARMAQVVDKHQVNILYTAPTAIRALMAEGdkaiEGTDRS--SLRI 382
Cdd:PRK09274 225 ---FALFGP-ALGMTSV----IPDMdPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYG----EANGIKlpSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 383 LGSVGEPINPEAWEWYwKKIGNEKCPVVDTWWQTETggfmitpLP----GATEL--KAGSATRPFFGVqpaLVdneGNPL 456
Cdd:PRK09274 293 VISAGAPVPIAVIERF-RAMLPPDAEILTPYGATEA-------LPissiESREIlfATRAATDNGAGI---CV---GRPV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 457 EGATEGSLVITD----SWpGQARTLF----------GDHerFEQTYF----STFKN------------MyfsGDGARRDE 506
Cdd:PRK09274 359 DGVEVRIIAISDapipEW-DDALRLAtgeigeivvaGPM--VTRSYYnrpeATRLAkipdgqgdvwhrM---GDLGYLDA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPhnIKGQAIYAY-VTLNHGEEPSPE-LYAEVR 580
Cdd:PRK09274 433 QGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLcVELEPGVACSKSaLYQELR 506
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
376-616 |
2.01e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.89 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 376 DRSSLRILGSVGEPINPEAWEwYWKKIGNekCPVVDTWWQTETGGFMITPLPGATELkaGSATRPFFGVQPALVDNEGNP 455
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAE-RWKEVTG--CAICEGYGMTETSPVVSVNPSQAIQV--GTIGIPVPSTLCKVIDDDGNE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 456 L------EGATEGSLVITDSWPGQARTlfgDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK05677 399 LplgevgELCVKGPQVMKGYWQRPEAT---DEILDSDGWLKT-------GDIALIQEDGYMRIVDRKKDMILVSGFNVYP 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 530 AEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK05677 469 NELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
....*..
gi 446000384 610 IMRRILR 616
Cdd:PRK05677 546 ILRRELR 552
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
507-617 |
5.25e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.09 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGeePSPELyAEVRNWVRKE 586
Cdd:PRK07824 246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGG--PAPTL-EALRAHVART 322
|
90 100 110
....*....|....*....|....*....|.
gi 446000384 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 323 LDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
237-584 |
2.05e-15 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 79.43 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 237 WHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYlVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPLACGATTLMFEGVPNWPTPARMAQ-----------------VVDK---HQVNILYTAPTaIRALMaeGDKAIEGTD 376
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEDVQRARptlffsvprlwtkfqqgVQDKipqQKLNLLLKIPV-VNSLV--KRKVLKGLG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 377 RSSLRILGSVGEPINPEAWEWYwKKIGnekCPVVDTWWQTETGGFMITPLPGATelKAGSATRPFFGVQpalvdnegnpL 456
Cdd:cd05932 274 LDQCRLAGCGSAPVPPALLEWY-RSLG---LNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVE----------V 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 457 EGATEGSLVITDswPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTAEIES 534
Cdd:cd05932 338 RISEDGEILVRS--PA---LMMGYYKDPEATAEAFTADGFLrTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIEN 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446000384 535 ALVAHPKIAEAAVVG--IPHNIkgqaiyAYVTLNhgEEPSPELYAEVRNWVR 584
Cdd:cd05932 413 KLAEHDRVEMVCVIGsgLPAPL------ALVVLS--EEARLRADAFARAELE 456
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
3.55e-15 |
|
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: 76.96 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYwctadvgwvtghsyLLYGPL------ACGATTLMF 330
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQALVLAVLQAIDEGTVF--------------LNSGPLfhigtlMFTLATFHA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 331 EG----VPNWpTPARMAQVVDKHQVNILY-TAPT--AIRALMAEGdkaieGTDRSSLRILgsvgepinPEAWEWywkkig 403
Cdd:cd17636 66 GGtnvfVRRV-DAEEVLELIEAERCTHAFlLPPTidQIVELNADG-----LYDLSSLRSS--------PAAPEW------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 404 NEKCPVVDTWW--------QTETGGFMITPLPGATElkAGSATRPFFGVQPALVDNEGNPL------EGATEGSLVITDS 469
Cdd:cd17636 126 NDMATVDTSPWgrkpggygQTEVMGLATFAALGGGA--IGGAGRPSPLVQVRILDEDGREVpdgevgEIVARGPTVMAGY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 470 W--PG--QARTLFGDHErfeqtyfstfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd17636 204 WnrPEvnARRTRGGWHH---------------TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADA 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 546 AVVGIPHNIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 269 AVIGVPDPRWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
108-617 |
6.39e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 71.23 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfspeavagriidsNSRLvitsd 187
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI----------------NYNL----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 egvragRSIPLKKNVddalknpNVTSVEHVVVlkrtggkidwqegrdlwwhdlveqasdqhqaeemnaeDPLFILYTSGS 267
Cdd:cd05940 63 ------RGESLAHCL-------NVSSAKHLVV-------------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 268 TGKPKGVLHTTGGYLVYAALtFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPTparmaq 344
Cdd:cd05940 93 TGLPKAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDD------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 345 vVDKHQVNILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEKcpVVDTWWQTE--TGGFM 422
Cdd:cd05940 166 -IRKYQATIFQYIGELCRYLLNQ--PPKPTERKHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 423 ITPLPGATElKAGSATRPFFGVQPALVDNE-GNPLEGATEGSLVITDSWPGQARTLFGDHERF----------EQTYFST 491
Cdd:cd05940 239 FFGKPGAIG-RNPSLLRKVAPLALVKYDLEsGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFdgytdpaateKKILRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 492 FK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP-HNIKGQAIYAYVTLNH 567
Cdd:cd05940 318 FKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMAAIVLQP 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446000384 568 GEEPSPELYAevrNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 398 NEEFDLSALA---AHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
109-616 |
9.27e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAI-----YMPMVpeaavAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLV 183
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTlawngYRHLE-----AYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 184 ---ITSdegvragrsIPLKKNVDDALKNpnvtsVEHVVVL----KRTGGKIDWqegrdLWWHDLVEQASDQHQAEEMNAE 256
Cdd:PRK07008 116 lfdLTF---------LPLVDALAPQCPN-----VKGWVAMtdaaHLPAGSTPL-----LCYETLVGAQDGDYDWPRFDEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYA---ALTfkyvfdyhpgDIYWCTA-DV-----------GWVTGHSYLLYGpl 321
Cdd:PRK07008 177 QASSLCYTSGTTGNPKGALYSHRSTVLHAygaALP----------DAMGLSArDAvlpvvpmfhvnAWGLPYSAPLTG-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 322 acgaTTLMFegvpnwPTPA----RMAQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLR---ILGSVGEPINPEA 394
Cdd:PRK07008 245 ----AKLVL------PGPDldgkSLYELIEAERVTFSAGVPTVWLGLLNHMREA--GLRFSTLRrtvIGGSACPPAMIRT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 395 WEwywKKIGNEkcpVVDTWWQTEtggfmITPLPGATELKAGSATRP--------------FFGVQPALVDNEGNPL--EG 458
Cdd:PRK07008 313 FE---DEYGVE---VIHAWGMTE-----MSPLGTLCKLKWKHSQLPldeqrkllekqgrvIYGVDMKIVGDDGRELpwDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 459 ATEGSLVITDSWPGQaRTLFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 538
Cdd:PRK07008 382 KAFGDLQVRGPWVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 539 HPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-549 |
1.15e-12 |
|
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: 70.47 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 106 KHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSvifggfspeavagriidsnsrlvit 185
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDV------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 186 sdegVRAGRSiplkkNVDDALKnpNVTSVEHVVVlkrtggkidwqegrdlwwhdLVEQASDqhqaeemnaeDPLFILYTS 265
Cdd:cd17640 59 ----VRGSDS-----SVEELLY--ILNHSESVAL--------------------VVENDSD----------DLATIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWCTADVgWvtgHSY---LLYGPLACGATTLmfegvpnWPTPARM 342
Cdd:cd17640 98 GTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 343 AQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILG---SVGE---PIN-----PEAWEWYWKKIGnekCPVVD 411
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 TWWQTETGGFMITPLPGATelKAGSATRPFFGVQPALVDNEGN-PLEGATEGSLVITDswPGQARTLFGDHERFEQTYFS 490
Cdd:cd17640 243 GYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRG--PQVMKGYYKNPEATSKVLDS 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446000384 491 tfKNMYFSGDGARRDEDGYYWITGRVDD--VLNvSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd17640 319 --DGWFNTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-580 |
1.68e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 69.80 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 255 AEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAlTFKYVFDYHPGDIYWCTADVgwvtghsYLLYGPlACGATTLMFEGVP 334
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 335 NWP---TPARMAQVVDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYwKKIGNEKCPVVD 411
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARL-RKMLSDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 TWWQTET-------GGFMITPLPGATELKAGSAT-RPFFGVQPALV--DNEGNPLEGATE-------GSLVITDswPGQA 474
Cdd:cd05910 232 PYGATEAlpvssigSRELLATTTAATSGGAGTCVgRPIPGVRVRIIeiDDEPIAEWDDTLelprgeiGEITVTG--PTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 475 RTLfgdHERFEQTYFSTFKN-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd05910 310 PTY---VNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
330 340 350
....*....|....*....|....*....|.
gi 446000384 550 IPHNIKGQAIYAYVTLNHGEEPSPELYAEVR 580
Cdd:cd05910 387 VGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
254-615 |
2.89e-12 |
|
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: 69.35 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 254 NAEDPLFILYTSGSTGKPKGVLHTTGGYL----------------VYAALTF-KYVFDYHpgdIYWCTADVgwVTGHSYL 316
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseryfgrdngDEAVLFFsNYVFDFF---VEQMTLAL--LNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPlacgattlmfEGVPnwpTPARMAQVVDKHQVNILYTAPTAIralmaegdKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:cd17648 167 VPPD----------EMRF---DPDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 397 wywKKIGNEKCPVVDTWWQTETGGF-MITPLPGATELKAgSATRPFFGVQPALVDNEGNPLEGATEGSLVITDSwpGQAR 475
Cdd:cd17648 226 ---KLRSRFAGLIINAYGPTETTVTnHKRFFPGDQRFDK-SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGD--GVAR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 476 tlfGDH-------ERFEQTYFST--------FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 540
Cdd:cd17648 300 ---GYLnrpeltaERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 541 KIAEAAVVGIPHNIKGQA-----IYAYVTLNHGEEPSpelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17648 377 GVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPE----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
111-617 |
3.27e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.44 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 111 KELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITsDEGV 190
Cdd:PLN02860 36 HEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-DETC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 191 RagrSIPLKknvddaLKNPNVTSVEHVVVLKRTGGKI-----DWQEGRDLWWHDLVEQASDQHQAeemnAEDPLFILYTS 265
Cdd:PLN02860 115 S---SWYEE------LQNDRLPSLMWQVFLESPSSSVfiflnSFLTTEMLKQRALGTTELDYAWA----PDDAVLICFTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 266 GSTGKPKGVL--HTTggyLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLygplacgaTTLMFEG----VPNWPTP 339
Cdd:PLN02860 182 GTTGRPKGVTisHSA---LIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL--------AMLMVGAchvlLPKFDAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 340 ARMaQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLR-IL---GSVGEPINPEAWEWYWK-KIGN-----EKC-- 407
Cdd:PLN02860 251 AAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRkILnggGSLSSRLLPDAKKLFPNaKLFSaygmtEACss 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 408 ----PVVDTWWQT--ETGGFMITPLPGATELKAGS-----ATRPFFGVQPALVDNEGNPLegaTEGSLVITDSWpgqART 476
Cdd:PLN02860 330 ltfmTLHDPTLESpkQTLQTVNQTKSSSVHQPQGVcvgkpAPHVELKIGLDESSRVGRIL---TRGPHVMLGYW---GQN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 477 LFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKG 556
Cdd:PLN02860 404 SETASVLSNDGWLDT-------GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLT 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 557 QAIYAYVTL--------------NHGEEPSPE---LYAEVRNWVRKEIGPLatpdVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02860 477 EMVVACVRLrdgwiwsdnekenaKKNLTLSSEtlrHHCREKNLSRFKIPKL----FVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-617 |
1.46e-11 |
|
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: 67.06 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 106 KHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 186 SdegvragrsiplkknvddaLKNPnvtsvehvvvlkrtggkidwqegrdlwwhdLVEQASD-QHQAEEMNAEDPLFILYT 264
Cdd:cd05939 82 N-------------------LLDP------------------------------LLTQSSTePPSQDDVNFRDKLFYIYT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 265 SGSTGKPKGVLHTTGGYLVYAALTFkYVFDYHPGDI-YWC-----TAdvGWVTGHSYLLYGplacGATTLM---FEGVPN 335
Cdd:cd05939 113 SGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVvYDClplyhSA--GGIMGVGQALLH----GSTVVIrkkFSASNF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 WPTparmaqvVDKHQVNILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGNEK--------- 406
Cdd:cd05939 186 WDD-------CVKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQigefygate 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 407 --CPVVDTWWQTETGGFMITPLPGATELK-------AGSATRPFFGV----QP----ALVD--NEGNPLEgATEGSLVIT 467
Cdd:cd05939 255 gnSSLVNIDNHVGACGFNSRILPSVYPIRlikvdedTGELIRDSDGLcipcQPgepgLLVGkiIQNDPLR-RFDGYVNEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 468 DSWPGQARTLF--GDherfeqtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd05939 334 ATNKKIARDVFkkGD-------------SAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446000384 546 AVVG--IPHnIKGQAIYAYVTLNHGEEPSPELYAEvrnwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05939 401 VVYGveVPG-VEGRAGMAAIVDPERKVDLDRFSAV----LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
90-610 |
3.04e-11 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 65.96 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 90 GDRTAIIwegDDASQSK-HISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggFSP 168
Cdd:cd17654 1 PDRPALI---IDQTTSDtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA-------YAP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 169 eavagriIDSnsrlviTSDEGvragRSIPLKKNvddalknpnvTSVEHVVVLKRTGGKIdwqegrdLWWHDLVEQASDQH 248
Cdd:cd17654 71 -------IDP------ASPEQ----RSLTVMKK----------CHVSYLLQNKELDNAP-------LSFTPEHRHFNIRT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 249 QAeemnaedPL-FILYTSGSTGKPKGVlHTTGGYLVYAALTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPLAC 323
Cdd:cd17654 117 DE-------CLaYVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLTSpltfDPSVVE-----IFLSLSS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 324 GATTLMfegVPNW--PTPARMAQVVDK-HQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:cd17654 184 GATLLI---VPTSvkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 401 KIGNeKCPVVDTWWQTETGGFMIT--------PLPGATELkAGSATRpffgvqpaLVDNEGNPLEGategslviTDSWPG 472
Cdd:cd17654 261 GKGN-RTRIFNIYGITEVSCWALAykvpeedsPVQLGSPL-LGTVIE--------VRDQNGSEGTG--------QVFLGG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 473 QARTLFGDHErfEQTYFSTfknMYFSGDGARRdEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIaEAAVVGIPH 552
Cdd:cd17654 323 LNRVCILDDE--VTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSD 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446000384 553 NikgQAIYAYVTlnhgeepSPELYAEVRNWVRKEIGPL-ATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17654 396 Q---QRLIAFIV-------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-625 |
8.03e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.63 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 TWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNegnplegaTEGSLVItdswpgQARTLF-GdherfeqtYFS 490
Cdd:PRK07445 260 TYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPAN--------QTGNITI------QAQSLAlG--------YYP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 491 TFKNMY---FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNH 567
Cdd:PRK07445 318 QILDSQgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 568 GeEPSPElyaEVRNWVRKEIGPLATPDvlHW--TDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PRK07445 398 P-SISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-615 |
8.79e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.53 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 82 LDRHLQENGDRTAIIWEGDDasqskhISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIG----- 156
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEK------LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 157 -AVHSvifggfSPEAVAgRIID-SNSRLVI-TSDEGVRAGrSIPLKK--NVDDALKNPNVTSVEHVVvlkrtggkidwqe 231
Cdd:PRK04813 82 vDVSS------PAERIE-MIIEvAKPSLIIaTEELPLEIL-GIPVITldELKDIFATGNPYDFDHAV------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 232 grdlwwhdlveqasdqhqaeemNAEDPLFILYTSGSTGKPKGVlhttggYLVYAAL-TFkyvfdyhpgdIYWCTADVGWV 310
Cdd:PRK04813 141 ----------------------KGDDNYYIIFTSGTTGKPKGV------QISHDNLvSF----------TNWMLEDFALP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 311 TGHSYL-------------LYGPLACGATTLMfegVPNWPT--PARMAQVVDKHQVNILYTAPTAIRalMAEGDKAIEGT 375
Cdd:PRK04813 183 EGPQFLnqapysfdlsvmdLYPTLASGGTLVA---LPKDMTanFKQLFETLPQLPINVWVSTPSFAD--MCLLDPSFNEE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 376 DRSSLRILGSVGEPI-NPEAwewywKKIgNEKCP---VVDTWWQTETGGFM----IT--------PLP-GATelKAGSAT 438
Cdd:PRK04813 258 HLPNLTHFLFCGEELpHKTA-----KKL-LERFPsatIYNTYGPTEATVAVtsieITdemldqykRLPiGYA--KPDSPL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 439 rpffgvqpALVDNEGNPLEGATEGSLVITdswpGQARTL--FGDHERFEQTYFsTFKNM--YFSGDGARRDeDGYYWITG 514
Cdd:PRK04813 330 --------LIIDEEGTKLPDGEQGEIVIS----GPSVSKgyLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE-DGLLFYQG 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 515 RVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGE-EPSPELYAEVRNWVRKEIGPLATP 593
Cdd:PRK04813 396 RIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDfEREFELTKAIKKELKERLMEYMIP 475
|
570 580
....*....|....*....|..
gi 446000384 594 DVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK04813 476 RKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
250-615 |
9.52e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 AEEMNAEDPLFILYTSGSTGKPKGV----------LHttggylVYAAlTFKYVFDYHPgdIYWCTadvgwVTgHSYllyg 319
Cdd:PRK08308 95 AVNYLAEEPSLLQYSSGTTGEPKLIrrswteidreIE------AYNE-ALNCEQDETP--IVACP-----VT-HSY---- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 320 PLACGATTLMFEG-VP---NWPTPARMAQVVDKHQVNILYTAPTAIRAL--MAEGDKAIEgtdrsslRILGSvGEPInPE 393
Cdd:PRK08308 156 GLICGVLAALTRGsKPviiTNKNPKFALNILRNTPQHILYAVPLMLHILgrLLPGTFQFH-------AVMTS-GTPL-PE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 394 AWewyWKKIGNEKCPVVDTWWQTETG-----------GFMITPLPGATeLKAGSatrpffgvqpalvdNEGNPLEgateg 462
Cdd:PRK08308 227 AW---FYKLRERTTYMMQQYGCSEAGcvsicpdmkshLDLGNPLPHVS-VSAGS--------------DENAPEE----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 463 sLVITdswpgqartlFGDHErfeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK08308 284 -IVVK----------MGDKE-------------IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGV 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 543 AEAAVVGIPHNIKGQAIYAYVTLNHGEEPspelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 340 QEAVVYRGKDPVAGERVKAKVISHEEIDP-----VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
103-559 |
2.29e-10 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 63.39 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 103 SQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRL 182
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 183 VITSDegvragrsiplkknvddalknpnvtsvehvvvlkrtggkidwqegrdlwwhdlveqasdqhqaeemNAEDPLFIL 262
Cdd:cd17639 81 IFTDG------------------------------------------------------------------KPDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 263 YTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDiywctADVgwvtghsYLLYGPLA----------C---GAT--- 326
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGN-LVAGIAGLGDRVPELLGP-----DDR-------YLAYLPLAhifelaaenvClyrGGTigy 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 327 ----TL------------------MFEGVP------------NWPTPARMAQVVDKH-------QVNILYTAP------- 358
Cdd:cd17639 162 gsprTLtdkskrgckgdltefkptLMVGVPaiwdtirkgvlaKLNPMGGLKRTLFWTayqsklkALKEGPGTPlldelvf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 359 TAIRALMaeGDKaiegtdrssLRILGSVGEPINPEAWEWywkkIGNEKCPVVDTWWQTETGGFMITPLPGatELKAGSAT 438
Cdd:cd17639 242 KKVRAAL--GGR---------LRYMLSGGAPLSADTQEF----LNIVLCPVIQGYGLTETCAGGTVQDPG--DLETGRVG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 439 RPFFGVQPALVD-NEGNplegategslVITDSWPGQARTLFG---------------DHERFEQTYFSTfknmyfsGDGA 502
Cdd:cd17639 305 PPLPCCEIKLVDwEEGG----------YSTDKPPPRGEILIRgpnvfkgyyknpektKEAFDGDGWFHT-------GDIG 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 503 RRDEDGYYWITGRVDD-VLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAI 559
Cdd:cd17639 368 EFHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAI 425
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-322 |
2.69e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.60 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 188 EgvragrsiPLKKNVDDALKnpnVTSVEHVVVLKRTGGKIDWQEGRDLWWhdLVEQASDQHQAEEMNAEDPLF------- 260
Cdd:PLN02387 187 K--------QLKKLIDISSQ---LETVKRVIYMDDEGVDSDSSLSGSSNW--TVSSFSEVEKLGKENPVDPDLpspndia 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446000384 261 -ILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIywctadvgwvtghsYLLYGPLA 322
Cdd:PLN02387 254 vIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
254-621 |
2.89e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 63.79 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 254 NAEDPLFILYTSGSTGKPKGV-----------------LHTTGGYLVYAALTFKYVFDYHpgdiywctadvgwVTghsyl 316
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVmlshhnilsnieqisdvFNLRNDDVILSSLPFFHSFGLT-------------VT----- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 317 LYGPLACGATTLMfegVPNwPTPARM-AQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAW 395
Cdd:PRK08633 842 LWLPLLEGIKVVY---HPD-PTDALGiAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVA 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 396 EWYWKKIG---------NEKCPVV----------DTWWQTETggfmitplpgatelKAGSATRPFFGVQPALVD-NEGNP 455
Cdd:PRK08633 916 DAFEEKFGirilegygaTETSPVAsvnlpdvlaaDFKRQTGS--------------KEGSVGMPLPGVAVRIVDpETFEE 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 456 LEGATEGSLVITDS-----WPGQA-RTLFGDHERFEQTYfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHR--L 527
Cdd:PRK08633 982 LPPGEDGLILIGGPqvmkgYLGDPeKTAEVIKDIDGIGW-------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMvpL 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 528 GTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTlnHGEEPSPELYAEVRNwvrKEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK08633 1055 GAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHT--CGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGS 1129
|
410
....*....|....
gi 446000384 608 GKIMRRILRKIAAG 621
Cdd:PRK08633 1130 GKLDLKGLKELALA 1143
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-279 |
1.08e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 61.53 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 69 WYEDGTL--NLAANCldrhlQENGDRTAI---------------------IWEGDDASQSKHISYKELHRDVCRFANTLL 125
Cdd:PTZ00216 65 WYYGPNFlqRLERIC-----KERGDRRALayrpvervekevvkdadgkerTMEVTHFNETRYITYAELWERIVNFGRGLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 126 ELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVragrsiplkKNVDDA 205
Cdd:PTZ00216 140 ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNV---------PNLLRL 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446000384 206 LKNPNVTSVEhVVVLKRTGGKIDWQEGRDLWWHDLVE---QASDQHQAE-EMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 211 MKSGGMPNTT-IIYLDSLPASVDTEGCRLVAWTDVVAkghSAGSHHPLNiPENNDDLALIMYTSGTTGDPKGVMHTHG 287
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
91-275 |
1.25e-07 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 55.07 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAII-WEGDDASQSKH--ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:TIGR03443 251 DRTCVVeTPSFLDPSSKTrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 168 PE------AVAgriidSNSRLVITSDegvrAGRSIPL-KKNVDDALKnpNVTSVEHVVVLKR---TGGKIDWQEGRDLww 237
Cdd:TIGR03443 331 PArqtiylSVA-----KPRALIVIEK----AGTLDQLvRDYIDKELE--LRTEIPALALQDDgslVGGSLEGGETDVL-- 397
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446000384 238 hdlveqASDQHQAEE-----MNAEDPLFILYTSGSTGKPKGVL 275
Cdd:TIGR03443 398 ------APYQALKDTptgvvVGPDSNPTLSFTSGSEGIPKGVL 434
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-322 |
1.33e-07 |
|
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: 54.53 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 108 ISYKELHRDVCRFANTLLELGIK--KGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagRIIDSNSRL-VI 184
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAI--EYILNHAEIsIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 185 TSDEGVRagrsiplkknvddalknpnVTSvehvvvlkrtggkidwqegrdlwWHDLVEQ-ASDQHQAEEMNAEDPLFILY 263
Cdd:cd05927 84 FCDAGVK-------------------VYS-----------------------LEEFEKLgKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446000384 264 TSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYH---PGDIYWctadvgwvtghSYLlygPLA 322
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDVYI-----------SYL---PLA 169
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
107-613 |
6.25e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 52.31 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 107 HISYKELHRDVCRFANTLLELGIKKGDVVAIY--MP--MVPEAAVAMLACARIGAVHSvifggfsPEAvagriidsNSRL 182
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPveIAPTAQGLWMRGASLTMLHQ-------PTP--------RTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 183 VITSDEGVRAGRSIPLKKNVddaLKNPNVTSVEhvvVLKRTGGKIDwqEGRDLWwhdlveqASDQHQAEEMNAEDPLFIL 262
Cdd:PRK07768 94 AVWAEDTLRVIGMIGAKAVV---VGEPFLAAAP---VLEEKGIRVL--TVADLL-------AADPIDPVETGEDDLALMQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 263 YTSGSTGKPKGVLHTTG-----GYLVYAALTFKYVFDYHpgdIYW--CTADVGWVTGhsylLYGPLACGATTLMFEGVPN 335
Cdd:PRK07768 159 LTSGSTGSPKAVQITHGnlyanAEAMFVAAEFDVETDVM---VSWlpLFHDMGMVGF----LTVPMYFGAELVKVTPMDF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 336 WPTPARMAQVVDKHQVNILyTAPTAIRALMAE--GDKAIEGT-DRSSLRILGSVGEPINPEAWEWYW---KKIGNEKCPV 409
Cdd:PRK07768 232 LRDPLLWAELISKYRGTMT-AAPNFAYALLARrlRRQAKPGAfDLSSLRFALNGAEPIDPADVEDLLdagARFGLRPEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 410 VDTWWQTET---------GGFMITPLPGATELKA--------GSATRPFF-------GVQPALVDNEGNPL--------- 456
Cdd:PRK07768 311 LPAYGMAEAtlavsfspcGAGLVVDEVDADLLAAlrravpatKGNTRRLAtlgpplpGLEVRVVDEDGQVLpprgvgvie 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 457 ---EGATEGSLVITDSWPGQArtlfgdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK07768 391 lrgESVTPGYLTMDGFIPAQD----------ADGWLDT-------GDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 534 SALVAHPKIAEAAVVGI----PHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGplATPDVLHWTD--SLPKTRS 607
Cdd:PRK07768 454 RAAARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTPS 531
|
....*.
gi 446000384 608 GKIMRR 613
Cdd:PRK07768 532 GKLRRA 537
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-277 |
1.20e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.80 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 54 KVKNTSFAPGNVSIKWYEDGTLNLAAN------------CLDRHLQENGDRTAIIwEGDDASQSKHISYKELHRDVCRFA 121
Cdd:PRK08180 5 RYRPVAFAPPAVEVERRADGTIYLRSAeplgdyprrltdRLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 122 NTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSP------------EAVAGRIidsNSRLVITSDEG 189
Cdd:PRK08180 84 QALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SPayslvsqdfgklRHVLELL---TPGLVFADDGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 190 VRAgrsiplkknvdDALKNPNVTSVEHVVVLKRTGGkidwqeGRDLWWHDLVEQASDQHQAEEMNAEDPLFI---LYTSG 266
Cdd:PRK08180 157 AFA-----------RALAAVVPADVEVVAVRGAVPG------RAATPFAALLATPPTAAVDAAHAAVGPDTIakfLFTSG 219
|
250
....*....|.
gi 446000384 267 STGKPKGVLHT 277
Cdd:PRK08180 220 STGLPKAVINT 230
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
124-620 |
4.02e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 50.35 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 124 LLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfgGFSpeAVAGRIIDS----NSRLVITSDEGVRAGRSIPLK 199
Cdd:PRK06814 674 KLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSAckaaQVKTVLTSRAFIEKARLGPLI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 200 KNVDDALKnpnVTSVEHVVVLKRTGGKIDwqegrdlwwhDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PRK06814 750 EALEFGIR---IIYLEDVRAQIGLADKIK----------GLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHR 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 280 GYLVYAALTFKYVfDYHPGDIYWCTADVgwvtGHSYLLYGplacGATTLMFEGVPN--WPTPAR---MAQVVdkHQVN-- 352
Cdd:PRK06814 817 NLLANRAQVAARI-DFSPEDKVFNALPV----FHSFGLTG----GLVLPLLSGVKVflYPSPLHyriIPELI--YDTNat 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 353 ILYTAPTAIR--ALMAegdkaiEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEkcpVVDTWWQTETGGF--MITPLpg 428
Cdd:PRK06814 886 ILFGTDTFLNgyARYA------HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIR---ILEGYGVTETAPViaLNTPM-- 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 429 atELKAGSATRPFFGVQPALVdnegnPLEGATEGS-LVI-----------TDSwPGQartlfgdHERFEQTYFSTfknmy 496
Cdd:PRK06814 955 --HNKAGTVGRLLPGIEYRLE-----PVPGIDEGGrLFVrgpnvmlgylrAEN-PGV-------LEPPADGWYDT----- 1014
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 497 fsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEpspely 576
Cdd:PRK06814 1015 --GDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTTASDATR------ 1086
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446000384 577 AEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKI----MRRILRKIAA 620
Cdd:PRK06814 1087 AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAA 1135
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
91-393 |
6.98e-06 |
|
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: 49.02 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIWEGDdaSQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACarigavhsvIFGGFSPEA 170
Cdd:cd05908 1 PEGIIFILGD--KKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWAC---------LLGGMIAVP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 171 VAgriidsnsrlvITSDEGVRagrsipLKKN-VDDALKNPNVTSVEHVvvlkrtggkidWQEgrdlwwhdlveqasdqhq 249
Cdd:cd05908 70 VS-----------IGSNEEHK------LKLNkVWNTLKNPYLITEEEV-----------LCE------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 250 aeemNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIY--W--CTADVGWVTGHsyllYGPLACGA 325
Cdd:cd05908 104 ----LADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGM 174
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446000384 326 TTLMFegvpnwPT------PARMAQVVDKHQVNILYTAPTAIRALMAE-GDKAIEGTDRSSLRILGSVGEPINPE 393
Cdd:cd05908 175 NQYLM------PTrlfirrPILWLKKASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
109-275 |
1.23e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.48 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagRIIDSNSRLVITSDE 188
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAV--EFIISHSEVSIVFVE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 gvragrsiplKKNVDDALKN-PNVTSVEHVVVlkrTGGKIDWQEGRDLWWHDLVEQASD---------QHQAEEMNAEDP 258
Cdd:PLN02614 159 ----------EKKISELFKTcPNSTEYMKTVV---SFGGVSREQKEEAETFGLVIYAWDeflklgegkQYDLPIKKKSDI 225
|
170
....*....|....*..
gi 446000384 259 LFILYTSGSTGKPKGVL 275
Cdd:PLN02614 226 CTIMYTSGTTGDPKGVM 242
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
109-607 |
8.96e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.86 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 109 SYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhSVIFGGFSPEAVAGRIIDSNSrlVITSDE 188
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV-AVLMPPDTDLAAAVRLGGVTE--IITDPT 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 GVRAGRSIPlkknvddalknpnvtsvEHVVVLKrtGGkidwqEGRDLwwhDLVEQAS--DQHQAEEMNAEDP-------- 258
Cdd:PRK07868 551 NLEAARQLP-----------------GRVLVLG--GG-----ESRDL---DLPDDADviDMEKIDPDAVELPgwyrpnpg 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 259 -----LFILY-TSGSTGKPKGVlhtTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEG 332
Cdd:PRK07868 604 lardlAFIAFsTAGGELVAKQI---TNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRG 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 333 VpnwpTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRIlGSvGEPINpeawewYWKKIGNEKCP--VV 410
Cdd:PRK07868 681 L----DPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI-GS-GMPTG------LWERVVEAFAPahVV 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 411 DTWWQTEtGGFMITPLPGAtelKAGSATRPFFG-----------VQPALVDNEGNPLEGATEGSLVI--------TDSWP 471
Cdd:PRK07868 749 EFFATTD-GQAVLANVSGA---KIGSKGRPLPGagrvelaaydpEHDLILEDDRGFVRRAEVNEVGVllarargpIDPTA 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 472 GQARTLFGDHErfeqTYFSTfKNMYfsgdgaRRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:PRK07868 825 SVKRGVFAPAD----TWIST-EYLF------RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVE 893
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446000384 552 HNIKGQAIYAyVTLNHGEEPSPelyAEVRNWVRkEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK07868 894 VGGRQLAVAA-VTLRPGAAITA---ADLTEALA-SLPVGLGPDIVHVVPEIPLSAT 944
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
91-193 |
1.14e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.20 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 91 DRTAIIwEGDDASQSKH--ISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:cd17647 3 ERTCVV-ETPSLNSSKTrsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446000384 169 E-----------------AVAGRII--DSNSRLVITS-DEGVRAG 193
Cdd:cd17647 82 ArqniylgvakprgliviRAAGVVVgpDSNPTLSFTSgSEGIPKG 126
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
124-322 |
1.37e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.09 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 124 LLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagRIIDSNSRL---------------VITSDE 188
Cdd:PLN02736 95 LVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAV--KFIVNHAEVaaifcvpqtlntllsCLSEIP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 189 GVRAgrsIPLKKNVDDALKNPNVTSVEHVVVLKRTggkidWQEGRdlwwhdlveqaSDQHQAEEMNAEDPLFILYTSGST 268
Cdd:PLN02736 173 SVRL---IVVVGGADEPLPSLPSGTGVEIVTYSKL-----LAQGR-----------SSPQPFRPPKPEDVATICYTSGTT 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446000384 269 GKPKGVLHTTGGyLVYAALTFKYVFDYHPGDIYWctadvgwvtghSYLlygPLA 322
Cdd:PLN02736 234 GTPKGVVLTHGN-LIANVAGSSLSTKFYPSDVHI-----------SYL---PLA 272
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
264-617 |
8.62e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.06 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 264 TSGSTGKPKGVLHT-----TGGYLVYAALTFKYVfdyHPGDIYWCTADVGWVTGHSYLLYGPLACGATTlmfegVPNWP- 337
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdldRWAELFARSLRAAGV---RPGDRVQNAFGYGLFTGGLGLHYGAERLGATV-----IPAGGg 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 338 TPARMAQVVDKHQVNILYTAPTAIRALmaeGDKAIE-GTD--RSSLR--ILGsvGEPInPEAW-EWYWKKIGnekCPVVD 411
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGTPSYLLYL---AEVAEEeGIDprDLSLKkgIFG--GEPW-SEEMrKEIEERWG---IKAYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 412 TWWQTETGgfmitplPG-ATELKAGSATRpffgVQPALV------DNEGNPL-EGAtEGSLVITdswpgqarTLF----- 478
Cdd:COG1541 234 IYGLTEVG-------PGvAYECEAQDGLH----IWEDHFlveiidPETGEPVpEGE-EGELVVT--------TLTkeamp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 479 ------GDHERFEQTYFST-FKNMYFSGdgarrdedgyywITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:COG1541 294 liryrtGDLTRLLPEPCPCgRTHPRIGR------------ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVD 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446000384 552 HNIKGQAIYAYVTLNHGEEPsPELYAEVRNWVRKEIGplATPDV-LHWTDSLPktRSGKIMRRILRK 617
Cdd:COG1541 362 REGGLDELTVRVELAPGASL-EALAEAIAAALKAVLG--LRAEVeLVEPGSLP--RSEGKAKRVIDR 423
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
532-645 |
9.92e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 42.06 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446000384 532 IESALVAHPKIAEAAVVGIPHNIKGQAIYAYVtlnhgEEPSPELYAEVRNWVRKEIGPLAtPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....*
gi 446000384 612 RRILRKIAAGDTSNLGDTSTL-ADPGVVEKLLEEK 645
Cdd:PRK09188 319 DDILRLIAMNQIDELDDLLREpEIRGLVEAIAAHR 353
|
|
| |
