|
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: 1343.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 6 KHAIPANIADRCLINPEQYETKYKQSINDPDTFWGEQGKILDWITPYqkvkNTSFAPGNVSIKWYEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 86 LQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 166 FSPEAVAGCIIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNPNvtSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKAS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 246 PEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGA 325
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 326 TTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKE 405
Cdd:PRK00174 315 TTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 406 KCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFE 485
Cdd:PRK00174 395 RCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 486 QTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTL 565
Cdd:PRK00174 475 KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 566 NHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTsNLGDTSTLADPGVVEKLLEEK 645
Cdd:PRK00174 555 KGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEAR 633
|
....
1PG3_A 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: 1212.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 18 LINPEQYETKYKQSINDPDTFWGEQGK-ILDWITPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQENGDRTAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 97 WEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCII 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 177 DSSSRLVITADEGVRAGRSIPLKKNVDDALKNPNvTSVEHVIVLKRTGSDID-WQEGRDLWWRDLIEKASPEHQPEAMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCP-VSVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 336 WPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQ 415
Cdd:TIGR02188 317 YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 416 TETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGN-LVITDSWPGQARTLFGDHERFEQTYFSTFKN 494
Cdd:TIGR02188 397 TETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGyLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 495 MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPE 574
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 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: 1191.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 22 EQYETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFapGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK--GPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 102 TSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSR 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 182 LVITADEGVRAGRSIPLKKNVDDALKNpnVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQPEAMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEK--CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPAR 341
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 342 MCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTETGGF 421
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 422 MITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDG 501
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRN 581
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 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: 1094.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 24 YETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDTS 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 104 QSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 184 ITADEGVRAGRSIPLKKNVDDALkNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQPEAMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 264 TSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMC 343
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 344 QVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTETGGFMI 423
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 424 TPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGAR 503
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWV 583
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
1PG3_A 584 RKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
68-643 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 944.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 68 KWYEDGTLNLAANCLDRHLQENGDRTAIIWEGDDtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGED-GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 148 AMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNpnVTSVEHVIVLKRTGSDI 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEE--LPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 228 DWQEgrDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 GWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINPEAWEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:COG0365 316 EPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSWPGQARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLG 627
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR--PLG 549
|
570
....*....|....*.
1PG3_A 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: 829.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 20 NPEQYETKYKQSINDPDTFWGEQGKILDWITPY--QKV--KNTSFAPGNVSIKWYEDGTLNLAANCLDRHLQE-NGDRTA 94
Cdd:PLN02654 28 SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegDEVcsENLDVRKGPISIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 95 IIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGC 174
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 175 IIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNP--NVTSV------EHVIVLKRtgSDIDWQEGRDLWWRDLIEKASP 246
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESakNGVSVgicltyENQLAMKR--EDTKWQEGRDVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 EHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 TLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEK 406
Cdd:PLN02654 346 VLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 407 CPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQ 486
Cdd:PLN02654 426 CPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYET 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 487 TYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLN 566
Cdd:PLN02654 506 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PG3_A 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: 659.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 24 YETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLQE-NGDRTAIIWEGDDT 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPP---FTRWFVGGRLNTCYNALDRHVEAgRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 103 SQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 183 VITADEGVRAGRSIPLKKNVDDALKNPNvTSVEHVIVLKRTGSDID-WQEGRDLWWRDLIEKASPeHQPEAMNAEDPLFI 261
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSG-HKPHHVLVLNRPQVPADlTKPGRDLDWSELLAKAEP-VDCVPVAATDPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVP-NWPTPA 340
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 341 RMCQVVDKHQVNILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKekcPVVDTWWQTET 418
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 GGFMITPLPG--AIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSW-PGQARTLFGDHERFEQTYFSTFKNM 495
Cdd:cd05967 393 GWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPE- 574
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEe 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 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: 620.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 22 EQYETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTS---FApgnvsiKWYEDGTLNLAANCLDRHLQENGDRTAIIWE 98
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSnppFA------RWFVGGRTNLCHNAVDRHLAKRPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 99 GDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDS 178
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 179 SSRLVITADEGVRAGRSIPLKKNVDDALKNPNVTSvEHVIVLKRTGSDIDWQEGRDLWWRDLIEKASPEHQP-EAMNAED 257
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKP-RHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARVPvEWLESNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWP 337
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 338 TPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKekcPVVDTWWQTE 417
Cdd:PRK10524 315 DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 418 TGGFMITPLPG--AIELKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVITDSW-PGQARTLFGDHERFEQTYFSTF- 492
Cdd:PRK10524 392 TGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHG---- 568
Cdd:PRK10524 472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsla 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 569 -EEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG-DTsnlGDTSTLADPGVVEKLleeKQ 646
Cdd:PRK10524 552 dREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGrDP---GDLTTIEDPAALQQI---RQ 625
|
...
1PG3_A 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: 547.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 22 EQYETKYKQSINDPDTFWGEQGKILD--WITPYQKVKNTSfaPGNVSIKWYEDGTLNLAANCLDRHLQENGDRTAIIWEG 99
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 100 DDtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSS 179
Cdd:cd05968 85 ED-GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 180 SRLVITADEGVRAGRSIPLKKNVDDALKNpnVTSVEHVIVLKRTGSDIDWQEGRDLWWRDliEKASPEHQPEAMNAEDPL 259
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACAQ--CPTVEKVVVVRHLGNDFTPAKGRDLSYDE--EKETAGDGAERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTaDVGWVTGhSYLLYGPLACGATTLMFEGVPNWPT 338
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 339 PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVVDTWWQTET 418
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 -----GGFMITPLpgaielKAGSATRPFFGVQPALVDNEGHPQEGaTEGNLVITDSWPGQARTLFGDHERFEQTYFSTFK 493
Cdd:cd05968 398 sggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 494 NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSP 573
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 574 ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDtsNLGDTSTLADP 635
Cdd:cd05968 551 ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-628 |
5.73e-179 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 520.22 E-value: 5.73e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 69 WYEDGTLNLAANCLDRHLQEN-GDRTAIIWEGDDTSQSkhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGrKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 148 AMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVRagrsiplKKNVDDalknpnVTSVEHVIVlkrTGSDI 227
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADD------LPSLKHVLL---VGEDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 228 DWQEGrDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCTADV 307
Cdd:PRK04319 178 EEGPG-TLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 GWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVG 387
Cdd:PRK04319 256 GWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINPEAWEWYWKKIGKekcPVVDTWWQTETGGFMITPLPgAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:PRK04319 333 EPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSWPGQARTLFGDHERFEQtYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:PRK04319 409 KGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK----IAAGDT 623
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAwelgLPEGDL 565
|
....*
1PG3_A 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 |
4.94e-147 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 433.85 E-value: 4.94e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 gvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdLIEKASPEhqpeamnaeDPLFILYTSGST 268
Cdd:cd05969 82 ---------------------------------------------------LYERTDPE---------DPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 269 GKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwptPARMCQVVDK 348
Cdd:cd05969 102 GTPKGVLHVHDAMIFYYFTG-KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 349 HQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKekcPVVDTWWQTETGGFMITPLPG 428
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 429 aIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEqtyfSTFKN-MYFSGDGARRDED 507
Cdd:cd05969 255 -MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYK----NSFIDgWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEI 587
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|..
1PG3_A 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 |
1.30e-122 |
|
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: 370.51 E-value: 1.30e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITade 188
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 gvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamNAEDPLFILYTSGST 268
Cdd:cd05972 79 -----------------------------------------------------------------DAEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 269 GKPKGVLHTTGgYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNwpTPARMCQVVDK 348
Cdd:cd05972 94 GLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLER 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 349 HQVNILYTAPTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEWyWKKIGKEkcPVVDTWWQTETGgFMITPLPG 428
Cdd:cd05972 171 YGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEW-WRAATGL--PIRDGYGQTETG-LTVGNFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 429 aIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDG 508
Cdd:cd05972 244 -MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDY---YLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 509 YYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIG 588
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLA 399
|
490 500
....*....|....*....|....*....
1PG3_A 589 PLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-523 |
1.62e-114 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 349.30 E-value: 1.62e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIiwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEgvragrsiPLKKNVDDALknPNVTSVEHVIVLKRTgsdiDWQEGRDLWWRDLI 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEAL--GKLEVVKLVLVLDRD----PVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKASPEhQPEAMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTFKYV----FDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 142 ADVPPP-PPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 318 YGPLACGATTLMFEGVPNwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEW 397
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 398 YWKKIGkekCPVVDTWWQTETGGFMITPLPGAIEL-KAGSATRPFFGVQPALVD-NEGHPQEGATEGNLVItdSWPGQAR 475
Cdd:pfam00501 297 FRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCV--RGPGVMK 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1PG3_A 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 |
1.22e-108 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 335.24 E-value: 1.22e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITAdegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdli 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekaspehqpeamnaedplFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTLMfegVPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:COG0318 165 LAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPEFA--RYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 402 IGkekCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTLFGDH 481
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 482 ERFEQTyfstFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIY 560
Cdd:COG0318 314 EATAEA----FRDgWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 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 |
5.31e-102 |
|
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: 314.22 E-value: 5.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVtGHSYLLYGPLACGATTLMFEGvpnw 336
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 337 PTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWWQT 416
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 417 ETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQartlfGDHERFEQTYFSTFKNMY 496
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK-----GYWNNPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPEly 576
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
1PG3_A 577 aEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
24-639 |
2.88e-89 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 291.31 E-value: 2.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 24 YETKYKQSINDPDTFWGEqgkILDWI-----TPYQKVKNTSFAPGNvsiKWYEDGTLNLAANCLdRHlqENGDRTAIIWE 98
Cdd:PRK03584 36 YAALWRWSVEDLEAFWQS---VWDFFgvigsTPYTVVLAGRRMPGA---RWFPGARLNYAENLL-RH--RRDDRPAIIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 99 GDDTSQSKhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagciID- 177
Cdd:PRK03584 107 GEDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGV----LDr 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 178 ---SSSRLVITADeGVR-AGRSIPLKKNVD---DALKnpnvtSVEHVIVLKRTGSDIDWQEG-RDLWWRDLIEKASP-EH 248
Cdd:PRK03584 182 fgqIEPKVLIAVD-GYRyGGKAFDRRAKVAelrAALP-----SLEHVVVVPYLGPAAAAAALpGALLWEDFLAPAEAaEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTAdVGW------VTGhsyllygpL 321
Cdd:PRK03584 256 EFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------L 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:PRK03584 327 LVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEH 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 402 IGKekcpvvDTWWQTETGG------FMI-TPL----PGaiELKAgsatrPFFGVQPALVDNEGHPQEGATeGNLVITDSW 470
Cdd:PRK03584 407 VKA------DVWLASISGGtdicscFVGgNPLlpvyRG--EIQC-----RGLGMAVEAWDEDGRPVVGEV-GELVCTKPF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 471 PGQARTLFGD--HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:PRK03584 473 PSMPLGFWNDpdGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 549 GIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM----RRILRKIAAGDTS 624
Cdd:PRK03584 553 GQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKKAV 632
|
650
....*....|....*
1PG3_A 625 NLGdtsTLADPGVVE 639
Cdd:PRK03584 633 NRD---ALANPEALD 644
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
24-639 |
4.26e-88 |
|
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: 287.25 E-value: 4.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 24 YETKYKQSINDPDTFWGEqgkILDWI-----TPYQKV-KNTSFAPGNvsiKWYEDGTLNLAANCLDRHlqENGDRTAIIw 97
Cdd:cd05943 19 YAALHRWSVDDPGAFWAA---VWDFSgvrgsKPYDVVvVSGRIMPGA---RWFPGARLNYAENLLRHA--DADDPAAIY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 98 eGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVagciID 177
Cdd:cd05943 90 -AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGV----LD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 178 SSS----RLVITADEGVRAGRSIPLKKNVDDALKnpNVTSVEHVIVLKRTGSD--IDWQE-GRDLWWRDLI-EKASPEHQ 249
Cdd:cd05943 165 RFGqiepKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVAAgqPDLSKiAKALTLEDFLaTGAAGELE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 250 PEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSylLYGPLACGATTLM 329
Cdd:cd05943 243 FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW--LVSGLAVGATIVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 330 FEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKekcpv 409
Cdd:cd05943 321 YDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP----- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 410 vDTWWQTETGG------FMIT-PL----PGaiELKAgsatrPFFGVQPALVDNEGHPQEGATeGNLVITDSWPGQARTLF 478
Cdd:cd05943 396 -DVLLASISGGtdiiscFVGGnPLlpvyRG--EIQC-----RGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPSMPVGFW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 479 GDHE--RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKG 556
Cdd:cd05943 467 NDPDgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 557 QAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGdtSNLGDTSTLADPG 636
Cdd:cd05943 547 ERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG--RPVKNAGALANPE 624
|
...
1PG3_A 637 VVE 639
Cdd:cd05943 625 SLD 627
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-617 |
7.54e-87 |
|
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: 278.25 E-value: 7.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrsiplkkNVDDalknpnvtsvehvivlkrtgsdidwqegrdlwwRDLIekaspehqpeamnAEDPLFILYTSGS 267
Cdd:cd05973 79 -------------DAAN---------------------------------RHKL-------------DSDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATtFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPnwpTPARMCQVVD 347
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGF---SVESTWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 348 KHQVNILYTAPTAIRALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWWQTETGGFMITPLP 427
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 428 GAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVI-TDSWPgqaRTLFGDHERFEQTYFStfKNMYFSGDGARRDE 506
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSP---LMWFRGYQLPDTPAID--GGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKE 586
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKR 406
|
490 500 510
....*....|....*....|....*....|.
1PG3_A 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-616 |
8.48e-82 |
|
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: 267.31 E-value: 8.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 78 AANCLDRHLQEN-GDRTAIIwegDDTSqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEGrGDKTAFI---DDAG---SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 157 AVHSVIFGGFSPEAVAGCIIDSSSRLVITADEgvragrsipLKKNVDDALkNPNVTSVEHVIVLKRTGSdidwqEGRDLW 236
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAAL-TKSEHTLVVLIVSGGAGP-----EAGALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05959 144 LAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATTLMFegvPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:cd05959 224 LTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 WYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT-DSwpgqar 475
Cdd:cd05959 299 RWKARFGLD---ILDGIGSTEMLHIFLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRgPS------ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 476 TLFGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAI 554
Cdd:cd05959 368 SATMYWNNRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 555 KGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05959 447 GLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-616 |
1.21e-80 |
|
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: 265.13 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 64 NVSIKWYEdgTLNLAANCLDRHLQENGDRTAIIWeGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVP 143
Cdd:cd05970 7 NFSINVPE--NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 144 EAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVragrsipLKKNVDDALKN-PNVTsvehviVLKR 222
Cdd:cd05970 84 EFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAAPEcPSKP------KLVW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 223 TGSDIdwqegRDLW--WRDLIEKASPEHQPEAMNA----EDPLFILYTSGSTGKPKGVLHTTG---GYLVyaatTFKYVF 293
Cdd:cd05970 151 VGDPV-----PEGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 294 DYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGvpNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGdkaIE 373
Cdd:cd05970 222 NVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED---LS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 374 GTDRSSLRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGaIELKAGSATRPFFGVQPALVDNEG 453
Cdd:cd05970 297 RYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPW-MEPKPGSMGKPAPGYEIDLIDREG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 454 HPQEGATEGNLVITDSwPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:cd05970 372 RSCEAGEEGEIVIRTS-KGKPVGLFGGYYKDAEKTAEVWHDgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 533 ESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05970 451 ESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
....
1PG3_A 613 RILR 616
Cdd:cd05970 531 VEIR 534
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
18-617 |
2.56e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 261.99 E-value: 2.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 18 LINPEQYETKYKQSINDPDTFWGEQG-KILDWITPYQKVkntsFAPGNVSIKWYEDGTLNLAANCLDRHLQ--ENGDRTA 94
Cdd:PTZ00237 4 LSDPFDYENDSNYANSNPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVKnpLKRDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 95 IIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGC 174
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 175 IIDSSSRLVITADEGVRAGRSIPLKKNVDDALK----NPNvtsveHVIVLKRTG--SDIDWQEGRD-------LWWRDLI 241
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIElstfKPS-----NVITLFRNDitSESDLKKIETiptipntLSWYDEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EK-----ASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYl 316
Cdd:PTZ00237 235 KKikennQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATTLMFEG--VPNWPTPARMCQVVDKHQVNILYTAPTAIRALM---AEGDKAIEGTDRSSLRILGSVGEPIN 391
Cdd:PTZ00237 314 LYGSLSLGNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIktdPEATIIRSKYDLSNLKEIWCGGEVIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 PEAWEWYWKKIgkeKCPVVDTWWQTETGgfmITPLPGAIELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNLVITDS 469
Cdd:PTZ00237 394 ESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCYGHINIPYNAtgVPSIFIKPSILSEDGKELNVNEIGEVAFKLP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 470 W-PGQARTLFGDHERFEQTyFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:PTZ00237 468 MpPSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 549 GIPHAIKGQAIYAYVTLNHGEEPSP----ELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PTZ00237 547 GIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-616 |
9.79e-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: 246.58 E-value: 9.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 105 SKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 185 TaDEgvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 265 SGSTGKPKGVLHTTGgYLVYAATTFKYVFDYHP--GDIYWCTADVGWVTGHSYLLYGPLACGATTLM-----FEgvpnwp 337
Cdd:cd05971 97 SGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrmtkFD------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 338 tPARMCQVVDKHQVNILYTAPTAIRaLMAEGDKAIEGTDRSsLRILGSVGEPINPEAWEWywkkiGKE--KCPVVDTWWQ 415
Cdd:cd05971 170 -PKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVK-LRAIATGGESLGEELLGW-----AREqfGVEVNEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 416 TEtGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQARTLFGDHERFEQTYFSTFknm 495
Cdd:cd05971 242 TE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDW--- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 496 YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPEL 575
Cdd:cd05971 318 LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1PG3_A 576 YAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05971 398 AREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
1.53e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 240.47 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 72 DGTLNLAaNCLDRHLQENGDRTAIIWEGDDTSqskhisYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDGRRTT------YAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 152 CARIGAV-HSV-IFggFSPEAVAGCIIDSSSRLVITADEGVragrsiPLKKNVDDALknpnvTSVEHVIVLK---RTGSD 226
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQL-----PTVRTVIVEGdgpAAPLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 227 IDWQEgrdlwWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyaattfKYVFDYHPG 298
Cdd:PRK06187 143 PEVGE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVvlshrnlfLHSLAV---------CAWLKLSRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 299 DIYWCTADV----GWVTGhsyllYGPLACGATTLM---FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEgdKA 371
Cdd:PRK06187 209 DVYLVIVPMfhvhAWGLP-----YLALMAGAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQMLLKA--PR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 372 IEGTDRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWWQTETGGFM-ITPL----PGAIElKAGSATRPFFGVQP 446
Cdd:PRK06187 275 AYFVDFSSLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPedqlPGQWT-KRRSAGRPLPGVEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 447 ALVDNEGH--PQEGATEGNLVITDSWPGQArtLFGDHERFEqtyfSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK06187 351 RIVDDDGDelPPDGGEVGEIIVRGPWLMQG--YWNRPEATA----ETIDGgWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 524 GHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK06187 425 GENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELP 501
|
570 580
....*....|....*....|
1PG3_A 604 KTRSGKIMRRILR-KIAAGD 622
Cdd:PRK06187 502 RTSVGKILKRVLReQYAEGK 521
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
108-616 |
3.77e-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: 236.97 E-value: 3.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITad 187
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamNAEDPLFILYTSGS 267
Cdd:cd05919 89 ------------------------------------------------------------------SADDIAYLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV--GWVTGHSylLYGPLACGATTLMFegvPNWPTPARMCQV 345
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLAT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 346 VDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEwYWKKIGKekCPVVDTWWQTETGGFMITP 425
Cdd:cd05919 178 LARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFG--GPILDGIGATEVGHIFLSN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 426 LPGAIELkaGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRD 505
Cdd:cd05919 253 RPGAWRL--GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFNGGW---YRTGDKFCRD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 506 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRK 585
Cdd:cd05919 326 ADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLE 405
|
490 500 510
....*....|....*....|....*....|.
1PG3_A 586 EIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05919 406 RLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-612 |
1.12e-70 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 235.58 E-value: 1.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVItadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdli 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekaspehqpeamnaEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTLMFEGvpnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVGEPInPEAWEWYWKK 401
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 402 IGkekCPVVDTWWQTETGGfMITPLPGAIEL-KAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARtlfGD 480
Cdd:cd17631 236 RG---VKFVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMA---GY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 481 HERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAI 559
Cdd:cd17631 307 WNRPEATA-AAFRDGWFhTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17631 386 VAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-617 |
4.86e-70 |
|
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: 236.59 E-value: 4.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 76 NLAANCLDR--HLQENGDRTA--IIWEGDDTSQSKHISYRELHRDVCRFANTLLDL-GIKKGDVVAIYMPMVPEAAVAML 150
Cdd:cd05928 6 NFASDVLDQwaDKEKAGKRPPnpALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 151 ACARIGAVhsvifggFSPEAVAGCIIDSSSRLVITADEGVRAGRSipLKKNVDD-ALKNPNVTSvehvivlKRTGSDidw 229
Cdd:cd05928 86 ACIRTGLV-------FIPGTIQLTAKDILYRLQASKAKCIVTSDE--LAPEVDSvASECPSLKT-------KLLVSE--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 230 qEGRDLW--WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:cd05928 147 -KSRDGWlnFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 GWVTGHSYLLYGPLACGATTLMFEgVPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEgtdRSSLRILGSVG 387
Cdd:cd05928 226 GWIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYK---FPSLQHCVTGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINPEAWEWYWKKIGKEkcpVVDTWWQTETGgfMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:cd05928 301 EPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSwPGQARTLFGDHERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAA 546
Cdd:cd05928 376 VK-PIRPFGLFSGYVDNPEKTAATIRgDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 547 VVGIPHAIKGQAIYAYVTLN-----HGEEpspELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05928 455 VVSSPDPIRGEVVKAFVVLApqflsHDPE---QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-616 |
1.01e-68 |
|
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: 231.30 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 159 HSVIFGgfsPEAVAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrDLWWR 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIV------------------------------------------------AVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 239 DLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-----------IYWCTAdv 307
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDdvvlaalplfhVFGLTV-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 gwvtghSYLLygPLACGATTLMfegVPNwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVG 387
Cdd:cd05936 186 ------ALLL--PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLCISGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINPEAWEWYWKKIGkekCPVVDTWWQTETG-GFMITPLPGAIelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVI 466
Cdd:cd05936 252 APLPVEVAERFEELTG---VPIVEGYGLTETSpVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 467 TdswpGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd05936 327 R----GPQVMK-GYWNRPEETA-EAFVDGWLrTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-624 |
9.40e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 219.80 E-value: 9.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEgdDTSqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK08316 26 DKTALVFG--DRS----WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEgvragrsipLKKNVDDALKNPNVTSVEHVIVLKRTGSDidwqeGRDLWWRDLIEKASPEHQP 250
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREAP-----GGWLDFADWAEAGSVAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 EAMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaATTFKYV-----FDYHPGDI-------YWCTAdvgwvtGHSYLly 318
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHR------ALIAEYVscivaGDMSADDIplhalplYHCAQ------LDVFL-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 GP-LACGATTLMFEGvpnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRiLGSVGEPINPEAwew 397
Cdd:PRK08316 232 GPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR-KGYYGASIMPVE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 398 YWKKIgKEKCPVVDTW---WQTEtggfmITPL-----PGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVitds 469
Cdd:PRK08316 302 VLKEL-RERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 470 wpgqART------LFGDHERFEQtyfsTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK08316 372 ----HRSpqlmlgYWDDPEKTAE----AFRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 543 AEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK08316 444 AEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
..
1PG3_A 623 TS 624
Cdd:PRK08316 521 FT 522
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
102-617 |
1.13e-62 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 216.02 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 102 TSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSR 181
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 182 LVITADEGVRagrsiplkknvdDALKNPNVTSVEHVIVLKRTGSDIDWQEGRDLwwrDLIEKASPEHQPE-AMNAEDPLF 260
Cdd:cd05926 89 LVLTPKGELG------------PASRAASKLGLAILELALDVGVLIRAPSAESL---SNLLADKKNAKSEgVPLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 261 ILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWP 337
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLpprFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 338 tparmcQVVDkHQVNiLYTA-PTAIRAL--MAEGDKAIEgtdRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWW 414
Cdd:cd05926 233 ------DVRD-YNAT-WYTAvPTIHQILlnRPEPNPESP---PPKLRFIRSCSASLPPAVLEALEATFG---APVLEAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 415 QTETGGFMIT-PLPGAIElKAGSATRPFfGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFGDHErfeQTYFSTFK 493
Cdd:cd05926 299 MTEAAHQMTSnPLPPGPR-KPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNPE---ANAEAAFK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 494 NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLnhgEEPS 572
Cdd:cd05926 372 DGWFrTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL---REGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
1PG3_A 573 PELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-616 |
4.57e-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: 212.15 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 107 HISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITa 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 187 degvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 267 STGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVV 346
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 347 DKHQVNILYTAPTAIRALMAEGDKAiegTDRSS-LRILGsvGEPINPEAWEWYWKKIGkekCPVVDTWWQTETGGFMITP 425
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSP---DDRAHrLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 426 LPGAIelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITdSWPGQARTLfGDHERFEQTYfSTFKNMYF-SGDGARR 504
Cdd:cd05934 239 RDEPR--RPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR-GLRGWGFFK-GYYNMPEATA-EAMRNGWFhTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVR 584
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCE 390
|
490 500 510
....*....|....*....|....*....|..
1PG3_A 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05934 391 GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-617 |
7.43e-62 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 219.18 E-value: 7.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 28 YKQSINDPDTFWG---EQGKILDWITPYQKVKNTSFA-PGNvsiKWYEDGTLNLAANCLDRHLQENGDRTAIIW--EGDD 101
Cdd:PLN03052 126 QRFSVENPEVYWSivlDELSLVFSVPPRCILDTSDESnPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 102 TSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSR 181
Cdd:PLN03052 203 DLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 182 LVITADEGVRAGRSIPLKKNVDDAlKNPNvtsvehVIVLKRTGSDIDWQ-EGRDLWWRDLIEKASP-----EHQPEAMNA 255
Cdd:PLN03052 283 AIFTQDVIVRGGKSIPLYSRVVEA-KAPK------AIVLPADGKSVRVKlREGDMSWDDFLARANGlrrpdEYKAVEQPV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIY-WCTaDVGWVTGHsYLLYGPLACGATTLMFEGVP 334
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSP 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 335 NWPTPARMCQvvdKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEkcPVVDTWW 414
Cdd:PLN03052 433 LGRGFAKFVQ---DAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCG 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 415 QTETGGFMIT--PL-PGAIelkaGSATRPFFGVQPALVDNEGH--PQEGATEGNLVITDSWPGQARTLF-GDHerfEQTY 488
Cdd:PLN03052 506 GTELGGGFVTgsLLqPQAF----AAFSTPAMGCKLFILDDSGNpyPDDAPCTGELALFPLMFGASSTLLnADH---YKVY 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 489 fstFKNM-YFSGDGARRDED-------GYYWITGRVDDVLNVSGHRLGTAEIESAL-VAHPKIAEAAVVGIPHAIKGQ-- 557
Cdd:PLN03052 579 ---FKGMpVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPeq 655
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 558 -AIYAYVTLNHGEEPSPELYAEVRN-WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN03052 656 lVIAAVLKDPPGSNPDLNELKKIFNsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
73-617 |
1.44e-61 |
|
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: 213.16 E-value: 1.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 73 GTLNLAANCLDRHLQE-NGDRTAIIwegDDTSQskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEgRGGKTAFI---DDISS---LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 152 CARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEgvragrSIPLKKNVddALKNPNVtsvEHVIVLKRtgsdidwQE 231
Cdd:TIGR02262 75 AIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA------LLPVIKAA--LGKSPHL---EHRVVVGR-------PE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 232 GRDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVT 311
Cdd:TIGR02262 137 AGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 312 GHSYLLYGPLACGATTLMFegvPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRssLRILGSVGEPIn 391
Cdd:TIGR02262 217 GLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVR--LRLCTSAGEAL- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 PEAWEWYWK-KIGKEkcpVVDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSW 470
Cdd:TIGR02262 291 PAEVGQRWQaRFGVD---IVDGIGSTEMLHIFLSNLPGDVRY--GTSGKPVPGYRLRLVGDGGQDVADGEPGELLI--SG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 471 PGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI 550
Cdd:TIGR02262 364 PSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 551 P---HAIKGQaiyAYVTLNHGEEpspELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR02262 441 AdedGLIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-617 |
7.66e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.99 E-value: 7.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEgvragrSIPLKKNVDDALknPNvtsVEHVIVLkRTGSDIDwQEGRDLWWRDLI 241
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGL------FLGVDYSATTRL--PA---LEHVVIC-ETEEDDP-HTEKMKTFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTA--------DVGWVTgh 313
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAANpffhvfgyKAGVNA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 314 syllygPLACGATTLMfegVPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEgtDRSSLRILGSVGEPINPE 393
Cdd:PRK07656 229 ------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE--DLSSLRLAVTGAASMPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 394 AWEWYWKKIGkekCPVVDTWWQ-TETGGFM-ITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswP 471
Cdd:PRK07656 297 LLERFESELG---VDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG--P 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:PRK07656 372 NVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 552 HAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-611 |
1.59e-58 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 204.37 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 101 DTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 181 RLVITADEGVragrsiplkKNVDDALKNpnVTSVEHVIVLKRTGSDI-------DWQEGRDLWWRDLIEKASPEhqpeam 253
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAKE--LGPKDKIIVLDDKPDGVlsiedllSPTLGEEDEDLPPPLKDGKD------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 254 naeDPLFILYTSGSTGKPKGVLHTTGGYLvyaaTTFKYVFDYHPGDIYWCTADVG-----WVTGHSYLLYGPLaCGATTL 328
Cdd:cd05911 147 ---DTAAILYSSGTTGLPKGVCLSHRNLI----ANLSQVQTFLYGNDGSNDVILGflplyHIYGLFTTLASLL-NGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 329 MFegvpNWPTPARMCQVVDKHQVNILYTAPtAIRALMAEgDKAIEGTDRSSLRILGSVGEPINPEAWEwywkKIGK--EK 406
Cdd:cd05911 219 IM----PKFDSELFLDLIEKYKITFLYLVP-PIAAALAK-SPLLDKYDLSSLRVILSGGAPLSKELQE----LLAKrfPN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 407 CPVVDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPALVDNEGHPQEGATE-GNLVItdsWPGQArtLFGDHERFE 485
Cdd:cd05911 289 ATIKQGYGMTETGGILTVNPDG--DDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEpGEICV---RGPQV--MKGYYNNPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 486 QTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVT 564
Cdd:cd05911 362 ATKETFDEDGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 565 LNHGEEPSPElyaEVRNWVRKEIgplatPDVLHW------TDSLPKTRSGKIM 611
Cdd:cd05911 442 RKPGEKLTEK---EVKDYVAKKV-----ASYKQLrggvvfVDEIPKSASGKIL 486
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
109-616 |
3.20e-57 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 199.63 E-value: 3.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGcIIDSSSRLVITAD 187
Cdd:cd05958 12 TYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY-ILDKARITVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EGVRAgrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFILYTSGS 267
Cdd:cd05958 91 HALTA--------------------------------------------------------------SDDICILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVD 347
Cdd:cd05958 109 TGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 348 KHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWWQTETGGFMITPLP 427
Cdd:cd05958 185 RYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISARP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 428 GAIelKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARTLFgdhERFEQTYFSTFKNmyFSGDGARRDED 507
Cdd:cd05958 260 GDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCRYLA---DKRQRTYVQGGWN--ITGDTYSRDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEI 587
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHI 410
|
490 500
....*....|....*....|....*....
1PG3_A 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05958 411 APYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-613 |
4.68e-57 |
|
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: 199.29 E-value: 4.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqp 250
Cdd:cd05930 76 LAYILEDSGAKLVLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 eamNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPLACGAT 326
Cdd:cd05930 91 ---DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE-----IFGALLAGAT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 TLMfegVPN--WPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEwYWKKIGk 404
Cdd:cd05930 162 LVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVR-RWRELL- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 405 EKCPVVDTWWQTETGGFM----ITPLpgaiELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVITDswPGQARTL 477
Cdd:cd05930 233 PGARLVNLYGPTEATVDAtyyrVPPD----DEEDGRVPigRPIPNTRVYVLDENLRPVpPGVP-GELYIGG--AGLARGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 478 FGDHE----RFEQTYFSTFKNMYFSGDGARRDEDG--YYwiTGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:cd05930 306 LNRPEltaeRFVPNPFGPGERMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARE 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 552 HAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd05930 384 DGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-624 |
7.56e-57 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 201.44 E-value: 7.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVItadegvragrsIP-LKKNVDDA-----LKnPNVTSVEHVIVLkrtGSDidwqeGRDL 235
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLV-----------VPkTFRGFDHAamarrLR-PELPALRHVVVV---GGD-----GADS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 236 WWRDLIEKASpEHQPEAMN--------AEDPLFILYTSGSTGKPKGVLHTT----GGYLVYAATtfkyvFDYHPGDIYWC 303
Cdd:PRK13295 170 FEALLITPAW-EQEPDAPAilarlrpgPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAER-----LGLGADDVILM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 304 TADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMCQVVDKHQVNilYT-APTAIRALMAEGDKAiEGTDRSSLRI 382
Cdd:PRK13295 244 ASPMAHQTGFMYGLMMPVMLGATAVLQD---IW-DPARAAELIRTEGVT--FTmASTPFLTDLTRAVKE-SGRPVSSLRT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEG 462
Cdd:PRK13295 317 FLCAGAPIPGALVERARAALGAK---IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 463 NLVITdswpgqARTLFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK13295 394 RLQVR------GCSNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 543 AEAAVVGIPHAIKGQAIYAYVTLNHGEEPSpelYAEVRNWVR-KEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAG 621
Cdd:PRK13295 468 AQVAIVAYPDERLGERACAFVVPRPGQSLD---FEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
...
1PG3_A 622 DTS 624
Cdd:PRK13295 545 EDA 547
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-619 |
5.83e-56 |
|
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: 196.25 E-value: 5.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspeavagcIIDSSSRLviTAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------VIPATTLL--TPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EgvragrsipLKKNVDdalknpnvtsvehvivlkrtgsdidwqegrdlwwrdlIEKASPEHQPEAMNAEDPLFILYTSGS 267
Cdd:cd05974 63 D---------LRDRVD-------------------------------------RGGAVYAAVDENTHADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFegvpNWP--TPARMCQV 345
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYArfDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 346 VDKHQVNILYTAPTAIRALMAEGDKAIegtdRSSLRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGGfMITP 425
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLIQQDLASF----DVKLREVVGAGEPLNPEVIEQVRRAWGLT---IRDGYGQTETTA-LVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 426 LPGAIeLKAGSATRPFFGVQPALVDNEGHPqegATEGN--LVITDSWP-GQARTLFGDHERfeqTYFSTFKNMYFSGDGA 502
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGAP---ATEGEvaLDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNW 582
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*..
1PG3_A 583 VRKEIGPLATPDVLHWTDsLPKTRSGKIMRRILRKIA 619
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-620 |
4.76e-54 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 195.56 E-value: 4.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIW--EGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 160 SvIFGGFSPEAVAGCIIDSSSRLVITAdeGVRAGRSIPLKknVDDALknPNVTSVEHVIVLKRTGSDIDWQEGRDLWWR- 238
Cdd:PRK07529 111 P-INPLLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQK--VAEVL--AALPELRTVVEVDLARYLPGPKRLAVPLIRr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 239 ----------DLIEKASPEH--QPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTAD 306
Cdd:PRK07529 184 kaharildfdAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 307 VGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA---------RMCQVVDKHQVNILYTAPTAIRALMaegDKAIEGTDR 377
Cdd:PRK07529 263 LFHVNALLVTGLAPLARGAHVV-------LATPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 378 SSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTWWQTE-TGGFMITPLPGaiELKAGSATRPFFG--VQPALVDNEGH 454
Cdd:PRK07529 333 SSLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 455 -PQEGATE--GNLVItdSWPGQART-LFGDHER---FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK07529 408 yLRDCAVDevGVLCI--AGPNVFSGyLEAAHNKglwLEDGWLNT-------GDLGRIDADGYFWLTGRAKDLIIRGGHNI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 528 GTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIG-PLATPDVLHWTDSLPKTR 606
Cdd:PRK07529 479 DPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELLAFARDHIAeRAAVPKHVRILDALPKTA 555
|
570
....*....|....
1PG3_A 607 SGKIMRRILRKIAA 620
Cdd:PRK07529 556 VGKIFKPALRRDAI 569
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
91-615 |
6.76e-53 |
|
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: 188.29 E-value: 6.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGDdtsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17643 2 EAVAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqp 250
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 eamNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTfkYVFDYHPGDIywctadvgWVTGHSYL-------LYGPLA 322
Cdd:cd17643 91 ---DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 323 CGATTLMfegVPNWP--TPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLR--ILGsvGEPINPEAWEWY 398
Cdd:cd17643 158 HGGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 WKKIGKEKCPVVDTWWQTETGGFM-ITPLPGAiELKAGSAT---RPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQA 474
Cdd:cd17643 231 AGRFGLDRPQLVNMYGITETTVHVtFRPLDAA-DLPAAAASpigRPLPGLRVYVLDADGRPVPPGVVGELYV--SGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 475 RTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd17643 308 RGYLGrpelTAERFvANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 550 IPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17643 388 REDEPGDTRLVAYVVADDGAAADI---AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
109-617 |
4.43e-52 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 185.66 E-value: 4.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADE 188
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 gvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwWRdliekaspEHQPEAMNAeDPLFILYTSGST 268
Cdd:cd05903 83 ------------------------------------------------FR--------QFDPAAMPD-AVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEgvpNWpTPARMCQVVDK 348
Cdd:cd05903 106 GEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IW-DPDKALALMRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 349 HQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKCPVvdtWWQTETGGFMITPLPG 428
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEEA--GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGAVTSITPA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 429 AIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFSTFKNMYF-SGDGARRDED 507
Cdd:cd05903 256 PEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS------RGPSVFLGYLDRPDLTADAAPEGWFrTGDLARLDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 508 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVrnWVRKEI 587
Cdd:cd05903 330 GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAY--LDRQGV 407
|
490 500 510
....*....|....*....|....*....|
1PG3_A 588 GPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05903 408 AKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-620 |
8.58e-52 |
|
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: 187.28 E-value: 8.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIwEGDdtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 159 ------HSVI--FGGFSpEAVAgCIIDSSSRL---VITADEgVRAGrsiplkknvddalknpnVTSVEHVIVLKRTGSDI 227
Cdd:COG1021 105 alpahrRAEIshFAEQS-EAVA-YIIPDRHRGfdyRALARE-LQAE-----------------VPSLRHVLVVGDAGEFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 228 DWQegrdlwwrDLIEKASPEHQPEAmNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:COG1021 165 SLD--------ALLAAPADLSEPRP-DPDDVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAEICGLDADTVYLAALPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 GwvtgHSYllygPLAC---------GATTLMfegVPNwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRS 378
Cdd:COG1021 235 A----HNF----PLSSpgvlgvlyaGGTVVL---APD-PSPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 379 SLRILGSVGEPINPEAWewywKKIGkekcPVVDTWWQ-----TEtGGFMITPLPGAIELKAGSATRPffgVQPA----LV 449
Cdd:COG1021 301 SLRVLQVGGAKLSPELA----RRVR----PALGCTLQqvfgmAE-GLVNYTRLDDPEEVILTTQGRP---ISPDdevrIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 450 DNEGHPQEGATEGNLV------IT---DSwPGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVL 520
Cdd:COG1021 369 DEDGNPVPPGEVGELLtrgpytIRgyyRA-PEHNARAF-TPDGF-----------YRTGDLVRRTPDGYLVVEGRAKDQI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 521 NVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNhGEEPSPelyAEVRNWVRkEIGpLAT---PDVLH 597
Cdd:COG1021 436 NRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTL---AELRRFLR-ERG-LAAfklPDRLE 509
|
570 580
....*....|....*....|...
1PG3_A 598 WTDSLPKTRSGKIMRRILRKIAA 620
Cdd:COG1021 510 FVDALPLTAVGKIDKKALRAALA 532
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-617 |
2.55e-50 |
|
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: 182.83 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDTSQskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12119 2 LEHAARLHGDREIVSRTHEGEVH--RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEGVragrsiPLKKNVDDALKNpnvtsVEHVIVLKrTGSDIDWQEGRDLW-WRDL 240
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFL------PLLEAIAPRLPT-----VEHVVVMT-DDAAMPEPAGVGVLaYEEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 241 IEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGV--------LHTTGGylvyAATTFKYVfdyHPGDIY----------- 301
Cdd:cd12119 148 LAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshrslvLHAMAA----LLTDGLGL---SESDVVlpvvpmfhvna 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 302 WCTADVGWVTGHSYLLYGPlacgattlmfegvpnWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLR 381
Cdd:cd12119 221 WGLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 382 ILGSVGEPINPEAWEWyWKKIGkekCPVVDTWWQTETG--GFMITPLPGAIELKAG-------SATRPFFGVQPALVDNE 452
Cdd:cd12119 284 RVVIGGSAVPRSLIEA-FEERG---VRVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 453 GH--PQEGATEGNLVITDSWpgQARTLFGDHER----FEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:cd12119 360 GRelPWDGKAVGELQVRGPW--VTKSYYKNDEEsealTEDGWLRT-------GDVATIDEDGYLTITDRSKDVIKSGGEW 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 527 LGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:cd12119 431 ISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTS 507
|
570
....*....|.
1PG3_A 607 SGKIMRRILRK 617
Cdd:cd12119 508 TGKIDKKALRE 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-616 |
6.36e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 179.03 E-value: 6.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 73 GTLNLAAncLDRHlqenGDRTAIIWegDDTSqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLAC 152
Cdd:PRK06188 15 GHLLVSA--LKRY----PDRPALVL--GDTR----LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 153 ARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVItADEGVRAGRSIPLKKNVDdalknpnvtSVEHVIVLKRTGsdidwqEG 232
Cdd:PRK06188 83 QLAGLRRTALHPLGSLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVP------DG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 233 RDLWwrDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfkyvfdyhpgdiyWCTADVGWVTG 312
Cdd:PRK06188 147 VDLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSYLLYGPL--ACGAT---TLM----------FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDkaIEGTDR 377
Cdd:PRK06188 210 PRFLMCTPLshAGGAFflpTLLrggtvivlakFD-------PAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 378 SSLRILGSVGEPINP----EAWEwywkKIGkekcPV-VDTWWQTETGGFmITPLP-----GAIELKAGSATRPFFGVQPA 447
Cdd:PRK06188 281 SSLETVYYGASPMSPvrlaEAIE----RFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 448 LVDNEGHPQEGATEGNLVItdSWPGQARtlfGDHERFEQTYfSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK06188 352 LLDEDGREVAQGEVGEICV--RGPLVMD---GYWNRPEETA-EAFRDGWLhTGDVAREDEDGFYYIVDRKKDMIVTGGFN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 527 LGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK06188 426 VFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTA 502
|
570
....*....|
1PG3_A 607 SGKIMRRILR 616
Cdd:PRK06188 503 LGKPDKKALR 512
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-617 |
7.29e-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: 7.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 104 QSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLV 183
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 184 ITADEgvragrsiPLKKNVDDALKNPNVTSVEHVIVLKRTGSDIDWQEGRDlwWRDLiEKASPEHQPEAMNAEDPLFILY 263
Cdd:TIGR03098 102 VTSSE--------RLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPAS--WPKL-LALGDADPPHPVIDSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 264 TSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegvpNWPTPAR 341
Cdd:TIGR03098 171 TSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH-----DYLLPRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 342 MCQVVDKHQVNILYTAPtAIRALMAEGDkaIEGTDRSSLRILGSVGEPINPEAWEWYwkkigKEKCPVVDTWWQ---TEt 418
Cdd:TIGR03098 243 VLKALEKHGITGLAAVP-PLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRL-----RSFLPNARLFLMyglTE- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 gGFMITPL-PGAIELKAGSATR--PFFGVQPALVDNE----GHPQEGATEGNLVITDSWPGQARTlfgdHERFE-----Q 486
Cdd:TIGR03098 314 -AFRSTYLpPEEVDRRPDSIGKaiPNAEVLVLREDGSecapGEEGELVHRGALVAMGYWNDPEKT----AERFRplppfP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 487 TYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLN 566
Cdd:TIGR03098 389 GELHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPP 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1PG3_A 567 HGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:TIGR03098 469 GGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
91-616 |
4.45e-47 |
|
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: 172.17 E-value: 4.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17649 2 DAVALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwQEGRDLWWrdliekaspehqp 250
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------------HHPRQLAY------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 eamnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMf 330
Cdd:cd17649 99 ----------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 331 EGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGtDRSSLRILGSVGEPINPEAWeWYWKKIGkekCPVV 410
Cdd:cd17649 166 RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELL-RRWLKAP---VRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 411 DTWWQTETggfMITPL--PGAIELKAGSAT----RPFFGVQPALVDNEGHPQEGATEGNLVITDswPGQARtlfGDHERF 484
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASmpigRPLGGRSAYILDADLNPVPVGVTGELYIGG--EGLAR---GYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 485 EQT--------YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIkG 556
Cdd:cd17649 313 ELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 557 QAIYAYVTLNHGEEpSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17649 392 KQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-616 |
1.14e-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: 172.14 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHLQENGDRTAIIWEGDDTSqskhisYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLT------YAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 164 GGFSPEAVAGCIIDSSSRLVITADE--GVRAGRSIPlkknvddalknpnvtsvehvivlkrtGSDIDWQEGRDLwwrdli 241
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlaGELAVELVA--------------------------VTLLDQPGAAAG------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekASPEHQPeAMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyVFDYHPGDIYWCTADVGW-VTGHSylLY 318
Cdd:cd17651 125 --ADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQAR---ASSLGPGARTLQFAGLGFdVSVQE--IF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 GPLACGATtLMFEGvPNW-PTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEP--INPEAW 395
Cdd:cd17651 197 STLCAGAT-LVLPP-EEVrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 396 EWYWKKIGKEkcpVVDTWWQTETGgfMITplpgAIELKAGSAT--------RPFFGVQPALVDNEGHPQEGATEGNLVIt 467
Cdd:cd17651 273 EFCAGLPGLR---LHNHYGPTETH--VVT----ALSLPGDPAAwpapppigRPIDNTRVYVLDAALRPVPPGVPGELYI- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 dSWPGQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIA 543
Cdd:cd17651 343 -GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 544 EAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAYVVGDPEAPVDA---AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
91-615 |
1.47e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 172.84 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08314 25 DKTAIVFYG------RAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITADEgvRAGRSIPLKKNvddalknpnvTSVEHVIV------LKRTGSDI--DW----------QE 231
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSE--LAPKVAPAVGN----------LRLRHVIVaqysdyLPAEPEIAvpAWlraepplqalAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 232 GRDLWWRDLIEKAspeHQPEAMNA--EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGW 309
Cdd:PRK08314 167 GGVVAWKEALAAG---LAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 310 VTGHSYLLYGPLACGATTLMfegVPNW--PTPARMcqvVDKHQVNILYTAPTAIRALMAEGDkaIEGTDRSSLRILGSVG 387
Cdd:PRK08314 243 VTGMVHSMNAPIYAGATVVL---MPRWdrEAAARL---IERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPInPEAwewywkkIG---KEKC--PVVDTWWQTETGGFMITPLPGAIELK-AGSatrPFFGVQPALVDneghPQEGAT- 460
Cdd:PRK08314 315 AAM-PEA-------VAerlKELTglDYVEGYGLTETMAQTHSNPPDRPKLQcLGI---PTFGVDARVID----PETLEEl 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 ----EGNLVItdSWPGQARTLFGDHERFEQTyFSTF--KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:PRK08314 380 ppgeVGEIVV--HGPQVFKGYWNRPEATAEA-FIEIdgKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVEN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 535 ALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLN--HGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK08314 457 LLYKHPAIQEACVIATPDPRRGETVKAVVVLRpeARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILW 533
|
...
1PG3_A 613 RIL 615
Cdd:PRK08314 534 RQL 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-616 |
2.63e-45 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 168.46 E-value: 2.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 139 MPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVRAGRSIPLKKNVDDAlkNPNVtsvehVI 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA--APAK-----AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 219 VLKRTGSDIDWQ-EGRDLWWRDLIEKASP-------EHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFK 290
Cdd:PLN03051 74 VLPAAGEPVAVPlREQDLSWCDFLGVAAAqgsvggnEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 291 YVfDYHPGDIYWCTADVGWVTGhSYLLYGPLACGATTLMFEGVpnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDK 370
Cdd:PLN03051 154 HM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA---PLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 371 AIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEKcPVVDTWWQTETGGFMI--TPL-PGAIelkaGSATRPFFGVQPA 447
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLqPQAP----GAFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 448 LVDNEG--HPQEGATEGNLVITDSWPGQA-RTLFGDHerfEQTYFSTFKnMYFS--------GDGARRDEDGYYWITGRV 516
Cdd:PLN03051 304 LLNDNGvpYPDDQPCVGEVALAPPMLGASdRLLNADH---DKVYYKGMP-MYGSkgmplrrhGDIMKRTPGGYFCVQGRA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 517 DDVLNVSGHRLGTAEIESALV-AHPKIAEAAVVGIPhAIKGQAIYAYVTLNHGEEPS-------PELYAEVRNWVRKEIG 588
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTNLN 458
|
490 500
....*....|....*....|....*...
1PG3_A 589 PLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PLN03051 459 PLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-547 |
4.73e-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: 165.52 E-value: 4.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDL-GIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EGVRAGRSIPLkknvddalknpnvtsvEHVIVlkrtgsdidwqegRDLWWRDLIEKASPEHQPEAMNAEDPLFILYTSGS 267
Cdd:TIGR01733 81 ALASRLAGLVL----------------PVILL-------------DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTA----DVgwvtghSYL-LYGPLACGATTLMFEGVPNWPTPARM 342
Cdd:TIGR01733 132 TGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFAslsfDA------SVEeIFGALLAGATLVVPPEDEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 343 CQVVDKHQVNILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWE-WYWKKigkEKCPVVDTWWQTE-TGG 420
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPALVDrWRARG---PGARLINLYGPTEtTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 421 FMITPLPGAIELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVItdSWPGQARTLFGD----HERF-EQTYF-ST 491
Cdd:TIGR01733 277 STATLVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVpVGVV-GELYI--GGPGVARGYLNRpeltAERFvPDPFAgGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 492 FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:TIGR01733 354 GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-615 |
6.96e-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: 167.07 E-value: 6.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVIT-ADEGVRAGRSiplkknvddalknPNVTSVEHVIVLKRTGSDIDwqegrdlwwrdl 240
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTtADLAARLPAG-------------GDVALLGDEALAAPPATPPL------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 241 iekasPEHQPEamnaeDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGW-VTGhsYLLYG 319
Cdd:cd17646 133 -----VPPRPD-----NLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 320 PLACGATTLMFEgvPNWPT-PARMCQVVDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:cd17646 200 PLVAGARLVVAR--PGGHRdPAYLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 WKKIGKE----KCP---VVD-TWWQTeTGGFMITPLP-GaielkagsatRPFFGVQPALVDNEGHPQEGATEGNLVITDs 469
Cdd:cd17646 274 LALPGAElhnlYGPteaAIDvTHWPV-RGPAETPSVPiG----------RPVPNTRLYVLDDALRPVPVGVPGELYLGG- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 470 wPGQARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd17646 342 -VQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHA 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17646 421 VVVARAAPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-615 |
1.44e-44 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 166.64 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 87 QENGDRTAIIwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGF 166
Cdd:cd05904 16 SAHPSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 167 SPEAVAGCIIDSSSRLVITADEGVragrsiplKKNVDDALKnpnvtsvehVIVLkrtGSDIDwqeGRDLWWRDLIEKASP 246
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAFTTAELA--------EKLASLALP---------VVLL---DSAEF---DSLSFSDLLFEADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 EHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFD--YHPGDIYWCTADVGWVTGHSYLLYGPLACG 324
Cdd:cd05904 149 EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 325 ATTL---MFEGvpnwptpARMCQVVDKHQVNILYTAPTAIRAlMAEGDKAiEGTDRSSLRILGSVGEPINPEAWEWYWKK 401
Cdd:cd05904 228 ATVVvmpRFDL-------EELLAAIERYKVTHLPVVPPIVLA-LVKSPIV-DKYDLSSLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 402 IGKekCPVVDTWWQTE-TGGFMITPLPGAIELKAGSATRPFFGVQPALVD-NEGHPQEGATEGNLVITDswPGQARTLFG 479
Cdd:cd05904 299 FPN--VDLGQGYGMTEsTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG--PSIMKGYLN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 480 DHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAI 559
Cdd:cd05904 375 NPEATAATI--DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05904 453 MAFVVRKPGSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
88-615 |
2.25e-42 |
|
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: 159.67 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 88 ENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:cd12117 9 RTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 168 PEAVAGCIIDSSSRLVITaDEGVRAGrsiplkknvddalknpnvtsvehvivlkrtgsdidWQEGRDLWWRDLIEKASPE 247
Cdd:cd12117 83 AERLAFMLADAGAKVLLT-DRSLAGR-----------------------------------AGGLEVAVVIDEALDAGPA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 248 HQPEAMN-AEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVfDYHPGDIYWCTADVGWvTGHSYLLYGPLACGAT 326
Cdd:cd12117 127 GNPAVPVsPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT-NYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGAR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 -TLMFEGVPnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEPINPEawewyWKKIGKE 405
Cdd:cd12117 204 lVLAPKGTL--LDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPP-----HVRRVLA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 406 KCP---VVDTWWQTETGGFMITPLPGAIELKAGSAT--RPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTLFGD 480
Cdd:cd12117 272 ACPglrLVNGYGPTENTTFTTSHVVTELDEVAGSIPigRPIANTRVYVLDEDGRPVPPGVPGELYV--GGDGLALGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 481 ----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKG 556
Cdd:cd12117 350 paltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGD 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 557 QAIYAYVTLNHGEEPspelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12117 430 KRLVAYVVAEGALDA-----AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
84-615 |
2.34e-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: 159.02 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHLQENGDRTAIIwegddtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd12115 7 AQAARTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 164 GGFSPEAVAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliek 243
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 244 aspehqpeamNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATTFkyvfdyhPGDiYWctADVGWVTG-----HSY 315
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAF-------SAE-EL--AGVLASTSicfdlSVF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 316 LLYGPLACGATTLMFEGVPNWPTPARMCQVvdkhqvNILYTAPTAIRALMAEGDKAiegtdrSSLRILGSVGEPINPEAW 395
Cdd:cd12115 163 ELFGPLATGGKVVLADNVLALPDLPAAAEV------TLINTVPSAAAELLRHDALP------ASVRVVNLAGEPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 396 EWYWKKIGKEKcpVVDTWWQTETGGF-MITPLPGAIElKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQA 474
Cdd:cd12115 231 QRLYARLQVER--VVNLYGPSEDTTYsTVAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYI--GGAGVA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 475 RTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGI 550
Cdd:cd12115 306 RGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 551 PHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
91-617 |
1.68e-41 |
|
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: 156.30 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwegDDTSQskhISYRELHRDVCRFANTLLDLG-IKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspe 169
Cdd:cd05941 1 DRIAIV---DDGDS---ITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVagciidsssrlvitadegvragrsiPLkknvddALKNPnVTSVEHVIvlkrTGSDIDwqegrdLWWRDliekaspehq 249
Cdd:cd05941 64 AV-------------------------PL------NPSYP-LAELEYVI----TDSEPS------LVLDP---------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 250 peAMnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpgdIYWCTADV-----------GWVTGhsylLY 318
Cdd:cd05941 92 --AL-------ILYTSGTTGRPKGVVLTHANLAANVRALVDA--------WRWTEDDVllhvlplhhvhGLVNA----LL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 GPLACGATTLMfegVPNwPTPARMCQVVDKHQVNILYTAPT-------AIRALMAEGDKAIEGTDRSsLRILGSVGEPIN 391
Cdd:cd05941 151 CPLFAGASVEF---LPK-FDPKEVAISRLMPSITVFMGVPTiytrllqYYEAHFTDPQFARAAAAER-LRLMVSGSAALP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 PEAWEwYWKKIGKEkcPVVDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPALVDNE-GHPQEGATEGNL------ 464
Cdd:cd05941 226 VPTLE-EWEAITGH--TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIqvrgps 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 465 VITDSWPGQARTlfgdHERF-EQTYFSTfknmyfsGDGARRDEDGYYWITGRV-DDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:cd05941 301 VFKEYWNKPEAT----KEEFtDDGWFKT-------GDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGV 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 543 AEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05941 370 SECAVIGVPDPDWGERVVAVVVLRAGAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
94-616 |
2.05e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 157.37 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 94 AIIWEGDDTsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAG 173
Cdd:PRK08276 2 AVIMAPSGE----VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 174 CIIDSSSRLVITADEGVRAGRSIPlkknvdDALKNpnvtsveHVIVLKRTGSDIDwqeGRDLW--WRDliekASPEHQPE 251
Cdd:PRK08276 78 IVDDSGAKVLIVSAALADTAAELA------AELPA-------GVPLLLVVAGPVP---GFRSYeeALA----AQPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 252 AMNAEDPLfiLYTSGSTGKPKGVLHTTGGYLVYAA---TTFKYVFDYH--PGDIYWCTADvgwvtghsylLY--GPLACG 324
Cdd:PRK08276 138 DETAGADM--LYSSGTTGRPKGIKRPLPGLDPDEApgmMLALLGFGMYggPDSVYLSPAP----------LYhtAPLRFG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 325 ATTLMFEGV----PNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA----WE 396
Cdd:PRK08276 206 MSALALGGTvvvmEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVkramID 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 WyWKKIgkekcpVVDTWWQTETGGF-MITPlPGAIElKAGSATRPFFGVQpALVDNEGHPQEGATEGNlvITDSWPGQAR 475
Cdd:PRK08276 285 W-WGPI------IHEYYASSEGGGVtVITS-EDWLA-HPGSVGKAVLGEV-RILDEDGNELPPGEIGT--VYFEMDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 476 TLFGDHERFEQTY----FSTFknmyfsGDGARRDEDGYYWITGRVDDVLnVSGhrlGT----AEIESALVAHPKIAEAAV 547
Cdd:PRK08276 353 EYHNDPEKTAAARnphgWVTV------GDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08276 423 FGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-649 |
3.22e-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: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDdtsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEgvragrsiplkknVDDALKNPNVTSVehvivlkrtgsDIDWQEgrdlwwrdlI 241
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLTQSA-------------LAARLPELGVPVL-----------ALDALA---------L 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIywctadVGWVTGHS-----YL 316
Cdd:COG1020 603 AAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfdasvWE 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATTLMF--EGVPNwptPARMCQVVDKHQVNILYTAPTAIRALMAEGdkaieGTDRSSLRILGSVGEPINPEA 394
Cdd:COG1020 676 IFGALLSGATLVLAppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAA-----PEALPSLRLVLVGGEALPPEL 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 395 WEwYWKKIGKEkCPVVDTWWQTETGGFMITPLPGAIELKAGSAT--RPFFGVQPALVDNEGHPQ-EGATeGNLVItdSWP 471
Cdd:COG1020 748 VR-RWRARLPG-ARLVNLYGPTETTVDSTYYEVTPPDADGGSVPigRPIANTRVYVLDAHLQPVpVGVP-GELYI--GGA 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQARtlfGDHERFEQT--YF--STFKN----MYFSGDGARRDEDG---YywiTGRVDDVLNVSGHR--LGtaEIESALVA 538
Cdd:COG1020 823 GLAR---GYLNRPELTaeRFvaDPFGFpgarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRieLG--EIEAALLQ 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 539 HPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRnwvRKEIGPLATPDVLHWTDSLPKTRSGKimrrILRKI 618
Cdd:COG1020 895 HPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL---ALLLPPYMVPAAVVLLLPLPLTGNGK----LDRLA 967
|
570 580 590
....*....|....*....|....*....|.
1PG3_A 619 AAGDTSNLGDTSTLADPGVVEKLLEEKQAIA 649
Cdd:COG1020 968 LPAPAAAAAAAAAAPPAEEEEEEAALALLLL 998
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-616 |
4.60e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 156.77 E-value: 4.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIIWEgDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITADEGVRAGRSIplKKNVDDALKNpnvtsvehvIVLKRTGSD-----IDWQEGRDLwwrdliEKA 244
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQI--QQEDATPLRH---------ICLTRVALPaddgvSSFTQLKAQ------QPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 245 SPEHQPeAMNAEDPLFILYTSGSTGKPKGVLHTT-----GGYlvYAATTFKYVFDyhpgDIYW-----------CTAdvg 308
Cdd:PRK08008 163 TLCYAP-PLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSAWQCALRDD----DVYLtvmpafhidcqCTA--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 wvtghsylLYGPLACGATTLMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTD--RSSLRILgsv 386
Cdd:PRK08008 233 --------AMAAFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHclREVMFYL--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 387 gePINPEAWEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAiELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVI 466
Cdd:PRK08008 298 --NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 467 TDSwPGqaRTLFgdherfeQTYF----STFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:PRK08008 372 KGV-PG--KTIF-------KEYYldpkATAKVLeadgwLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 538 AHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08008 442 THPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
86-615 |
6.70e-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: 155.10 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 86 LQENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHsvifgg 165
Cdd:cd05945 1 AAANPDRPAVVEGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAY------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 166 fspeavagciidsssrlvitadegvragrsIPLkknvddalknpnvtsvehvivlkrtgsDIDWQEGRdlwWRDLIEKAS 245
Cdd:cd05945 69 ------------------------------VPL---------------------------DASSPAER---IREILDAAK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 246 PEhqpEAMNAEDPLF-ILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGW---VTGhsylLYGPL 321
Cdd:cd05945 89 PA---LLIADGDDNAyIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPFSFdlsVMD----LYPAL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTlmfegvpnWPTP-------ARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGEPI-NPE 393
Cdd:cd05945 161 ASGATL--------VPVPrdatadpKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLpHKT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 394 AWEWywkkigKE---KCPVVDTWWQTET----GGFMITPlpgaiELKAGSAT----RPFFGVQPALVDNEGHPQEGATEG 462
Cdd:cd05945 231 ARAL------QQrfpDARIYNTYGPTEAtvavTYIEVTP-----EVLDGYDRlpigYAKPGAKLVILDEDGRPVPPGEKG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 463 NLVITDswPGQARTLFGDHERFEQTYFSTFKN-MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPK 541
Cdd:cd05945 300 ELVISG--PSVSKGYLNNPEKTAAAFFPDEGQrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 542 IAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05945 378 VKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLT--KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-615 |
7.27e-41 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 155.74 E-value: 7.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITAD--EGVRAGRSIPLKknvddalknpnvtsVEHVIVLKRTGSDidwqegrdlwwrdliEKASPEH 248
Cdd:cd05923 92 LAELIERGEMTAAVIAVdaQVMDAIFQSGVR--------------VLALSDLVGLGEP---------------ESAGPLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATTFKYVFDYH-------PgdIYWctadvgwVTGHSYLLY 318
Cdd:cd05923 143 EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHnvvlglmP--LYH-------VIGFFAVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 GPLACGATTLmfegVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWY 398
Cdd:cd05923 214 AALALDGTYV----VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFA--GLKLSSLRHVTFAGATMPDAVLERV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 WKKIGKEKcpvVDTWWQTETGGFMITPLPgaielKAGSATRPFFGVQPALVDNEGHPQEGAT---EGNLVITDS----WP 471
Cdd:cd05923 288 NQHLPGEK---VNIYGTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEALAngeEGELIVAAAadaaFT 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQARtlfgdheRFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:cd05923 360 GYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 552 HAIKGQAIYAYVTLNHGEEPSPELYAEVRNwvrKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05923 433 DERWGQSVTACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
87-618 |
1.13e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 156.24 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 87 QENGDRTAIIwegDDTSQskhISYRELHRDVCRFANTLLDLGIKKGDVVAI----YMPMVpeaaVAMLACARIGAVHSVI 162
Cdd:PRK07788 60 RRAPDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 FGGFSPEAVAGCIIDSSSRLVITADEGVRAGRSIPlkknvddalknPNVTSVeHVIVLKRTGSDIDWQEGRDLwwRDLIE 242
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRL-RAWGGNPDDDEPSGSTDETL--DDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 KASPEHQPEAmnAEDPLFILYTSGSTGKPKGVLHTTggylVYAATTFKYVFDYHP---GDIYWCTADVGWVTGHSYLLYG 319
Cdd:PRK07788 196 GSSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRPE----PSPLAPLAGLLSRVPfraGETTLLPAPMFHATGWAHLTLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 320 pLACGATTLM---FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWE 396
Cdd:PRK07788 270 -MALGSTVVLrrrFD-------PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 WYWKKIGkekcPVV-DTWWQTETGgFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWPGQAR 475
Cdd:PRK07788 342 RALEAFG----PVLyNLYGSTEVA-FATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 476 TLFGDHERFeqtyfstfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIK 555
Cdd:PRK07788 417 TDGRDKQII--------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 556 GQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK07788 489 GQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-617 |
5.23e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 154.04 E-value: 5.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 75 LNLAaNCLDRHLQENGDRTAIIWeGDdtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 155 IGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD---EGVRAGRSIPLkknvddalknpnvtSVEHVIVLKRTGSDIDWQe 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASP--------------DLTHVVAIGGARAGLDYE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 232 grdlwwrDLI-EKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGgylvyaatTFKYVFDYHPGDIYWCT--ADVG 308
Cdd:PRK07470 145 -------ALVaRHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG--------QMAFVITNHLADLMPGTteQDAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 WVT-------GHSYLLygPLACGATTLMFEGVPNwpTPARMCQVVDKHQVNILYTAPTaIRALMAEgDKAIEGTDRSSLR 381
Cdd:PRK07470 210 LVVaplshgaGIHQLC--QVARGAATVLLPSERF--DPAEVWALVERHRVTNLFTVPT-ILKMLVE-HPAVDRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 382 ILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGGfMITPLPGAI-------ELKAGSATRPFFGVQPALVDNEGH 454
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTG-NITVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 455 P-QEGATEGNLVItdswpGQArtLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK07470 360 ElPPGETGEICVI-----GPA--VFAGYYNNPEANAKAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGSNVYPREI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 533 ESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:PRK07470 433 EEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
....*
1PG3_A 613 RILRK 617
Cdd:PRK07470 510 KMVRE 514
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-615 |
1.14e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 152.06 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIiwEGDDTSqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd12116 1 PDATAV--RDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITadegvragrsiplkknvDDALKNP---NVTSVEHVIvlkrtgsdidwqegrdlwWRDlieKASP 246
Cdd:cd12116 75 RLRYILEDAEPALVLT-----------------DDALPDRlpaGLPVLLLAL------------------AAA---AAAP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 EHQPEAMNAEDPLFILYTSGSTGKPKGV----------LHTTGGYL-------VYAATTfkYVFDYhpgdiywctadvgw 309
Cdd:cd12116 117 AAPRTPVSPDDLAYVIYTSGSTGRPKGVvvshrnlvnfLHSMRERLglgpgdrLLAVTT--YAFDI-------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 310 vtghSYL-LYGPLACGATTLMFEGVPNwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGdkaieGTDRSSLRIL-GsvG 387
Cdd:cd12116 181 ----SLLeLLLPLLAGARVVIAPRETQ-RDPEALARLIEAHSITVMQATPATWRMLLDAG-----WQGRAGLTALcG--G 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINP-----------EAWEWYwkkiGkekcPVVDTWWQTETggfMITPLPGAIELkagsaTRPFFGVQPALVDNEGHPQ 456
Cdd:cd12116 249 EALPPdlaarllsrvgSLWNLY----G----PTETTIWSTAA---RVTAAAGPIPI-----GRPLANTQVYVLDAALRPV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 EGATEGNLVITDswPGQARTLFGD----HERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:cd12116 313 PPGVPGELYIGG--DGVAQGYLGRpaltAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 532 IESALVAHPKIAEAAVVGIPhAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd12116 391 IEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
....
1PG3_A 612 RRIL 615
Cdd:cd12116 467 RKAL 470
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-615 |
5.30e-39 |
|
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: 149.17 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EgvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFILYTSGS 267
Cdd:cd05935 82 E------------------------------------------------------------------LDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYlvyAATTFKYVFDYH--PGDIYWCTADVGWVTGHSYLLYGPLACGATTLMfegVPNWPTPArMCQV 345
Cdd:cd05935 96 TGLPKGCMHTHFSA---AANALQSAVWTGltPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL---MARWDRET-ALEL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 346 VDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGGFMITP 425
Cdd:cd05935 169 IEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 426 LPGAieLKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVItdSWPGQARTLFGDHERFEQTYFSTFKNMYF-SGDGAR 503
Cdd:cd05935 244 PPLR--PKLQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIEIKGRRFFrTGDLGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNhgeepsPELYAEVR--- 580
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR------PEYRGKVTeed 393
|
490 500 510
....*....|....*....|....*....|....*..
1PG3_A 581 --NWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05935 394 iiEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-609 |
5.00e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 148.49 E-value: 5.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIIWeGDDTsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITADEgvRAGRsiplkknVDDALknPNVTSVEHVIVLkRTGSDIDWQEGrDLWWRDLIEKASPEHQ 249
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPR-------VAEVL--PRLPKLRTLVVV-EDGSGNDLLPG-AVDYEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 250 PEAMNAEDpLFILYTSGSTGKPKGVLHTT--------GGYLVYAATTfkyvfdyhPGDIYWCTADVGWVTGHSYLLYGPL 321
Cdd:PRK07798 158 FGERSPDD-LYLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEP--------IEDEEELAKRAAAGPGMRRFPAPPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTL-----MFEG----VPNWPT--PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPI 390
Cdd:PRK07798 229 MHGAGQWaafaaLFSGqtvvLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGALF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 391 NPEAWEWYWKKIgkekcP---VVDTWWQTETG-GFMITPLPGAielkaGSATRPFFGVQP--ALVDNEGHPQEGATEGNL 464
Cdd:PRK07798 309 SPSVKEALLELL-----PnvvLTDSIGSSETGfGGSGTVAKGA-----VHTGGPRFTIGPrtVVLDEDGNPVEPGSGEIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 465 VItdswpgqART------LFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALV 537
Cdd:PRK07798 379 WI-------ARRghiplgYYKDPEKTAETFPTIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALK 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 538 AHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK07798 452 AHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-631 |
1.32e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 147.23 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 79 ANCLDRHLQENGDRTAIIWEGDDTSqskhisYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNTTT------WRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 159 HSVIFGGFSPEAVAGCIIDSSSRLVITadEGVRAgrsiPLKKNVDDAlknpnVTSVEHVIVLKRTGSDidwqegRDLWWR 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALA----PVATAVRDI-----VPLLSTVVVAGGSSDD------SVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 239 DLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAATTFKYVFDYH-PGDIYWCTADVGWVTGHSY 315
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 316 LLYGpLACGATTLMFegvpnwPT----PARMCQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRsSLRILGSVGEPIN 391
Cdd:PRK07786 234 MLPG-LLLGAPTVIY------PLgafdPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDL-ALRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 P----EAWEWYwkkigkEKCPVVDTWWQTEtggfmITP----LPG--AIElKAGSATRPFFGVQPALVDNE------GHP 455
Cdd:PRK07786 304 DtllrQMAATF------PEAQILAAFGQTE-----MSPvtcmLLGedAIR-KLGSVGKVIPTVAARVVDENmndvpvGEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 456 QEGATEGNLVITDSWPGQARTLfgdhERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK07786 372 GEIVYRAPTLMSGYWNNPEATA----EAFAGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 536 LVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEpSPELyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK07786 441 LASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDA-ALTL-EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
570
....*....|....*..
1PG3_A 616 RK-IAAGDTSNLGDTST 631
Cdd:PRK07786 519 RErYGACVNVERRSASA 535
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
91-617 |
5.69e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 142.58 E-value: 5.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwegDDTSQSkhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK06087 38 DKIAVV---DNHGAS--YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVI--TADEGVR-AGRSIPLKKNVDdalknpnvtSVEHVIVLKRTGSdidwqEGRDLWWRDLIEKASPE 247
Cdd:PRK06087 113 LVWVLNKCQAKMFFapTLFKQTRpVDLILPLQNQLP---------QLQQIVGVDKLAP-----ATSSLSLSQIIADYEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 248 HQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATT 327
Cdd:PRK06087 179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 328 LMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEWYWKKiGKEKC 407
Cdd:PRK06087 258 VLLDIF----TPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTIPKKVARECQQR-GIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 408 PVvdtWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNE------GHPQEGATEGnlvitdswPGQARTLFGDH 481
Cdd:PRK06087 331 SV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEArktlppGCEGEEASRG--------PNVFMGYLDEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 482 ERfeqtyfsTFKNM-----YFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKG 556
Cdd:PRK06087 400 EL-------TARALdeegwYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLG 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 557 QAIYAYVTLNhGEEPSPELyAEVRNWV-RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06087 473 ERSCAYVVLK-APHHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-623 |
6.09e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 141.48 E-value: 6.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 GVRAGRSIPLkkNVDDalknpnvtsvehvivlkrtgsdidwqegrdlwWRDLIEKASPEHQPEAmNAEDPLFILYTSGST 268
Cdd:PRK09088 103 AVAAGRTDVE--DLAA--------------------------------FIASADALEPADTPSI-PPERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVDK 348
Cdd:PRK09088 148 GQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF----EPKRTLGRLGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 349 HQVNI--LYTAPTAIRALMAEgdkaiEGTDRSSLRILGSV---GEPiNPEAWEWYWKKIGkekCPVVDTWWQTETGGFMI 423
Cdd:PRK09088 223 PALGIthYFCVPQMAQAFRAQ-----PGFDAAALRHLTALftgGAP-HAAEDILGWLDDG---IPMVDGFGMSEAGTVFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 424 TPL-PGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT--DSWPGQARTLFGDHERF-EQTYFSTfknmyfsG 499
Cdd:PRK09088 294 MSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRgpNLSPGYWRRPQATARAFtGDGWFRT-------G 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 500 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGeepSPELYAEV 579
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERI 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
1PG3_A 580 RNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR-KIAAGDT 623
Cdd:PRK09088 444 RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRdALAAGRK 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
88-621 |
7.80e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 145.49 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 88 ENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFS 167
Cdd:PRK12316 4563 MTPDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 168 PEAVAGCIIDSSSRLVITADegvRAGRSIPLKKNVddalknpnvtsveHVIVLKRTGsdiDWqEGRdlwwrdliekasPE 247
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQS---HLLQRLPIPDGL-------------ASLALDRDE---DW-EGF------------PA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 248 HQPE-AMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfkyvfdyhpGDIYWCTADVGWVTGHSYL-------LYG 319
Cdd:PRK12316 4685 HDPAvRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYH 4755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 320 PLACGATTLMFEgvPNWPTPARMCQVVDKHQVNILYTAPTAIRALmAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYW 399
Cdd:PRK12316 4756 PLINGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAW 4830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 400 KKI---------GKEKCPVVDTWWQTETGgfmitPLPGAIELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVITDSw 470
Cdd:PRK12316 4831 RALkpvylfngyGPTETTVTVLLWKARDG-----DACGAAYMPIG---TPLGNRSGYVLDGQLNPLPVGVAGELYLGGE- 4901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 471 pGQARTLFG----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:PRK12316 4902 -GVARGYLErpalTAERFVPDPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 546 AVVGIPHAIkGQAIYAYVTLNHGE-EPSPELYAEVRNWVRKEIGPlATPDVL---HWT--DSLPKTRSGKIMRRILRKIA 619
Cdd:PRK12316 4981 VVIAQEGAV-GKQLVGYVVPQDPAlADADEAQAELRDELKAALRE-RLPEYMvpaHLVflARMPLTPNGKLDRKALPQPD 5058
|
..
1PG3_A 620 AG 621
Cdd:PRK12316 5059 AS 5060
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
91-615 |
9.30e-36 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 140.93 E-value: 9.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEgDDTsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17655 12 DHTAVVFE-DQT-----LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADegvragrsiPLKKNVDDAlknpnvtsvEHVIVLKrtgsDIDWQEGRDlwwrdliekaspEHQP 250
Cdd:cd17655 86 IQYILEDSGADILLTQS---------HLQPPIAFI---------GLIDLLD----EDTIYHEES------------ENLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 EAMNAEDPLFILYTSGSTGKPKGVLHTTGG--YLVYAATTfKYVFDYHpgdiywctADVGWVTGHSYLL-----YGPLAC 323
Cdd:cd17655 132 PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGvvNLVEWANK-VIYQGEH--------LRVALFASISFDAsvteiFASLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 324 GATTLMFEGVPNWPTPArMCQVVDKHQVNILYTAPTAIRALMAEGDkaiegTDRSSLRILGSVGEPINPEAWEwYWKKIG 403
Cdd:cd17655 203 GNTLYIVRKETVLDGQA-LTQYIRQNRITIIDLTPAHLKLLDAADD-----SEGLSLKHLIVGGEALSTELAK-KIIELF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 404 KEKCPVVDTWWQTETG-GFMITPL-PGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTLFG-- 479
Cdd:cd17655 276 GTNPTITNAYGPTETTvDASIYQYePETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYI--GGEGVARGYLNrp 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 480 --DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQ 557
Cdd:cd17655 354 elTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQN 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 558 AIYAYVTlnhGEEPSPElyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17655 434 YLCAYIV---SEKELPV--AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-618 |
1.05e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 140.87 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEGVRagrsiplkknvddalknpnvtsvEHVIvlkrtGSDIDWQEgrdlwwrdLIEKASPEHQP 250
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA-----------------------KLIP-----GISVKFAE--------LMNGPKEEAEI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 -EAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL----YG-PLacg 324
Cdd:PRK03640 135 qEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMrsviYGmRV--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 325 atTLM--FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDkaiEGTDRSSLR--ILGsvGEPINPEAWEwywk 400
Cdd:PRK03640 211 --VLVekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLG---EGTYPSSFRcmLLG--GGPAPKPLLE---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 401 kIGKEK-CPVVDTWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNeGHPQEGATEGNLVItdswpgQARTLFG 479
Cdd:PRK03640 273 -QCKEKgIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV------KGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 480 DHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQA 558
Cdd:PRK03640 345 GYLNREDATRETFQDGWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 559 IYAYVTlnHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK03640 425 PVAFVV--KSGEVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
263-620 |
1.09e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 138.00 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegvpnWPTPA-- 340
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV-------LAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 341 -------RMCQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIGkekCPVVDTW 413
Cdd:cd05944 81 rnpglfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 414 WQTE-TGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQE---GATEGNLVItdswpgQARTLFGDHERFEQTYF 489
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLRdcaPDEVGEICV------AGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 490 STFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHG 568
Cdd:cd05944 228 AFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 569 EEPSPElyaEVRNWVRKEIGP-LATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05944 308 AVVEEE---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-549 |
1.34e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 142.16 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDTSQSkhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEGVragrsipLKKnVDDALKnpNVTSVEHVIVLKRTGsdiDWQEGRDLWWRDLI 241
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRD--ELPSLRHIVVLDPRG---LRDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKASPEHQPE-------AMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY-----WCtadvgW 309
Cdd:COG1022 162 ALGREVADPAelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----H 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 310 VTGHSyLLYGPLACGAT-------------------TLMFeGVP-------------------------NWPTP---ARM 342
Cdd:COG1022 236 VFERT-VSYYALAAGATvafaespdtlaedlrevkpTFML-AVPrvwekvyagiqakaeeagglkrklfRWALAvgrRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 343 CQVVDKHQVNILYTAPTA---------IRALMaeGDKaiegtdrssLRILGSVGEPINPEAWEWYWkKIGkekCPVVDTW 413
Cdd:COG1022 314 RARLAGKSPSLLLRLKHAladklvfskLREAL--GGR---------LRFAVSGGAALGPELARFFR-ALG---IPVLEGY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 414 WQTETGGFMITPLPGAIelKAGSATRPFFGVQpalV----DNE----------G-HPQEGATegnlvitdswpgqARTLF 478
Cdd:COG1022 379 GLTETSPVITVNRPGDN--RIGTVGPPLPGVE---VkiaeDGEilvrgpnvmkGyYKNPEAT-------------AEAFD 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 479 GDHerfeqtYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGhrlGT----AEIESALVAHPKIAEAAVVG 549
Cdd:COG1022 441 ADG------WLHT-------GDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-615 |
1.27e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.01 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 106 KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 186 ADegvragRSIPLKKNVDDAlknpnvTSVEHVIVL-------------------KRTGSDIDWQEGRDLWWRDLIEKASP 246
Cdd:PRK06710 128 LD------LVFPRVTNVQSA------TKIEHVIVTriadflpfpknllypfvqkKQSNLVVKVSESETIHLWNSVEKEVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 EHQPEAMNAEDPLFIL-YTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDiywctaDVGWVTGHSYLLYGPLACGA 325
Cdd:PRK06710 196 TGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 326 TTLMfEG-----VPNWPTPArMCQVVDKHQVNILYTAPTAIRALMaeGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:PRK06710 270 LSIM-QGykmvlIPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 401 KIG---------KEKCPVVDT--WWQTETGGFMITPLPGA----IELKAGSATRPffgvqpalvdneGHPQEGATEGNLV 465
Cdd:PRK06710 346 VTGgklvegyglTESSPVTHSnfLWEKRVPGSIGVPWPDTeamiMSLETGEALPP------------GEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 466 ITDSWpgqartlfgdhERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:PRK06710 414 MKGYW-----------NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK06710 483 VTIGVPDPYRGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-616 |
1.30e-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: 137.19 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 117 VCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEavagcIIDSSSRLVITadegVRAGRSI 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 197 PLKKNVDDALKnpnvtsvehvIVLKRTGSDIDWQEGRDLW-WRDLIEKASPEHqpeamnaEDPLFILYTSGSTGKPKGVL 275
Cdd:cd05922 74 LADAGAADRLR----------DALPASPDPGTVLDADGIRaARASAPAHEVSH-------EDLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 276 --HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFE-GVPnwptPARMCQVVDKHQVN 352
Cdd:cd05922 137 lsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTNdGVL----DDAFWEDLREHGAT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 353 ILYTAPTaIRALMAEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYwkkigKEKCP---VVDTWWQTETGGFMITPLPGA 429
Cdd:cd05922 209 GLAGVPS-TYAMLTRLGFDPAKL--PSLRYLTQAGGRLPQETIARL-----RELLPgaqVYVMYGQTEATRRMTYLPPER 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 430 IELKAGSATRPFFGVQPALVDNEGHPQ------EGATEGNLVITDSWPGQArtlfgdherfEQTYFSTFKNMYFSGDGAR 503
Cdd:cd05922 281 ILEKPGSIGLAIPGGEFEILDDDGTPTppgepgEIVHRGPNVMKGYWNDPP----------YRRKEGRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 504 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIkGQAIYAYVTLNHGEEPSPelyaeVRNWV 583
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-----VLRSL 424
|
490 500 510
....*....|....*....|....*....|...
1PG3_A 584 RKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-616 |
2.10e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 137.52 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 83 DRHLQENGDRTAIIWEGDDTSqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK13391 4 GIHAQTTPDKPAVIMASTGEV----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 FGGFSPEAVAGCIIDSSSRLVITAdegvRAGRSIplkknVDDALKNpnVTSVEHVIVLKRTGSdidwQEGrdlwWRDLIE 242
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITS----AAKLDV-----ARALLKQ--CPGVRHRLVLDGDGE----LEG----FVGYAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 kaSPEHQPEAMNAEDPL--FILYTSGSTGKPKGVLH--------TTGGYLVYaattFKYVFDYHPGDIYWCTADVGwvtg 312
Cdd:PRK13391 141 --AVAGLPATPIADESLgtDMLYSSGTTGRPKGIKRplpeqppdTPLPLTAF----LQRLWGFRSDMVYLSPAPLY---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSyllyGPLA-------CGATTLMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGS 385
Cdd:PRK13391 211 HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 386 VGEPINPEAWE----WyWKkigkekcPVVDTWW-QTETGGFMITPLPGAIElKAGSATRPFFGVqPALVDNEGHPQEgat 460
Cdd:PRK13391 283 AAAPCPPQVKEqmidW-WG-------PIIHEYYaATEGLGFTACDSEEWLA-HPGTVGRAMFGD-LHILDDDGAELP--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 egnlvitdswPGQARTLFGDHER-FEqtYF----------STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK13391 350 ----------PGEPGTIWFEGGRpFE--YLndpaktaearHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYP 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 530 AEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK13391 418 QEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGK 497
|
....*..
1PG3_A 610 IMRRILR 616
Cdd:PRK13391 498 LYKRLLR 504
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
82-620 |
2.23e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 137.98 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEgddtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12583 24 FDATVARFPDREALVVR----HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADeGVRA-------GRSIP-LKKNVDDALKNPNVTSVEHVIVL--KRTGSDIDWQE 231
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTsdyhamlQELLPgLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 232 ----GRDLWWRDLIEKASpehqpeAMNAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTF----KYVFdyhPG 298
Cdd:PRK12583 179 lqarGETVSREALAERQA------SLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtehdRLCV---PV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 299 DIYWC----TADVGWVTGHSYLLY-----GPLAcgatTLmfegvpnwptparmcQVVDKHQVNILYTAPTAIRALMAEGD 369
Cdd:PRK12583 250 PLYHCfgmvLANLGCMTVGACLVYpneafDPLA----TL---------------QAVEEERCTALYGVPTMFIAELDHPQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 370 KAieGTDRSSLRILGSVGEPINPEAWEwywKKIGKEKCP-VVDTWWQTETGGfmITPLPGA---IELKAGSATRPFFGVQ 445
Cdd:PRK12583 311 RG--NFDLSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP--VSLQTTAaddLERRVETVGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 446 PALVDNEGH--PQ----EGATEGNLVITDSWpgqartlfGDHERfeqTYFSTFKN--MYfSGDGARRDEDGYYWITGRVD 517
Cdd:PRK12583 384 VKVVDPDGAtvPRgeigELCTRGYSVMKGYW--------NNPEA---TAESIDEDgwMH-TGDLATMDEQGYVRIVGRSK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 518 DVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLH 597
Cdd:PRK12583 452 DMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFR 528
|
570 580
....*....|....*....|...
1PG3_A 598 WTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK12583 529 FVDEFPMTVTGKVQKFRMREISI 551
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-622 |
6.42e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvRAGRSIPLKKNVDdalknpnvtsvehVIVLKRTGSdidWQEGRdlwwrdliekasPEHQPE-AMNAEDPLFILYTSG 266
Cdd:PRK12316 617 ---HLGRKLPLAAGVQ-------------VLDLDRPAA---WLEGY------------SEENPGtELNPENLAYVIYTSG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 267 STGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHsYLLYGPLACGATtLMFEGVPNWPTPARMCQVV 346
Cdd:PRK12316 666 STGKPKGAGNRHRA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGAR-LVVAAPGDHRDPAKLVELI 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 347 DKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKigKEKCPVVDTWWQTETggfmitpl 426
Cdd:PRK12316 743 NREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAK--LPQAGLYNLYGPTEA-------- 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 427 pgAIEL------KAGSAT----RPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERFEQTYFSTF 492
Cdd:PRK12316 809 --AIDVthwtcvEEGGDSvpigRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAG 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVgiphAIKGQAIYAYVTLnhgEEPS 572
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVL---ESEG 957
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
1PG3_A 573 PELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 958 GDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-617 |
1.00e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 138.94 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITaDEGVRAGRSIPlkknvddalknpnvtsvEHVIVLkrtgsDIDwqegRDLWWRDliekaSPEHQP 250
Cdd:PRK12316 2092 LAYMLEDSGAALLLT-QRHLLERLPLP-----------------AGVARL-----PLD----RDAEWAD-----YPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 EAMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVTGHSYLLYgPLACGATTLM 329
Cdd:PRK12316 2140 AVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQWFH-PLLNGARVLI 2217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 330 FEGvPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEgdKAIEGtDRSSLRILGSVGEPINPEAWEWYWKKIGKEKcpV 409
Cdd:PRK12316 2218 RDD-ELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEH--AERDG-RPPAVRVYCFGGEAVPAASLRLAWEALRPVY--L 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 410 VDTWWQTETggfMITPL---------PGAIELKAGSAtrpfFGVQPALVDNEGH---PQEGAteGNLVITDSwpGQARTL 477
Cdd:PRK12316 2291 FNGYGPTEA---VVTPLlwkcrpqdpCGAAYVPIGRA----LGNRRAYILDADLnllAPGMA--GELYLGGE--GLARGY 2359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 478 FG----DHERFEQTYFS-TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPH 552
Cdd:PRK12316 2360 LNrpglTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDG 2439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 553 AiKGQAIYAYVTlnhGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12316 2440 A-SGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
70-617 |
4.49e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 134.36 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 70 YEDGTLnlaANCLDRHLQENGDRTAIIWEGDDTSqskhisYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAM 149
Cdd:PRK05605 29 YGDTTL---VDLYDNAVARFGDRPALDFFGATTT------YAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 150 LACARIGAV---HSVIFggfSPEAVAGCIIDSSSRLVITADegvragrsiplkKNVDDALKNPNVTSVEHVI-------- 218
Cdd:PRK05605 100 YAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIVWD------------KVAPTVERLRRTTPLETIVsvnmiaam 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 219 -VLKRTGSDI---DWQEGRD---------LWWRDLIEKASPEH----QPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGY 281
Cdd:PRK05605 165 pLLQRLALRLpipALRKARAaltgpapgtVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 282 LVYAATTfkyvfdyhpgdiywctadVGWVTG---------------HSY-----LLYGPLaCGATTLMFegvpnwPTPaR 341
Cdd:PRK05605 245 FANAAQG------------------KAWVPGlgdgpervlaalpmfHAYgltlcLTLAVS-IGGELVLL------PAP-D 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 342 MCQVVD---KHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEawewywkkigkekcpVVDTWwQTET 418
Cdd:PRK05605 299 IDLILDamkKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMALPVS---------------TVELW-EKLT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 GGFMI--------TPL----PGAIELKAGSATRPFFGVQPALVD--NEGHPQEGATEGNLVItdswpgQARTLF-GDHER 483
Cdd:PRK05605 361 GGLLVegygltetSPIivgnPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLV------RGPQVFkGYWNR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 484 FEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYV 563
Cdd:PRK05605 435 PEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAV 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
1PG3_A 564 TLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK05605 515 VLEPGAALDPE---GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-619 |
5.40e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 133.72 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 79 ANCLDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 159 HSVIFGGFSPEAVAGCIIDSSSRLVITADegvrAGRSIPLKKNVDDALKNpNVTSVEHVIVLKRTGSDI-DWQEGRdlwW 237
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPD-ALPPLRAIAVVDDAADATpAPAPGA---R 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 238 RDLIEKASPEHQPEAMNA---EDPLFILY-TSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIYWCTADVGWVTGH 313
Cdd:PRK06164 159 VQLFALPDPAPPAAAGERaadPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 314 SYLLyGPLACGATTLM---FEGvpnwptpARMCQVVDKHQVNILYTAPTAIRALMAEGDkaiEGTDRSSLRILGSVG-EP 389
Cdd:PRK06164 238 STLL-GALAGGAPLVCepvFDA-------ARTARALRRHRVTHTFGNDEMLRRILDTAG---ERADFPSARLFGFASfAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 390 INPEAWEWywkkigkekcpvvdtwwqTETGGFMITPLPGAIELKAgsatrpFFGVQPA-------------LVDNEGH-- 454
Cdd:PRK06164 307 ALGELAAL------------------ARARGVPLTGLYGSSEVQA------LVALQPAtdpvsvriegggrPASPEARvr 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 455 ---PQEGA-----TEGNLVItdSWPGQARTLFGDHERFEQTYFStfkNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGH 525
Cdd:PRK06164 363 ardPQDGAllpdgESGEIEI--RAPSLMRGYLDNPDATARALTD---DGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 526 RLGTAEIESALVAHPKIAEAAVVGIPHaiKGQAI-YAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPK 604
Cdd:PRK06164 438 LVNPAEIEHALEALPGVAAAQVVGATR--DGKTVpVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPV 512
|
570
....*....|....*...
1PG3_A 605 TRSG---KIMRRILRKIA 619
Cdd:PRK06164 513 TESAngaKIQKHRLREMA 530
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
100-615 |
1.20e-32 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 131.05 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 100 DDTSQskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSS 179
Cdd:cd17650 8 DATRQ---LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 180 SRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehQPEamnaeDPL 259
Cdd:cd17650 85 AKLLLT---------------------------------------------------------------QPE-----DLA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 260 FILYTSGSTGKPKGVLHTTGGYL-VYAATTFKYVFDYHPGDIYWctadvgwVTGHSY-LLYGPLAcgaTTLMFEG----V 333
Cdd:cd17650 97 YVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFdVFAGDFA---RSLLNGGtlviC 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 334 PN--WPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRIL--GSVGEPINPEAWEWywKKIGkEKCPV 409
Cdd:cd17650 167 PDevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLLivGSDGCKAQDFKTLA--ARFG-QGMRI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 410 VDTWWQTET---GGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFGD----HE 482
Cdd:cd17650 242 INSYGVTEAtidSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpeltAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 483 RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVgIPHAIKGQA-IYA 561
Cdd:cd17650 320 RFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
1PG3_A 562 YVTLNHgeepSPELyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17650 399 YVVAAA----TLNT-AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
85-616 |
2.75e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.16 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 85 HLQENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 165 GFSPEAVAGCIIDSSSRLVITaDEGVRAGRSIPLKKNVDDALKNPNVTsvehviVLKRTGSDIdwqegrdlwwrdlieka 244
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLV-DEEFDAIVALETPKIVIDAAAQADSR------RLAQGGLEI----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 245 spehQPEAMNAEDPLF-ILYTSGSTGKPKGVLHTTggylvyaattfkyvfdyhpGDIYWCTAD----VGWVTGHSYLLYG 319
Cdd:PRK06145 141 ----PPQAAVAPTDLVrLMYTSGTTDRPKGVMHSY-------------------GNLHWKSIDhviaLGLTASERLLVVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 320 PL----AC---GATTLMFEG---VPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRilgsvgep 389
Cdd:PRK06145 198 PLyhvgAFdlpGIAVLWVGGtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLA-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 390 inpeawewyWKKIGKEKCP---------------VVDTWWQTET-GGFMITPLPGAIElKAGSATRPFFGVQPALVDNEG 453
Cdd:PRK06145 268 ---------WCIGGGEKTPesrirdftrvftrarYIDAYGLTETcSGDTLMEAGREIE-KIGSTGRALAHVEIRIADGAG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 454 HPQEGATEGNLVITDswPGQARTLFGDHERFEQTYFSTFknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 533
Cdd:PRK06145 338 RWLPPNMKGEICMRG--PKVTKGYWKDPEKTAEAFYGDW---FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 534 SALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK06145 413 RVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKR 489
|
...
1PG3_A 614 ILR 616
Cdd:PRK06145 490 VLR 492
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
102-616 |
4.17e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.59 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 102 TSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSR 181
Cdd:PRK12406 6 ISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 182 -LVITAD--EGVRAgrSIPLKKNVDDALKNPNVTSVEHVIVLKRT--GSDIDWQEgrdlwWrdlIEKASPEHQPEAmnaE 256
Cdd:PRK12406 86 vLIAHADllHGLAS--ALPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG-----W---LAQQEPYDGPPV---P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHT--TGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEg 332
Cdd:PRK12406 153 QPQSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQprFD- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 333 vpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA----WEWyWKkigkekcP 408
Cdd:PRK12406 232 ------PEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEW-WG-------P 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 409 VV-DTWWQTETGGFMITPLPGAIElKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpgqARTLFGDHERFEQT 487
Cdd:PRK12406 298 VIyEYYGSTESGAVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA----GNPDFTYHNKPEKR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 488 YFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNH 567
Cdd:PRK12406 373 AEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
1PG3_A 568 GEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK12406 453 GATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-617 |
4.64e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.75 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 83 DRHLQENGDRTAIIWEGDdtsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:PRK12467 519 EAQARQHPERPALVFGEQ------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 FGGFSPEAVAGCIIDSSSRLVITADEGVRagrsiplKKNVDDALKnpnvtsvehVIVLKRTGsdiDWQEGRdlwwrdlie 242
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLA-------QLPVPAGLR---------SLCLDEPA---DLLCGY--------- 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 kasPEHQPEAMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvfdyhpgdiYWCTADVGWVTGHSY------ 315
Cdd:PRK12467 645 ---SGHNPEVALDPDNLaYVIYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgv 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 316 -LLYGPLACGATTLMFEGVPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIegtDRSSLRILgsVGEPINPEA 394
Cdd:PRK12467 713 tELFGALASGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL---PRPQRALV--CGGEALQVD 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 395 WEWYWKKIGKEkCPVVDTWWQTETG-GFMITPLPGAIELKAGSAT-RPFFGVQPALVDNEGHPQEGATEGNLVITDSwpG 472
Cdd:PRK12467 787 LLARVRALGPG-ARLINHYGPTETTvGVSTYELSDEERDFGNVPIgQPLANLGLYILDHYLNPVPVGVVGELYIGGA--G 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 473 QARTLFG----DHERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:PRK12467 864 LARGYHRrpalTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 548 VGIPHAIKGQAIyAYVTLNHGEEPS--PELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK12467 944 LAQPGDAGLQLV-AYLVPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
108-617 |
6.02e-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: 128.62 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAvhsvifggfspEAVagciidsssrlvitad 187
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA-----------EAV---------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrsiplkknvddaLKNPNVTSVEHVIVLKRTGSDIDwqegrdlwwrdliEKASpehqpeamnaedplfILYTSGS 267
Cdd:cd05912 55 ------------------LLNTRLTPNELAFQLKDSDVKLD-------------DIAT---------------IMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvpnwptPARMCQV 345
Cdd:cd05912 89 TGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVdkFD-------AEQVLHL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 346 VDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLR--ILGsvGEPINPEAWEwywkkIGKEK-CPVVDTWWQTETGGFM 422
Cdd:cd05912 161 INSGKVTIISVVPTMLQRLLEILG----EGYPNNLRciLLG--GGPAPKPLLE-----QCKEKgIPVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 423 ITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEgatEGNLV-----ITDSWPGQARTlfgDHERFEQTYFSTfknmyf 497
Cdd:cd05912 230 VTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYE---VGEILlkgpnVTKGYLNRPDA---TEESFENGWFKT------ 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 498 sGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNhgeepSPELYA 577
Cdd:cd05912 298 -GDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE-----RPISEE 371
|
490 500 510 520
....*....|....*....|....*....|....*....|
1PG3_A 578 EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05912 372 ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-549 |
6.53e-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: 129.25 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFILYTSGS 267
Cdd:cd05907 86 -------------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYhPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPT------PAR 341
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDdlsevrPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 342 MCQV---VDKHQVNILYTAPTAIRALMAegDKAIEGtdrsSLRILGSVGEPINPEAWEWYwKKIGkekCPVVDTWWQTET 418
Cdd:cd05907 178 FLAVprvWEKVYAAIKVKAVPGLKRKLF--DLAVGG----RLRFAASGGAPLPAELLHFF-RALG---IPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 GGFMITPLPGAIelKAGSATRPFFGVQPALVDNeghpQEGATEGNLVITdswpgqartlfGDHERFEQTYFSTFKNMYF- 497
Cdd:cd05907 248 SAVVTLNPPGDN--RIGTVGKPLPGVEVRIADD----GEILVRGPNVML-----------GYYKNPEATAEALDADGWLh 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 498 SGDGARRDEDGYYWITGRVDDVL-NVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd05907 311 TGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
87-623 |
1.50e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 129.78 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 87 QENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggf 166
Cdd:PRK06178 44 RERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 167 SPEAVAGCII----DSSSRLVITADegvragRSIPLKKNVDDAlknpnvTSVEHVIVlkrTG-SD-------------ID 228
Cdd:PRK06178 114 SPLFREHELSyelnDAGAEVLLALD------QLAPVVEQVRAE------TSLRHVIV---TSlADvlpaeptlplpdsLR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 229 WQEGRDLWWRDLIE--KASPEHQPEAMNAEDPLFIL-YTSGSTGKPKGVLHTTGgYLVYAATTFKYVfdYHPGDiywcTA 305
Cdd:PRK06178 179 APRLAAAGAIDLLPalRACTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQR-DMVYTAAAAYAV--AVVGG----ED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 306 DVG-------WVTGHSYLLYGPLACGATTLMfegVPNWPTPARMcQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRS 378
Cdd:PRK06178 252 SVFlsflpefWIAGENFGLLFPLFSGATLVL---LARWDAVAFM-AAVERYRVTRTVMLVDNAVELMDHPRFA--EYDLS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 379 SLRILGSVG--EPINPEawewYWKKigkekcpvvdtwWQTETGGFMITPLPGAIE------LKAGSAT-------RPFF- 442
Cdd:PRK06178 326 SLRQVRVVSfvKKLNPD----YRQR------------WRALTGSVLAEAAWGMTEthtcdtFTAGFQDddfdllsQPVFv 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 443 -----GVQPALVDNE-GHPQEGATEGNLVItdswpgqaRT---LFGDHERFEQTYFSTFKNMYFSGDGARRDEDGYYWIT 513
Cdd:PRK06178 390 glpvpGTEFKICDFEtGELLPLGAEGEIVV--------RTpslLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 514 GRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATP 593
Cdd:PRK06178 462 GRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAVYKVP 538
|
570 580 590
....*....|....*....|....*....|
1PG3_A 594 DVlHWTDSLPKTRSGKIMRRILRKIAAGDT 623
Cdd:PRK06178 539 EI-RIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-615 |
1.72e-31 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 128.21 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIweGDDTsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsv 161
Cdd:cd05920 21 LARSAARHPDRIAVV--DGDR----RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 ifggfspeavagciidsssrlVITADEGVRAgRSIplkknvdDALknpnvtsVEHV----IVLKRTGSDIDWQEgrdlWW 237
Cdd:cd05920 92 ---------------------PVLALPSHRR-SEL-------SAF-------CAHAeavaYIVPDRHAGFDHRA----LA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 238 RDLIEKaspehQPeamnaeDPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPGDIYWCTADVGwvtgHSYLL 317
Cdd:cd05920 132 RELAES-----IP------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 318 YGP-----LACGATTLMfegVPNwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINP 392
Cdd:cd05920 196 ACPgvlgtLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 393 EAWEwywkKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPffgVQP----ALVDNEGHPQEGATEGNLVITD 468
Cdd:cd05920 270 ALAR----RVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRP---MSPddeiRVVDEEGNPVPPGEEGELLTRG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 469 swPGQARTLFGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd05920 343 --PYTIRGYYRAPEHNARAF--TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 549 GIPHAIKGQAIYAYVTLNhgeEPSPELyAEVRNWVRkEIGpLAT---PDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd05920 419 AMPDELLGERSCAFVVLR---DPPPSA-AQLRRFLR-ERG-LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
91-615 |
3.90e-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: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwEGDDTsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd12114 2 DATAVI-CGDGT-----LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEgvragrsiPLKKNVDDAlknpnvtsvehvivlkrtgsdidwqegRDLWWRDLIEKASPEHQP 250
Cdd:cd12114 76 REAILADAGARLVLTDGP--------DAQLDVAVF---------------------------DVLILDLDALAAPAPPPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 EAMNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTFKYVFDyhPGDIYWCTADVGW---VtghsYLLYGPLACGAT 326
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSSLSFdlsV----YDIFGALSAGAT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 tLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLR-ILGSvGEPIN---PEAWEWYWKKi 402
Cdd:cd12114 195 -LVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL--EAAQALLPSLRlVLLS-GDWIPldlPARLRALAPD- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 403 gkekCPVVDTWWQTETG----GFMITPLPGaiELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARTLF 478
Cdd:cd12114 270 ----ARLISLGGATEASiwsiYHPIDEVPP--DWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWI--GGRGVALGYL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 479 GDHERFEQTYFS--TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAiKG 556
Cdd:cd12114 342 GDPELTAARFVThpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GG 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 557 QAIYAYVTLnhGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd12114 421 KRLAAFVVP--DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
91-621 |
7.82e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 127.83 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWegddtsQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PLN03102 29 NRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEGVRAGRSIPLKKNVDDALKNPNVTSVEHVIVLKRTGSdidwqegRDLWWRDLIEKASPEHQP 250
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSS-------EELDYECLIQRGEPTPSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 EA-----MNAEDPLFILYTSGSTGKPKGVLHT-TGGYLVYAATTFKYVFDYHPgdIYWCTADV----GWVtghsyLLYGP 320
Cdd:PLN03102 176 VArmfriQDEHDPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMfhcnGWT-----FTWGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 321 LACGATTLMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIRALMaEGDKAIEGTDRSSLRILGSVGEPinPEAwewYWK 400
Cdd:PLN03102 249 AARGGTSVCMRHV----TAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAA---LVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 401 KIGKEKCPVVDTWWQTETGGFMI----------TPLPGAIELKAGSATRpFFGVQPALVDN----EGHPQEGATEGNLVI 466
Cdd:PLN03102 319 KVQRLGFQVMHAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGVS-ILGLADVDVKNketqESVPRDGKTMGEIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 467 TDSwpgqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:PLN03102 398 KGS------SIMKGYLKNPKATSEAFKHGWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPE----LYAEVRN---WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PLN03102 472 AVVAMPHPTWGETPCAFVVLEKGETTKEDrvdkLVTRERDlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
...
1PG3_A 619 AAG 621
Cdd:PLN03102 552 AKG 554
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-615 |
9.52e-31 |
|
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: 125.44 E-value: 9.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGDdtsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17652 2 DAPAVVFGDE------TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqp 250
Cdd:cd17652 76 IAYMLADARPALLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 eamNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTFkyvFDYHPGDIYWCTADVGWVTGHSYLLyGPLACGATTL 328
Cdd:cd17652 91 ---TPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAA---FDVGPGSRVLQFASPSFDASVWELL-MALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 329 MFEGVPNWPTPArMCQVVDKHQVNILYTAPTAIRALMAEGDKAiegtdrssLRILGSVGEPINPEawewywkkigkekcp 408
Cdd:cd17652 164 LAPAEELLPGEP-LADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPAE--------------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 409 VVDTWWQ----------TET--GGFMITPLPGAIELKAGsatRPFFGVQPALVDNEGHPQEGATEGNLVItdSWPGQARt 476
Cdd:cd17652 220 LVDRWAPgrrminaygpTETtvCATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYI--AGAGLAR- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 477 lfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVV 548
Cdd:cd17652 294 --GYLnrpgltaERFVADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PG3_A 549 GIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17652 372 VRDDRPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
531-609 |
2.27e-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: 113.79 E-value: 2.27e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 531 EIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-620 |
3.51e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 127.97 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITadegvragrsiplKKNVDDALknPNVTSVeHVIVLKRtgsdidwqegrDLWWrdli 241
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT-------------QAHLLEQL--PAPAGD-TALTLDR-----------LDLN---- 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekASPEHQPEA-MNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLVYAATT----FKYVFDyhpgdiywcta 305
Cdd:PRK12467 3224 --GYSENNPSTrVMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFD----------- 3290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 306 dvgwvtGHSYLLYGPLACGATtLMFEGVPNWpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDkaieGTDRSSLRILGS 385
Cdd:PRK12467 3291 ------GAQERFLWTLICGGC-LVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVF 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 386 VGEPINPEAWEWYWKKI---------GKEKCPVVDTWWQTETGGfmitpLPGAIELKAGsatRPFFGVQPALVDNEGHPQ 456
Cdd:PRK12467 3359 GGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA-----VCEAPYAPIG---RPVAGRSIYVLDGQLNPV 3430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 EGATEGNLVITDSwpGQARtlfGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLG 528
Cdd:PRK12467 3431 PVGVAGELYIGGV--GLAR---GYHqrpsltaERFVADPFSGSgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 529 TAEIESALVAHPKIAEAAVVGIPHAiKGQAIYAYVTLNhgeEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
570
....*....|..
1PG3_A 609 KIMRRILRKIAA 620
Cdd:PRK12467 3582 KVDRKALPDPDA 3593
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-622 |
4.31e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.77 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 106 KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVIT 185
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 186 ADEgvragrsiplkknvddaLKNPNVTSVEhVIVLKRTGsdidwqegrdlwwrdliEKASPEHQPEAMNAEDPLFILYTS 265
Cdd:PRK12316 3161 QSH-----------------LRLPLAQGVQ-VLDLDRGD-----------------ENYAEANPAIRTMPENLAYVIYTS 3205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 266 GSTGKPKGVLHTTGGYLVYAATTfkyvfdyhpGDIYWCTAD--VGWVTGHSY-----LLYGPLACGATTLMfEGVPNWPT 338
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWM---------QQAYGLGVGdrVLQFTTFSFdvfveELFWPLMSGARVVL-AGPEDWRD 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 339 PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWEWYWKKIgkekcPVVDTWWQTET 418
Cdd:PRK12316 3276 PALLVELINSEGVDVLHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADLQQQVFAGL-----PLYNLYGPTEA 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 419 ggfMITPLPGAIELKAGSAT---RPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERFEQTYFST 491
Cdd:PRK12316 3347 ---TITVTHWQCVEEGKDAVpigRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNrpglTAERFVPDPFVP 3421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 492 FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVgiphAIKGQAIYAYVTLnhgEEP 571
Cdd:PRK12316 3422 GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVP---EDE 3494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1PG3_A 572 SPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAAGD 622
Cdd:PRK12316 3495 AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
85-616 |
1.71e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 122.81 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 85 HLQENGDRTAIIWegddTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFG 164
Cdd:PRK13390 6 HAQIAPDRPAVIV----AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 165 GFSPEAVAGCIIDSSSRLVIT--ADEGV--RAGRSIPLKKNVddalknpnvtsvehvivlkrtGSDIDWQEGrdlwWRDL 240
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVAsaALDGLaaKVGADLPLRLSF---------------------GGEIDGFGS----FEAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 241 IEKASPEHQPEAMNAedplFILYTSGSTGKPKGV--------LHTTGGYLVYAATTFkyvFDYHPGDIYWCTADVGwvtg 312
Cdd:PRK13390 137 LAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSyllyGPL-------ACGATTLM---FEGvpnwptpARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRI 382
Cdd:PRK13390 206 HA----APLrwcsmvhALGGTVVLakrFDA-------QATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEP------------INPEAWEWYWkkigkekcpvvdtwwQTETGGFMITPLPGAIElKAGSATRPFFGVQpALVD 450
Cdd:PRK13390 275 VIHAAAPcpvdvkhamidwLGPIVYEYYS---------------STEAHGMTFIDSPDWLA-HPGSVGRSVLGDL-HICD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 451 NEGHPQEGATEGNLVIT-DSWPgqartlFGDHERFEQTYFSTFKNMYF---SGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK13390 338 DDGNELPAGRIGTVYFErDRLP------FRYLNDPEKTAAAQHPAHPFwttVGDLGSVDEDGYLYLADRKSFMIISGGVN 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 527 LGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK13390 412 IYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTP 491
|
570
....*....|
1PG3_A 607 SGKIMRRILR 616
Cdd:PRK13390 492 TGKLVKGLLR 501
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-619 |
2.07e-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: 118.97 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYV-FDyhPGDIYWCTADVGWVTGHSYLLYGpLACGATTLMFEgvPN 335
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLgFG--GGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 336 WPTparmcqVVDKHQVNILYTA--PTAIRALMAEGdkaIEGTDRSSLRILGSVGEPINPEAWEwywkKIGKEKCPVVDTW 413
Cdd:cd17630 76 QAL------AEDLAPPGVTHVSlvPTQLQRLLDSG---QGPAALKSLRAVLLGGAPIPPELLE----RAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 414 WQTETGGfMITPLPgAIELKAGSATRPFFGVQPALVDNEghpqEGATEGNLVITDSWPGQARTLFgdherFEQTYFSTfk 493
Cdd:cd17630 143 GMTETAS-QVATKR-PDGFGRGGVGVLLPGRELRIVEDG----EIWVGGASLAMGYLRGQLVPEF-----NEDGWFTT-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 494 nmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPsp 573
Cdd:cd17630 210 -----KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP-- 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
1PG3_A 574 elyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd17630 283 ---AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
257-612 |
2.66e-29 |
|
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: 118.91 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM--FEgvp 334
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 335 nwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLRILGSVGEPINPEAWEwywkkigkEKCPVvdTWW 414
Cdd:cd17637 77 ----PAEALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLRHVLGLDAPETIQRFE--------ETTGA--TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 415 ----QTETGGFMITplpGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFS 490
Cdd:cd17637 141 slygQTETSGLVTL---SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV------RGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 491 TFKN-MYFSGDGARRDEDGYYWITGRV--DDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNH 567
Cdd:cd17637 212 TFRNgWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
1PG3_A 568 GEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17637 292 GATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-628 |
3.84e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 122.17 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK06155 27 LARQAERYPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEGVRAGRSIPlkknvddalknPNVTSVEHVIVLkrtgsDIDWQEGRDLWWRDLI 241
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLVVEAALLAALEAAD-----------PGDLPLPAVWLL-----DAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKASPEHQPEA-MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIYWCTADVGWVTGHSyLLYGP 320
Cdd:PRK06155 165 LPPLDAPAPAAaVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-AFFQA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 321 LACGATTLM---FEGVPNWPTPARmcqvvdkHQ----------VNILYTAPTAiralmaEGDKAiegtdrSSLRILGSVG 387
Cdd:PRK06155 243 LLAGATYVLeprFSASGFWPAVRR-------HGatvtyllgamVSILLSQPAR------ESDRA------HRVRVALGPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPinPEAWEWYWKKIGkekCPVVDTWWQTETGGFMITPLPgaiELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:PRK06155 304 VP--AALHAAFRERFG---VDLLDGYGSTETNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSWPGQ-ARTLFGDHERFEQTYfstfKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:PRK06155 376 ADEPFAfATGYFGMPEKTVEAW----RNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPE---LYAEVRnwvrkeIGPLATPDVLHWTDSLPKTRSGKIMRRILRkiAAGD 622
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDGTALEPValvRHCEPR------LAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQGV 523
|
....*.
1PG3_A 623 TSNLGD 628
Cdd:PRK06155 524 TADTWD 529
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-620 |
4.64e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 121.84 E-value: 4.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADegvrAGRS----------IP-LKKNVDDALKNPNVTSVEHVIVL--KRTGSDID 228
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD----GFKDsdyvamlyelAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 229 WQEgrdlwWRDLIEKASPEHQPEAM---NAEDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhPGD- 299
Cdd:PRK08315 174 FDE-----LLALGRAVDDAELAARQatlDPDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------EEDr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 300 ------IYWCtadVGWVTGHsyllygpLAC---GATT-LMFEGVpnwpTPARMCQVVDKHQVNILYTAPTairalM--AE 367
Cdd:PRK08315 243 lcipvpLYHC---FGMVLGN-------LACvthGATMvYPGEGF----DPLATLAAVEEERCTALYGVPT-----MfiAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 368 -GDKAIEGTDRSSLR--IL-GSVgepinpeawewywkkigkekCP------VVD---------TWWQTETG-GFMITPLP 427
Cdd:PRK08315 304 lDHPDFARFDLSSLRtgIMaGSP--------------------CPievmkrVIDkmhmsevtiAYGMTETSpVSTQTRTD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 428 GAIELKAGSATRPFFGVQPALVDNE-------GHPQEGATEGNLVITDSWPGQART---LfgDHERFeqtyfstfknMYf 497
Cdd:PRK08315 364 DPLEKRVTTVGRALPHLEVKIVDPEtgetvprGEQGELCTRGYSVMKGYWNDPEKTaeaI--DADGW----------MH- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 498 SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElya 577
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE--- 507
|
570 580 590 600
....*....|....*....|....*....|....*....|...
1PG3_A 578 EVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
84-619 |
1.71e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 119.50 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHLQENGDRTAIIWEgddtsqSKHISYRELHRDVCRFANTLLDLGiKKGDVVAIYMpmvpEAAVAMLAcarigavhsvIF 163
Cdd:PRK07638 9 KHASLQPNKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILL----ENRIEFLQ----------LF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 164 GGfspEAVAGCI---IDSSSrlviTADEgvragrsipLKKNVddALKNPNVtsvehVIVLKRTGSDIDWQEGRdLW---- 236
Cdd:PRK07638 68 AG---AAMAGWTcvpLDIKW----KQDE---------LKERL--AISNADM-----IVTERYKLNDLPDEEGR-VIeide 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVY---AATTFKYVFDYH---PGDIYwctadvgwv 310
Cdd:PRK07638 124 WKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSfdcNVHDFHMKREDSvliAGTLV--------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 311 tgHSYLLYGP---LACGAT-TLMFEGVPNwptparmcQVVDK---HQVNILYTAPTAIRALMAEgdkaiEGTDRSSLRIL 383
Cdd:PRK07638 195 --HSLFLYGAistLYVGQTvHLMRKFIPN--------QVLDKletENISVMYTVPTMLESLYKE-----NRVIENKMKII 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 384 GSVGEpinpeawewyWKKIGKEKcpVVDTW--------WQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNEGhp 455
Cdd:PRK07638 260 SSGAK----------WEAEAKEK--IKNIFpyaklyefYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAG-- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 456 qegategnlviTDSWPGQARTLFGDHERFeqtyFSTFKNMYFS------------GDGARRDEDGYYWITGRVDDVLNVS 523
Cdd:PRK07638 326 -----------EEVQKGEIGTVYVKSPQF----FMGYIIGGVLarelnadgwmtvRDVGYEDEEGFIYIVGREKNMILFG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 524 GHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVtlnHGEEPSPELyaevRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK07638 391 GINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQL----KSFCLQRLSSFKIPKEWHFVDEIP 463
|
570
....*....|....*.
1PG3_A 604 KTRSGKIMRRILRKIA 619
Cdd:PRK07638 464 YTNSGKIARMEAKSWI 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
237-616 |
3.31e-28 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 118.63 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAMNAED--PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHP--GDIYWCTADVGWVTG 312
Cdd:cd05929 104 DGLEDYEAAEGGSPETPIEDEaaGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSYLLYGPLACGATTLM--FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPI 390
Cdd:cd05929 184 FRWSMTALFMGGTLVLMekFD-------PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPC 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 391 NP---EAWEWYWKkigkekcPVVDTWWQ-TETGGFmiTPLPGAIELK-AGSATRPFFGVQpALVDNEGHPQEGATEGNLV 465
Cdd:cd05929 257 PPwvkEQWIDWGG-------PIIWEYYGgTEGQGL--TIINGEEWLThPGSVGRAVLGKV-HILDEDGNEVPPGEIGEVY 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 466 ITDSWPgqartlFGDHERFEQTYFSTFKNMYFS-GDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:cd05929 327 FANGPG------FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLD 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PG3_A 545 AAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05929 401 AAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
91-618 |
7.58e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 117.65 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwegddtSQSKHISYRELHRDVCRFANTLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITADEGVRAGRSIPlkknvddalknpNVTSVEHVIvlkrtgsdidwqegrdlWWRDLIEkaSPEHQ 249
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSMQ------------KVSYVQRVI-----------------SITSLKE--IEDRK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 250 P---EAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGAT 326
Cdd:PRK06839 140 IdnfVEKNESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 TLmfegVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPInPEAWEWYWKKIGkek 406
Cdd:PRK06839 219 II----VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVRWFYNGGAPC-PEELMREFIDRG--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 407 CPVVDTWWQTETGG--FMItpLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVItdswpgQARTLFGDHERF 484
Cdd:PRK06839 289 FLFGQGFGMTETSPtvFML--SEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI------RGPNVMKEYWNR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 485 EQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYV 563
Cdd:PRK06839 361 PDATEETIQDGWLcTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 564 TLNHGeepSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKI 618
Cdd:PRK06839 441 VKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-615 |
1.12e-27 |
|
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: 116.80 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEgddtsqSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVitadegvragrsiplkknvddalknpnVTSVEHVIVLKRTGSD--IDWqegrdlwwrDLIEKASPEH 248
Cdd:cd17656 77 RIYIMLDSGVRVV---------------------------LTQRHLKSKLSFNKSTilLED---------PSISQEDTSN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVyaATTFKYVFDYHPGDIYW---CTADVGWVTGHSYLLYGP--- 320
Cdd:cd17656 121 IDYINNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSGGtly 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 321 LACGATTLMFEgvpnwptpaRMCQVVDKHQVNILYTaPTAIRALMAEGDKAIEGTDRSSLRILgSVGEP--INPEAWEWY 398
Cdd:cd17656 199 IIREETKRDVE---------QLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFPTCVKHII-TAGEQlvITNEFKEML 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 WKK-------IGKEKCPVVDTwwqtetggFMITPLPGAIELKagSATRPFFGVQPALVDNEGHPQEGATEGNLVItdSWP 471
Cdd:cd17656 268 HEHnvhlhnhYGPSETHVVTT--------YTINPEAEIPELP--PIGKPISNTWIYILDQEQQLQPQGIVGELYI--SGA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQARTLFGD----HERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd17656 336 SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 548 VGIPHAIKGQAIYAYVTlnhgeePSPEL-YAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17656 416 LDKADDKGEKYLCAYFV------MEQELnISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
105-615 |
1.16e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.88 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 105 SKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVI 184
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 185 T---------ADEGVRAgrsiplkknvddalknpnvtsvehvIVLKRTGsdiDWQEGRdlwwrdliekasPEHQPEAMNA 255
Cdd:PRK12467 1677 TqshlqarlpLPDGLRS-------------------------LVLDQED---DWLEGY------------SDSNPAVNLA 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPL-FILYTSGSTGKPKGVLHTTGGYL-VYAATTFKYVFdyhpgdiywCTADVgWVTGHSYL-------LYGPLACGAT 326
Cdd:PRK12467 1717 PQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCATQEAYQL---------SAADV-VLQFTSFAfdvsvweLFWPLINGAR 1786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 TLMfegVPNWP--TPARMCQVVDKHQVNILYTAPTAIRALMaEGDKAIEGTdrSSLRILGSVGEPINPEAWEWYWKKIGK 404
Cdd:PRK12467 1787 LVI---APPGAhrDPEQLIQLIERQQVTTLHFVPSMLQQLL-QMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPD 1860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 405 EKcpVVDTWWQTETggfMITPLPGAIELK--AGSATRPfFGVQPA-----LVDNEGHPQEGATEGNLVITDSwpGQARtl 477
Cdd:PRK12467 1861 TG--LFNLYGPTET---AVDVTHWTCRRKdlEGRDSVP-IGQPIAnlstyILDASLNPVPIGVAGELYLGGV--GLAR-- 1930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 478 fGDH-------ERFEQTYFSTF-KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:PRK12467 1931 -GYLnrpaltaERFVADPFGTVgSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA 2009
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 550 IPHAiKGQAIYAYVT-----LNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK12467 2010 QDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
87-616 |
1.38e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 117.17 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 87 QENGDRTAIIwegDDTSQskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAvHSVIFG-G 165
Cdd:PRK13382 54 QRCPDRPGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 166 FSPEAVAGCIIDSSSRLVITADEgvragrSIPLkknVDDALKN-PNVTSVEhvivlkrtgsdiDWQEGRDLWWRDLIEKA 244
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDEE------FSAT---VDRALADcPQATRIV------------AWTDEDHDLTVEVLIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 245 SPEHQPEAMNAEDPLfILYTSGSTGKPKGVLHT-TGGYLvyaatTFKYVFDYHPgdiywctadvgWVTGHSYLLYGPL-- 321
Cdd:PRK13382 186 HAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP-----------WRAEEPTVIVAPMfh 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATTLMFEGVPNWP-------TPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEA 394
Cdd:PRK13382 249 AWGFSQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 395 WEWYWKKIGkekcPVV-DTWWQTETGgfMI-TPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpg 472
Cdd:PRK13382 329 VIAFMDQFG----DVIyNNYNATEAG--MIaTATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND--- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 473 qarTLF-----GDHERFEQTYFStfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:PRK13382 400 ---TQFdgytsGSTKDFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAV 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK13382 470 IGVDDEQYGQRLAAFVVLKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
91-617 |
1.72e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.09 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGDDTSQSKHIsyrelhRDVCRFANTLLDLGIKKGDV-VAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHI------RGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITADEgvragrSIPLkknVDDALKNpnvtsVEHVivlkrtgsDIDWQEgrdlwWRDLIEK-ASPEH 248
Cdd:PRK07867 92 ALARDIAHADCQLVLTESA------HAEL---LDGLDPG-----VRVI--------NVDSPA-----WADELAAhRDAEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTAD--------VGWVTGhsyllygp 320
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 321 LACGATTLM---FEGVPNWPTPARM----CQVVDKHQVNILYTAPtairalmaegdkaiEGTDRS-SLRIL-GSVGEPIN 391
Cdd:PRK07867 216 LAAGASIALrrkFSASGFLPDVRRYgatyANYVGKPLSYVLATPE--------------RPDDADnPLRIVyGNEGAPGD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 PEAWEwywKKIGkekCPVVDTWWQTEtGGFMITPLPGAielKAGSATRPFFGVQ-----------PALVDNEGHPQEGAT 460
Cdd:PRK07867 282 IARFA---RRFG---CVVVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgtecpPAEDADGRLLNADEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 EGNLVITDSwPGQARTLFGDHERFEQtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 540
Cdd:PRK07867 352 IGELVNTAG-PGGFEGYYNDPEADAE---RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PG3_A 541 KIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07867 428 DATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-621 |
2.92e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 116.23 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 75 LNLAANCLDRhLQENGDRTAIIwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI----DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 155 IGAVHSVIFGGFSPEAVAGCIIDSSSRLVITadegvragrsipLKKNVDdalKNPNVTSVEHVIVLKrtgsdIDWQEGRD 234
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIIT------------QSCYVD---KLKGLAEDDGVTVVT-----IDDPPEGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 235 LWWRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAttfKYV------FDYHPGDIYWCTADVG 308
Cdd:PLN02246 158 LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 wvtgHSYLLYGPLACG-----ATTLM--FEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALmAEGDkAIEGTDRSSLR 381
Cdd:PLN02246 235 ----HIYSLNSVLLCGlrvgaAILIMpkFE-------IGALLELIQRHKVTIAPFVPPIVLAI-AKSP-VVEKYDLSSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 382 ILGSVGEPInpeawewywkkiGKE-------KCPVV---DTWWQTETG-------GFMITPLPgaieLKAGSATRPFFGV 444
Cdd:PLN02246 302 MVLSGAAPL------------GKEledafraKLPNAvlgQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 445 QPALVDneghPQEGATEG-NLvitdswPGQ-------------------ARTLfgDHERFEQTyfstfknmyfsGDGARR 504
Cdd:PLN02246 366 ELKIVD----PETGASLPrNQ------PGEicirgpqimkgylndpeatANTI--DKDGWLHT-----------GDIGYI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 505 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVR 584
Cdd:PLN02246 423 DDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVA 499
|
570 580 590
....*....|....*....|....*....|....*...
1PG3_A 585 KEIGPLATPDVLHWTDSLPKTRSGKIMRRILR-KIAAG 621
Cdd:PLN02246 500 KQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRaKLAAG 537
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-616 |
3.42e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 113.14 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPLFILYTSGSTGKPKGVLHT-----TGGYLVYAATTFKyvfdyhPGDI-------YWCTADVGwvtghsyllyGPLAC 323
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERLGLT------EQDRlcipvplFHCFGSVL----------GVLAC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 324 ---GATTLMFEgvpnwPT--PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIegTDRSSLR--ILGsvGEPINPEAWE 396
Cdd:cd05917 66 lthGATMVFPS-----PSfdPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDK--FDLSSLRtgIMA--GAPCPPELMK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 WYWKKIGKEKCPVVdtWWQTET--GGFMITPlPGAIELKAGSATRPFFGVQPALVDNEGHPQ-------EGATEGNLVIT 467
Cdd:cd05917 137 RVIEVMNMKDVTIA--YGMTETspVSTQTRT-DDSIEKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpgELCIRGYSVMK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSWpgqartlfGDHERFEQTYfsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd05917 214 GYW--------NDPEKTAEAI--DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd05917 284 VGVPDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-613 |
5.15e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 115.75 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 79 ANCLDRHLQENGDRTAIIWegddTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 159 hsvifggFSPEAVAGCIIDSSSRLVitadegvRAGRSIPLKKNVDDALKNPNVTSVEHVIVlkRTGSDIDWQEGRDLWWR 238
Cdd:PRK05852 95 -------VVPLDPALPIAEQRVRSQ-------AAGARVVLIDADGPHDRAEPTTRWWPLTV--NVGGDSGPSGGTLSVHL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 239 DliEKASPEHQ---PEAMNAEDPLfILYTSGSTGKPKGVLHTTGGYlvyAATTFKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:PRK05852 159 D--AATEPTPAtstPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANI---ASSVRAIITGYRLSPRDATVAVMPLYHGHGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 316 L--LYGPLACGATTLMfegvpnwPTPARMCQVV---DKHQVN-ILYTA-PTAIRALMAEGDKAIEGTDRSSLRILGSVGE 388
Cdd:PRK05852 233 IaaLLATLASGGAVLL-------PARGRFSAHTfwdDIKAVGaTWYTAvPTIHQILLERAATEPSGRKPAALRFIRSCSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 389 PINPEAWEWYWKKIGkekCPVVDTWWQTET---------GGFMITPLPGAIELKAGSATrpffGVQPALVDNEGHPQEGA 459
Cdd:PRK05852 306 PLTAETAQALQTEFA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 460 TEGNLVItdSWPGQARTLFGDHE----RFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 535
Cdd:PRK05852 379 AVGEVWL--RGTTVVRGYLGDPTitaaNFTDGWLRT-------GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 536 LVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRR 613
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-617 |
5.81e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 114.70 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEgddtsqSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVItadegvragrsiplkknVDdalknpnvTSVEHVIVLKRTGSDIDWQEGRDlwwrdli 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-----------------VD--------REFEYEDLLAEGDPDFEWIPPAD------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekaspEHQPEAMNaedplfilYTSGSTGKPKGVLHT-TGGYLvyAATTFKYVFDYHPGDIYWCTADV----GWVtghsyL 316
Cdd:cd12118 132 -----EWDPIALN--------YTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATTLMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAwe 396
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVHVMTAGAPPPAA-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 wYWKKIGKEKCPVVDTWWQTETGGfmitplPGAI------------ELKAGSATR---PFFGVQPALV-DNEGH---PQE 457
Cdd:cd12118 263 -VLAKMEELGFDVTHVYGLTETYG------PATVcawkpewdelptEERARLKARqgvRYVGLEEVDVlDPETMkpvPRD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 458 GAT------EGNLVitdswpgqARTLFGDHERFEQTyfstFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:cd12118 336 GKTigeivfRGNIV--------MKGYLKNPEATAEA----FRGGWFhSGDLAVIHPDGYIEIKDRSKDIIISGGENISSV 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 531 EIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDsLPKTRSGKI 610
Cdd:cd12118 404 EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
....*..
1PG3_A 611 MRRILRK 617
Cdd:cd12118 480 QKFVLRD 486
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-580 |
3.33e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 113.43 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEGVRAGRSIPlkknvdDALKNPNVTSVEhvivlkrTGSDIDWQEGrdlwWRDLI 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEAR------ADLARPPRLWVA-------GGDTLDDPEG----YEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 EKAS--PEHQP---EAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAtTFKYVFDYHPGDIYWCT--------ADVG 308
Cdd:PRK08279 180 AAAAgaPTTNPasrSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCClplyhntgGTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 WVTGhsyllygpLACGATTLM---FEGVPNWPTparmcqvVDKHQVnilyTAPTAI----RALMAEGDKAiegTDRS-SL 380
Cdd:PRK08279 259 WSSV--------LAAGATLALrrkFSASRFWDD-------VRRYRA----TAFQYIgelcRYLLNQPPKP---TDRDhRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 381 RILgsVGEPINPEAWEWYWKKIGKEKcpVVDTWWQTE-TGGFMitplpgAIELKAGSATR-PFFGVQP-ALV-------- 449
Cdd:PRK08279 317 RLM--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASEgNVGFI------NVFNFDGTVGRvPLWLAHPyAIVkydvdtge 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 450 ---DNEGHPQEGATE--GNLV--ITDSWP--GQA----------RTLF--GDherfeqTYFSTfknmyfsGDGARRDEDG 508
Cdd:PRK08279 387 pvrDADGRCIKVKPGevGLLIgrITDRGPfdGYTdpeasekkilRDVFkkGD------AWFNT-------GDLMRDDGFG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 509 YYWITGRVDDVL-----NVSghrlgTAEIESALVAHPKIAEAAVVG--IPHAiKGQAIYAYVTLNHGEEPSP-ELYAEVR 580
Cdd:PRK08279 454 HAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGveVPGT-DGRAGMAAIVLADGAEFDLaALAAHLY 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
109-617 |
6.01e-26 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 112.54 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITaDE 188
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 GVragrsIPLKKNVDDALKnpnvtSVEHVIV-----------LKRTGSDIDWQEGRDlwwRDLIEKASPEHQPEAMnaed 257
Cdd:PRK06018 120 TF-----VPILEKIADKLP-----SVERYVVltdaahmpqttLKNAVAYEEWIAEAD---GDFAWKTFDENTAAGM---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 258 plfiLYTSGSTGKPKGVLHTTGGYLVYAATTFkyvfdyHPGDIYWCTADV-----------GWVTGHSyllyGPlACGAT 326
Cdd:PRK06018 183 ----CYTSGTTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADTmlpvvplfhanSWGIAFS----AP-SMGTK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 TLMfegvpnwPTP----ARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiegtDRSSLRILGSV--GEPINPEAWEWYWK 400
Cdd:PRK06018 248 LVM-------PGAkldgASVYELLDTEKVTFTAGVPTVWLMLLQYMEK-----EGLKLPHLKMVvcGGSAMPRSMIKAFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 401 KIGKEkcpVVDTWWQTETGGF-MITPLPGAIELKAGSAT--------RPFFGVQPALVDNEGH--PQEGATEGNLVItdS 469
Cdd:PRK06018 316 DMGVE---VRHAWGMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGVEMKITDDAGKelPWDGKTFGRLKV--R 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 470 WPGQARTLF--GDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:PRK06018 391 GPAVAAAYYrvDGEILDDDGFFDT-------GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-619 |
1.18e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 111.58 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 70 YEDGTLNLAANC--------LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 142 VPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGV--------RAGRSIPLKKNVDDAL--KNPNV 211
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAevarealaLLPGPKPLVIDVDDPEypGGRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 212 TSVEHVIVLKRTGSDIDWQEGRDLWwrDLIekaspehqpeAMNaedplfilYTSGSTGKPKGVL-HTTGGYLVYAATTFK 290
Cdd:PRK08162 158 GALDYEAFLASGDPDFAWTLPADEW--DAI----------ALN--------YTSGTTGNPKGVVyHHRGAYLNALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 291 YVFDYHPgdIY-W------CTadvGWvtghsyllygplaCGATTLMFEGVPN----WPTPARMCQVVDKHQVNILYTAPT 359
Cdd:PRK08162 218 WGMPKHP--VYlWtlpmfhCN---GW-------------CFPWTVAARAGTNvclrKVDPKLIFDLIREHGVTHYCGAPI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 360 AIRALMAEGDKAIEGTDRsslRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETGGfmitplPGAIELK-AGSAT 438
Cdd:PRK08162 280 VLSALINAPAEWRAGIDH---PVHAMVAGAAPPAAVIAKMEEIGFD---LTHVYGLTETYG------PATVCAWqPEWDA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 439 RPFfGVQPALVDNEG---HPQEGAT----------------------EGNLVITDSWPGQARTlfgdHERFEQTYFSTfk 493
Cdd:PRK08162 348 LPL-DERAQLKARQGvryPLQEGVTvldpdtmqpvpadgetigeimfRGNIVMKGYLKNPKAT----EEAFAGGWFHT-- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 494 nmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSP 573
Cdd:PRK08162 421 -----GDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
1PG3_A 574 ElyaEVRNWVRKEIGPLATPDVLHWTdSLPKTRSGKIMRRILRKIA 619
Cdd:PRK08162 496 E---EIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQA 537
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-621 |
1.48e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 111.25 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 76 NLAANCLDRHLQENGDRTAIIW--EGDDTSQskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQPEAIAlrRCDGTSA---LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 154 RIGAVHSVIFGGFSPEAVA--GCIIDSSSrlVITADEGVRAGRSIPlkknvddalknPNVTSVEHVIVLKRTGSDIDWQE 231
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIErfCQITDPAA--ALVAPGSKMASSAVP-----------EALHSIPVIAVDIAAVTRESEHS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 232 GrdlwwrdliEKASPEHQPEaMNAEDPLFILYTSGSTGKPKGVLhttggylvYAATTFKYVFD-YHPGDIYWctadVGWV 310
Cdd:PRK05857 155 L---------DAASLAGNAD-QGSEDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VTWV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 311 TGHSylLYGPLACG--------ATTLMFEG--VPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSL 380
Cdd:PRK05857 213 VGET--TYSPLPAThigglwwiLTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSA--NATVPSL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 381 RILGSVGEpinpEAWEWYWKKIGKEKCPVVDTWWQTETGGFMITpLP---GAI-ELKAGSATRPFFGVQPALVD-NEGHP 455
Cdd:PRK05857 289 RLVGYGGS----RAIAADVRFIEATGVRTAQVYGLSETGCTALC-LPtddGSIvKIEAGAVGRPYPGVDVYLAAtDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 456 Q-----EGATEGNLVITDswPGQARTLFGDHERFEQTYFSTFKNmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:PRK05857 364 TapgagPSASFGTLWIKS--PANMLGYWNNPERTAEVLIDGWVN---TGDLLERREDGFFYIKGRSSEMIICGGVNIAPD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 531 EIESALVAHPKIAEAAVVGIPH----AIKGQAIYAYVTLNhgEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK05857 439 EVDRIAEGVSGVREAACYEIPDeefgALVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQ 516
|
570
....*....|....*
1PG3_A 607 SGKIMRRILRKIAAG 621
Cdd:PRK05857 517 SGKVMRASLAAAATA 531
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-619 |
2.16e-25 |
|
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: 110.11 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFAnTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:cd05909 8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EGVRAGRSIPLKknvdDALKNPNVTSVEHVIvlkrtgSDIDWQEG---------RDLWWrdLIEKASPEHQPEamnaeDP 258
Cdd:cd05909 87 QFIEKLKLHHLF----DVEYDARIVYLEDLR------AKISKADKckaflagkfPPKWL--LRIFGVAPVQPD-----DP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 259 LFILYTSGSTGKPKGVLHTTGGYL--VYAATTfkyVFDYHPGDIywctadvgwVTG-----HSYLLYG----PLACGATT 327
Cdd:cd05909 150 AVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV---------VFGalpffHSFGLTGclwlPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 328 LMFegvPNwPTPAR-MCQVVDKHQVNILYTAPTAIRALMaegdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGK-- 404
Cdd:cd05909 218 VFH---PN-PLDYKkIPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIri 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 405 -------EKCPVVDtwwqtetggfMITPLPGAielKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwPGQARTL 477
Cdd:cd05909 290 legygttECSPVIS----------VNTPQSPN---KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 478 FGDHerfEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH-PKIAEAAVVGIPHAIKG 556
Cdd:cd05909 356 LNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 557 QAIYAYVTlnhGEEPSPElyaEVRNWVRK-EIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIA 619
Cdd:cd05909 433 EKIVLLTT---TTDTDPS---SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-617 |
2.29e-25 |
|
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: 110.21 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 115 RDVC-RFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVR-A 192
Cdd:cd05915 31 YQRArRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPlV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 193 GRSIPLKKNVDDalkNPNvtsvehvivlkrtgsdidwQEGRDLWWRDLIEKASPEHQP-EAMNAEDPLFILYTSGSTGKP 271
Cdd:cd05915 111 EAIRGELKTVQH---FVV-------------------MDEKAPEGYLAYEEALGEEADpVRVPERAACGMAYTTGTTGLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 272 KGVLHT-TGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLlYGPLACGATTLMFEGVPNwptPARMCQVVDKHQ 350
Cdd:cd05915 169 KGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLD---PASLVELFDGEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 351 VNILYTAPTAIRaLMAEGDKAIEGTDRSSLRILGSVGEPinPEAWeWYWKKIGKEK------CPVV-----DTWWQTEtg 419
Cdd:cd05915 245 VTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAA--PRSL-IARFERMGVEvrqgygLTETspvvvQNFVKSH-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 420 gFMITPLPGAIELKAGSATRPFFGVQPAL-VDNEGHPQEGAT------EGNLVITDswpgqartLFGDHERFEQTYFStf 492
Cdd:cd05915 319 -LESLSEEEKLTLKAKTGLPIPLVRLRVAdEEGRPVPKDGKAlgevqlKGPWITGG--------YYGNEEATRSALTP-- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 493 KNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPS 572
Cdd:cd05915 388 DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
1PG3_A 573 PELYaevrNWVRKEIGPLAT-PDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05915 468 EELN----EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
106-617 |
2.24e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 107.76 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 106 KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsviFGGFSPEAVAGCIID----SSSR 181
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEIKKqaeaAGAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 182 LVITADEGVRAGRSIPLKknvddalknpnvtsvehVIVLKRTGSDidwqegRDLWWRDLIE---KASPEHQPEAMNAEDP 258
Cdd:PLN02330 130 LIVTNDTNYGKVKGLGLP-----------------VIVLGEEKIE------GAVNWKELLEaadRAGDTSDNEEILQTDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 259 LFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIywctADVGWVTghSYLLYGPLACGATTLMFEG---VPN 335
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV----VTLGLIP--FFHIYGITGICCATLRNKGkvvVMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 336 WPTPARMCQVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRI--LGSVGEPINPEAWEWYWKKIgkEKCPVVDTW 413
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKF--PGVQVQEAY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 414 WQTETGgfMITPLPGAIELKAGSATRPFFG-VQPALVDNEGHPQEGATegnlvITDSWPGQ--ART---LFGDHERFEQT 487
Cdd:PLN02330 337 GLTEHS--CITLTHGDPEKGHGIAKKNSVGfILPNLEVKFIDPDTGRS-----LPKNTPGElcVRSqcvMQGYYNNKEET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 488 YFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLN 566
Cdd:PLN02330 410 DRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1PG3_A 567 HGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02330 490 PKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-617 |
3.78e-24 |
|
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: 106.94 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGiKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 164 GGFSPEAVAgciidsssRLV-ITADEGVRAgrsiplkknvddALknpnvTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIE 242
Cdd:cd05931 80 PPTPGRHAE--------RLAaILADAGPRV------------VL-----TTAAALAAVRAFAASRPAAGTPRLLVVDLLP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 KASPEH-QPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIY--W--CTADVGWVTGhsylL 317
Cdd:cd05931 135 DTSAADwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG----L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 318 YGPLACGATTLMFEgvpnwPT-----PARMCQVVDKHQVNILYtAPT-----AIRALMAEGdkaIEGTDRSSLRILGSVG 387
Cdd:cd05931 210 LTPLYSGGPSVLMS-----PAaflrrPLRWLRLISRYRATISA-APNfaydlCVRRVRDED---LEGLDLSSWRVALNGA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 388 EPINPEAWEWYWKK--------------------------IGKEKCPVVDTW--WQTETGGFMITPL-PGAIELKagSAT 438
Cdd:cd05931 281 EPVRPATLRRFAEAfapfgfrpeafrpsyglaeatlfvsgGPPGTGPVVLRVdrDALAGRAVAVAADdPAARELV--SCG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 439 RPFFGVQPALVDNEGH-PQEGATEGNLVITDS------W--PGQARTLFG--DHERfEQTYFSTfknmyfsGD-GARRde 506
Cdd:cd05931 359 RPLPDQEVRIVDPETGrELPDGEVGEIWVRGPsvasgyWgrPEATAETFGalAATD-EGGWLRT-------GDlGFLH-- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 507 DGYYWITGRVDDVLNVSGHRLGTAEIE-SALVAHPKIAE--AAVVGIPHAIKGQ-AIYAYVTLNHGEEPSPELYAEVRNW 582
Cdd:cd05931 429 DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDDGEERlVVVAEVERGADPADLAAIAAAIRAA 508
|
570 580 590
....*....|....*....|....*....|....*.
1PG3_A 583 VRKEIGpLATPDV-LHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05931 509 VAREHG-VAPADVvLVRPGSIPRTSSGKIQRRACRA 543
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-609 |
4.57e-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: 104.39 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPN 335
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 336 WPT----------PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAwewywKKIGKE 405
Cdd:cd05924 82 GGQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEV-----KQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 406 KCP---VVDTWWQTETGGFMI-TPLPGAIElkagsaTRPFFGVQP--ALVDNEGHPQEGATEGnlvitdswPGQ-ART-- 476
Cdd:cd05924 157 LVPnitLVDAFGSSETGFTGSgHSAGSGPE------TGPFTRANPdtVVLDDDGRVVPPGSGG--------VGWiARRgh 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 477 ----LFGDHERFEQTYFSTFKNMY-FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:cd05924 223 iplgYYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 552 HAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:cd05924 303 DERWGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
248-616 |
4.84e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 105.84 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 248 HQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYlvyAATtfkyvFDYHPGDIYWCTADV-----------GWVTGhsyl 316
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI---AAD-----LDALAEAWQWTADDVlvhglplfhvhGLVLG---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGAT--------------------TLMFeGVPN-WptpARMCQvvdkhqvnilytAPTAIRALmaegdkaiegt 375
Cdd:PRK07787 188 VLGPLRIGNRfvhtgrptpeayaqalseggTLYF-GVPTvW---SRIAA------------DPEAARAL----------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 376 drSSLRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETggFMITPLPGAIELKAGSATRPFFGVQPALVDNEGH- 454
Cdd:PRK07787 241 --RGARLLVSGSAALPVPVFDRLAALTGHR---PVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGGp 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 455 -PQEGATEGNLVItdswpgQARTLF-GDHERFEQT--------YFSTfknmyfsGDGARRDEDGYYWITGRVD-DVLNVS 523
Cdd:PRK07787 314 vPHDGETVGELQV------RGPTLFdGYLNRPDATaaaftadgWFRT-------GDVAVVDPDGMHRIVGREStDLIKSG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 524 GHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTlnHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLP 603
Cdd:PRK07787 381 GYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALP 455
|
410
....*....|...
1PG3_A 604 KTRSGKIMRRILR 616
Cdd:PRK07787 456 RNAMGKVLKKQLL 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
91-616 |
8.13e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 105.34 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGDDTSqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK07514 15 DRDAPFIETPDGL---RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEGVRAGRSIPLKKNvddalknpnvtsVEHVIVL--KRTGSDIdwqegrdlwwrDLIEKASPEH 248
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAG------------APHVETLdaDGTGSLL-----------EAAAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGD-------IYwctadvgwvtgHSYLLY--- 318
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDY-WRFTPDDvlihalpIF-----------HTHGLFvat 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 -GPLACG--------------------ATTLMfeGVPNwptparmcqvvdkhqvniLYTaptaiRALMAEG-DKaiEGTD 376
Cdd:PRK07514 217 nVALLAGasmiflpkfdpdavlalmprATVMM--GVPT------------------FYT-----RLLQEPRlTR--EAAA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 377 RSSLRILGSVgePINPE---AWEwywKKIGKekcPVVDTWWQTETGgfMITPLPGAIELKAGSATRPFFGVQPALVDNE- 452
Cdd:PRK07514 270 HMRLFISGSA--PLLAEthrEFQ---ERTGH---AILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPEt 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 453 GHPQEGATEGNL------VITDSW--PGQARTLFGdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK07514 340 GAELPPGEIGMIevkgpnVFKGYWrmPEKTAEEFR-----ADGFFIT-------GDLGKIDERGYVHIVGRGKDLIISGG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 525 HRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPK 604
Cdd:PRK07514 408 YNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAALKGRLARFKQPKRVFFVDELPR 484
|
570
....*....|..
1PG3_A 605 TRSGKIMRRILR 616
Cdd:PRK07514 485 NTMGKVQKNLLR 496
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
257-612 |
9.54e-24 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 102.48 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYaattfkyvFDYHPGDIYWCTADVGWVTG---HSYLLYGPL--------ACGA 325
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGAIsalylggtFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 326 TTLmfegvpnwpTPARMCQVVDKHQVNILYTAPTAIRALmaegdkAIEGTDRSSLRILGSVGEPINPEAWE---WYWKKI 402
Cdd:cd17633 73 RKF---------NPKSWIRKINQYNATVIYLVPTMLQAL------ARTLEPESKIKSIFSSGQKLFESTKKklkNIFPKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 403 GkekcpVVDTWWQTETGgfMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQ-----------EGATEGNLVITDSWp 471
Cdd:cd17633 138 N-----LIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIgkifvksemvfSGYVRGGFSNPDGW- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 gqartlfgdherfeqtyFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIP 551
Cdd:cd17633 210 -----------------MSV-------GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 552 HAIKGQ---AIYAYVTLNhgeepspelYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17633 266 DARFGEiavALYSGDKLT---------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-618 |
1.29e-23 |
|
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: 105.30 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIIwegdDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17642 31 PGTIAFT----DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITAdegvragrsiplKKNVDDALK-NPNVTSVEHVIVLKrtgSDIDWQEGRDLWwrDLIEKASP-- 246
Cdd:cd17642 107 ELDHSLNISKPTIVFCS------------KKGLQKVLNvQKKLKIIKTIIILD---SKEDYKGYQCLY--TFITQNLPpg 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 ----EHQPEAMNAEDPL-FILYTSGSTGKPKGVLHT--------------TGGYLVYAATTFKYVFDYHPGdiYWCTADV 307
Cdd:cd17642 170 fneyDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFHHG--FGMFTTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 GWVTghsyllygplaCGATTLM---FEgvpnwptPARMCQVVDKHQVNILYTAPTairaLMAEGDKA--IEGTDRSSLRI 382
Cdd:cd17642 248 GYLI-----------CGFRVVLmykFE-------EELFLRSLQDYKVQSALLVPT----LFAFFAKStlVDKYDLSNLHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEPINPEAWEWYWKKIgkeKCPVV-DTWWQTE-TGGFMITP----LPGAIelkagSATRPFFGVQpaLVDNEGHPQ 456
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRF---KLPGIrQGYGLTEtTSAILITPegddKPGAV-----GKVVPFFYAK--VVDLDTGKT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 EGATE-GNLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 534
Cdd:cd17642 376 LGPNErGELCVKG--PMIMKGYVNNPE---ATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELES 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 535 ALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLA-TPDVLHWTDSLPKTRSGKIMRR 613
Cdd:cd17642 451 ILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK---EVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRR 527
|
....*
1PG3_A 614 ILRKI 618
Cdd:cd17642 528 KIREI 532
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
82-620 |
7.30e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 102.76 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQenGDRTAIIwegddtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsV 161
Cdd:PRK10946 31 LTRHAA--SDAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPE-----AVAGCIidsSSRLVItadegvrAGRSIPLKKNVD--DALKNpNVTSVEHVIVLKRTGsdidwqeGRD 234
Cdd:PRK10946 101 VNALFSHQrselnAYASQI---EPALLI-------ADRQHALFSDDDflNTLVA-EHSSLRVVLLLNDDG-------EHS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 235 LwwRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADvgwvTGHS 314
Cdd:PRK10946 163 L--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYY-YSVRRSVEICGFTPQTRYLCALP----AAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 315 YLLYGPLA-----CGATTLMfegVPNwPTPARMCQVVDKHQVNILYTAPTA----IRALMAEGDKAiegtDRSSLRILgS 385
Cdd:PRK10946 236 YPMSSPGAlgvflAGGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAvslwLQAIAEGGSRA----QLASLKLL-Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 386 VGEPINPEAWEwywKKIGKE-KCPVVDTWWQTEtGGFMITPLPGAIELKAGSATRPffgVQPA----LVDNEGHPQEGAT 460
Cdd:PRK10946 307 VGGARLSETLA---RRIPAElGCQLQQVFGMAE-GLVNYTRLDDSDERIFTTQGRP---MSPDdevwVADADGNPLPQGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 EGNLVITDSW--------PGQARTLFgDHERFeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEI 532
Cdd:PRK10946 380 VGRLMTRGPYtfrgyyksPQHNASAF-DANGF-----------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 533 ESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPspelyAEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK10946 448 ENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA-----VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....*....
1PG3_A 612 RRILRKIAA 620
Cdd:PRK10946 523 KKQLRQWLA 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-615 |
1.00e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.09 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITadEGVRAGRsiplkknvddalknpnVTSVEHVIVLKRTGSDID-Wqegrdlwwrdl 240
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLT--QSHLLER----------------LPQAEGVSAIALDSLHLDsW----------- 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 241 iekasPEHQPE-AMNAEDPLFILYTSGSTGKPKGVLHTTGGY---LVYAATTfkYVFDyhPGDIYWCTADVGWVTGhSYL 316
Cdd:PRK05691 1262 -----PSQAPGlHLHGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQAT--YALD--DSDVLMQKAPISFDVS-VWE 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATtLMFEGVPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAiegtDRSSLRILGSVGEPINPEAWE 396
Cdd:PRK05691 1332 CFWPLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEALPAELRN 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 397 WYWKKI---------GKEKCPVVDTWWQTETGGFMITPLpgaielkagsaTRPFFGVQPALVDNEGHPQEGATEGNLVIT 467
Cdd:PRK05691 1407 RVLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIG 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSwpGQARTLFG----DHERF-EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK05691 1476 GA--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV 1553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 543 AEAAVVgIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 1554 AQAAVL-VREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-615 |
1.39e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 103.20 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDdtsqskHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK10252 464 VAQQAAKTPDAPALADARY------QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEgvRAGR--SIPlkknvDDALKNPNVtsvehvivlkrtgsdidwqegrdLWWRd 239
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD--QLPRfaDVP-----DLTSLCYNA-----------------------PLAP- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 240 liekasPEHQPEAMNA-EDPLFILYTSGSTGKPKGVL--HTTggyLV---------YAATTFKYVFDYHPgdiywCTADV 307
Cdd:PRK10252 587 ------QGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMvgQTA---IVnrllwmqnhYPLTADDVVLQKTP-----CSFDV 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 G-WVtghsylLYGPLACGATTLMFEgvpnwPT----PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRI 382
Cdd:PRK10252 653 SvWE------FFWPFIAGAKLVMAE-----PEahrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQ 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEPINPEAW-EWYwkkiGKEKCPV----------VD-TWWqtetggfmitPLPGAIELKAGSAT----RPFFGVQP 446
Cdd:PRK10252 722 VFCSGEALPADLCrEWQ----QLTGAPLhnlygpteaaVDvSWY----------PAFGEELAAVRGSSvpigYPVWNTGL 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 447 ALVDNEGHPQEGATEGNLVITdswpG-Q-ARTLFG----DHERFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVL 520
Cdd:PRK10252 788 RILDARMRPVPPGVAGDLYLT----GiQlAQGYLGrpdlTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 521 NVSGHRLGTAEIESALVAHPKIAEAAVV------GIPHAIKGQAIYAYVTLNHGEEPSPELyaeVRNWVRKEIGPLATPD 594
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSA---LQAQLRERLPPHMVPV 940
|
570 580
....*....|....*....|.
1PG3_A 595 VLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK10252 941 VLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-636 |
4.10e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 100.63 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIIWEGDDTSQskhISYRELHRDVCRFANTLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 169 EAVAGcIIDSSSRLVITADEgVRAGRSIPLKKNVDdalknpnvtSVEHVIVLkrTGSDIDWQEGRDLW------WRDLIE 242
Cdd:PRK05620 101 DQIVH-IINHAEDEVIVADP-RLAEQLGEILKECP---------CVRAVVFI--GPSDADSAAAHMPEgikvysYEALLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 KASPEHQPEAMNAEDPLFILYTSGSTGKPKGV-------------LHTTGGYLVYAATTFKY-VFDYHPgdIYWCTADVG 308
Cdd:PRK05620 168 GRSTVYDWPELDETTAAAICYSTGTTGAPKGVvyshrslylqslsLRTTDSLAVTHGESFLCcVPIYHV--LSWGVPLAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 WVTGhsyllygplacgaTTLMFEGVPnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGE 388
Cdd:PRK05620 246 FMSG-------------TPLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLK--NPPERMSLQEIYVGGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 389 PINP---EAWEwywKKIGKEkcpVVDTWWQTETG--GFMITPlPGAIELKAGSATRPFFGVQPA----LVDNEGHPQEGA 459
Cdd:PRK05620 309 AVPPiliKAWE---ERYGVD---VVHVWGMTETSpvGTVARP-PSGVSGEARWAYRVSQGRFPAsleyRIVNDGQVMEST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 460 --------TEGNLVI-------TDSWPGQARTLFGDHERFEQTYFsTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSG 524
Cdd:PRK05620 382 drnegeiqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRF-TADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 525 HRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPK 604
Cdd:PRK05620 461 EWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDK 540
|
570 580 590
....*....|....*....|....*....|...
1PG3_A 605 TRSGKIMRRILRK-IAAGDTsnlgDTSTLADPG 636
Cdd:PRK05620 541 TSVGKFDKKDLRQhLADGDF----EIIKLKGPG 569
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-616 |
5.18e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 100.10 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-ATTFKYvfDYHPGDIYWCTADVGwvtgHS- 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYVSMPLF----HSn 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 315 --YLLYGP-LACGATTLMfegvPNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRssLRIlgSVGEPIN 391
Cdd:PRK13388 205 avMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNP--LRV--AFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 392 PEAWEWYWKKIGkekCPVVDTWWQTETGGfMITPLPGAielKAGSATRPFFGVQ-----------PALVDNEGHPQEGAT 460
Cdd:PRK13388 277 PRDIAEFSRRFG---CQVEDGYGSSEGAV-IVVREPGT---PPGSIGRGAPGVAiynpetltecaVARFDAHGALLNADE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 E-GNLVITdswpgQARTLF--------GDHERFEQtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK13388 350 AiGELVNT-----AGAGFFegyynnpeATAERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAP 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 532 IESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNwVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK13388 418 IERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLA-AQPDLGTKAWPRYVRIAADLPSTATNKVL 496
|
....*
1PG3_A 612 RRILR 616
Cdd:PRK13388 497 KRELI 501
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
256-612 |
5.95e-22 |
|
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: 97.72 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDyhpgdiyWCTADVGWVTGHSYLLYGpLACGATTLMFEGV-- 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 334 --PNWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDrsSLRILGSVGE-PINPEAWEWYWKKIGKekcpVV 410
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADVRFIEATGLTN----TA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 411 DTWWQTETGGFMITPLpGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSWpgqarTLFGDHERFEQTYFS 490
Cdd:cd17635 147 QVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 491 TFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNhgEE 570
Cdd:cd17635 221 LIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
1PG3_A 571 PSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-620 |
8.23e-22 |
|
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: 99.15 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHLQENGDRTAI-IWEGDdtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAvhsvi 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 fggfspeavAGCIIDSS---SRLvitadegvragRSIplkknVDDalknpnvTSVEHVIVlkrtgsdidwqegrdlwwrd 239
Cdd:cd05918 75 ---------AFVPLDPShplQRL-----------QEI-----LQD-------TGAKVVLT-------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 240 liekaspeHQPeamnaEDPLFILYTSGSTGKPKGVL--H---TTG----GYLVYAATTFK------YVFDYHPGDIywct 304
Cdd:cd05918 103 --------SSP-----SDAAYVIFTSGSTGKPKGVVieHralSTSalahGRALGLTSESRvlqfasYTFDVSILEI---- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 305 advgwvtghsyllYGPLACGATTLmfegVP-NWPTPARMCQVVDKHQVNILYTAPTAIRALMAEgdkaiegtDRSSLRIL 383
Cdd:cd05918 166 -------------FTTLAAGGCLC----IPsEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLRTL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 384 GSVGEPINPEawewywkkigkekcpVVDTWWQ----------TETGGFMITPLPGAIElKAGSATRPfFGVQPALVDNEG 453
Cdd:cd05918 221 VLGGEALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVPST-DPRNIGRP-LGATCWVVDPDN 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 454 HPQ---EGATeGNLVItdSWPGQARtlfGDHERFEQTYFSTFKN--------------MYFSGDGARRDEDG--YYwiTG 514
Cdd:cd05918 284 HDRlvpIGAV-GELLI--EGPILAR---GYLNDPEKTAAAFIEDpawlkqegsgrgrrLYRTGDLVRYNPDGslEY--VG 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 515 RVDDVLNVSGHRLGTAEIESALVAHP---KIAEAAVVGIPHAIKGQAIYAYVTLNhGEEPSPELYAEVRNWVRKEIGPLA 591
Cdd:cd05918 356 RKDTQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQLVAFVVLD-GSSSGSGDGDSLFLEPSDEFRALV 434
|
570 580 590 600
....*....|....*....|....*....|....*....|....
1PG3_A 592 T---------------PDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:cd05918 435 AelrsklrqrlpsymvPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
254-615 |
1.71e-21 |
|
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: 97.89 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 254 NAEDPLFILYTSGSTGKPKGVL--------HTTGGYLVYAATTFKYV-------FDYHPGDIYwctadVGWVTGHSYLLy 318
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 319 gplacgATTLMFegvpnwPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKA-IEGTDRSSLRILGsvGEPINPEAWEw 397
Cdd:cd17644 178 ------RPEEMR------SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStIDLPSSLRLVIVG--GEAVQPELVR- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 398 YWKKIGKEKCPVVDTWWQTE----TGGFMITPLPGAIELKAgSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQ 473
Cdd:cd17644 243 QWQKNVGNFIQLINVYGPTEatiaATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHIGGV--GL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 474 ARTLFG----DHERFEQTYF--STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd17644 320 ARGYLNrpelTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVV 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 548 VGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-615 |
3.85e-21 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 96.47 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWEGddtsQSkhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG----QS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 251 eamNAEDPLFILYTSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWvTGHSYLLYGPLACGATTL 328
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 329 MFEGVPNWPTpARMCQVVDKHQVNILYTAPTAIRALMAegdkaiegTDRSSLRILGSVGEPInpeawewywKKIGKEKCP 408
Cdd:cd17645 175 VVPSERRLDL-DALNDYFNQEGITISFLPTGAAEQFMQ--------LDNQSLRVLLTGGDKL---------KKIERKGYK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 409 VVDTWWQTETGgFMITPLPGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpGQARTLFG----DHERF 484
Cdd:cd17645 237 LVNNYGPTENT-VVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNrpelTAEKF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 485 EQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVT 564
Cdd:cd17645 314 IVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1PG3_A 565 LNhgEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:cd17645 394 AP--EEIPHE---ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
4.71e-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: 86.76 E-value: 4.71e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 24 YETKYKQSINDPDTFWGEQGKILDWITPYQKVKNTSFAPGnvsIKWYEDGTLNLAANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-625 |
4.92e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.22 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 48 WITPYQKVKNTSFAPgnvsIKWYEDGTLNLAANCLDRHlQENGDrTAIIwegdDTSQSKHISYRELHRDVCRFANTLLD- 126
Cdd:PLN02574 17 WYSPETGIYSSKHPP----VPLPSDPNLDAVSFIFSHH-NHNGD-TALI----DSSTGFSISYSELQPLVKSMAAGLYHv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 127 LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVraGRSIPLKKNVddal 206
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPV---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 207 knpnvtsvehVIVLKRTGSDIDWQEGRDLWWRdLIEKASPEHQPeAMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAA 286
Cdd:PLN02574 161 ----------IGVPENYDFDSKRIEFPKFYEL-IKEDFDFVPKP-VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 287 TTFKY---VFDYHPGD-IYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVDKHQVNILYTAPTAIR 362
Cdd:PLN02574 229 LFVRFeasQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 363 ALMAEGdKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIgkekcPVVD---TWWQTE-----TGGFMITPLP--GAIEL 432
Cdd:PLN02574 305 ALTKKA-KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDfiqGYGMTEstavgTRGFNTEKLSkySSVGL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 433 KAGSatrpffgVQPALVDNE-GHPQEGATEGNLVITDswPGQARTLFGDHErfeQTYFSTFKNMYF-SGDGARRDEDGYY 510
Cdd:PLN02574 379 LAPN-------MQAKVVDWStGCLLPPGNCGELWIQG--PGVMKGYLNNPK---ATQSTIDKDGWLrTGDIAYFDEDGYL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 511 WITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPL 590
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE---AVINYVAKQVAPY 523
|
570 580 590
....*....|....*....|....*....|....*
1PG3_A 591 ATPDVLHWTDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PLN02574 524 KKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
104-617 |
1.20e-20 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 95.58 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 104 QSKHISYRELHRDVCRFANTLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRL 182
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 183 VItadegvragrsiplkknVDDalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnaEDPLFIL 262
Cdd:cd05937 82 VI-----------------VDP---------------------------------------------------DDPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 263 YTSGSTGKPKGVLHTTGGYLVyAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPtp 339
Cdd:cd05937 94 YTSGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsrkFSASQFWK-- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 340 armcQVVDKHQVNILYTAPTaIRALMAegdKAIEGTDRSSlRILGSVGEPINPEAWEWYWKKIGkekCPVVD-------- 411
Cdd:cd05937 171 ----DVRDSGATIIQYVGEL-CRYLLS---TPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFN---VPEIGefyaateg 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 412 --TWWQTETGGFMItplpGAIELKaGSATRPFFGVQPALV--DNEG-----HPQEGATEGNLVITdswPGQA--RTLFGD 480
Cdd:cd05937 239 vfALTNHNVGDFGA----GAIGHH-GLIRRWKFENQVVLVkmDPETddpirDPKTGFCVRAPVGE---PGEMlgRVPFKN 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 481 HERFeQTYFSTFK--------------NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd05937 311 REAF-QGYLHNEDatesklvrdvfrkgDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEA 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 546 AVVGI--PHAiKGQAIYAYVTL-NHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05937 390 NVYGVkvPGH-DGRAGCAAITLeESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
102-620 |
4.67e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 94.17 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 102 TSQSKHISYRELHRDVCRFANTLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDS-S 179
Cdd:PRK08751 45 HSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSgA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 180 SRLVITADEGVRAGRSI---PLKK----NVDDALKNPNVTSVEhvIVLKRTGSDI-DWQEGRDLWWRDLIEKASPEHQPE 251
Cdd:PRK08751 125 SVLVVIDNFGTTVQQVIadtPVKQvittGLGDMLGFPKAALVN--FVVKYVKKLVpEYRINGAIRFREALALGRKHSMPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 252 A-MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvfdyhpgdiyWCTADVGWVTGHSYL-----LYGPLACGA 325
Cdd:PRK08751 203 LqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-----------WLAGTGKLEEGCEVVitalpLYHIFALTA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 326 TTLMFEGVPNW----PTPARMCQVVdKHQVNILYTAPTAIRALMAE--GDKAIEGTDRSSLRILGSVGEPINPEAWEwYW 399
Cdd:PRK08751 272 NGLVFMKIGGCnhliSNPRDMPGFV-KELKKTRFTAFTGVNTLFNGllNTPGFDQIDFSSLKMTLGGGMAVQRSVAE-RW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 400 KKIgkEKCPVVDTWWQTETG-GFMITPLpgAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwpgqaRTLF 478
Cdd:PRK08751 350 KQV--TGLTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP-----QVMK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 479 GDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQ 557
Cdd:PRK08751 421 GYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 558 AIYAYVTlnhgeEPSPELYAE-VRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRKIAA 620
Cdd:PRK08751 501 IVKVVIV-----KKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
5.56e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 93.93 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIwegddtSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PRK07059 29 LEESFRQYADRPAFI------CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVITADEgvragrsipLKKNVDDALKNpnvTSVEHVIV------LKRTGSDID------- 228
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVLEN---------FATTVQQVLAK---TAVKHVVVasmgdlLGFKGHIVNfvvrrvk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 229 -----WQEGRDLWWRD-LIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKG--VLHT--------TGGYLVYAATTFKYV 292
Cdd:PRK07059 171 kmvpaWSLPGHVRFNDaLAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGatLLHRnivanvlqMEAWLQPAFEKKPRP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 293 FD---------YHpgdIYWCTAdvgwvtghSYLLygPLACGATTLMfegVPNWPTPARMCQVVDKHQVNILYTAPTAIRA 363
Cdd:PRK07059 251 DQlnfvcalplYH---IFALTV--------CGLL--GMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 364 LMAEGDkaIEGTDRSSLRI-LG---SVGEPInpeAWEWYwKKIGkekCPVVDTWWQTETGGFMITPLPGAIELkAGSATR 439
Cdd:PRK07059 315 LLNNPD--FDKLDFSKLIVaNGggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSPVATCNPVDATEF-SGTIGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 440 PFFGVQPALVDNEGH------PQEGATEGNLVITDSWpgqartlfgdhERFEQTYFSTFKNMYF-SGDGARRDEDGYYWI 512
Cdd:PRK07059 385 PLPSTEVSIRDDDGNdlplgePGEICIRGPQVMAGYW-----------NRPDETAKVMTADGFFrTGDVGVMDERGYTKI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 513 TGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTlnhgeEPSPELY-AEVRNWVRKEIGPLA 591
Cdd:PRK07059 454 VDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-----KKDPALTeEDVKAFCKERLTNYK 528
|
570 580
....*....|....*....|....*
1PG3_A 592 TPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07059 529 RPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-621 |
6.81e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.24 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 233 RDLWWRDLIEKASPEHQPEAMNAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIYWCTADVGWVT 311
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTASQSFDI 3923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 312 GHSYLLYGPLAcGATTlmfEGVPNWPT--PARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEGtdrssLRILGSVGEP 389
Cdd:PRK05691 3924 SVWQFLAAPLF-GARV---EIVPNAIAhdPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDG-----LRWMLPTGEA 3994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 390 INPE-AWEWY--WKKIGkekcpVVDTWWQTETG---GFMITPLP---GAIeLKAGSATRP----FFGVQPALVdneghPQ 456
Cdd:PRK05691 3995 MPPElARQWLqrYPQIG-----LVNAYGPAECSddvAFFRVDLAstrGSY-LPIGSPTDNnrlyLLDEALELV-----PL 4063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 eGATeGNLVITDSwpGQARTLFGDHERFEQTYF-----STFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAE 531
Cdd:PRK05691 4064 -GAV-GELCVAGT--GVGRGYVGDPLRTALAFVphpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGE 4139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 532 IESALVAHPKIAEAAvVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK05691 4140 IEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
410
....*....|
1PG3_A 612 RRILRKIAAG 621
Cdd:PRK05691 4219 RKALPALDIG 4228
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
108-616 |
1.95e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 92.79 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITad 187
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrSIPLKknvdDALKNPNVTSVEHVIvlkrtgSDIDWQEGRDLwwrdliekaspehqpEAMNAEDPLFILYTSGS 267
Cdd:PRK06060 109 -------SDALR----DRFQPSRVAEAAELM------SEAARVAPGGY---------------EPMGGDALAYATYTSGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLmfegVPNWPTPARMCQVVD 347
Cdd:PRK06060 157 TGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV----INSAPVTPEAAAILS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 348 -KHQVNILYTAPTairaLMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGKekCPVVDTWWQTETGGFMITPl 426
Cdd:PRK06060 233 aRFGPSVLYGVPN----FFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 427 pGAIELKAGSATRPFFGVQPALVDNEGHPQEGATEGNL-----VITDSWPGQARTLFGDHERFEqtyfstfknmyfSGDG 501
Cdd:PRK06060 306 -RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLwvrgpAIAKGYWNRPDSPVANEGWLD------------TRDR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 502 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAEVRN 581
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHR 452
|
490 500 510
....*....|....*....|....*....|....*
1PG3_A 582 WVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK06060 453 GLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
82-616 |
1.99e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.04 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGddtsqsKHISYRELHRDVCRFANTLL-DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHS 160
Cdd:PRK08974 29 FEQAVARYADQPAFINMG------EVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 161 VIFGGFSPEAVAGCIIDSSSRLVItadegVRAGRSIPLKKNVDDalknpnvTSVEHVIvLKRTGSDIDWQEgrdlwwRDL 240
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAKAIV-----IVSNFAHTLEKVVFK-------TPVKHVI-LTRMGDQLSTAK------GTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 241 -------IEKASPE-HQPEA-------------------MNAEDPLFILYTSGSTGKPKGVLHTTGGYLvyaATTFKYVF 293
Cdd:PRK08974 164 vnfvvkyIKRLVPKyHLPDAisfrsalhkgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNML---ANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 294 DY----HPGDIYWCTAdvgwvtghsYLLYGPLACGATTLMFegvpnwptparmcqvVDKHQVNILYTAPTAIRALMAEGD 369
Cdd:PRK08974 241 AYgpllHPGKELVVTA---------LPLYHIFALTVNCLLF---------------IELGGQNLLITNPRDIPGFVKELK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 370 K----AIEGT----------------DRSSLRILGSVGEPINPEAWEwYWKKIgkEKCPVVDTWWQTETGGfMITPLPGA 429
Cdd:PRK08974 297 KypftAITGVntlfnallnneefqelDFSSLKLSVGGGMAVQQAVAE-RWVKL--TGQYLLEGYGLTECSP-LVSVNPYD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 430 IELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLvitdsWPGQARTLFGDHERFEQTYfSTFKNMYFS-GDGARRDEDG 508
Cdd:PRK08974 373 LDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGEL-----WVKGPQVMLGYWQRPEATD-EVIKDGWLAtGDIAVMDEEG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 509 YYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNhgeepSPELYA-EVRNWVRKEI 587
Cdd:PRK08974 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK-----DPSLTEeELITHCRRHL 521
|
570 580
....*....|....*....|....*....
1PG3_A 588 GPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK08974 522 TGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-615 |
5.62e-19 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 90.95 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EgvragrsiplkKNVDDALK-NPNVTSVEHVIVLKRTGSDiDWQEGRDLWWRDLIEKASPEHQPE---------AMNAED 257
Cdd:cd17641 92 E-----------EQVDKLLEiADRIPSVRYVIYCDPRGMR-KYDDPRLISFEDVVALGRALDRRDpglyerevaAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvFDY-HPGDIYWCTADVGWVTGHSYLLYGPLACG--------ATTL 328
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPlGPGDEYVSVLPLPWIGEQMYSVGQALVCGfivnfpeePETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 329 M-----------------FEGVPNwPTPARMC------QVVDKHQVNILYTA----------PTAIRALMAEGDKAIEGT 375
Cdd:cd17641 238 MedlreigptfvllpprvWEGIAA-DVRARMMdatpfkRFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 376 DR-----SSLRILGSVGEPINPEAWEWYwKKIGkekCPVVDTWWQTETGGFMITPLPGAIelKAGSATRPFFGVQpALVD 450
Cdd:cd17641 317 LRdrlgfSRLRSAATGGAALGPDTFRFF-HAIG---VPLKQLYGQTELAGAYTVHRDGDV--DPDTVGVPFPGTE-VRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 451 NEGHpqegategnlvITDSWPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLG 528
Cdd:cd17641 390 EVGE-----------ILVRSPG---VFVGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 529 TAEIESALVAHPKIAEAAVVG-----------IPHAI-------KGQAIYAYVTLNHgeepSPELYAEVRNWVRKEIGPL 590
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLGagrpyltaficIDYAIvgkwaeqRGIAFTTYTDLAS----RPEVYELIRKEVEKVNASL 531
|
570 580 590
....*....|....*....|....*....|....
1PG3_A 591 ATPDVLHWTDSLPK---------TRSGKIMRRIL 615
Cdd:cd17641 532 PEAQRIRRFLLLYKeldaddgelTRTRKVRRGVI 565
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
246-615 |
1.08e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.38 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 246 PEHQPeamnaedplFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGD----IYWCTADVGwvtghSYLLYGPL 321
Cdd:PRK05691 2332 PQHQA---------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLLVPL 2396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 322 ACGATtLMFEGVPNWPTpARMCQVVDKHQVNILYTAPT----AIRALMAEGDkaiegtdRSSLRILGSVGEPINPEawew 397
Cdd:PRK05691 2397 LCGAR-VVLRAQGQWGA-EEICQLIREQQVSILGFTPSygsqLAQWLAGQGE-------QLPVRMCITGGEALTGE---- 2463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 398 YWKKIGKEKCPVV--DTWWQTETggfMITPL--PGAIELKAGSATRPFFGVQPALV------DNEGHPQeGATeGNLVIT 467
Cdd:PRK05691 2464 HLQRIRQAFAPQLffNAYGPTET---VVMPLacLAPEQLEEGAASVPIGRVVGARVayildaDLALVPQ-GAT-GELYVG 2538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 468 DSwpGQARtlfGDH-------ERFEQTYFSTFK-NMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH 539
Cdd:PRK05691 2539 GA--GLAQ---GYHdrpgltaERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEH 2613
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 540 PKIAEAAVVGIpHAIKGQAIYAYV---TLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK05691 2614 PAVREAVVLAL-DTPSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-617 |
3.66e-18 |
|
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: 87.36 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 83 DRHLQENGDRTAIiwegDDTSQSkhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:cd17653 4 ERIAAAHPDAVAV----ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 FGGfSPEAVAGCIIDSS-SRLVITADegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdli 241
Cdd:cd17653 78 DAK-LPSARIQAILRTSgATLLLTTD------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 242 ekaspehqpeamNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPGD--------IYWCTADVgwvtgh 313
Cdd:cd17653 103 ------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQP-PARLDVGPGSrvaqvlsiAFDACIGE------ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 314 sylLYGPLACGATTLMFEGVPNWPTPARMCqvvdkhqvNILYTAPTAIRALmaegdkaiEGTDRSSLRILGSVGEPINPe 393
Cdd:cd17653 164 ---IFSTLCNGGTLVLADPSDPFAHVARTV--------DALMSTPSILSTL--------SPQDFPNLKTIFLGGEAVPP- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 394 awewywkkigkekcPVVDTWWQ----------TETggfmiTPLPGAIELKAGSAT---RPFFGVQPALVDNEGHPQEGAT 460
Cdd:cd17653 224 --------------SLLDRWSPgrrlynaygpTEC-----TISSTMTELLPGQPVtigKPIPNSTCYILDADLQPVPEGV 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 EGNLVItdSWPGQARTLFGDHE----RFEQTYFSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd17653 285 VGEICI--SGVQVARGYLGNPAltasKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVV 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 537 VAHPKIAEAAVVgIPHaikGQAIYAYVTlnhgeePSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:cd17653 363 LQSQPEVTQAAA-IVV---NGRLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
.
1PG3_A 617 K 617
Cdd:cd17653 433 E 433
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
261-612 |
3.69e-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: 86.02 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 261 ILYTSGSTGKPKGVL--HTTGgYLVYAAttfkyvfdyhpgdiyWCtaDVGWVT-GHSYLLYGP-----------LAC--- 323
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT-LRAAAA---------------WA--DCADLTeDDRYLIINPffhtfgykagiVACllt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 324 GATTL---MFEgvpnwptPARMCQVVDKHQVNILYTAPTAIRALMAEGDKaiEGTDRSSLRILGSVGEPINPEAWEWYWK 400
Cdd:cd17638 67 GATVVpvaVFD-------VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 401 KIGKEKcpVVDTWWQTETG-GFMITPLPGAiELKAGSATRPFFGVQPALVDneghpqegatEGNLVITDswPGQARTLFG 479
Cdd:cd17638 138 ELGFET--VLTAYGLTEAGvATMCRPGDDA-ETVATTCGRACPGFEVRIAD----------DGEVLVRG--YNVMQGYLD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 480 DHERFEQTYFStfKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAI 559
Cdd:cd17638 203 DPEATAEAIDA--DGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
1PG3_A 560 YAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd17638 281 KAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
108-619 |
1.31e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 86.41 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTL---LDLgiKKGDVVAIYMPMVPEAAVAMLACARigavhsvifggfspeavAGCIIDSSSRLVi 184
Cdd:PRK12492 50 LSYAELERHSAAFAAYLqqhTDL--VPGDRIAVQMPNVLQYPIAVFGALR-----------------AGLIVVNTNPLY- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 185 TA--------DEGVRAGRSIPL-KKNVDDALKNpnvTSVEHVIVLKRTgsdiDWQEGRDLWW----RDLIEKASPE---- 247
Cdd:PRK12492 110 TAremrhqfkDSGARALVYLNMfGKLVQEVLPD---TGIEYLIEAKMG----DLLPAAKGWLvntvVDKVKKMVPAyhlp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 248 ----------------HQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDiywctadvgwvt 311
Cdd:PRK12492 183 qavpfkqalrqgrglsLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN-LVANMLQVRACLSQLGPD------------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 312 GHsyllygPLACGATTLMFEGVPNWP----TPARMCQVVDKHQvNILYTAPTAIRALMAEGDK----AIEG--------- 374
Cdd:PRK12492 250 GQ------PLMKEGQEVMIAPLPLYHiyafTANCMCMMVSGNH-NVLITNPRDIPGFIKELGKwrfsALLGlntlfvalm 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 375 -------TDRSSLRILGSVGEPINPEAWEwYWKKIgkEKCPVVDTWWQTETGGFMITPlPGAIELKAGSATRPFFGVQPA 447
Cdd:PRK12492 323 dhpgfkdLDFSALKLTNSGGTALVKATAE-RWEQL--TGCTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 448 LVDNEGHPQEGATEGNLVITDSwpgqaRTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHR 526
Cdd:PRK12492 399 VIDDDGNELPLGERGELCIKGP-----QVMKGYWQQPEATAEALDAEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 527 LGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPELYAevrnWVRKEIGPLATPDVLHWTDSLPKTR 606
Cdd:PRK12492 474 VYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTP 549
|
570
....*....|...
1PG3_A 607 SGKIMRRILRKIA 619
Cdd:PRK12492 550 VGKILRRELRDIA 562
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
88-618 |
4.73e-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: 84.64 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 88 ENGDRTAIIWEGDDTSQSKhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACarigavhsvIFGGFS 167
Cdd:cd05906 21 ERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 168 PeavagciidsssrlvitadegvragrsIPLKKNVDDALKNPNVTSVEHV-------IVL--KRTGSDIDWQEGRDLW-- 236
Cdd:cd05906 91 P---------------------------APLTVPPTYDEPNARLRKLRHIwqllgspVVLtdAELVAEFAGLETLSGLpg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAM----NAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIY--WCTAD--VG 308
Cdd:cd05906 144 IRVLSIEELLDTAADHDlpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLDhvGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 309 WVTGHSYLLYgpLACG----ATTLMFEGVPNWptparmCQVVDKHQVNILYtAPTAIRALMAEGDKAIEGT--DRSSLRI 382
Cdd:cd05906 223 LVELHLRAVY--LGCQqvhvPTEEILADPLRW------LDLIDRYRVTITW-APNFAFALLNDLLEEIEDGtwDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEPINPEAWEWYWKKIGKEKCP---VVDTWWQTETGGFMI-------TPLPGAIELKagSATRPFFGVQPALVDNE 452
Cdd:cd05906 294 LVNAGEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCSGVIysrsfptYDHSQALEFV--SLGRPIPGVSMRIVDDE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 453 GHPQEGATEGNLVItdswpgQARTLFGDHERFEQTYFSTFKN--MYFSGDGARRDeDGYYWITGRVDDVLNVSGHRLGTA 530
Cdd:cd05906 372 GQLLPEGEVGRLQV------RGPVVTKGYYNNPEANAEAFTEdgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 531 EIESAL-----VAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSpELYAEVRNWVRKEIG-------PLAtpdvlhw 598
Cdd:cd05906 445 EIEAAVeevpgVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALS-ETLRAIRSVVSREVGvspayliPLP------- 516
|
570 580
....*....|....*....|
1PG3_A 599 TDSLPKTRSGKIMRRILRKI 618
Cdd:cd05906 517 KEEIPKTSLGKIQRSKLKAA 536
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
91-615 |
5.02e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 84.66 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIweGDDTSqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEA 170
Cdd:PRK13383 50 GRTAII--DDDGA----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 171 VAGCIIDSSSRLVITADEGVR----AGRSI----PLKKNVDDALKNPNVTSvehvivlkrtgsdidwqEGRdlwwrdlie 242
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAEriagADDAVavidPATAGAEESGGRPAVAA-----------------PGR--------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 243 kaspehqpeamnaedplFILYTSGSTGKPKGVLHT--------------------TGGYLVYAATTFKyvfdyhpgdiyw 302
Cdd:PRK13383 178 -----------------IVLLTSGTTGKPKGVPRApqlrsavgvwvtildrtrlrTGSRISVAMPMFH------------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 303 ctadvGWVTGhsyLLYGPLACGATTLMFEgvpNWPTPARMCQVvDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRI 382
Cdd:PRK13383 229 -----GLGLG---MLMLTIALGGTVLTHR---HFDAEAALAQA-SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 383 LGSVGEPINPEAWEWYWKKIGKekcPVVDTWWQTETG-GFMITPlpgaIELKAGSAT--RPFFGVQPALVDNEGHPQEGA 459
Cdd:PRK13383 297 VMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVGiGALATP----ADLRDAPETvgKPVAGCPVRILDRNNRPVGPR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 460 TEGNLVITDSWPGQARTLFGDHerfeqtyfSTFKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH 539
Cdd:PRK13383 370 VTGRIFVGGELAGTRYTDGGGK--------AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAH 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 540 PKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK13383 442 PAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
101-612 |
6.05e-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: 84.03 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 101 DTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSS 180
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 181 RLVITADEgvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnaEDPLF 260
Cdd:cd05914 81 KAIFVSDE-------------------------------------------------------------------DDVAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 261 ILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTL------------ 328
Cdd:cd05914 94 INYTSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkipsakiia 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 329 --MFEGVPNWPTPaRMCQVVDKHQVNI------------LYTAPTAIRALMAEGDKAIEGTDrSSLRILGSVGEPINPEA 394
Cdd:cd05914 173 laFAQVTPTLGVP-VPLVIEKIFKMDIipkltlkkfkfkLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGAKINPDV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 395 wEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPALVDneghPQEGATEGNLVITDSwpgqa 474
Cdd:cd05914 251 -EEFLRTIG---FPYTIGYGMTETAPIISYSPPN--RIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGP----- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 475 RTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDV-LNVSGHRLGTAEIESALVAHPKIAEAAVVGIPH 552
Cdd:cd05914 316 NVMKGYYKNPEATAEAFDKDGWFhTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PG3_A 553 AIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGpLATP------DVLHWTDSLPKTRSGKIMR 612
Cdd:cd05914 396 KLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPnykkisKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-396 |
1.27e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 83.41 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 84 RHL----QENGDRTAII----WEGDDTSQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 156 GAVHSVIFGGFSPEAVAGCIIDSSSRLVITadegvragrsIPlKKNVDDALKNPNVTSVEHVIVLkrtgsdidwqeGRDL 235
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIG----------IP-KAHLARRLFGWGKPSVRRLVTV-----------GGRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 236 WWR----DLIEKASPEHQPE--AMNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAttfKYVFDYHPGDIYWCTADV 307
Cdd:PRK09274 148 LWGgttlATLLRDGAAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEIDLPTFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 308 gwvtghsYLLYGPlACGATTLmfegVPNW-PT------PARMCQVVDKHQVNILYTAPTAIRALMAEGdkaiEGTDRS-- 378
Cdd:PRK09274 225 -------FALFGP-ALGMTSV----IPDMdPTrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYG----EANGIKlp 288
|
330
....*....|....*...
1PG3_A 379 SLRILGSVGEPINPEAWE 396
Cdd:PRK09274 289 SLRRVISAGAPVPIAVIE 306
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
376-616 |
1.85e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.89 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 376 DRSSLRILGSVGEPINPEAWEwYWKKIgkEKCPVVDTWWQTETGGFMITPLPGAIELkaGSATRPFFGVQPALVDNEGH- 454
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAE-RWKEV--TGCAICEGYGMTETSPVVSVNPSQAIQV--GTIGIPVPSTLCKVIDDDGNe 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 455 -----PQEGATEGNLVITDSWPGQARTlfgDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 529
Cdd:PRK05677 399 lplgeVGELCVKGPQVMKGYWQRPEAT---DEILDSDGWLKT-------GDIALIQEDGYMRIVDRKKDMILVSGFNVYP 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 530 AEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK 609
Cdd:PRK05677 469 NELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
....*..
1PG3_A 610 IMRRILR 616
Cdd:PRK05677 546 ILRRELR 552
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
507-617 |
5.11e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.09 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 507 DGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGeePSPELyAEVRNWVRKE 586
Cdd:PRK07824 246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGG--PAPTL-EALRAHVART 322
|
90 100 110
....*....|....*....|....*....|.
1PG3_A 587 IGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PRK07824 323 LDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
82-619 |
5.59e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.43 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEgddtsqSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSV 161
Cdd:PLN02479 26 LERAAVVHPTRKSVVHG------SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 162 IFGGFSPEAVAGCIIDSSSRLVIT-------ADEGVR-----AGRSI--PL----------KKNVDDALKNpnvTSVEHV 217
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVdqefftlAEEALKilaekKKSSFkpPLlivigdptcdPKSLQYALGK---GAIEYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 218 IVLKRTGSDIDWQEGRDLWwrdliekaspehqpeamnaeDPLFILYTSGSTGKPKGV-LHTTGGYLvyAATTFKYVFDYH 296
Cdd:PLN02479 177 KFLETGDPEFAWKPPADEW--------------------QSIALGYTSGTTASPKGVvLHHRGAYL--MALSNALIWGMN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 297 PGDIY-----------WC-TADVGWVTGHSYLL--------YGPLA-------CGATtLMFEGVPNWPTPARMCQVVDKH 349
Cdd:PLN02479 235 EGAVYlwtlpmfhcngWCfTWTLAALCGTNICLrqvtakaiYSAIAnygvthfCAAP-VVLNTIVNAPKSETILPLPRVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 350 QVNILYTAPTAIrALMAEGDKAIEGTDRSSLrilgsvGEPINPE---AWEWYWKKIgkekcPVVDTWWQTETGGFMITPL 426
Cdd:PLN02479 314 HVMTAGAAPPPS-VLFAMSEKGFRVTHTYGL------SETYGPStvcAWKPEWDSL-----PPEEQARLNARQGVRYIGL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 427 PG--AIELKAGSATrpffgvqpalvdneghPQEGATEGNLVITDS--WPGQARTLFGDHERFEQTYFStfknmyfSGDGA 502
Cdd:PLN02479 382 EGldVVDTKTMKPV----------------PADGKTMGEIVMRGNmvMKGYLKNPKANEEAFANGWFH-------SGDLG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 503 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPE--LYAEVR 580
Cdd:PLN02479 439 VKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIM 518
|
570 580 590
....*....|....*....|....*....|....*....
1PG3_A 581 NWVRKEIGPLATPDVLHWtDSLPKTRSGKIMRRILRKIA 619
Cdd:PLN02479 519 KFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
237-584 |
8.82e-16 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 80.59 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 237 WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTGGYlVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 317 LYGPLACGATTLMFEGVPNWPTPARMCQ-----------------VVDK---HQVNILYTAPTaIRALMaeGDKAIEGTD 376
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEDVQRARptlffsvprlwtkfqqgVQDKipqQKLNLLLKIPV-VNSLV--KRKVLKGLG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 377 RSSLRILGSVGEPINPEAWEWYwKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPFFGVQPALVDneghpq 456
Cdd:cd05932 274 LDQCRLAGCGSAPVPPALLEWY-RSLG---LNILEAYGMTENFAYSHLNYPG--RDKIGTVGNAGPGVEVRISE------ 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 egatEGNLVITDswPGqarTLFGDHERFEQTYFSTFKNMYF-SGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTAEIES 534
Cdd:cd05932 342 ----DGEILVRS--PA---LMMGYYKDPEATAEAFTADGFLrTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIEN 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
1PG3_A 535 ALVAHPKIAEAAVVG--IPHAIkgqaiyAYVTLNhgEEPSPELYAEVRNWVR 584
Cdd:cd05932 413 KLAEHDRVEMVCVIGsgLPAPL------ALVVLS--EEARLRADAFARAELE 456
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-617 |
1.08e-14 |
|
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: 77.08 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 106 KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 186 adegvragrsiplkknvddalknpnvtsvEHVivlkrtgsdidwqegrdlwwrDLIEKASPEHQPEA--MNAEDPLFILY 263
Cdd:cd05939 82 -----------------------------NLL---------------------DPLLTQSSTEPPSQddVNFRDKLFYIY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 264 TSGSTGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDI-YWC-----TAdvGWVTGHSYLLYGplacGATTLM---FEGVP 334
Cdd:cd05939 112 TSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVvYDClplyhSA--GGIMGVGQALLH----GSTVVIrkkFSASN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 335 NWptpaRMCqvvDKHQVNILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGKEK-------- 406
Cdd:cd05939 185 FW----DDC---VKYNCTIVQYIGEICRYLLAQ--PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQigefygat 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 407 ---CPVVDTWWQTETGGFM------ITPL------PGAIELKAGS-----ATRP-----FFGV---QPALVDNEGHPQEG 458
Cdd:cd05939 254 egnSSLVNIDNHVGACGFNsrilpsVYPIrlikvdEDTGELIRDSdglciPCQPgepglLVGKiiqNDPLRRFDGYVNEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 459 ATEGNLvitdswpgqARTLF--GDherfeqtyfstfkNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd05939 334 ATNKKI---------ARDVFkkGD-------------SAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 537 VAHPKIAEAAVVG--IPHAiKGQAIYAYVTLNHGEEPSPELYAEvrnwVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRI 614
Cdd:cd05939 392 SNVLGLEDVVVYGveVPGV-EGRAGMAAIVDPERKVDLDRFSAV----LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTD 466
|
...
1PG3_A 615 LRK 617
Cdd:cd05939 467 LQK 469
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-608 |
2.87e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.26 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 257 DPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYwctadvgwvtghsyLLYGPL------ACGATTLMF 330
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQALVLAVLQAIDEGTVF--------------LNSGPLfhigtlMFTLATFHA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 331 EG----VPNWpTPARMCQVVDKHQVNILY-TAPT--AIRALMAEGdkaieGTDRSSLRILgsvgepinPEAWEWywkkig 403
Cdd:cd17636 66 GGtnvfVRRV-DAEEVLELIEAERCTHAFlLPPTidQIVELNADG-----LYDLSSLRSS--------PAAPEW------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 404 KEKCPVVDTWW--------QTETGGFMITPLPGaiELKAGSATRPFFGVQPALVDNEGH--PQ----EGATEGNLVITDS 469
Cdd:cd17636 126 NDMATVDTSPWgrkpggygQTEVMGLATFAALG--GGAIGGAGRPSPLVQVRILDEDGRevPDgevgEIVARGPTVMAGY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 470 W--PG--QARTLFGDHErfeqtyfstfknmyfSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEA 545
Cdd:cd17636 204 WnrPEvnARRTRGGWHH---------------TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADA 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1PG3_A 546 AVVGIPHAIKGQAIYAYVTLNHGEEPSPelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSG 608
Cdd:cd17636 269 AVIGVPDPRWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
109-616 |
8.34e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 74.36 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAI-----YMPMVpeaavAMLACARIGAVHSVIFGGFSPEAVAgCIIDSSSRLV 183
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTlawngYRHLE-----AYYGVSGSGAVCHTINPRLFPEQIA-YIVNHAEDRY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 184 ITADEGVragrsIPLKKNVDDALKNpnvtsVEHVIVL----KRTGSDIDWqegrdLWWRDLIEKASPEHQPEAMNAEDPL 259
Cdd:PRK07008 115 VLFDLTF-----LPLVDALAPQCPN-----VKGWVAMtdaaHLPAGSTPL-----LCYETLVGAQDGDYDWPRFDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 260 FILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyvfdyhPgDIYWCTA-DV-----------GWVTGHSYLLYGplacga 325
Cdd:PRK07008 180 SLCYTSGTTGNPKGALysHRSTVLHAYGAAL--------P-DAMGLSArDAvlpvvpmfhvnAWGLPYSAPLTG------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 326 TTLMFegvpnwPTPA----RMCQVVDKHQVNILYTAPTAIRALMAEGDKAieGTDRSSLR---ILGSVGEPINPEAWEwy 398
Cdd:PRK07008 245 AKLVL------PGPDldgkSLYELIEAERVTFSAGVPTVWLGLLNHMREA--GLRFSTLRrtvIGGSACPPAMIRTFE-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 wKKIGKEkcpVVDTWWQTEtggfmITPLPGAIELKAGSATRP--------------FFGVQPALVDNEGH--PQEGATEG 462
Cdd:PRK07008 315 -DEYGVE---VIHAWGMTE-----MSPLGTLCKLKWKHSQLPldeqrkllekqgrvIYGVDMKIVGDDGRelPWDGKAFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 463 NLVITDSWPGQaRTLFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKI 542
Cdd:PRK07008 386 DLQVRGPWVID-RYFRGDASPLVDGWFPT-------GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1PG3_A 543 AEAAVVGIPHAIKGQAIYAYVTLNHGEEPSPElyaEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILR 616
Cdd:PRK07008 458 AEAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
108-617 |
1.92e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 72.77 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIidsssrlvitad 187
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCL------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 egvragrsiplkknvddalknpNVTSVEHVIVlkrtgsdidwqegrdlwwrdliekaspehqpeamnaeDPLFILYTSGS 267
Cdd:cd05940 72 ----------------------NVSSAKHLVV-------------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 268 TGKPKGVLHTTGGYLvYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLM---FEGVPNWPTparmcq 344
Cdd:cd05940 93 TGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDD------ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 345 vVDKHQVNILYTAPTAIRALMAEgdKAIEGTDRSSLRILgsVGEPINPEAWEWYWKKIGKEKcpVVDTWWQTE--TGGFM 422
Cdd:cd05940 166 -IRKYQATIFQYIGELCRYLLNQ--PPKPTERKHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATEgnSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 423 ITPLPGAIElKAGSATRPFFGVQPALVDNE-GHPQEGATEGNLVITDSWPGQARTLFGDHERF----------EQTYFST 491
Cdd:cd05940 239 FFGKPGAIG-RNPSLLRKVAPLALVKYDLEsGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFdgytdpaateKKILRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 492 FK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVG--IPHAiKGQAIYAYVTLN 566
Cdd:cd05940 318 FKkgDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGvqVPGT-DGRAGMAAIVLQ 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
1PG3_A 567 HGEEPSPELYAevrNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:cd05940 397 PNEEFDLSALA---AHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
91-615 |
9.10e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 70.89 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIWeGDdtsqsKHISYRELHRDVCRFANTLLDLG-IKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPE 169
Cdd:cd17648 2 DRVAVVY-GD-----KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 170 AVAGCIIDSSSRLVITadegvragrsiplkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehq 249
Cdd:cd17648 76 RIQFILEDTGARVVIT---------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 250 peamNAEDPLFILYTSGSTGKPKGVLHTTGG-----------YLV----YAATTF--KYVFDYHpgdIYWCTADVgwVTG 312
Cdd:cd17648 92 ----NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslserYFGrdngDEAVLFfsNYVFDFF---VEQMTLAL--LNG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSYLLYGPlacgattlmfEGVPnwpTPARMCQVVDKHQVNILYTAPTAIralmaegdKAIEGTDRSSLRILGSVGEPINP 392
Cdd:cd17648 163 QKLVVPPD----------EMRF---DPDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 393 EAWEwywKKIGKEKCPVVDTWWQTETGGF-MITPLPGAiELKAGSATRPFFGVQPALVDNEGHPQEGATEGNLVITDSwp 471
Cdd:cd17648 222 PVFE---KLRSRFAGLIINAYGPTETTVTnHKRFFPGD-QRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGD-- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQARtlfGDH-------ERFEQTYFST--------FKNMYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 536
Cdd:cd17648 296 GVAR---GYLnrpeltaERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAAL 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 537 VAHPKIAEAAVVGIPHAIKGQA-----IYAYVTLNHGEEPSpelyAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIM 611
Cdd:cd17648 373 ASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPE----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
....
1PG3_A 612 RRIL 615
Cdd:cd17648 449 VRAL 452
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-580 |
1.44e-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: 70.18 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVItade 188
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 gvragrSIPLkknvddalknpnvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFILYTSGST 268
Cdd:cd05910 80 ------GIPK--------------------------------------------------------ADEPAAILFTSGST 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 269 GKPKGVLHTTgGYLVYAATTFKYVFDYHPGDIYWCTADVgwvtghsYLLYGPlACGATTLMFEGVPNWP---TPARMCQV 345
Cdd:cd05910 98 GTPKGVVYRH-GTFAAQIDALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDPTRParaDPQKLVGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 346 VDKHQVNILYTAPTAIRALMAEGdkAIEGTDRSSLRILGSVGEPINPEAWEWYwKKIGKEKCPVVDTWWQTETggfmitp 425
Cdd:cd05910 169 IRQYGVSIVFGSPALLERVARYC--AQHGITLPSLRRVLSAGAPVPIALAARL-RKMLSDEAEILTPYGATEA------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 426 LP----GAIELKA--------GSAT---RPFFGVQPALV--DNEGHPQEGATE-------GNLVITDswPGQARTLfgdH 481
Cdd:cd05910 239 LPvssiGSRELLAtttaatsgGAGTcvgRPIPGVRVRIIeiDDEPIAEWDDTLelprgeiGEITVTG--PTVTPTY---V 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 482 ERFEQTYFSTFKN-----MYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKG 556
Cdd:cd05910 314 NRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQ 393
|
490 500
....*....|....*....|....
1PG3_A 557 QAIYAYVTLNHGEEPSPELYAEVR 580
Cdd:cd05910 394 LPVLCVEPLPGTITPRARLEQELR 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-549 |
4.06e-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: 68.92 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 106 KHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggfspEAVAGCIIDSSSRLVIT 185
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV----------DVVRGSDSSVEELLYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 186 ADegvragrsiplkknvddalknpnvtSVEHVIVLKRTGSDIdwqegrdlwwrdliekASpehqpeamnaedplfILYTS 265
Cdd:cd17640 74 NH-------------------------SESVALVVENDSDDL----------------AT---------------IIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 266 GSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVgWvtgHSY---LLYGPLACGATTLmfegvpnWPTPARM 342
Cdd:cd17640 98 GTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 343 CQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILG---SVGE---PIN-----PEAWEWYWKKIGkekCPVVD 411
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflSGGIfkfGISgggalPPHVDTFFEAIG---IEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 412 TWWQTETGGFMITPLPGAIelKAGSATRPFFGVQPALVDneghpqegaTEGNLVITdswPGQARTLF--GDHerFEQTYF 489
Cdd:cd17640 243 GYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVD---------PEGNVVLP---PGEKGIVWvrGPQ--VMKGYY 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 490 ----STFKNM----YF-SGDGARRDEDGYYWITGRVDD--VLNvSGHRLGTAEIESALVAHPKIAEAAVVG 549
Cdd:cd17640 307 knpeATSKVLdsdgWFnTGDLGWLTCGGELVLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-322 |
4.92e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.99 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITAD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 188 EgvragrsiPLKKNVDDALKnpnVTSVEHVIVLKRTGSDIDWQEGRDLWWR----DLIEKASPEH--QPEAMNAEDPLFI 261
Cdd:PLN02387 187 K--------QLKKLIDISSQ---LETVKRVIYMDDEGVDSDSSLSGSSNWTvssfSEVEKLGKENpvDPDLPSPNDIAVI 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIywctadvgwvtghsYLLYGPLA 322
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-625 |
8.11e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 67.71 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 412 TWWQTETGGFMITPLPGAIELKAGSATRPFFGVQPALVDNeghpqegaTEGNLVItdswpgQARTLF-GdherfeqtYFS 490
Cdd:PRK07445 260 TYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPAN--------QTGNITI------QAQSLAlG--------YYP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 491 TFKNMY---FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNH 567
Cdd:PRK07445 318 QILDSQgifETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 568 GeEPSPElyaEVRNWVRKEIGPLATPDvlHW--TDSLPKTRSGKIMRRILRKIAAGDTSN 625
Cdd:PRK07445 398 P-SISLE---ELKTAIKDQLSPFKQPK--HWipVPQLPRNPQGKINRQQLQQIAVQRLGL 451
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
111-617 |
1.75e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 67.13 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 111 RELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITaDEGV 190
Cdd:PLN02860 36 HEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-DETC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 191 RagrSIPLKknvddaLKNPNVTSVEHVIVLKRTGSDIDWQ----EGRDLWWRDLIEKASPEHqpeAMNAEDPLFILYTSG 266
Cdd:PLN02860 115 S---SWYEE------LQNDRLPSLMWQVFLESPSSSVFIFlnsfLTTEMLKQRALGTTELDY---AWAPDDAVLICFTSG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 267 STGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIYWCTADVGWVTGHSYLLygplacgaTTLMFEG----VPNWPTPARM 342
Cdd:PLN02860 183 TTGRPKGVTISHSALIVQSLAKIAIV-GYGEDDVYLHTAPLCHIGGLSSAL--------AMLMVGAchvlLPKFDAKAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 343 cQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLR-IL---GSVGEPINPEAWEWYWK-KIGK-----EKC----- 407
Cdd:PLN02860 254 -QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRkILnggGSLSSRLLPDAKKLFPNaKLFSaygmtEACssltf 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 408 -----PVVDTWWQTETGGFMITPLPGaiELKAGSATrpffGVQPALVDNEGHPQEGATEGNL------VITDSWpgqART 476
Cdd:PLN02860 333 mtlhdPTLESPKQTLQTVNQTKSSSV--HQPQGVCV----GKPAPHVELKIGLDESSRVGRIltrgphVMLGYW---GQN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 477 LFGDHERFEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKG 556
Cdd:PLN02860 404 SETASVLSNDGWLDT-------GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLT 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 557 QAIYAYVTL--------------NHGEEPSPE---LYAEVRNWVRKEIGPLatpdVLHWTDSLPKTRSGKIMRRILRK 617
Cdd:PLN02860 477 EMVVACVRLrdgwiwsdnekenaKKNLTLSSEtlrHHCREKNLSRFKIPKL----FVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
69-279 |
6.00e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.77 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 69 WYEDGTL--NLAANCldrhlQENGDRTAI---------------------IWEGDDTSQSKHISYRELHRDVCRFANTLL 125
Cdd:PTZ00216 65 WYYGPNFlqRLERIC-----KERGDRRALayrpvervekevvkdadgkerTMEVTHFNETRYITYAELWERIVNFGRGLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 126 DLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADEGVragrsiplkKNVDDA 205
Cdd:PTZ00216 140 ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNV---------PNLLRL 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PG3_A 206 LKNPNVTSVEhVIVLKRTGSDIDWQEGRDLWWRDLIEK----ASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 211 MKSGGMPNTT-IIYLDSLPASVDTEGCRLVAWTDVVAKghsaGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHG 287
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
90-610 |
1.30e-10 |
|
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: 64.03 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 90 GDRTAIIwegDDTSQSK-HISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVhsvifggFSP 168
Cdd:cd17654 1 PDRPALI---IDQTTSDtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA-------YAP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 169 eavagciIDSSSrlvitaDEGvragRSIPLKKNvddalknpnvTSVEHVIVLKRTGSdidwqegrdlwwrdLIEKASPEH 248
Cdd:cd17654 71 -------IDPAS------PEQ----RSLTVMKK----------CHVSYLLQNKELDN--------------APLSFTPEH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEAMNAEDPL-FILYTSGSTGKPKGVlHTTGGYLVYAATTFKYVFDYHPGDIYWCTA----DVGWVTghsylLYGPLAC 323
Cdd:cd17654 110 RHFNIRTDECLaYVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLTSpltfDPSVVE-----IFLSLSS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 324 GATTLMfegVPNW--PTPARMCQVVDK-HQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGE--PINPEAWEWY 398
Cdd:cd17654 184 GATLLI---VPTSvkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEpfPSLVILSSWR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 399 WKKIGKEKCPVVDTwwqTETGGFMIT--------PLPGaielkaGSatrPFFGVQPALVDNEGHPQEGategnlviTDSW 470
Cdd:cd17654 261 GKGNRTRIFNIYGI---TEVSCWALAykvpeedsPVQL------GS---PLLGTVIEVRDQNGSEGTG--------QVFL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 471 PGQARTLFGDHErfEQTYFSTfknMYFSGDGARRdEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVgi 550
Cdd:cd17654 321 GGLNRVCILDDE--VTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-- 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 551 phAIKGQAIYAYVTlnhgeepSPELYAEVRNWVRKEIGPL-ATPDVLHWTDSLPKTRSGKI 610
Cdd:cd17654 393 --LSDQQRLIAFIV-------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-615 |
1.39e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.90 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 497 FSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPspely 576
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP----- 368
|
90 100 110
....*....|....*....|....*....|....*....
1PG3_A 577 AEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGKIMRRIL 615
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
82-615 |
1.66e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 63.76 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 82 LDRHLQENGDRTAIIWEGDDtsqskhISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIG----- 156
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEK------LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 157 -AVHSvifggfSPEAVAGcIIDSS-SRLVITADEgvragrsIPLkknvdDALKNPNVTSVEhvivLKrtgsdidwqegrd 234
Cdd:PRK04813 82 vDVSS------PAERIEM-IIEVAkPSLIIATEE-------LPL-----EILGIPVITLDE----LK------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 235 lwwrDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGV--LHTTggyLVyaatTFkyvfdyhpgdIYWCTADVGWVTG 312
Cdd:PRK04813 126 ----DIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVqiSHDN---LV----SF----------TNWMLEDFALPEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 HSYL-------------LYGPLACGATTLMfegVPNWPT--PARMCQVVDKHQVNILYTAPTAIRalMAEGDKAIEGTDR 377
Cdd:PRK04813 185 PQFLnqapysfdlsvmdLYPTLASGGTLVA---LPKDMTanFKQLFETLPQLPINVWVSTPSFAD--MCLLDPSFNEEHL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 378 SSLRILGSVGEPI-NPEAwewywKKIgKEKCP---VVDTWWQTETGGFM----IT--------PLPgaielkAGSAtRPf 441
Cdd:PRK04813 260 PNLTHFLFCGEELpHKTA-----KKL-LERFPsatIYNTYGPTEATVAVtsieITdemldqykRLP------IGYA-KP- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 442 fGVQPALVDNEGHPQEGATEGNLVITdswpGQARTL--FGDHERFEQTYFsTFKNM--YFSGDGARRDeDGYYWITGRVD 517
Cdd:PRK04813 326 -DSPLLIIDEEGTKLPDGEQGEIVIS----GPSVSKgyLNNPEKTAEAFF-TFDGQpaYHTGDAGYLE-DGLLFYQGRID 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 518 DVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGE-EPSPELYAEVRNWVRKEIGPLATPDVL 596
Cdd:PRK04813 399 FQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDfEREFELTKAIKKELKERLMEYMIPRKF 478
|
570
....*....|....*....
1PG3_A 597 HWTDSLPKTRSGKIMRRIL 615
Cdd:PRK04813 479 IYRDSLPLTPNGKIDRKAL 497
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
103-559 |
1.07e-09 |
|
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: 61.08 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 103 SQSKHISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRL 182
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 183 VITadegvragrsiplkknvddalkNPNvtsvehvivlkrtgsdidwqegrdlwwrdliekaspehqpeamnAEDPLFIL 262
Cdd:cd17639 81 IFT----------------------DGK--------------------------------------------PDDLACIM 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 263 YTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDiywctADVgwvtghsYLLYGPLA----------C---GAT--- 326
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGN-LVAGIAGLGDRVPELLGP-----DDR-------YLAYLPLAhifelaaenvClyrGGTigy 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 327 ----TL------------------MFEGVP------------NWPTPARMCQVVDKH-------QVNILYTAP------- 358
Cdd:cd17639 162 gsprTLtdkskrgckgdltefkptLMVGVPaiwdtirkgvlaKLNPMGGLKRTLFWTayqsklkALKEGPGTPlldelvf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 359 TAIRALMaeGDKaiegtdrssLRILGSVGEPINPEAWEWywkkIGKEKCPVVDTWWQTETGGFMITPLPGaiELKAGSAT 438
Cdd:cd17639 242 KKVRAAL--GGR---------LRYMLSGGAPLSADTQEF----LNIVLCPVIQGYGLTETCAGGTVQDPG--DLETGRVG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 439 RPFFGVQPALVDNEghpqegatEGNLvITDSWPGQARTLFG---------------DHERFEQTYFSTfknmyfsGDGAR 503
Cdd:cd17639 305 PPLPCCEIKLVDWE--------EGGY-STDKPPPRGEILIRgpnvfkgyyknpektKEAFDGDGWFHT-------GDIGE 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
1PG3_A 504 RDEDGYYWITGRVDD-VLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAI 559
Cdd:cd17639 369 FHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAI 425
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-277 |
1.71e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 60.66 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 54 KVKNTSFAPGNVSIKWYEDGTLNLAAN------------CLDRHLQENGDRTAIIwEGDDTSQSKHISYRELHRDVCRFA 121
Cdd:PRK08180 5 RYRPVAFAPPAVEVERRADGTIYLRSAeplgdyprrltdRLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 122 NTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPeAVAGCIIDsSSRL----------VITADEGVR 191
Cdd:PRK08180 84 QALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP-AYSLVSQD-FGKLrhvlelltpgLVFADDGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 192 AGRSIplkknvdDALKnpnvtsVEHVIVLKRTGSDIDwqeGRDLWWRDLIEKASPEHQPEAMNAEDPLFI---LYTSGST 268
Cdd:PRK08180 158 FARAL-------AAVV------PADVEVVAVRGAVPG---RAATPFAALLATPPTAAVDAAHAAVGPDTIakfLFTSGST 221
|
....*....
1PG3_A 269 GKPKGVLHT 277
Cdd:PRK08180 222 GLPKAVINT 230
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
88-621 |
1.64e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.01 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 88 ENGDRTAIIwegdDTSqSKHISYRELHRDVCRFANtLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAV-----HSVi 162
Cdd:PRK08633 627 RNWSRLAVA----DST-GGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAGKVpvnlnYTA- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 163 fggfSPEAVAGCIIDSSSRLVITADEGVRagrSIPLKKNVDDALKNPNVTSVEHvIVLKRTGSDIDWQEGR----DLWWR 238
Cdd:PRK08633 700 ----SEAALKSAIEQAQIKTVITSRKFLE---KLKNKGFDLELPENVKVIYLED-LKAKISKVDKLTALLAarllPARLL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 239 DLIEKASPehqpeamNAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYAATtfkyVFDYHPGDIywctadvgwVTG--- 312
Cdd:PRK08633 772 KRLYGPTF-------KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslp 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 313 --HSY----LLYGPLACGATTLMfegVPNwPTPARMC-QVVDKHQVNILYTAPTAIRALMAegDKAIEGTDRSSLRILGS 385
Cdd:PRK08633 832 ffHSFgltvTLWLPLLEGIKVVY---HPD-PTDALGIaKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVA 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 386 VGEPINPEAWEWYWKKIGK---------EKCPVV----------DTWWQTETggfmitplpgaielKAGSATRPFFGVQP 446
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIrilegygatETSPVAsvnlpdvlaaDFKRQTGS--------------KEGSVGMPLPGVAV 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 447 ALVD-NEGHPQEGATEGNLVITDS-----WPGQA-RTLFGDHERFEQTYfstfknmYFSGDGARRDEDGYYWITGRVDDV 519
Cdd:PRK08633 972 RIVDpETFEELPPGEDGLILIGGPqvmkgYLGDPeKTAEVIKDIDGIGW-------YVTGDKGHLDEDGFLTITDRYSRF 1044
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 520 LNVSGHR--LGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTlnHGEEPSPELYAEVRNwvrKEIGPLATPDVLH 597
Cdd:PRK08633 1045 AKIGGEMvpLGAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHT--CGAEDVEELKRAIKE---SGLPNLWKPSRYF 1119
|
570 580
....*....|....*....|....
1PG3_A 598 WTDSLPKTRSGKIMRRILRKIAAG 621
Cdd:PRK08633 1120 KVEALPLLGSGKLDLKGLKELALA 1143
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
108-612 |
2.22e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 56.92 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLD-LGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITA 186
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 187 DEgvragrsipLKKNVDD---ALKNPNVtsveHVIVLKRTGSdidwQEG-RDLwwRDLIEKASPEHQPEAMNAE----DP 258
Cdd:cd05938 86 PE---------LQEAVEEvlpALRADGV----SVWYLSHTSN----TEGvISL--LDKVDAASDEPVPASLRAHvtikSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 259 LFILYTSGSTGKPKGVLHTTggYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGhsyLLYGPLAC---GATTLM---FEG 332
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISH--LRVLQCSGFLSLCGVTADDVIYITLPLYHSSG---FLLGIGGCielGATCVLkpkFSA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 333 VPNWPTparmCQvvdKHQVN-ILYTAPTaIRALMAEGDKAIEGTDRSSLrilgSVGEPINPEAWEWYWKKIGKEKcpVVD 411
Cdd:cd05938 222 SQFWDD----CR---KHNVTvIQYIGEL-LRYLCNQPQSPNDRDHKVRL----AIGNGLRADVWREFLRRFGPIR--IRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 412 TWWQTE-TGGFM-ITPLPGAIelkaGSATR------PF----FGVQPA--LVDNEGH--PQEGATEGNLV--ITDSWP-- 471
Cdd:cd05938 288 FYGSTEgNIGFFnYTGKIGAV----GRVSYlykllfPFelikFDVEKEepVRDAQGFciPVAKGEPGLLVakITQQSPfl 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 472 GQArtlfGDHERFEQTYF-STFK--NMYF-SGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAV 547
Cdd:cd05938 364 GYA----GDKEQTEKKLLrDVFKkgDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNV 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 548 VGIP---HaiKGQAIYAYVTLNHGEEPSPE-LYAEVRNWvrkeIGPLATPDVLHWTDSLPKTRSGKIMR 612
Cdd:cd05938 440 YGVTvpgH--EGRIGMAAVKLKPGHEFDGKkLYQHVREY----LPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
124-620 |
8.06e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.74 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 124 LLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfgGFSpeAVAGCIIDSSS----RLVITADEGVRAGRSIPLK 199
Cdd:PRK06814 674 KLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSACKaaqvKTVLTSRAFIEKARLGPLI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 200 KNVDDALKnpnvtsvehVIVLKrtgsdiDWQEGRDLW--WRDLIEKASPEHQPEAMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK06814 750 EALEFGIR---------IIYLE------DVRAQIGLAdkIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLS 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 278 TGGYLVYAATTFKYVfDYHPGDIYWCTADVgwvtGHSYLLYGplacGATTLMFEGVPNWptparmcqvvdkhqvniLYTA 357
Cdd:PRK06814 815 HRNLLANRAQVAARI-DFSPEDKVFNALPV----FHSFGLTG----GLVLPLLSGVKVF-----------------LYPS 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 358 PTAIRA----LMAEGDKAIEGTD-------RS-------SLRILGSVGEPINPEAWEWYWKKIGKEkcpVVDTWWQTETG 419
Cdd:PRK06814 869 PLHYRIipelIYDTNATILFGTDtflngyaRYahpydfrSLRYVFAGAEKVKEETRQTWMEKFGIR---ILEGYGVTETA 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 420 GF--MITPLpgaiELKAGSATRPFFGVQPALVDNEGHPQEG--------------ATEGNLVI---TDSWpgqartlfgd 480
Cdd:PRK06814 946 PViaLNTPM----HNKAGTVGRLLPGIEYRLEPVPGIDEGGrlfvrgpnvmlgylRAENPGVLeppADGW---------- 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 481 herfeqtyfstfknmYFSGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIY 560
Cdd:PRK06814 1012 ---------------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERII 1076
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
1PG3_A 561 AYVTLNHGEEpspelyAEVRNWVRKE-IGPLATPDVLHWTDSLPKTRSGKI----MRRILRKIAA 620
Cdd:PRK06814 1077 LLTTASDATR------AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAA 1135
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
79-621 |
1.30e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 79 ANCLDRHLQENGDRTAIIWEGDDTSQSKHISYRELHRDVCRFANTLLDLGiKKGDVVAIYMPMVPEAAVAMLAC--ARIG 156
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGClyAGVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 157 AVHSvifggFSPEAV--------AGCIIDSSSRLVITAdegvrAGRSIPLKKNvdDALKNPNVTSVEHVIVLKRTGSDiD 228
Cdd:PRK05691 91 AVPA-----YPPESArrhhqerlLSIIADAEPRLLLTV-----ADLRDSLLQM--EELAAANAPELLCVDTLDPALAE-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 229 WQEgrdlwwrdliekaspehqpEAMNAEDPLFILYTSGSTGKPKGVlHTTGGYLVYAATTFKYVF--DYHPGDIYwctad 306
Cdd:PRK05691 158 WQE-------------------PALQPDDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFgiDLNPDDVI----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 307 VGWVT-GHSYLLYGPLACGattlMFEGVPN--------WPTPARMCQVVDKHQVNILYTAPTAIRaLMAE--GDKAIEGT 375
Cdd:PRK05691 213 VSWLPlYHDMGLIGGLLQP----IFSGVPCvlmspayfLERPLRWLEAISEYGGTISGGPDFAYR-LCSErvSESALERL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 376 DRSSLRILGSVGEPINPEAWEWYWKKI---GKEKCPVVDTWWQTETGGFMITPLPG----AIEL--KAGSATRPFFGVQP 446
Cdd:PRK05691 288 DLSRWRVAYSGSEPIRQDSLERFAEKFaacGFDPDSFFASYGLAEATLFVSGGRRGqgipALELdaEALARNRAEPGTGS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 447 ALV----DNEGH------PQEGATEGNLVITDSW---PGQARTLFGDHERFEQTYFSTFKNMYF-SGD-GARRdeDGYYW 511
Cdd:PRK05691 368 VLMscgrSQPGHavlivdPQSLEVLGDNRVGEIWasgPSIAHGYWRNPEASAKTFVEHDGRTWLrTGDlGFLR--DGELF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 512 ITGRVDDVLNVSGHRLGTAEIESALVahpkiAEAAVVGiphaiKGQaIYAYVTLNHGEEpSPELYAEVRNWVRKEIGPLA 591
Cdd:PRK05691 446 VTGRLKDMLIVRGHNLYPQDIEKTVE-----REVEVVR-----KGR-VAAFAVNHQGEE-GIGIAAEISRSVQKILPPQA 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
1PG3_A 592 TPDVLHWT-----------------DSLPKTRSGKIMRRILR-KIAAG 621
Cdd:PRK05691 514 LIKSIRQAvaeacqeapsvvlllnpGALPKTSSGKLQRSACRlRLADG 561
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-322 |
2.57e-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: 53.76 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 108 ISYRELHRDVCRFANTLLDLGIK--KGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAgCIIDSSSRLVIT 185
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIE-YILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 186 ADEGVRagrsiplkknvddalknpnVTSVEHVIvlkrtgsdidwqegrdlwwrDLIEKASPEHQPEAmnAEDPLFILYTS 265
Cdd:cd05927 85 CDAGVK-------------------VYSLEEFE--------------------KLGKKNKVPPPPPK--PEDLATICYTS 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 266 GSTGKPKGVLHTTGGYLVYAATTFKYVFDYH---PGDIYWctadvgwvtghSYLlygPLA 322
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDVYI-----------SYL---PLA 169
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
107-613 |
1.41e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 51.15 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 107 HISYRELHRDVCRFANTLLDLGIKKGDVVAIY--MP--MVPEAAVAMLACARIGAVHSvifggfsPEAvagciidsSSRL 182
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPveIAPTAQGLWMRGASLTMLHQ-------PTP--------RTDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 183 VITADEGVRAGRSIPLKKNVddaLKNPNVTSVEhviVLKRTGsdIDWQEGRDLWwrdliekASPEHQPEAMNAEDPLFIL 262
Cdd:PRK07768 94 AVWAEDTLRVIGMIGAKAVV---VGEPFLAAAP---VLEEKG--IRVLTVADLL-------AADPIDPVETGEDDLALMQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 263 YTSGSTGKPKGVLHTTG-----GYLVYAATTFKYVFDYHpgdIYW--CTADVGWVTGhsylLYGPLACGA-----TTLMF 330
Cdd:PRK07768 159 LTSGSTGSPKAVQITHGnlyanAEAMFVAAEFDVETDVM---VSWlpLFHDMGMVGF----LTVPMYFGAelvkvTPMDF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 331 EGVP-NWPtparmcQVVDKHQVNILyTAPTAIRALMAE--GDKAIEGT-DRSSLRILGSVGEPINPEAWEWYW---KKIG 403
Cdd:PRK07768 232 LRDPlLWA------ELISKYRGTMT-AAPNFAYALLARrlRRQAKPGAfDLSSLRFALNGAEPIDPADVEDLLdagARFG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 404 KEKCPVVDTWWQTET---------GGFMITPLPGAIELKA--------GSATRPFF-------GVQPALVDNEGHPQ--- 456
Cdd:PRK07768 305 LRPEAILPAYGMAEAtlavsfspcGAGLVVDEVDADLLAAlrravpatKGNTRRLAtlgpplpGLEVRVVDEDGQVLppr 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 457 ---------EGATEGNLVITDSWPGQArtlfgdherfEQTYFSTfknmyfsGDGARRDEDGYYWITGRVDDVLNVSGHRL 527
Cdd:PRK07768 385 gvgvielrgESVTPGYLTMDGFIPAQD----------ADGWLDT-------GDLGYLTEEGEVVVCGRVKDVIIMAGRNI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 528 GTAEIESALVAHPKIAEAAVVGI----PHAIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGplATPDVLHWTD--S 601
Cdd:PRK07768 448 YPTDIERAAARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgS 525
|
570
....*....|..
1PG3_A 602 LPKTRSGKIMRR 613
Cdd:PRK07768 526 IPKTPSGKLRRA 537
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
109-277 |
5.05e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.81 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 109 SYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGCIIDSSSRLVITADE 188
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 189 GVRAgrsiplkknvddaLKNPNVTSVEHV--IVLKRTGSDIDWQEGRDLW-----WRDLIEKAspEHQPEAMNAEDPL-- 259
Cdd:PLN02430 158 KIKE-------------LLEPDCKSAKRLkaIVSFTSVTEEESDKASQIGvktysWIDFLHMG--KENPSETNPPKPLdi 222
|
170
....*....|....*....
1PG3_A 260 -FILYTSGSTGKPKGVLHT 277
Cdd:PLN02430 223 cTIMYTSGTSGDPKGVVLT 241
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
124-607 |
8.70e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 48.95 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 124 LLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIfggfSPEA--VAGCIIDSSSRlVITADEGVRAGRSIPlkkn 201
Cdd:PRK07868 489 LIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM----PPDTdlAAAVRLGGVTE-IITDPTNLEAARQLP---- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 202 vddalknpnvtsvEHVIVLKRTGS-DIDWQEGRDLWwrDLiEKASPE-------HQPEAMNAEDPLFILY-TSGSTGKPK 272
Cdd:PRK07868 560 -------------GRVLVLGGGESrDLDLPDDADVI--DM-EKIDPDavelpgwYRPNPGLARDLAFIAFsTAGGELVAK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 273 GVlhTTGGYLVYAATTFKYVfDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVpnwpTPARMCQVVDKHQVN 352
Cdd:PRK07868 624 QI--TNYRWALSAFGTASAA-ALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL----DPDRFVQEVRQYGVT 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 353 ILYTAPTAIRALMAEGDKAIEGTDRSSLRIlGSvGEPINpeawewYWKKIGKEKCP--VVDTWWQTEtGGFMITPLPGAi 430
Cdd:PRK07868 697 VVSYTWAMLREVVDDPAFVLHGNHPVRLFI-GS-GMPTG------LWERVVEAFAPahVVEFFATTD-GQAVLANVSGA- 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 431 elKAGSATRPFFGVQPA------------LVDNEGHPQEGAT-EGNLVI------TDSWPGQARTLFGDHErfeqTYFST 491
Cdd:PRK07868 767 --KIGSKGRPLPGAGRVelaaydpehdliLEDDRGFVRRAEVnEVGVLLarargpIDPTASVKRGVFAPAD----TWIST 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 492 fKNMYfsgdgaRRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAyVTLNHGEEP 571
Cdd:PRK07868 841 -EYLF------RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAA-VTLRPGAAI 912
|
490 500 510
....*....|....*....|....*....|....*.
1PG3_A 572 SPelyAEVRNWVRkEIGPLATPDVLHWTDSLPKTRS 607
Cdd:PRK07868 913 TA---ADLTEALA-SLPVGLGPDIVHVVPEIPLSAT 944
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
124-322 |
1.41e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 48.17 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 124 LLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAV-----------AGCIIDSSSRLV--ITADEGV 190
Cdd:PLN02736 95 LVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVkfivnhaevaaIFCVPQTLNTLLscLSEIPSV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 191 RAgrsIPLKKNVDDALKNPNVTSVEHVIVLKRTGSdidwqEGRdlwwrdliekASPEHqPEAMNAEDPLFILYTSGSTGK 270
Cdd:PLN02736 175 RL---IVVVGGADEPLPSLPSGTGVEIVTYSKLLA-----QGR----------SSPQP-FRPPKPEDVATICYTSGTTGT 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1PG3_A 271 PKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWctadvgwvtghSYLlygPLA 322
Cdd:PLN02736 236 PKGVVLTHGN-LIANVAGSSLSTKFYPSDVHI-----------SYL---PLA 272
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
15-162 |
2.03e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.14 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 15 DRCLINPEQYETKYKQSINDPDTfwgEQGKIlDWITPYQKvkntSFAPgnvsikwyeDGTLNLA----ANCLDRHLQENG 90
Cdd:TIGR03443 184 DRITIVADQLAQLLSAASSNPDE---PIGKV-SLITPSQK----SLLP---------DPTKDLDwsgfRGAIHDIFADNA 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1PG3_A 91 ----DRTAII-WEGDDTSQSKH--ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVI 162
Cdd:TIGR03443 247 ekhpDRTCVVeTPSFLDPSSKTrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
254-393 |
7.92e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 45.56 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 254 NAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY--W--CTADVGWVTGHsyllYGPLACGATTLM 329
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNQYL 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1PG3_A 330 FegvpnwPT------PARMCQVVDKHQVNILYTAPTAIRALMAE-GDKAIEGTDRSSLRILGSVGEPINPE 393
Cdd:cd05908 179 M------PTrlfirrPILWLKKASEHKATIVSSPNFGYKYFLKTlKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
91-544 |
1.33e-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: 44.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 91 DRTAIIwEGDDTSQSKH--ISYRELHRDVCRFANTLLDLGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSP 168
Cdd:cd17647 3 ERTCVV-ETPSLNSSKTrsFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 169 EavagciidsssrlvitadegvragrsiplKKNVDDALKNPnvtsvEHVIVLKRTGSDIdwqegrdlwwrdliekaSPEH 248
Cdd:cd17647 82 A-----------------------------RQNIYLGVAKP-----RGLIVIRAAGVVV-----------------GPDS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 249 QPEamnaedplfILYTSGSTGKPKGVL---HTTGGYLVYAATTFKYVfdyhPGDIYWCTADVgwvtGHSYL---LYGPLA 322
Cdd:cd17647 111 NPT---------LSFTSGSEGIPKGVLgrhFSLAYYFPWMAKRFNLS----ENDKFTMLSGI----AHDPIqrdMFTPLF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 323 CGATTLmfegVP---NWPTPARMCQVVDKHQVNILYTAPTAIRALMAEGDKAIEG-----------TDRSSLRILGSVge 388
Cdd:cd17647 174 LGAQLL----VPtqdDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKlhhaffvgdilTKRDCLRLQTLA-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 389 pinpeawewywkkigkEKCPVVDTWWQTET----GGFMITPL---PGAIE-LKA-GSATRPFFGVQpALVDNEGHPQE-- 457
Cdd:cd17647 248 ----------------ENVRIVNMYGTTETqravSYFEVPSRssdPTFLKnLKDvMPAGRGMLNVQ-LLVVNRNDRTQic 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 458 -------------GATEGNL---------------VITDSWPGQARTLfgdHERFEQTYFSTFKNMYFSGDGARRDEDGY 509
Cdd:cd17647 311 gigevgeiyvragGLAEGYRglpelnkekfvnnwfVEPDHWNYLDKDN---NEPWRQFWLGPRDRLYRTGDLGRYLPNGD 387
|
490 500 510
....*....|....*....|....*....|....*
1PG3_A 510 YWITGRVDDVLNVSGHRLGTAEIESALVAHPKIAE 544
Cdd:cd17647 388 CECCGRADDQVKIRGFRIELGEIDTHISQHPLVRE 422
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
532-645 |
4.29e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 43.21 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 532 IESALVAHPKIAEAAVVGIPHAIKGQAIYAYVtlnhgEEPSPELYAEVRNWVRKEIGPLAtPDVLHWTDSLPKTRSGKIM 611
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....*
1PG3_A 612 RRILRKIAAGDTSNLGDTSTL-ADPGVVEKLLEEK 645
Cdd:PRK09188 319 DDILRLIAMNQIDELDDLLREpEIRGLVEAIAAHR 353
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
247-617 |
2.71e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 40.52 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 247 EHQPEAMNA---EDPLFILYTSGSTGKPKGVLHTTGGYLVYaATTFKYVF---DYHPGDIYWCTADVGWVTGHSYLLYGP 320
Cdd:COG1541 71 DNYPFGLFAvplEEIVRIHASSGTTGKPTVVGYTRKDLDRW-AELFARSLraaGVRPGDRVQNAFGYGLFTGGLGLHYGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 321 LACGATTlmfegVPNWP-TPARMCQVVDKHQVNILYTAPTAIRALmaeGDKAIE-GTD--RSSLR--ILGsvGEPInPEA 394
Cdd:COG1541 150 ERLGATV-----IPAGGgNTERQLRLMQDFGPTVLVGTPSYLLYL---AEVAEEeGIDprDLSLKkgIFG--GEPW-SEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 395 W-EWYWKKIGkekCPVVDTWWQTETGgfmitplPG-AIELKAgsatrpffgvQPALVDNEGH-------PQEGAT----- 460
Cdd:COG1541 219 MrKEIEERWG---IKAYDIYGLTEVG-------PGvAYECEA----------QDGLHIWEDHflveiidPETGEPvpege 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 461 EGNLVITdswpgqarTLF-----------GDHERFEQTYFST-FKNMYFSGdgarrdedgyywITGRVDDVLNVSGHRLG 528
Cdd:COG1541 279 EGELVVT--------TLTkeampliryrtGDLTRLLPEPCPCgRTHPRIGR------------ILGRADDMLIIRGVNVF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PG3_A 529 TAEIESALVAHPKIAEAAVVGIPHAIKGQAIYAYVTLNHGEEPsPELYAEVRNWVRKEIGplATPDV-LHWTDSLPktRS 607
Cdd:COG1541 339 PSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASL-EALAEAIAAALKAVLG--LRAEVeLVEPGSLP--RS 413
|
410
....*....|
1PG3_A 608 GKIMRRILRK 617
Cdd:COG1541 414 EGKAKRVIDR 423
|
|
| |
