|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
14-653 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1318.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 14 LFDPPTEFSERAYVrSGREYEQLYSRAASNPEKFWGELAeQELHWFKKWDQVLDWQPPFAKWFVGGQLNISHNCLDRHLT 93
Cdd:PRK00174 1 VFPPPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQA-KRLDWFKPFDTVLDWNAPFIKWFEDGELNVSYNCLDRHLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 94 TWRrNKAAIIWEGE-PGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGF 172
Cdd:PRK00174 79 TRG-DKVAIIWEGDdPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 173 SAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKALEHgAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAH 252
Cdd:PRK00174 158 SAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALAN-CPSVEKVIVVRRTGGDVDWVEGRDLWWHELVAGASDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 253 CPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATT 332
Cdd:PRK00174 237 CEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 333 VMYEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKC 412
Cdd:PRK00174 317 LMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERC 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 413 PIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHT 492
Cdd:PRK00174 397 PIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 493 YWEHIQPKegqylYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAF 572
Cdd:PRK00174 477 YFSTFKGM-----YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 573 VSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEISGDTSTLEDRTVLDKLRE 652
Cdd:PRK00174 552 VTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKLIE 631
|
.
gi 6647434 653 G 653
Cdd:PRK00174 632 A 632
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-643 |
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: 1196.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 31 REYEQLYSRAASNPEKFWGELAEqELHWFKKWDQVLDW--QPPFAKWFVGGQLNISHNCLDRHLTTwRRNKAAIIWEGEP 108
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAK-ELDWFKPWDKVLDWskGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GD-SRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAK 187
Cdd:cd05966 79 PDqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 188 LVITADGGFRKDKAIALKQEVDKALEHgAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFIL 267
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEK-CPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCF 347
Cdd:cd05966 238 YTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 348 WDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTETGGIM 427
Cdd:cd05966 318 WDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 428 LTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHIqpkegQYLYF 507
Cdd:cd05966 398 ITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKF-----PGYYF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 508 AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKK 587
Cdd:cd05966 473 TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRK 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 588 DLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEISGDTSTLED 643
Cdd:cd05966 553 ELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
32-652 |
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: 1166.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 32 EYEQLYSRAASNPEKFWGELAEQELHWFKKWDQVLDWQ-PPFAKWFVGGQLNISHNCLDRHLTTwRRNKAAIIWEG-EPG 109
Cdd:TIGR02188 6 QYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSfPPFYKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWEGdEPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:TIGR02188 85 EVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADV-TMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILY 268
Cdd:TIGR02188 165 ITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVvPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCFW 348
Cdd:TIGR02188 245 TSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTETGGIML 428
Cdd:TIGR02188 325 EIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 429 TPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVE-SDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHIQPKegqylYF 507
Cdd:TIGR02188 405 TPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGY-----YF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 508 AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKK 587
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 588 DLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQ-EISGDTSTLEDRTVLDKLRE 652
Cdd:TIGR02188 560 ELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEaEILGDTSTLEDPSVVEELIE 625
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-652 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 957.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 74 KWFVGGQLNISHNCLDRHLTtWRRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAI 153
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 154 TMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKALEhGAPSVENVIVVQRTKADVT 233
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE-ELPSLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 234 MTAgrDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVG 313
Cdd:COG0365 159 MEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 314 WITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGE 393
Cdd:COG0365 237 WATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 394 PINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPGaIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQ 473
Cdd:COG0365 317 PLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 474 PWPSMIRDVYGDTDRFRHTYWEHIqpkEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVA 553
Cdd:COG0365 393 PWPGMFRGYWNDPERYRETYFGRF---PG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 554 EAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQE 633
Cdd:COG0365 468 EAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRP 547
|
570
....*....|....*....
gi 6647434 634 IsGDTSTLEDRTVLDKLRE 652
Cdd:COG0365 548 L-GDTSTLEDPEALDEIKE 565
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-621 |
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: 737.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 33 YEQLYSRAASNPEKFWGELAEQ-ELHWFKKWDQVLDWQP--PFAKWFVGGQLNISHNCLDRHLTTwRRNKAAIIWEGEPG 109
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKIlDWITPYQKVKNTSFAPgaPSIKWFEDATLNLAANALDRHLRE-NGDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 -DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:cd17634 80 sQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILY 268
Cdd:cd17634 160 LITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCFW 348
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTETGGIML 428
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 429 TPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHIqpkEGqyLYFA 508
Cdd:cd17634 400 TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTF---KG--MYFS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 509 GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKD 588
Cdd:cd17634 475 GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAE 554
|
570 580 590
....*....|....*....|....*....|...
gi 6647434 589 LVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIM 621
Cdd:cd17634 555 LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
6-650 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 736.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 6 ESILQEER-LFDPPTEFSERAYVRSGREYEQLYSRAASNPEKFWGELAEQeLHWFKKW--DQV----LDWQ--PPFAKWF 76
Cdd:PLN02654 4 ESLASEENdLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQ-FYWKQKWegDEVcsenLDVRkgPISIEWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 77 VGGQLNISHNCLDRHLTTWRRNKAAIIWEG-EPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITM 155
Cdd:PLN02654 83 KGGKTNICYNCLDRNVEAGNGDKIAIYWEGnEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 156 LACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKALEHGAP---------SVENVIVVQ 226
Cdd:PLN02654 163 LACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKngvsvgiclTYENQLAMK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 227 RTkaDVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVY 306
Cdd:PLN02654 243 RE--DTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 307 WCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLR 386
Cdd:PLN02654 321 WCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 387 LLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQG 466
Cdd:PLN02654 401 VLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 467 GFLVIKQPWPSMIRDVYGDTDRFRHTYWehiQPKEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESAL 546
Cdd:PLN02654 481 GYLCVKKSWPGAFRTLYGDHERYETTYF---KPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 547 VSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PLN02654 556 VSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
650 660
....*....|....*....|....*
gi 6647434 627 SLASGQ-EISGDTSTLEDRTVLDKL 650
Cdd:PLN02654 636 KIASRQlDELGDTSTLADPGVVDQL 660
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
33-650 |
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: 685.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 33 YEQLYSRAASNPEKFWGELAEQeLHWFKKWDQVLD-WQPPFAKWFVGGQLNISHNCLDRHLTTWRRNKAAIIWE-GEPGD 110
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARL-IDWFKPPEKILDnSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDsPVTGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 111 SRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVI 190
Cdd:cd05967 80 ERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTA-GRDHWWHELQPQQSAHCPAePIDSEDMLFILYT 269
Cdd:cd05967 160 TASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKpGRDLDWSELLAKAEPVDCV-PVAATDPLYILYT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGGYN--LYTHMTTkwIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVP-RPSNPGC 346
Cdd:cd05967 239 SGTTGKPKGVVRDNGGHAvaLNWSMRN--IYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPvGTPDPGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 347 FWDVIERYGVNIFYTAPTAIRAfIRmgEAVPNAR-----DLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQT 421
Cdd:cd05967 317 FWRVIEKYQVNALFTAPTAIRA-IR--KEDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 422 ETGGIMLTPLPG--AIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPW-PSMIRDVYGDTDRFRHTYWEHIQ 498
Cdd:cd05967 391 ETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 499 PkegqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGN 578
Cdd:cd05967 471 G-----YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 579 AEPS-EELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEIsGDTSTLEDRTVLDKL 650
Cdd:cd05967 546 VKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDY-TIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
33-652 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 673.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 33 YEQLYSRAASNPEKFWGELAeQELHWFKKWDQVLDW-QPPFAKWFVGGQLNISHNCLDRHLTTwRRNKAAIIW-EGEPGD 110
Cdd:PRK10524 4 YSEFYQRSIDDPEAFWAEQA-RRIDWQTPFTQVLDYsNPPFARWFVGGRTNLCHNAVDRHLAK-RPEQLALIAvSTETDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 111 SRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVI 190
Cdd:PRK10524 82 ERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQ-SAHCPAEPIDSEDMLFILYT 269
Cdd:PRK10524 162 SADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGRDVDYATLRAQHlGARVPVEWLESNEPSYILYT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVP-RPsNPGCFW 348
Cdd:PRK10524 242 SGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPtRP-DAGIWW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIML 428
Cdd:PRK10524 321 RIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVIDNYWQTETGWPIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 429 TPLPG--AIPTKPGSCTKPFPGIVAEIVD-LDGNPVESDQGGFLVIKQPW-PSMIRDVYGDTDRFRHTYWEHIqpkeGQY 504
Cdd:PRK10524 398 AIARGveDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLF----GRQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 505 LYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFV-----SLEGNA 579
Cdd:PRK10524 474 VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVvpkdsDSLADR 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 580 EPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEiSGDTSTLEDRTVLDKLRE 652
Cdd:PRK10524 554 EARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRD-PGDLTTIEDPAALQQIRQ 625
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-643 |
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: 591.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 32 EYEQLYSRAASNPEKFWGELAEQEL-HWFKKWDQVLDWQP--PFAKWFVGGQLNISHNCLDRHLTTwRRNKAAIIWEGEP 108
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDVGiEWYEPPYQTLDLSGgkPWAAWFVGGRMNIVEQLLDKWLAD-TRTRPALRWEGED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITADGGFRKDKAIALKQEVDKALEHgAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHcpAEPIDSEDMLFILY 268
Cdd:cd05968 167 LITADGFTRRGREVNLKEEADKACAQ-CPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDG--AERTESEDPLMIIY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTD-VYWCTaDVGWITGhSYIVYGPLSNGATTVMYEGVPRPSNPGCF 347
Cdd:cd05968 244 TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 348 WDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCPIVDTWWQTE-TGGI 426
Cdd:cd05968 322 WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGGI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 427 MLTPLpgAIPTKPGSCTKPFPGIVAEIVDLDGNPVeSDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHIqpkEGQYLY 506
Cdd:cd05968 402 LGNVL--IKPIKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRF---DNVWVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 507 faGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELK 586
Cdd:cd05968 476 --GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALA 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 587 KDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEIsGDTSTLED 643
Cdd:cd05968 554 EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKEL-GDLSSLEN 609
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
62-643 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 584.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 62 WDQV---LDWQPpfakwfvGGQLNISHNCLDRHLTTWRRNKAAIIWEGEPGDsRIITYAQLHREVCQFANALKSLGVQKG 138
Cdd:PRK04319 27 WEEVekeFSWLE-------TGKVNIAYEAIDRHADGGRKDKVALRYLDASRK-EKYTYKELKELSNKFANVLKELGVEKG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 139 DRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALkqevdkalehgaPS 218
Cdd:PRK04319 99 DRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDL------------PS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 219 VENVIVVqrtKADVTMTAGRDHWWHELQpQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIF 298
Cdd:PRK04319 167 LKHVLLV---GEDVEEGPGTLDFNALME-QASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 299 DLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGvprPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPN 378
Cdd:PRK04319 242 DLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 379 ARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPgAIPTKPGSCTKPFPGIVAEIVDLDG 458
Cdd:PRK04319 319 KYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 459 NPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYWEHiqpkegqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLG 538
Cdd:PRK04319 395 NELPPNRMGNLAIKKGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 539 TMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSG 618
Cdd:PRK04319 467 PFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSG 546
|
570 580
....*....|....*....|....*
gi 6647434 619 KIMRRLLRSLASGQEiSGDTSTLED 643
Cdd:PRK04319 547 KIMRRVLKAWELGLP-EGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
115-630 |
2.25e-162 |
|
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: 473.14 E-value: 2.25e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADg 194
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhELqpqqsahcpAEPIDSEDMLFILYTSGSTG 274
Cdd:cd05969 81 -------------------------------------------------EL---------YERTDPEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 275 KPKGVVHTTGGYNLYtHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGvprPSNPGCFWDVIERY 354
Cdd:cd05969 103 TPKGVLHVHDAMIFY-YFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 355 GVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPGa 434
Cdd:cd05969 179 KVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 435 IPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYwehiqpKEGQYLyfAGDGARR 514
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSF------IDGWYL--TGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 515 DKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVT 594
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVR 406
|
490 500 510
....*....|....*....|....*....|....*.
gi 6647434 595 EEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLAS 630
Cdd:cd05969 407 QKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
115-626 |
1.23e-134 |
|
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: 401.72 E-value: 1.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITadg 194
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepiDSEDMLFILYTSGSTG 274
Cdd:cd05972 79 ----------------------------------------------------------------DAEDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 275 KPKGVVHTTGGynLYTHMTT-KWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGvpRPSNPGCFWDVIER 353
Cdd:cd05972 95 LPKGVLHTHSY--PLGHIPTaAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEG--PRFDAERILELLER 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 354 YGVNIFYTAPTAIRAFIRMGeavPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGgIMLTPLPG 433
Cdd:cd05972 171 YGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFPD 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 434 aIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRDVYGDTDRFRHTYwehiqpkEGQYlYFAGDGAR 513
Cdd:cd05972 244 -MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASI-------RGDY-YLTGDRAY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 514 RDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHV 593
Cdd:cd05972 315 RDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|...
gi 6647434 594 TEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
107-533 |
3.10e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.22 E-value: 3.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 107 EPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEA 186
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 187 KLVITADggfrkdkaiALKQEVDKALEHGAPSVENVIVVQRTKADVTmtagrDHWWHELQPQQSAHCPAEPIDSEDMLFI 266
Cdd:pfam00501 95 KVLITDD---------ALKLEELLEALGKLEVVKLVLVLDRDPVLKE-----EPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 267 LYTSGSTGKPKGVVHTTGG--YNLYTH-MTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSn 343
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNlvANVLSIkRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 344 PGCFWDVIERYGVNIFYTAPTAIRAFIRMGEavPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTET 423
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 424 GGIMLTPLPGAIP-TKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPWpsMIRDVYGDTDRFRHTYWEhiqpkE 501
Cdd:pfam00501 315 TGVVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPG--VMKGYLNDPELTAEAFDE-----D 387
|
410 420 430
....*....|....*....|....*....|..
gi 6647434 502 GqyLYFAGDGARRDKDGYFWVMGRVDDVINVS 533
Cdd:pfam00501 388 G--WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
88-633 |
3.11e-106 |
|
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: 329.08 E-value: 3.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTwRRNKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSV 167
Cdd:COG0318 5 LRRAAAR-HPDRPALVFGG-----RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFGGFSAEALRDRLVDAEAKLVITAdggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqp 247
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 qqsahcpaepidsedmlFILYTSGSTGKPKGVVHTTGgyNLYTH-MTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPL 326
Cdd:COG0318 104 -----------------LILYTSGTTGRPKGVMLTHR--NLLANaAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 SNGATTVMYEGVprpsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGTVGEPINPEAWMWYHRV 406
Cdd:COG0318 165 LAGATLVLLPRF----DPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 407 IGggkCPIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWpsmirdV---- 482
Cdd:COG0318 239 FG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPN------Vmkgy 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 YGDTDRFRHTYwehiqpKEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:COG0318 310 WNDPEATAEAF------RDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPD 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 563 ELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQE 633
Cdd:COG0318 382 EKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
262-621 |
2.79e-94 |
|
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: 294.19 E-value: 2.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 262 DMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWItGHSYIVYGPLSNGATTVMYEGvprp 341
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 342 SNPGCFWDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQT 421
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLK--APESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 422 ETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSM-IRDVYGDTDRFRHTYWehiqpk 500
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKgYWNNPEATAAVDEDGW------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 501 egqylYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAE 580
Cdd:cd04433 224 -----YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD 298
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 6647434 581 PSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIM 621
Cdd:cd04433 299 LDAE---ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
114-626 |
3.72e-94 |
|
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: 297.51 E-value: 3.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAd 193
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenviVVQRTKADvtmtagrdhwwhelqpqqsahcpaepidsEDMLFILYTSGST 273
Cdd:cd05973 80 ------------------------------AANRHKLD-----------------------------SDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGgYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGvprPSNPGCFWDVIER 353
Cdd:cd05973 101 GLPKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEG---GFSVESTWRVIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 354 YGVNIFYTAPTAIRAFIRMGEAVPnARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPG 433
Cdd:cd05973 177 LGVTNLAGSPTAYRLLMAAGAEVP-ARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHAL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 434 AIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIkqpwpsmirdvygDTDR-----FRhTYWEHIQPKEGQYLYFA 508
Cdd:cd05973 253 EHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAI-------------DIANsplmwFR-GYQLPDTPAIDGGYYLT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 509 GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKD 588
Cdd:cd05973 319 GDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 6647434 589 LVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05973 399 LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
33-634 |
3.33e-91 |
|
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: 295.72 E-value: 3.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 33 YEQLYSRAASNPEKFWGELAE-QELHWFKKWDQVL--DWQPPFAKWFVGGQLNISHNCLdRHLTTwrRNKAAIIwEGEPG 109
Cdd:cd05943 19 YAALHRWSVDDPGAFWAAVWDfSGVRGSKPYDVVVvsGRIMPGARWFPGARLNYAENLL-RHADA--DDPAAIY-AAEDG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd05943 95 ERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGGFRKDKAIALKQEVdKALEHGAPSVENVIVVQRTKADVTMTAG---RDHWWHE-LQPQQSAHCPAEPIDSEDMLF 265
Cdd:cd05943 175 FAVDAYTYNGKRHDVREKV-AELVKGLPSLLAVVVVPYTVAAGQPDLSkiaKALTLEDfLATGAAGELEFEPLPFDHPLY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ILYTSGSTGKPKGVVHTTGGyNLYTHMTTKWI-FDLKDTDVYWCTADVGWITGHSYIvyGPLSNGATTVMYEGVPRPSNP 344
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGG-TLLQHLKEHILhCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSPFYPDT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 345 GCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkcpivDTWWQTETG 424
Cdd:cd05943 331 NALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 425 GI-MLTPLPGAIPTKP---GSCTKPFPGIVAEIVDLDGNPVeSDQGGFLVIKQPWPSMIRDVYGDTD--RFRHTY----- 493
Cdd:cd05943 405 GTdIISCFVGGNPLLPvyrGEIQCRGLGMAVEAFDEEGKPV-WGEKGELVCTKPFPSMPVGFWNDPDgsRYRAAYfakyp 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 494 --WEHiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFA 571
Cdd:cd05943 484 gvWAH------------GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVIL 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 572 FVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEI 634
Cdd:cd05943 552 FVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPV 614
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
109-627 |
4.14e-90 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 287.02 E-value: 4.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA---PHSVVFGGfsaEALRDRLVDAE 185
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAiavPLFALFGP---EALEYRLSNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 186 AKLVITaDGgfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidSEDMLF 265
Cdd:cd05971 79 ASALVT-DG-----------------------------------------------------------------SDDPAL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ILYTSGSTGKPKGVVHT-------TGGYNLYTHMTTKwifdlkDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEgv 338
Cdd:cd05971 93 IIYTSGTTGPPKGALHAhrvllghLPGVQFPFNLFPR------DGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHR-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 339 PRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEavPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTW 418
Cdd:cd05971 165 MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGE--QLKHAQVKLRAIATGGESLGEELLGWAREQFG---VEVNEFY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTEtGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMIRdvygdtdrfrhTYWEH-- 496
Cdd:cd05971 240 GQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFL-----------GYWNNps 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 497 --IQPKEGQYLyFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:cd05971 308 atEKKMAGDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6647434 575 LEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:cd05971 387 LNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
11-625 |
9.96e-89 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 289.77 E-value: 9.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 11 EERLFDPP-TEFSERAYVRSGRE---YEQLYSRAASNPEKFWGELAEQ-ELHWFKKWDQVLDWQP-PFAKWFVGGQLNIS 84
Cdd:PRK03584 10 AERIAASRmTAFIRWLAARRGLSfddYAALWRWSVEDLEAFWQSVWDFfGVIGSTPYTVVLAGRRmPGARWFPGARLNYA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 85 HNCLdRHLttwRRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAP 164
Cdd:PRK03584 90 ENLL-RHR---RDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 165 HSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVdKALEHGAPSVENVIVVQRT-KADVTMTAGRDHWWH 243
Cdd:PRK03584 166 WSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKV-AELRAALPSLEHVVVVPYLgPAAAAAALPGALLWE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 244 E-LQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGG------YNLYTHMttkwifDLKDTDVY-WCTAdVGWI 315
Cdd:PRK03584 245 DfLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGillehlKELGLHC------DLGPGDRFfWYTT-CGWM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 316 TgHSYIVYGPLSnGATTVMYEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAfIRMGEAVPNAR-DLSSLRLLGTVGEP 394
Cdd:PRK03584 318 M-WNWLVSGLLV-GATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDA-CEKAGLVPGEThDLSALRTIGSTGSP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 395 INPEAWMWYHRVIGGgkcpivDTWWQTETGGI-MLTPLPGAIPTKP---GSCTKPFPGIVAEIVDLDGNPVEsDQGGFLV 470
Cdd:PRK03584 395 LPPEGFDWVYEHVKA------DVWLASISGGTdICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRPVV-GEVGELV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 471 IKQPWPSMirDVY--GDTD--RFRHTYWE-------HiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGT 539
Cdd:PRK03584 468 CTKPFPSM--PLGfwNDPDgsRYRDAYFDtfpgvwrH------------GDWIEITEHGGVVIYGRSDATLNRGGVRIGT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 540 MEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLegnaEPSEELKKDLVKHVTEEI--GAIAR--PAEIRFTDVLPKT 615
Cdd:PRK03584 534 AEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVL----AEGVTLDDALRARIRTTIrtNLSPRhvPDKIIAVPDIPRT 609
|
650
....*....|....
gi 6647434 616 RSGKIM----RRLL 625
Cdd:PRK03584 610 LSGKKVelpvKKLL 623
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
33-625 |
5.06e-88 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 287.79 E-value: 5.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 33 YEQLYSRAASNPEKFWGELAEQELHWFKKWDQVLDWQPPFAKWFVGGQLNISHNCLDRHLTT-WRRNKAAIIWEGePGDS 111
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNpLKRDQDALIYEC-PYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RII--TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PTZ00237 89 KTIklTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTK----------ADVTMTAGRDHWWHELQP----QQSAHCPA 255
Cdd:PTZ00237 169 ITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDitsesdlkkiETIPTIPNTLSWYDEIKKikenNQSPFYEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 256 EPIDSEDMLFILYTSGSTGKPKGVVHTTGG------YNLYTHMTTkwifdlKDTDVYWCTADVGWITGHSYIvYGPLSNG 329
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPhlvglkYYWRSIIEK------DIPTVVFSHSSIGWVSFHGFL-YGSLSLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 330 ATTVMYE-GVPRPSN-PGCFWDVIERYGVNIFYTAPTAIRAFIRM---GEAVPNARDLSSLRLLGTVGEPINPEAWMWYH 404
Cdd:PTZ00237 322 NTFVMFEgGIIKNKHiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 405 RVIgggKCPIVDTWWQTETGGIMLtpLPGAIPTKP-GSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPW-PSMIRDV 482
Cdd:PTZ00237 402 NKL---KIKSSRGYGQTEIGITYL--YCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMpPSFATTF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 YGDTDRFRHTYwehiqPKEGQYlYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:PTZ00237 477 YKNDEKFKQLF-----SKFPGY-YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYD 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 563 ELTGEAIFAFVSLEGNAEPSE----ELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PTZ00237 551 PDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
80-627 |
2.27e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 277.07 E-value: 2.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 80 QLNISHncLDRHLTTWRRNKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACS 159
Cdd:PRK06187 5 PLTIGR--ILRHGARKHPDKEAVYFDG-----RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 160 RIGA-PHSV-VFggFSAEALRDRLVDAEAKLVItADGGFRKdkaialkqEVDKALEHgAPSVENVIVVqrTKADVTMTAG 237
Cdd:PRK06187 78 KIGAvLHPInIR--LKPEEIAYILNDAEDRVVL-VDSEFVP--------LLAAILPQ-LPTVRTVIVE--GDGPAAPLAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 238 RDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTtggY-NLYTH-MTTKWIFDLKDTDVY--------- 306
Cdd:PRK06187 144 EVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS---HrNLFLHsLAVCAWLKLSRDDVYlvivpmfhv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 307 --WctadvGWItghsyivYGPLSNGATTVMyegvPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSS 384
Cdd:PRK06187 221 haW-----GLP-------YLALMAGAKQVI----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK--APRAYFVDFSS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 385 LRLLGTVGEPINP---EAWMWYHrvigggKCPIVDTWWQTETGGI--MLTPLPGAIP--TKPGSCTKPFPGIVAEIVDLD 457
Cdd:PRK06187 283 LRLVIYGGAALPPallREFKEKF------GIDLVQGYGMTETSPVvsVLPPEDQLPGqwTKRRSAGRPLPGVEARIVDDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 458 GNPVESDQG--GFLVIKQPWpsmIRDVY----GDTDRFRHTYWehiqpkegqylYFAGDGARRDKDGYFWVMGRVDDVIN 531
Cdd:PRK06187 357 GDELPPDGGevGEIIVRGPW---LMQGYwnrpEATAETIDGGW-----------LHTGDVGYIDEDGYLYITDRIKDVII 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 532 VSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEelkKDLVKHVTEEIGAIARPAEIRFTDV 611
Cdd:PRK06187 423 SGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDE 499
|
570
....*....|....*.
gi 6647434 612 LPKTRSGKIMRRLLRS 627
Cdd:PRK06187 500 LPRTSVGKILKRVLRE 515
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
88-626 |
5.52e-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: 267.70 E-value: 5.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTWRRNKAAIIwegepGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSV 167
Cdd:cd05959 9 VDLNLNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFGGFSAEALRDRLVDAEAKLVITADggfrkdkaiALKQEVDKALEHGAPSVENVIVVQRTKADvtmtAGRDhWWHELQP 247
Cdd:cd05959 84 VNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKSEHTLVVLIVSGGAGPE----AGAL-LLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 QQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTT--KWIFDLKDTDVYWCTADVGWITGHSYIVYGP 325
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHA--DIYWTAELyaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 326 LSNGATTVMYEGVPRPSNpgcFWDVIERYGVNIFYTAPTAIRAFIrmgeAVPNA--RDLSSLRLLGTVGEPINPEAWMWY 403
Cdd:cd05959 228 LSVGATTVLMPERPTPAA---VFKRIRRYRPTVFFGVPTLYAAML----AAPNLpsRDLSSLRLCVSAGEALPAEVGERW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 HRVIGggkCPIVDTWWQTETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVY 483
Cdd:cd05959 301 KARFG---LDILDGIGSTEMLHIFLSNRPGRV--RYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGP--SSATMYW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 484 GDTDRFRHTYwehiqpkEGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDE 563
Cdd:cd05959 374 NNRDKTRDTF-------QGEWTR-TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 564 LTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05959 446 DGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
98-627 |
1.52e-78 |
|
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: 259.73 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA----------PHSV 167
Cdd:cd05970 32 DKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAiaipathqltAKDI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFggfsaealrdRLVDAEAKLVITADGGfrkdkaiALKQEVDKALEHgAPSVENVIVVQRTKadvtmtagRDHW--WHEL 245
Cdd:cd05970 112 VY----------RIESADIKMIVAIAED-------NIPEEIEKAAPE-CPSKPKLVWVGDPV--------PEGWidFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 246 QPQQSA-----HCPAEPiDSEDMLFILYTSGSTGKPKGVVHTTGgYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSY 320
Cdd:cd05970 166 IKNASPdferpTANSYP-CGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 IVYGPLSNGATTVMYEGvpRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRmgeAVPNARDLSSLRLLGTVGEPINPEAw 400
Cdd:cd05970 244 KIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 401 mwYHRVIGGGKCPIVDTWWQTETGgIMLTPLPGAIPtKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVI----KQPWp 476
Cdd:cd05970 318 --FNTFKEKTGIKLMEGFGQTETT-LTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 SMIRDVYGDTDRfRHTYWehiqpKEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAA 556
Cdd:cd05970 393 GLFGGYYKDAEK-TAEVW-----HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 557 VVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:cd05970 465 VTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
98-622 |
3.87e-76 |
|
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: 250.22 E-value: 3.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:cd17631 10 DRTALVFGG-----RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVItadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaep 257
Cdd:cd17631 85 AYILADSGAKVLF------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 idsEDMLFILYTSGSTGKPKGVVHTTGgyNLyTHMTTKWIFDLKDT--DVYWCTADVGWITGHSYIVYGPLSNGATTVMy 335
Cdd:cd17631 98 ---DDLALLMYTSGTTGRPKGAMLTHR--NL-LWNAVNALAALDLGpdDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 egVPRPsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGTVGEPInPEAWMwyhRVIGGGKCPIV 415
Cdd:cd17631 171 --LRKF-DPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAPM-PERLL---RALQARGVKFV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGD---TDRFRHT 492
Cdd:cd17631 242 QGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVMAGYWNRpeaTAAAFRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 493 YWEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAF 572
Cdd:cd17631 320 GWFH-----------TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAV 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6647434 573 VSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMR 622
Cdd:cd17631 389 VVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
82-627 |
6.51e-74 |
|
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: 246.99 E-value: 6.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 82 NISHNCLDRhlttWRRNKA--------AIIWEGEPGDSRIITYAQLHREVCQFANAL-KSLGVQKGDRVAIYLPMIPEAA 152
Cdd:cd05928 6 NFASDVLDQ----WADKEKagkrppnpALWWVNGKGDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 153 ITMLACSRIGaphSVVFGG---FSAEALRDRLVDAEAKLVITADggfrkdkaiALKQEVDK-ALEhgAPSVENVIVVQRT 228
Cdd:cd05928 82 LVNVACIRTG---LVFIPGtiqLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSvASE--CPSLKTKLLVSEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 229 KadvtmtagRDHW--WHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVY 306
Cdd:cd05928 148 S--------RDGWlnFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 307 WCTADVGWITGHSYIVYGPLSNGATTVMYEgVPRpSNPGCFWDVIERYGVNIFYTAPTAIRAFIRmgeavpnaRDLSS-- 384
Cdd:cd05928 220 WNTSDTGWIKSAWSSLFEPWIQGACVFVHH-LPR-FDPLVILKTLSSYPITTFCGAPTVYRMLVQ--------QDLSSyk 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 385 ---LRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDLDGNPV 461
Cdd:cd05928 290 fpsLQHCVTGGEPLNPEVLEKWKAQTG---LDIYEGYGQTETGLICANFKGMKI--KPGSMGKASPPYDVQIIDDNGNVL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 462 ESDQGGFLVIK----QPWpSMIRDVYGDTDRFRHTYwehiqpkEGQYlYFAGDGARRDKDGYFWVMGRVDDVINVSGHRL 537
Cdd:cd05928 365 PPGTEGDIGIRvkpiRPF-GLFSGYVDNPEKTAATI-------RGDF-YLTGDRGIMDEDGYFWFMGRADDVINSSGYRI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 538 GTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEG--NAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKT 615
Cdd:cd05928 436 GPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKT 515
|
570
....*....|..
gi 6647434 616 RSGKIMRRLLRS 627
Cdd:cd05928 516 VTGKIQRNELRD 527
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
98-626 |
1.85e-73 |
|
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: 244.01 E-value: 1.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA---PHSVVFGgfsA 174
Cdd:cd05936 14 DKTALIFMGRK-----LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAvvvPLNPLYT---P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 175 EALRDRLVDAEAKLVITADGgFRKdkaialkqevdkALEHGAPSVENVIVvqrtkadvtmtagrdhwwhelqpqqsahcp 254
Cdd:cd05936 86 RELEHILNDSGAKALIVAVS-FTD------------LLAAGAPLGERVAL------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 aepiDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTT--KWIFDLKD-TDVYWCTADVgwitghsYIVYG------- 324
Cdd:cd05936 123 ----TPEDVAVLQYTSGTTGVPKGAMLTHR--NLVANALQikAWLEDLLEgDDVVLAALPL-------FHVFGltvalll 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 325 PLSNGATTVMyegVPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFIRMGEavPNARDLSSLRLLGTVGEPINPEAWMWYH 404
Cdd:cd05936 190 PLALGATIVL---IPRFRPIGVL-KEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 405 RVIGggkCPIVDTWWQTETG-GIMLTPLPGaiPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmirdvy 483
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSpVVAVNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 484 gdtDRFRhTYWEhiQPKEGQ------YLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAV 557
Cdd:cd05936 330 ---QVMK-GYWN--RPEETAeafvdgWLR-TGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6647434 558 VGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05936 403 VGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
110-626 |
4.36e-69 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 231.58 E-value: 4.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd05919 7 ADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ItadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepIDSEDMLFILYT 269
Cdd:cd05919 87 V-------------------------------------------------------------------TSADDIAYLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADV--GWITGHSyiVYGPLSNGATTVMYEGVPRPSNpgcF 347
Cdd:cd05919 100 SGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLNPGWPTAER---V 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 348 WDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSSLRLLGTVGEPINPEAWmwyHRVIGGGKCPIVDTWWQTETGGIM 427
Cdd:cd05919 175 LATLARFRPTVLYGVPTFYANLLD--SCAGSPDALRSLRLCVSAGEALPRGLG---ERWMEHFGGPILDGIGATEVGHIF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 428 LTPLPGAIptKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMirdvygdtdrfrhTYWEHIQPKEGQYL-- 505
Cdd:cd05919 250 LSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAV-------------GYWNNPEKSRATFNgg 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 506 -YFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEE 584
Cdd:cd05919 315 wYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQES 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6647434 585 LKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05919 395 LARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
110-621 |
9.05e-69 |
|
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: 232.10 E-value: 9.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITAdggfrkdkaialKQEVDKALE--HGAPSVENVIVVQRTKADVTmtaGRDHWWHELQPQQSAHCPAEPIDS-EDMLFI 266
Cdd:cd05911 87 FTD------------PDGLEKVKEaaKELGPKDKIIVLDDKPDGVL---SIEDLLSPTLGEEDEDLPPPLKDGkDDTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 267 LYTSGSTGKPKGVV--HttggYNL---YTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLsNGATTVMyegVPRP 341
Cdd:cd05911 152 LYSSGTTGLPKGVClsH----RNLianLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVII---MPKF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 342 sNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNarDLSSLRLLGTVGEPINPEAwmwYHRVIG-GGKCPIVDTWWQ 420
Cdd:cd05911 224 -DSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKY--DLSSLRVILSGGAPLSKEL---QELLAKrFPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 421 TETGGIMLTPLPGaiPTKPGSCTKPFPGIVAEIVDLDGNP-VESDQGGFLVIK--QPWP----------SMIrdvygDTD 487
Cdd:cd05911 298 TETGGILTVNPDG--DDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRgpQVMKgyynnpeatkETF-----DED 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 488 RFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGE 567
Cdd:cd05911 371 GWLHT----------------GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 568 AIFAFVSLEGNAEPSEelkKDLVKHVTEEIGAIAR-PAEIRFTDVLPKTRSGKIM 621
Cdd:cd05911 435 LPRAYVVRKPGEKLTE---KEVKDYVAKKVASYKQlRGGVVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
112-626 |
1.57e-66 |
|
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: 224.09 E-value: 1.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA---PHSVVFGGfsaEALRDRLVDAEAKL 188
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAvlvPINTALRG---DELAYIIDHSGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITAdggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcPAEpidsedmlfILY 268
Cdd:cd05934 79 VVVD-------------------------------------------------------------PAS---------ILY 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTtggYNLYTHM--TTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMyegVPRPSnPGC 346
Cdd:cd05934 89 TSGTTGPPKGVVIT---HANLTFAgyYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRFS-ASR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 347 FWDVIERYGVNIFYTAPTAIRAFIRMGEAvPNARDlSSLRLLGtvGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGI 426
Cdd:cd05934 162 FWSDVRRYGATVTNYLGAMLSYLLAQPPS-PDDRA-HRLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 427 MLTPLPGaiPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIK-QPWPSMIRDVYGDTD----RFRHTyWEHiqpke 501
Cdd:cd05934 235 VIGPRDE--PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYYNMPEataeAMRNG-WFH----- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 502 gqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEP 581
Cdd:cd05934 307 ------TGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL 380
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 6647434 582 SEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05934 381 DPE---ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
112-626 |
1.54e-65 |
|
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: 222.35 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvvfggfsaealrdrlvdaeaklVI 190
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGA-------------------------IA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADGGFRKDKaialkqEVDKALEHGAPSVenVIVVQRTKAdvtmtagrdhwwhelqpqqsahcpaepidSEDMLFILYTS 270
Cdd:cd05958 64 VATMPLLRPK------ELAYILDKARITV--ALCAHALTA-----------------------------SDDICILAFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 271 GSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGvprpSNPGCFWDV 350
Cdd:cd05958 107 GTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE----ATPDLLLSA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 351 IERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTP 430
Cdd:cd05958 183 IARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFHIFISA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 431 LPGAIptKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmiRDVYGDTDRFRHTYWEhiqpkeGQYLYfAGD 510
Cdd:cd05958 258 RPGDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-----TGCRYLADKRQRTYVQ------GGWNI-TGD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 511 GARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLV 590
Cdd:cd05958 324 TYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQ 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 6647434 591 KHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05958 404 DHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
98-626 |
1.73e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 216.34 E-value: 1.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:PRK08316 26 DKTALVFGD-----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITADGGF-RKDKAIALKQEVDKALEHGAPSVEnvivvqrtkadvtmTAGRDHWWHELQPQQSAHCPAE 256
Cdd:PRK08316 101 AYILDHSGARAFLVDPALApTAEAALALLPVDTLILSLVLGGRE--------------APGGWLDFADWAEAGSVAEPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 257 PIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDV-------YWCTA-DVgwitghsyiVYGP-LS 327
Cdd:PRK08316 167 ELADDDLAQILYTSGTESLPKGAMLTHRAL-IAEYVSCIVAGDMSADDIplhalplYHCAQlDV---------FLGPyLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 328 NGATTVMyegVPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSSLRLlGTVGEPINPEAwmwyhrVI 407
Cdd:PRK08316 237 VGATNVI---LDAPDPELIL-RTIEAERITSFFAPPTVWISLLR--HPDFDTRDLSSLRK-GYYGASIMPVE------VL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 G--GGKCPIVDTW---WQTETGgimltPL-----PGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpS 477
Cdd:PRK08316 304 KelRERLPGLRFYncyGQTEIA-----PLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP--Q 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 478 MIRDVYGDTDR----FRHTyWEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVA 553
Cdd:PRK08316 377 LMLGYWDDPEKtaeaFRGG-WFH-----------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 554 EAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK08316 445 EVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
108-626 |
4.61e-61 |
|
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: 211.79 E-value: 4.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 108 PGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA------PHSvvfggfSAEALRDRL 181
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAvvaplnPAY------KKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 182 VDAEAKLVITADGGFrkdkaialkqevdkalehgAPSVENVIVVQRTKADVTMTAGRDHWW---HELQPQQSAHCPAEPI 258
Cdd:cd05926 83 ADLGSKLVLTPKGEL-------------------GPASRAASKLGLAILELALDVGVLIRApsaESLSNLLADKKNAKSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 ---DSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTTkwIfdlkdTDVYWCT-ADVGWITGHSYIVYG-------PLS 327
Cdd:cd05926 144 gvpLPDDLALILHTSGTTGRPKGVPLTHR--NLAASATN--I-----TNTYKLTpDDRTLVVMPLFHVHGlvasllsTLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 328 NGATTVMyegvPRPSNPGCFWDVIERYGVNiFYTA-PTAIRAFIRMGEAVPNARdLSSLRLLGTVGEPINPEAWMWYHRV 406
Cdd:cd05926 215 AGGSVVL----PPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNRPEPNPESP-PPKLRFIRSCSASLPPAVLEALEAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 407 IGggkCPIVDTWWQTETGGIM-LTPLPgAIPTKPGSCTKPFpGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGD 485
Cdd:cd05926 289 FG---APVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 ---------TDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAA 556
Cdd:cd05926 362 peanaeaafKDGWFRT----------------GDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAV 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 557 VVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05926 426 AFGVPDEKYGEEVAAAVVLREGASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
98-626 |
2.46e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 210.15 E-value: 2.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:PRK07656 20 DKEAYVFGDQR-----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITADGgFrkdkaialkQEVDKALEHGAPSVENVIVVQRTKADvtMTAGRDHWWHELQPQQSAHCPAEP 257
Cdd:PRK07656 95 AYILARGDAKALFVLGL-F---------LGVDYSATTRLPALEHVVICETEEDD--PHTEKMKTFTDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHmTTKW--IFDLKDTDVYWCTA--------DVGWITghsyivygPLS 327
Cdd:PRK07656 163 VDPDDVADILFTSGTTGRPKGAMLTHR--QLLSN-AADWaeYLGLTEGDRYLAANpffhvfgyKAGVNA--------PLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 328 NGATTVmyegvPRPS-NPGCFWDVIERYGVNIFYTAPTAIRAFIrmgeAVPNAR--DLSSLRLLGTVGEPINPEAwmwYH 404
Cdd:PRK07656 232 RGATIL-----PLPVfDPDEVFRLIETERITVLPGPPTMYNSLL----QHPDRSaeDLSSLRLAVTGAASMPVAL---LE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 405 RVIGGGKCPIVDTWWQ-TETGGIM-LTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDV 482
Cdd:PRK07656 300 RFESELGVDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 YGDTDRFRHTywehIQPkEGqYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:PRK07656 378 YDDPEATAAA----IDA-DG-WLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPD 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6647434 563 ELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK07656 451 ERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
114-629 |
1.12e-59 |
|
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: 206.26 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA---PHSVVFGgfsAEALRDRLvdaeaklvi 190
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAvviPATTLLT---PDDLRDRV--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 tadggfrkdkaialkqevdkalEHGAPSVenVIVVQRTKADvtmtagrdhwwhelqpqqsahcpaepidseDMLFILYTS 270
Cdd:cd05974 69 ----------------------DRGGAVY--AAVDENTHAD------------------------------DPMLLYFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 271 GSTGKPKGVVHTTGGYNLyTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEgVPRpSNPGCFWDV 350
Cdd:cd05974 95 GTTSKPKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFN-YAR-FDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 351 IERYGVNIFYTAPTAIRAFIRMgeavPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGgIMLTP 430
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRMLIQQ----DLASFDVKLREVVGAGEPLNPEVIEQVRRAWG---LTIRDGYGQTETT-ALVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 431 LPGAiPTKPGSCTKPFPGIVAEIVDLDGNPVesDQGGF-LVIKQPWPSMIRDVY-GDTDRFRHTYwehiqpkEGQYlYFA 508
Cdd:cd05974 244 SPGQ-PVKAGSMGRPLPGYRVALLDPDGAPA--TEGEVaLDLGDTRPVGLMKGYaGDPDKTAHAM-------RGGY-YRT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 509 GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKD 588
Cdd:cd05974 313 GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALE 392
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 6647434 589 LVKHVTEEIGAIARPAEIRFTDvLPKTRSGKIMRRLLRSLA 629
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
96-627 |
4.68e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 198.67 E-value: 4.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRNKAAIIWegepgDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAE 175
Cdd:PRK06188 25 YPDRPALVL-----GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 176 ALRDRLVDAEAKLVITADGGFRkDKAIALKQevdkalehGAPSVENVIVVQRTKADVTMTAGRDHWwhELQPQQSAHCPA 255
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPAPFV-ERALALLA--------RVPSLKHVLTLGPVPDGVDLLAAAAKF--GPAPLVAAALPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 256 EPIdsedmlFILYTSGSTGKPKGVVHTTGGYnlyTHMTTkwifdlkdtdvyWCTADVGWITGHSYIVYGPLSN------- 328
Cdd:PRK06188 169 DIA------GLAYTGGTTGKPKGVMGTHRSI---ATMAQ------------IQLAEWEWPADPRFLMCTPLSHaggaffl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 329 -----GATTVMYEGVprpsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVpnARDLSSLRLLGTVGEPINP----EA 399
Cdd:PRK06188 228 ptllrGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLR--TRDLSSLETVYYGASPMSPvrlaEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 400 wmwyHRVIGggkcPI-VDTWWQTETGgIMLTPLPGA--IPTKP---GSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQ 473
Cdd:PRK06188 302 ----IERFG----PIfAQYYGQTEAP-MVITYLRKRdhDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 474 PwpsMIRDvygdtdrfrhTYWEhiQPKE------GQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALV 547
Cdd:PRK06188 373 P---LVMD----------GYWN--RPEEtaeafrDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 548 SHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:PRK06188 437 EHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
98-625 |
1.21e-55 |
|
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: 195.44 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA------PHsvvfgg 171
Cdd:cd05930 2 DAVAVVDGDQS-----LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAayvpldPS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 172 FSAEALRDRLVDAEAKLVITadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsa 251
Cdd:cd05930 71 YPAERLAYILEDSGAKLVLT------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 252 hcpaepiDSEDMLFILYTSGSTGKPKGVVHTTGGY-NLYTHMTTKwiFDLKDTDVYWCTA----DVGWitghsYIVYGPL 326
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRGLvNLLLWMQEA--YPLTPGDRVLQFTsfsfDVSV-----WEIFGAL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 SNGATTVMyegVPR--PSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpnaRDLSSLRLLGTVGEPINPEAWMWYH 404
Cdd:cd05930 157 LAGATLVV---LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL----AALPSLRLVLVGGEALPPDLVRRWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 405 RVIGGGK---------CPIVDTWWQTETGGIMLTPLP-GaiptkpgsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQP 474
Cdd:cd05930 230 ELLPGARlvnlygpteATVDATYYRVPPDDEEDGRVPiG----------RPIPNTRVYVLDENLRPVPPGVPGELYIGGA 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 475 wpSMIRDVYGDTD----RFRHTYWEhiqpkEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHR--LGtmEIESALVS 548
Cdd:cd05930 300 --GLARGYLNRPEltaeRFVPNPFG-----PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRieLG--EIEAALLA 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 549 HPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd05930 371 HPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-629 |
1.57e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 199.80 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLAcsriGAPHSVVF---GGFSAEALRDRLVDAEAKLVI 190
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANpinPLLEPEQIAELLRAAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TAdGGFRKdkaIALKQEVDKALEHgAPSVENVIVV----------------QRTKADVtmtagRDHWWHELQPQQSA--H 252
Cdd:PRK07529 135 TL-GPFPG---TDIWQKVAEVLAA-LPELRTVVEVdlarylpgpkrlavplIRRKAHA-----RILDFDAELARQPGdrL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 253 CPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGyNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATT 332
Cdd:PRK07529 205 FSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 333 VMyegvPRPS---NPGC---FWDVIERYGVNIFYTAPTAIRAFIRmgeaVP-NARDLSSLRLLGTVGEPINPEAWMWYHR 405
Cdd:PRK07529 284 VL----ATPQgyrGPGVianFWKIVERYRINFLSGVPTVYAALLQ----VPvDGHDISSLRYALCGAAPLPVEVFRRFEA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 406 VIGggkCPIVDTWWQTE-TGGIMLTPLPGaiPTKPGSCTKPFPGIVAEIVDLDGN-----PVESDQGGFLVIKQPwpsmi 479
Cdd:PRK07529 356 ATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYQRVRVVILDDAgrylrDCAVDEVGVLCIAGP----- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 480 rDVYGD--TDRFRHTYWehiqpKEGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAV 557
Cdd:PRK07529 426 -NVFSGylEAAHNKGLW-----LEDGWLN-TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 558 VGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGA-IARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK07529 499 VGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
88-632 |
2.48e-52 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 189.11 E-value: 2.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTWRRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSV 167
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFGGFSAEALRDRLVDAEAKLVItADGGFRK-DKAialkqEVDKALEHGAPSVENVIVVQRTKAD--VTMTAGRdHWwhE 244
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLV-VPKTFRGfDHA-----AMARRLRPELPALRHVVVVGGDGADsfEALLITP-AW--E 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 245 LQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGgynlyTHMTTKWIF----DLKDTDVYWCTADVGWITGHSY 320
Cdd:PRK13295 181 QEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAN-----TLMANIVPYaerlGLGADDVILMASPMAHQTGFMY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 IVYGPLSNGATTVMYEgvprPSNPGCFWDVIERYGVNiFYTAPTAiraFIR-MGEAVP-NARDLSSLRLLGTVGEPInPE 398
Cdd:PRK13295 256 GLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP---FLTdLTRAVKeSGRPVSSLRTFLCAGAPI-PG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 399 AWMWYHRVIGGGKcpIVDTWWQTETGGIMLTpLPGAIPTKPGS---CtkPFPGIVAEIVDLDGNPVESDQGGFLVIKQPW 475
Cdd:PRK13295 327 ALVERARAALGAK--IVSAWGMTENGAVTLT-KLDDPDERASTtdgC--PLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 476 --------PSMIRDvygDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALV 547
Cdd:PRK13295 402 nfggylkrPQLNGT---DADGWFDT----------------GDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 548 SHPLVAEAAVVGRPDELTGEAIFAFVSLegnaEPSEELKKDLVKHVTEEIGaIAR---PAEIRFTDVLPKTRSGKIMRRL 624
Cdd:PRK13295 463 RHPAIAQVAIVAYPDERLGERACAFVVP----RPGQSLDFEEMVEFLKAQK-VAKqyiPERLVVRDALPRTPSGKIQKFR 537
|
....*...
gi 6647434 625 LRSLASGQ 632
Cdd:PRK13295 538 LREMLRGE 545
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
112-627 |
8.35e-52 |
|
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: 186.91 E-value: 8.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIT 191
Cdd:TIGR03098 24 RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 ADGGFRKdkaialkqevdkaLEHGAPSVEN----VIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDSeDMLFIL 267
Cdd:TIGR03098 104 SSERLDL-------------LHPALPGCHDlrtlIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVIDS-DMAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVVHT-----TGGYNLYTHMttkwifDLKDTDVYWCTADVGWITGHSYIVYGpLSNGATTVMYEGV-PRp 341
Cdd:TIGR03098 170 YTSGSTGRPKGVVLShrnlvAGAQSVATYL------ENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDYLlPR- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 342 snpgcfwDVI---ERYGVNIFYTAPTairAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKcpIVDTW 418
Cdd:TIGR03098 242 -------DVLkalEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTETGGIMLTPlPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSM--IRDVYGDTDRFRHTYWEH 496
Cdd:TIGR03098 310 GLTEAFRSTYLP-PEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMgyWNDPEKTAERFRPLPPFP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 497 IQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLE 576
Cdd:TIGR03098 389 GELHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPP 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 6647434 577 GNAepsEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:TIGR03098 469 GGE---ELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
12-627 |
1.78e-51 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 189.91 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 12 ERLFDPPTEFSErayvrsgreyeqLYSRAASNPEKFWGE-LAEQELHWFKKWDQVLDWQP---PFAKWFVGGQLNISHNC 87
Cdd:PLN03052 113 SKYKDPISSFSE------------FQRFSVENPEVYWSIvLDELSLVFSVPPRCILDTSDesnPGGQWLPGAVLNVAECC 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 L----DRHLttwrrNKAAIIWEGEPGDS---RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACsr 160
Cdd:PLN03052 181 LtpkpSKTD-----DSIAIIWRDEGSDDlpvNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAI-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 161 IGAPHSVVF--GGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVdkaLEHGAPSvenVIVVQRTKADVTMT-AG 237
Cdd:PLN03052 254 ILAGCVVVSiaDSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRV---VEAKAPK---AIVLPADGKSVRVKlRE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 238 RDHWWHE-------LQPQQSAHCPAEPIDSedMLFILYTSGSTGKPKGV--VHTT---GGYNLYTHMttkwifDLKDTDV 305
Cdd:PLN03052 328 GDMSWDDflarangLRRPDEYKAVEQPVEA--FTNILFSSGTTGEPKAIpwTQLTplrAAADAWAHL------DIRKGDI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 306 Y-WCTaDVGWITGHsYIVYGPLSNGATTVMYEGVPRPSNPGCFwdvIERYGVNIFYTAPTAIRAFIRMGeaVPNARDLSS 384
Cdd:PLN03052 400 VcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSS 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 385 LRLLGTVGEPINPEAWMWyhrVIG-GGKCPIVDTWWQTETGGIMLTplpGAI--PTKPGSCTKPFPGIVAEIVDLDGNPV 461
Cdd:PLN03052 473 IRCFGSTGEASSVDDYLW---LMSrAGYKPIIEYCGGTELGGGFVT---GSLlqPQAFAAFSTPAMGCKLFILDDSGNPY 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 462 ESDQG--GFLVIkqpWPSMirdvYGDTDRF---RH--TYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSG 534
Cdd:PLN03052 547 PDDAPctGELAL---FPLM----FGASSTLlnaDHykVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGG 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 535 HRLGTMEIESAL-VSHPLVAEAAVV------GRPDELTgeaIFAFVSLEGNAEPS-EELKKDLVKHVTEEIGAIARPAEI 606
Cdd:PLN03052 620 IKVSSVEIERVCnAADESVLETAAIgvpppgGGPEQLV---IAAVLKDPPGSNPDlNELKKIFNSAIQKKLNPLFKVSAV 696
|
650 660
....*....|....*....|.
gi 6647434 607 RFTDVLPKTRSGKIMRRLLRS 627
Cdd:PLN03052 697 VIVPSFPRTASNKVMRRVLRQ 717
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
112-625 |
3.74e-51 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 184.75 E-value: 3.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIT 191
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 AdggfrkdkaialKQEVDKALEHGAPsvenVIVVQRTKADvtmtagRDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSG 271
Cdd:cd05904 111 T------------AELAEKLASLALP----VVLLDSAEFD------SLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 272 STGKPKGVVHTTGgyNLYTHMT-TKWIFDLKDT--DVYWCTADVGWITGHSYIVYGPLSNGATTVMyegVPRPSNPGCFw 348
Cdd:cd05904 169 TTGRSKGVMLTHR--NLIAMVAqFVAGEGSNSDseDVFLCVLPMFHIYGLSSFALGLLRLGATVVV---MPRFDLEELL- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggKCPIVDTWWQTETGGIM- 427
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFP--NVDLGQGYGMTESTGVVa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 428 LTPLPGAIPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPwpSMIRDVYG---------DTDRFRHTywehi 497
Cdd:cd05904 319 MCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGP--SIMKGYLNnpeataatiDKEGWLHT----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 498 qpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEG 577
Cdd:cd05904 392 -----------GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6647434 578 NAEPSEELKKDLV-KHVteeigaiARPAEIR---FTDVLPKTRSGKIMRRLL 625
Cdd:cd05904 461 GSSLTEDEIMDFVaKQV-------APYKKVRkvaFVDAIPKSPSGKILRKEL 505
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
88-629 |
1.26e-49 |
|
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: 181.11 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTWRR---NKAAIIwegepGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA- 163
Cdd:COG1021 27 LGDLLRRRAErhpDRIAVV-----DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAi 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 164 PhsvVF----------GGFSAEalrdrlvdAEAKLVITAD--GGFRKDK-AIALKQEVdkalehgaPSVENVIVVQRTKA 230
Cdd:COG1021 102 P---VFalpahrraeiSHFAEQ--------SEAVAYIIPDrhRGFDYRAlARELQAEV--------PSLRHVLVVGDAGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 231 DVTMTAGRDHwwhelqpqqSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTA 310
Cdd:COG1021 163 FTSLDALLAA---------PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 311 DVgwitGHSYI-----VYGPLSNGATTVMyegVPRPSNPGCFwDVIERYGVNIfyTA--PTAIRAFIrmgEAVPNAR-DL 382
Cdd:COG1021 233 PA----AHNFPlsspgVLGVLYAGGTVVL---APDPSPDTAF-PLIERERVTV--TAlvPPLALLWL---DAAERSRyDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 383 SSLRLLgtvgepinpeawmwyhrVIGGGKCP------IVDTWWQT--------EtGGIMLTPL---PGAIPT---KPGSc 442
Cdd:COG1021 300 SSLRVL-----------------QVGGAKLSpelarrVRPALGCTlqqvfgmaE-GLVNYTRLddpEEVILTtqgRPIS- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 443 tkpfPGIVAEIVDLDGNPVESDQGGFLVIKQPWpsMIRDVYG---------DTDRFRHTywehiqpkegqylyfaGDGAR 513
Cdd:COG1021 361 ----PDDEVRIVDEDGNPVPPGEVGELLTRGPY--TIRGYYRapehnarafTPDGFYRT----------------GDLVR 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 514 RDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGnaepsEELK-KDLVKH 592
Cdd:COG1021 419 RTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRG-----EPLTlAELRRF 493
|
570 580 590
....*....|....*....|....*....|....*...
gi 6647434 593 VTE-EIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:COG1021 494 LRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
115-626 |
8.41e-47 |
|
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: 171.02 E-value: 8.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD- 193
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPEr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 -GGFRkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwHELQPQQSAhcpaepidsedmlFILYTSGS 272
Cdd:cd05903 83 fRQFD---------------------------------------------PAAMPDAVA-------------LLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVVHTTGGYNLYTHMTTKWIfDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEgvprpsnpgcFWD--- 349
Cdd:cd05903 105 TGEPKGVMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----------IWDpdk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 350 ---VIERYGVNIFYTAPTAIRAFIRMGEAVPnaRDLSSLRLLGTVGEPINP----EAWMwyhrvIGGGKcpIVDTWWQTE 422
Cdd:cd05903 174 alaLMREHGVTFMMGATPFLTDLLNAVEEAG--EPLSRLRTFVCGGATVPRslarRAAE-----LLGAK--VCSAYGSTE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 423 TGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMirdVYGDTDRfrhtywEHIQPKEG 502
Cdd:cd05903 245 CPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP--SV---FLGYLDR------PDLTADAA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 503 QYLYF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEP 581
Cdd:cd05903 314 PEGWFrTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6647434 582 SEElkkDLVKHVTEEigAIAR---PAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05903 394 TFD---ELVAYLDRQ--GVAKqywPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
101-619 |
1.48e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 172.76 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWegepGDsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDR 180
Cdd:PRK07798 21 ALVC----GD-RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 181 LVDAEAKLVItADGGFRkDKAIALKQEvdkalehgAPSVENVIVVQRTKADVTMTAGRDhwWHELQPQQSAHCPAEPiDS 260
Cdd:PRK07798 96 LDDSDAVALV-YEREFA-PRVAEVLPR--------LPKLRTLVVVEDGSGNDLLPGAVD--YEDALAAGSPERDFGE-RS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHTT--------GGYNLYTHMTTKwifdlkdtDVYWCTADVGWITGHSYIVYGPLSNGA-- 330
Cdd:PRK07798 163 PDDLYLLYTGGTTGMPKGVMWRQedifrvllGGRDFATGEPIE--------DEEELAKRAAAGPGMRRFPAPPLMHGAgq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 -----------TTVMYegvPRPS-NPGCFWDVIERYGVN-IFYT----APTAIRAFIRMGEAvpnarDLSSLRLLGTVGE 393
Cdd:PRK07798 235 waafaalfsgqTVVLL---PDVRfDADEVWRTIEREKVNvITIVgdamARPLLDALEARGPY-----DLSSLFAIASGGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 394 PINPEAWMWYHRVIgggkcP---IVDTWWQTETGGIML-TPLPGAIPTkpGSCT-KPFPGIVaeIVDLDGNPVE--SDQG 466
Cdd:PRK07798 307 LFSPSVKEALLELL-----PnvvLTDSIGSSETGFGGSgTVAKGAVHT--GGPRfTIGPRTV--VLDEDGNPVEpgSGEI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 467 GFLVIKQPWPSmirDVYGDTDRFRHTYWEHiqpkEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESAL 546
Cdd:PRK07798 378 GWIARRGHIPL---GYYKDPEKTAETFPTI----DGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEAL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 547 VSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGK 619
Cdd:PRK07798 451 KAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
123-626 |
4.00e-46 |
|
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: 169.93 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 123 VCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVF----GGFSAEALRDRLVDAEAKLVITADGGFRK 198
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 199 DKAialkqevdkalehgapsvenVIVVQRtkaDVTMTAGRDHWWHELQPQqsahcPAEPIDSEDMLFILYTSGSTGKPKG 278
Cdd:cd05922 83 LRD--------------------ALPASP---DPGTVLDADGIRAARASA-----PAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 279 VVHTTggYNL-YTHMTTKWIFDLKDTDVYWCTADVGWITGHSyIVYGPLSNGATTVMYE-GVPrpsnPGCFWDVIERYGV 356
Cdd:cd05922 135 VRLSH--QNLlANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVLTNdGVL----DDAFWEDLREHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 357 NIFYTAPTAIRAFIRMGEAvPNArdLSSLRLLGTVGEPINPEAWMWYHRVIGGGKcpIVDTWWQTETGGIMLTPLPGAIP 436
Cdd:cd05922 208 TGLAGVPSTYAMLTRLGFD-PAK--LPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEATRRMTYLPPERIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 437 TKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPSMirdvygdtdrfrhTYWEHIQ----PKEGQYLYFAGDGA 512
Cdd:cd05922 283 EKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMK-------------GYWNDPPyrrkEGRGGGVLHTGDLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 513 RRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELtGEAIFAFVSLEGNAEPseelkKDLVKH 592
Cdd:cd05922 350 RRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP-----KDVLRS 423
|
490 500 510
....*....|....*....|....*....|....
gi 6647434 593 VTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05922 424 LAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
98-626 |
7.53e-46 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 170.25 E-value: 7.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVFGGFSAEAL 177
Cdd:PRK08008 22 HKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA----IMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDR----LVDAEAKLVITAD---GGFRkdkaiALKQEVDKALEH------GAPSVENVIVVQRTKAdvtmtagrdhwwhe 244
Cdd:PRK08008 98 REEsawiLQNSQASLLVTSAqfyPMYR-----QIQQEDATPLRHicltrvALPADDGVSSFTQLKA-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 245 lqpQQSAH-CPAEPIDSEDMLFILYTSGSTGKPKGVVHTTggYNL-YTHMTTKWIFDLKDTDVYW-----------CTAd 311
Cdd:PRK08008 159 ---QQPATlCYAPPLSTDDTAEILFTSGTTSRPKGVVITH--YNLrFAGYYSAWQCALRDDDVYLtvmpafhidcqCTA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 312 vgwitghsyiVYGPLSNGATTVMYEgvprPSNPGCFWDVIERYGVNIFYTAPTAIRAFIrMGEAVPNARDlSSLRLLgtv 391
Cdd:PRK08008 233 ----------AMAAFSAGATFVLLE----KYSARAFWGQVCKYRATITECIPMMIRTLM-VQPPSANDRQ-HCLREV--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 392 gepinpeawMWYHRVIGGGK--------CPIVDTWWQTETggimltpLPGAIPTKPG------SCTKPFPGIVAEIVDLD 457
Cdd:PRK08008 294 ---------MFYLNLSDQEKdafeerfgVRLLTSYGMTET-------IVGIIGDRPGdkrrwpSIGRPGFCYEAEIRDDH 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 458 GNPVESDQGGFLVIK-QPWPSMIRDVYGDTDR----FRHTYWEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINV 532
Cdd:PRK08008 358 NRPLPAGEIGEICIKgVPGKTIFKEYYLDPKAtakvLEADGWLH-----------TGDTGYVDEEGFFYFVDRRCNMIKR 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 533 SGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVL 612
Cdd:PRK08008 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDL 503
|
570
....*....|....
gi 6647434 613 PKTRSGKIMRRLLR 626
Cdd:PRK08008 504 PRNCSGKIIKKNLK 517
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
110-625 |
4.19e-45 |
|
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: 166.71 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepiDSEDMLFILYT 269
Cdd:cd17643 89 LT-------------------------------------------------------------------DPDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGgyNLYTHMT-TKWIFDLKDTDVywctadvgWITGHSYI-------VYGPLSNGATTVMYE-GVPR 340
Cdd:cd17643 102 SGSTGRPKGVVVSHA--NVLALFAaTQRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLVVVPyEVAR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 341 PsnPGCFWDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLRLLGTVGEPINPeAWM--WYHRVigGGKCP-IVDT 417
Cdd:cd17643 172 S--PEDFARLLRDEGVTVLNQTPSAFYQL--VEAADRDGRDPLALRYVIFGGEALEA-AMLrpWAGRF--GLDRPqLVNM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 418 WWQTET----GGIMLTP--LPGAIPTKPGsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYG----DTD 487
Cdd:cd17643 245 YGITETtvhvTFRPLDAadLPAAAASPIG---RPLPGLRVYVLDADGRPVPPGVVGELYVSGA--GVARGYLGrpelTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 488 RFRhtywEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGE 567
Cdd:cd17643 320 RFV----ANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDT 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 568 AIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17643 396 RLVAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
98-625 |
6.01e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 168.21 E-value: 6.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGepgdsRIITYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEA 176
Cdd:PRK08314 25 DKTAIVFYG-----RAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 177 LRDRLVDAEAKLVITADggfrkdkaiALKQEVDKAleHGAPSVENVIVVQ-----------------RTKADVTMTA-GR 238
Cdd:PRK08314 100 LAHYVTDSGARVAIVGS---------ELAPKVAPA--VGNLRLRHVIVAQysdylpaepeiavpawlRAEPPLQALApGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 239 DHWWHELQPQQSAHCPAEpIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWiFDLKDTDVYWCTADVGWITGH 318
Cdd:PRK08314 169 VVAWKEALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFHVTGM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 319 SYIVYGPLSNGATTVMyegVPRpsnpgcfWD------VIERYGVNIFYTAPTAIRAFIrmgeAVPN--ARDLSSLRLLGT 390
Cdd:PRK08314 247 VHSMNAPIYAGATVVL---MPR-------WDreaaarLIERYRVTHWTNIPTMVVDFL----ASPGlaERDLSSLRYIGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 391 VGEPInPEAwmwyhrvigggkcpiVDTWWQTETG-----GIMLTPLPGAIPTKPGSCTK------PFPGIVAEIVDLD-G 458
Cdd:PRK08314 313 GGAAM-PEA---------------VAERLKELTGldyveGYGLTETMAQTHSNPPDRPKlqclgiPTFGVDARVIDPEtL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 459 NPVESDQGGFLVIKQpwPSMIRDVYGDTDRFRHTYWEhiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLG 538
Cdd:PRK08314 377 EELPPGEVGEIVVHG--PQVFKGYWNRPEATAEAFIE----IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVW 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 539 TMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL--EGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTR 616
Cdd:PRK08314 451 PAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLrpEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSG 527
|
....*....
gi 6647434 617 SGKIMRRLL 625
Cdd:PRK08314 528 SGKILWRQL 536
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
114-625 |
7.98e-45 |
|
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: 165.73 E-value: 7.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhELqpqqsahcpaepidsEDMLFILYTSGST 273
Cdd:cd05935 82 --------------------------------------------------EL---------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGGYNLYTHMTTKWiFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSNPgcfwDVIER 353
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVW-TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETAL----ELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 354 YGVNIFYTAPTAIRAFIrmgeAVPN--ARDLSSLRLLGTVGEPInPEAWMwyHRVIGGGKCPIVDTWWQTETggimLTPL 431
Cdd:cd05935 172 YKVTFWTNIPTMLVDLL----ATPEfkTRDLSSLKVLTGGGAPM-PPAVA--EKLLKLTGLRFVEGYGLTET----MSQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 432 PGAIPTKPGSCTK--PFPGIVAEIVDL-DGNPVESDQGGFLVIKQPwpSMIRDVYGDTDRFRHTYWEhiqpKEGQYLYFA 508
Cdd:cd05935 241 HTNPPLRPKLQCLgiP*FGVDARVIDIeTGRELPPNEVGEIVVRGP--QIFKGYWNRPEETEESFIE----IKGRRFFRT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 509 GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL--EGNAEPSEElk 586
Cdd:cd05935 315 GDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLrpEYRGKVTEE-- 392
|
490 500 510
....*....|....*....|....*....|....*....
gi 6647434 587 kDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd05935 393 -DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
101-625 |
1.49e-44 |
|
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: 165.84 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDR 180
Cdd:cd12117 15 AVVYGD-----RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 181 LVDAEAKLVITADGGFRKDKAIALKQEVDKALEHGAPSVenvivvqrtkadvtmtagrdhwwhelqpqqsahcPAEPIDS 260
Cdd:cd12117 90 LADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGN----------------------------------PAVPVSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVvhttggynLYTH-------MTTKWIfDLKDTDVYWCTADVGWiTGHSYIVYGPLSNGATTV 333
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGV--------AVTHrgvvrlvKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 334 MYE-GVPRpsNPGCFWDVIERYGVN-IFYTAPTairaFIRMGEAVPNArdLSSLRLLGTVGEPINPEawmWYHRVIGggK 411
Cdd:cd12117 206 LAPkGTLL--DPDALGALIAEEGVTvLWLTAAL----FNQLADEDPEC--FAGLRELLTGGEVVSPP---HVRRVLA--A 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 412 CP---IVDTWWQTETGGI----MLTPLPGAIPTKP-GsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVY 483
Cdd:cd12117 273 CPglrLVNGYGPTENTTFttshVVTELDEVAGSIPiG---RPIANTRVYVLDEDGRPVPPGVPGELYVGGD--GLALGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 484 GDTDRFRHTYWEHIqPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDE 563
Cdd:cd12117 348 NRPALTAERFVADP-FGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6647434 564 LTGEAIFAFVSLEGnAEPSEELKkdlvKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd12117 427 GGDKRLVAYVVAEG-ALDAAELR----AFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
90-629 |
1.12e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 165.21 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 90 RHLTTWRRNKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVF 169
Cdd:PRK06178 40 RAWARERPQRPAIIFYG-----HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 170 GGFSAEALRDRLVDAEAKLVITADggfrkdkaiALKQEVDKALehGAPSVENVIVVqrTKADV-----------TMTAGR 238
Cdd:PRK06178 115 PLFREHELSYELNDAGAEVLLALD---------QLAPVVEQVR--AETSLRHVIVT--SLADVlpaeptlplpdSLRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 239 --DHWWHELQPQQSA---HCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTD-VYWCTADV 312
Cdd:PRK06178 182 laAAGAIDLLPALRActaPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDM-VYTAAAAYAVAVVGGEDsVFLSFLPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 313 GWITGHSYIVYGPLSNGATTVMyegVPRpSNPGCFWDVIERYGVNIfyTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVG 392
Cdd:PRK06178 261 FWIAGENFGLLFPLFSGATLVL---LAR-WDAVAFMAAVERYRVTR--TVMLVDNAVELMDHPRFAEYDLSSLRQVRVVS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 393 --EPINPEawmwYHRVigggkcpivdtwWQTETGGIMLTPLPGAIPT-------------------KPGSCTKPFPGIVA 451
Cdd:PRK06178 335 fvKKLNPD----YRQR------------WRALTGSVLAEAAWGMTEThtcdtftagfqdddfdllsQPVFVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 452 EIVDLD-GNPVESDQGGFLVIKQPwpSMIRDVYGDTDRFRHTY---WEHiqpkegqylyfAGDGARRDKDGYFWVMGRVD 527
Cdd:PRK06178 399 KICDFEtGELLPLGAEGEIVVRTP--SLLKGYWNKPEATAEALrdgWLH-----------TGDIGKIDEQGFLHYLGRRK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 528 DVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPaEIR 607
Cdd:PRK06178 466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYKVP-EIR 541
|
570 580
....*....|....*....|..
gi 6647434 608 FTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK06178 542 IVDALPMTATGKVRKQDLQALA 563
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
109-625 |
6.48e-43 |
|
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: 160.49 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:cd05945 12 EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITADGgfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidseDMLFILY 268
Cdd:cd05945 92 LIADGD-------------------------------------------------------------------DNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGGYNLYThmttKWI---FDLKDTDVYWCTAD------VgwitghsYIVYGPLSNGATTVMyegVP 339
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFT----NWMlsdFPLGPGDVFLNQAPfsfdlsV-------MDLYPALASGATLVP---VP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 RP--SNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNArdLSSLRLLGTVGEPI-NPEAWMWYHRViggGKCPIVD 416
Cdd:cd05945 171 RDatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPES--LPSLRHFLFCGEVLpHKTARALQQRF---PDARIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 417 TWWQTE-TGGIMLTPLPGAIPTKPGSCT--KPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIR---DVYGDTDRFR 490
Cdd:cd05945 246 TYGPTEaTVAVTYIEVTPEVLDGYDRLPigYAKPGAKLVILDEDGRPVPPGEKGELVISGP--SVSKgylNNPEKTAAAF 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 491 HTYwehiqpkEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIF 570
Cdd:cd05945 324 FPD-------EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELI 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 571 AFVSLEGNAE--PSEELKKDLVKHVTEeiGAIarPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd05945 397 AFVVPKPGAEagLTKAIKAELAERLPP--YMI--PRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
101-626 |
6.54e-43 |
|
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: 161.74 E-value: 6.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDR 180
Cdd:cd17651 13 ALVAEG-----RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 181 LVDAEAKLVITADggfrkdkaialkqevdkALEHGAPSVENVIvvqrtkadvtmtagrdhwWHELQPQQSAHCPAEPI-- 258
Cdd:cd17651 88 LADAGPVLVLTHP-----------------ALAGELAVELVAV------------------TLLDQPGAAAGADAEPDpa 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 -DSEDMLFILYTSGSTGKPKGVVHTTGGYNLYThmttKW---IFDLKDTDVYWCTADVGWITGHSYIvYGPLSNGATTVm 334
Cdd:cd17651 133 lDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV----AWqarASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLV- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 yegVPRPS---NPGCFWDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDLSSLRLLGTVGEPINPE-------AWMWYH 404
Cdd:cd17651 207 ---LPPEEvrtDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLAALRYLLTGGEQLVLTedlrefcAGLPGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 405 RVigggkcpiVDTWWQTET---GGIMLTPLPGAIPTKPgSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRD 481
Cdd:cd17651 282 RL--------HNHYGPTEThvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA--GLARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 482 VYGDTDRFRHTYWEHiQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRP 561
Cdd:cd17651 351 YLNRPELTAERFVPD-PFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 562 DELTGEAIFAFVSLEGNAEPS-EELKKDLVKHVTEEigaiARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd17651 430 DRPGEKRLVAYVVGDPEAPVDaAELRAALATHLPEY----MVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
100-626 |
1.94e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 160.45 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 100 AAIIWegepGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRD 179
Cdd:PRK08276 2 AVIMA----PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 180 RLVDAEAKLVITaDGGFRkdkaiALKQEVDKALEHGAPsvenvivvqrtkaDVTMTAGRDHWWHELqPQQSAHCPAEPID 259
Cdd:PRK08276 78 IVDDSGAKVLIV-SAALA-----DTAAELAAELPAGVP-------------LLLVVAGPVPGFRSY-EEALAAQPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 260 SE----DMLfilYTSGSTGKPKGV------VHTTGGYNLYTHMTTKWIFDLKDTdVYWC------TADVGWITGhsyivy 323
Cdd:PRK08276 138 DEtagaDML---YSSGTTGRPKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDS-VYLSpaplyhTAPLRFGMS------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 gPLSNGATTVMYEGVprpsNPGCFWDVIERYGVNIFYTAPTAiraFIRM---GEAVPNARDLSSLRllgtvgepinpeaw 400
Cdd:PRK08276 208 -ALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTM---FVRMlklPEEVRARYDVSSLR-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 401 mwyhRVI-GGGKCPI------VDtWW---------QTETGGIMLTPLPGAIpTKPGSCTKPFPGIVAeIVDLDGNPVESD 464
Cdd:PRK08276 266 ----VAIhAAAPCPVevkramID-WWgpiiheyyaSSEGGGVTVITSEDWL-AHPGSVGKAVLGEVR-ILDEDGNELPPG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 465 QGGFLVIKQPWPSMirDVYGDTDRFRHTYwehiqpkEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIES 544
Cdd:PRK08276 339 EIGTVYFEMDGYPF--EYHNDPEKTAAAR-------NPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIEN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 545 ALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRL 624
Cdd:PRK08276 410 LLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRR 489
|
..
gi 6647434 625 LR 626
Cdd:PRK08276 490 LR 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
114-625 |
4.00e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 160.58 E-value: 4.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAI----TMLACSRIGAPHSVvfggFSAEALRDRLVDAEAKLV 189
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIgyygTLLAGGIVVQTNPL----YTERELEYQLHDSGAKVI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGGFRK----DKAIALKQEVDKALEHGAPSVENVI--VVQRTKADVTMTAGRDHWWH-----ELQPQQSAHCPAEPi 258
Cdd:PRK06710 126 LCLDLVFPRvtnvQSATKIEHVIVTRIADFLPFPKNLLypFVQKKQSNLVVKVSESETIHlwnsvEKEVNTGVEVPCDP- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 dSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKD-TDVYWCTADVGWITGHSYIVYGPLSNGATTVMyeg 337
Cdd:PRK06710 205 -ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 VPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkcPIVDT 417
Cdd:PRK06710 281 IPKFDMKMVF-EAIKKHKVTLFPGAPTIYIAL--LNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGG---KLVEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 418 WWQTETGGIMLTPLPGAiPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPwpsmirdvygdtdRFRHTYWEh 496
Cdd:PRK06710 355 YGLTESSPVTHSNFLWE-KRVPGSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGP-------------QIMKGYWN- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 497 iQPKEGQYLY-----FAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFA 571
Cdd:PRK06710 420 -KPEETAAVLqdgwlHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6647434 572 FVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK06710 499 FVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
115-557 |
7.22e-42 |
|
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: 156.66 E-value: 7.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSL-GVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITaD 193
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GGFRKDKAialkqevDKALEHGAPSVENVIVVQRTKADVTmtagrdhwwhelqpqqsahcPAEPIDSEDMLFILYTSGST 273
Cdd:TIGR01733 80 SALASRLA-------GLVLPVILLDPLELAALDDAPAPPP--------------------PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGGY-NLYTHMTTKWIFDlkdtdvywctADVGWITGHSYI-------VYGPLSNGATTVMYEGVPRPSNPG 345
Cdd:TIGR01733 133 GRPKGVVVTHRSLvNLLAWLARRYGLD----------PDDRVLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 346 CFWDVIERYGVNIFYTAPTAIRAFIRMGEavpnaRDLSSLRLLGTVGEPINPE-AWMWYHRvigGGKCPIVDTWWQTE-T 423
Cdd:TIGR01733 203 LLAALIAEHPVTVLNLTPSLLALLAAALP-----PALASLRLVILGGEALTPAlVDRWRAR---GPGARLINLYGPTEtT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 424 GGIMLTPLPGAIPTKPGSCT--KPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwPSMIRDVYGD----TDRFR-HTYWeh 496
Cdd:TIGR01733 275 VWSTATLVDPDDAPRESPVPigRPLANTRLYVLDDDLRPVPVGVVGELYIGG--PGVARGYLNRpeltAERFVpDPFA-- 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 497 iqPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHR--LGtmEIESALVSHPLVAEAAV 557
Cdd:TIGR01733 351 --GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRieLG--EIEAALLRHPGVREAVV 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
88-625 |
1.29e-41 |
|
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: 157.87 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTWRR---NKAAIIwegepGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAp 164
Cdd:cd05920 17 LGDLLARSAArhpDRIAVV-----DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 165 hsvvfggfsaealrdrlvdaeakLVITADGGFRKdkaialkQEVDKALEHGAPSVenvIVVQRTKADVTmtagrdhwwHE 244
Cdd:cd05920 91 -----------------------VPVLALPSHRR-------SELSAFCAHAEAVA---YIVPDRHAGFD---------HR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 245 LQPQQSAHCPAEPIdsedmlFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGwitgHSYI--- 321
Cdd:cd05920 129 ALARELAESIPEVA------LFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPlac 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 322 --VYGPLSNGATTVMyegVPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLRLLGTVGEPINPEA 399
Cdd:cd05920 198 pgVLGTLLAGGRVVL---APDPSPDAAF-PLIEREGVTVTALVPALVSLW--LDAAASRRADLSSLRLLQVGGARLSPAL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 400 WMWYHRVIGGGkcpiVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPF-PGIVAEIVDLDGNPVESDQGGFLVIKQPWpsM 478
Cdd:cd05920 272 ARRVPPVLGCT----LQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPY--T 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 479 IRDVYGDTDRFRHTYWEhiqpkegQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVV 558
Cdd:cd05920 346 IRGYYRAPEHNARAFTP-------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 559 GRPDELTGEAIFAFVSLEGNAEPSEELKkdlvKHVTE-EIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd05920 419 AMPDELLGERSCAFVVLRDPPPSAAQLR----RFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
102-626 |
6.09e-41 |
|
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: 156.64 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 102 IIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAI-------YLpmipEAaitMLACSRIGAPHSVVFGGFSA 174
Cdd:cd12119 14 IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATlawnthrHL----EL---YYAVPGMGAVLHTINPRLFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 175 EALRDRLVDAEAKLVITaDGGFrkdkaIALkqeVDKALEHgAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCP 254
Cdd:cd12119 87 EQIAYIINHAEDRVVFV-DRDF-----LPL---LEAIAPR-LPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 AEPIDSEDMLFILYTSGSTGKPKGVVhttggynlYTH---------MTTKWIFDLKDTDVY-----------WCTADVGW 314
Cdd:cd12119 157 WPDFDENTAAAICYTSGTTGNPKGVV--------YSHrslvlhamaALLTDGLGLSESDVVlpvvpmfhvnaWGLPYAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 315 ITGHSYIVYGPLSNGATTVMyegvprpsnpgcfwdVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLgtvgep 394
Cdd:cd12119 229 MVGAKLVLPGPYLDPASLAE---------------LIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRV------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 395 inpeawmwyhrVIGGGKCP----------IVDT---WWQTETG--GIMLTPLPGAIPTKPG-------SCTKPFPGIVAE 452
Cdd:cd12119 286 -----------VIGGSAVPrslieafeerGVRVihaWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 453 IVDLDGNPVESDQG--GFLVIKQPWpsMIRDVYGDTDrfrhtywEHIQPKEGQYLYfAGDGARRDKDGYFWVMGRVDDVI 530
Cdd:cd12119 355 IVDDDGRELPWDGKavGELQVRGPW--VTKSYYKNDE-------ESEALTEDGWLR-TGDVATIDEDGYLTITDRSKDVI 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 531 NVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTeeiGAIAR---PAEIR 607
Cdd:cd12119 425 KSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLA---DKVAKwwlPDDVV 498
|
570
....*....|....*....
gi 6647434 608 FTDVLPKTRSGKIMRRLLR 626
Cdd:cd12119 499 FVDEIPKTSTGKIDKKALR 517
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
101-647 |
1.68e-40 |
|
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: 159.25 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA------PhsvvfgGFSA 174
Cdd:COG1020 494 AVVFGD-----QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvpldP------AYPA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 175 EALRDRLVDAEAKLVITadggfrkDKAIAlkqevDKALEHGAPsvenVIVVQRtkadvtmtagrdhwwhELQPQQSAHCP 254
Cdd:COG1020 563 ERLAYMLEDAGARLVLT-------QSALA-----ARLPELGVP----VLALDA----------------LALAAEPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 AEPIDSEDMLFILYTSGSTGKPKGVVHTTGG-YNLYTHMTTKwiFDLKDTDVywctadVGWITGHS-----YIVYGPLSN 328
Cdd:COG1020 611 PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAlVNLLAWMQRR--YGLGPGDR------VLQFASLSfdasvWEIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 329 GATTVMY-EGVPRpsNPGCFWDVIERYGVNIFYTAPTAIRAFIrmgEAVPnaRDLSSLRLLGTVGEPINPEAW-MWYHRV 406
Cdd:COG1020 683 GATLVLApPEARR--DPAALAELLARHRVTVLNLTPSLLRALL---DAAP--EALPSLRLVLVGGEALPPELVrRWRARL 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 407 IGggkCPIVD-----------TWWQTETGGIMLTPLP-GaiptkpgsctKPFPGIVAEIVDLDGNPV------Esdqggf 468
Cdd:COG1020 756 PG---ARLVNlygptettvdsTYYEVTPPDADGGSVPiG----------RPIANTRVYVLDAHLQPVpvgvpgE------ 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 469 LVI----------KQPwpsmirdvyGDT-DRFRhtywEHIQPKEGQYLYFAGDGARRDKDG---YfwvMGRVDDVINVSG 534
Cdd:COG1020 817 LYIggaglargylNRP---------ELTaERFV----ADPFGFPGARLYRTGDLARWLPDGnleF---LGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 535 HR--LGtmEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEigaIARPAEIRFTDVL 612
Cdd:COG1020 881 FRieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPP---YMVPAAVVLLLPL 955
|
570 580 590
....*....|....*....|....*....|....*
gi 6647434 613 PKTRSGKIMRRLLRSLASGQEISGDTSTLEDRTVL 647
Cdd:COG1020 956 PLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEE 990
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
110-627 |
1.85e-40 |
|
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: 153.60 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANAL-KSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPhsvvfggfsaealrdrlvdaeakl 188
Cdd:cd05941 8 DGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV------------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 vitadggfrkdkAIALkqevdkALEHGAPSVENVIvvqrTKADVTMTAgrdhwwhelqpqqsahcpaepidseDMLFILY 268
Cdd:cd05941 64 ------------AVPL------NPSYPLAELEYVI----TDSEPSLVL-------------------------DPALILY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGgyNLYTHMTT---KWifdlkdtdvYWCTADV-----GWITGHSYIV--YGPLSNGATTVMyegV 338
Cdd:cd05941 97 TSGTTGRPKGVVLTHA--NLAANVRAlvdAW---------RWTEDDVllhvlPLHHVHGLVNalLCPLFAGASVEF---L 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 339 PRPSnPGCFWDVIERYGVNIFYTAPTAiraFIRMGEAVP---------NARDLSSLRLLGTVGEPINP---EAWmwyhRV 406
Cdd:cd05941 163 PKFD-PKEVAISRLMPSITVFMGVPTI---YTRLLQYYEahftdpqfaRAAAAERLRLMVSGSAALPVptlEEW----EA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 407 IGGGkcPIVDTWWQTETGGIMLTPLPGaiPTKPGSCTKPFPGIVAEIVDLDGN-PVESDQGGFLVIKQPwpSMIRdvygd 485
Cdd:cd05941 235 ITGH--TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGP--SVFK----- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 tdrfrhTYWEhiQPKEGQYlYFAGDG-------ARRDKDGYFWVMGRV-DDVINVSGHRLGTMEIESALVSHPLVAEAAV 557
Cdd:cd05941 304 ------EYWN--KPEATKE-EFTDDGwfktgdlGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 558 VGRPDELTGEAIFAFVSLEGNAEPSEELkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:cd05941 375 IGVPDPDWGERVVAVVVLRAGAAALSLE--ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
115-626 |
5.47e-40 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 154.15 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADG 194
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 GFrkdkaialkqevdKALEHGAPSVENVIVVQRTKADVTMTAGRDhWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTG 274
Cdd:PRK06155 128 LL-------------AALEAADPGDLPLPAVWLLDAPASVSVPAG-WSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 275 KPKGVVHTTGGYNLYTHMTTKwIFDLKDTDVYWCTADVGWITGHSyIVYGPLSNGATTVMyegVPRPSNPGcFWDVIERY 354
Cdd:PRK06155 194 PSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVL---EPRFSASG-FWPAVRRH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 355 GVNIFYTaptaIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPGA 434
Cdd:PRK06155 268 GATVTYL----LGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG---VDLLDGYGSTETNFVIAVTHGSQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 435 iptKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWP-SMIRDVYGDTDRFRHTY---WEHiqpkegqylyfAGD 510
Cdd:PRK06155 341 ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPfAFATGYFGMPEKTVEAWrnlWFH-----------TGD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 511 GARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL-EGNA-EPseelkKD 588
Cdd:PRK06155 407 RVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLrDGTAlEP-----VA 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 6647434 589 LVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK06155 482 LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
145-636 |
8.94e-40 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 152.66 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 145 LPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKAlehgAPSVENVIV 224
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA----APAKAIVLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 225 VQRTKADVTMTAGRDHWWHELQPQQSAHCPA----EPI--DSEDMLFILYTSGSTGKPKGV--VHTT---GGYNLYTHMt 293
Cdd:PLN03051 77 AAGEPVAVPLREQDLSWCDFLGVAAAQGSVGgneySPVyaPVESVTNILFSSGTTGEPKAIpwTHLSplrCASDGWAHM- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 294 tkwifDLKDTDVYWCTADVGWITGhSYIVYGPLSNGATTVMYEGVprPSNPGcFWDVIERYGVNIFYTAPTAIRAFIRMG 373
Cdd:PLN03051 156 -----DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGA--PLGRG-FGKFVQDAGVTVLGLVPSIVKAWRHTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 374 EAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKcPIVDTWWQTETGG--IMLTPLpgaIPTKPGSCTKPFPGIVA 451
Cdd:PLN03051 227 AFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASgyISSTLL---QPQAPGAFSTASLGTRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 452 EIVDLDGNPVESDQ--GGFLVIKQPwpsmirdVYGDTDRF-----RHTYWEHI--QPKEGQYLYFAGDGARRDKDGYFWV 522
Cdd:PLN03051 303 VLLNDNGVPYPDDQpcVGEVALAPP-------MLGASDRLlnadhDKVYYKGMpmYGSKGMPLRRHGDIMKRTPGGYFCV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 523 MGRVDDVINVSGHRLGTMEIESALV-SHPLVAEAAVV------GRPDELTgeaIFAFVSLEG---NAEPSEELKKDLVKH 592
Cdd:PLN03051 376 QGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVgvappdGGPELLV---IFLVLGEEKkgfDQARPEALQKKFQEA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6647434 593 VTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASgQEISG 636
Cdd:PLN03051 453 IQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLK-KELSG 495
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
101-625 |
1.81e-39 |
|
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: 151.66 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDR 180
Cdd:cd17646 16 AVVDEG-----RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 181 LVDAEAKLVITadggfrkdkaialkqevDKALEHGAPSVENVIVVQrtkadvtmtagrdhwwHELQPQQSAHCPAEPIDS 260
Cdd:cd17646 91 LADAGPAVVLT-----------------TADLAARLPAGGDVALLG----------------DEALAAPPATPPLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHTTGGY-NLYTHMTTKwiFDLKDTDVYWCTA----DV-GWitghsyIVYGPLSNGATTVm 334
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKGVMVTHAGIvNRLLWMQDE--YPLGPGDRVLQKTplsfDVsVW------ELFWPLVAGARLV- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 yegVPRPSN---PGCFWDVIERYGVNIFYTAPTAIRAFIRMgeavPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggk 411
Cdd:cd17646 209 ---VARPGGhrdPAYLAALIREHGVTTCHFVPSMLRVFLAE----PAAGSCASLRRVFCSGEALPPELAARFLALPG--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 412 CPIVDTWWQTETG-GIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQPWPSMIR 480
Cdd:cd17646 279 AELHNLYGPTEAAiDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLggvqlargylGRPALTAER 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 DVygdTDRFRHtywehiqpkeGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGR 560
Cdd:cd17646 359 FV---PDPFGP----------GSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 561 PDELTGEAIFAFVSLEGNAEP--SEELKkdlvKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17646 426 AAPAGAARLVGYVVPAAGAAGpdTAALR----AHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
112-626 |
6.78e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.08 E-value: 6.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIT 191
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 ADggfrkdkaiALkQEVDKALEHGAPSVENVIVVQRTKADVTMtaGRDHWWHELQPqqsAHCPAE-PIDSEDMlfILYTS 270
Cdd:PRK07786 121 EA---------AL-APVATAVRDIVPLLSTVVVAGGSSDDSVL--GYEDLLAEAGP---AHAPVDiPNDSPAL--IMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 271 GSTGKPKGVV--HTTGGYNLYTHMTTkWIFDLKDtDVYWCTADVGWITGHSYIVYGpLSNGATTVMYegvPRPS-NPGCF 347
Cdd:PRK07786 184 GTTGRPKGAVltHANLTGQAMTCLRT-NGADINS-DVGFVGVPLFHIAGIGSMLPG-LLLGAPTVIY---PLGAfDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 348 WDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSsLRLLGTVGEPINPEAWMWYHRVIGGGKcpIVDTWWQTETGGIM 427
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAV--CAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQ--ILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 428 LTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDvygdtdrfrhtYWEHiqPK------E 501
Cdd:PRK07786 333 CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP--TLMSG-----------YWNN--PEataeafA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 502 GQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLegnAEP 581
Cdd:PRK07786 398 GGWFH-SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAV---RND 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 6647434 582 SEELK-KDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK07786 474 DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
98-632 |
8.14e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 149.73 E-value: 8.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphSVVF--GGFSAE 175
Cdd:PRK03640 17 DRTAIEFEEKK-----VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLlnTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 176 ALRDRLVDAEAKLVITADGgfrkdkaiaLKQEVdkalehgapsvenvIVVQRTKadvtmtagrdhwWHELQPQQSAHC-P 254
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDD---------FEAKL--------------IPGISVK------------FAELMNGPKEEAeI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 AEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSyIVYGPLSNGATTVM 334
Cdd:PRK03640 135 QEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 YEGvprpsnpgcfWDV------IERYGVNIFYTAPTAIRafiRMGEAVPNARDLSSLR--LLGtvGEPINP----EAWMW 402
Cdd:PRK03640 213 VEK----------FDAekinklLQTGGVTIISVVSTMLQ---RLLERLGEGTYPSSFRcmLLG--GGPAPKplleQCKEK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 403 yhrvigggKCPIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKP-FPGIVaEIVDlDGNPVESDQGGFLVIKQPwpSMIRD 481
Cdd:PRK03640 278 --------GIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPlFPCEL-KIEK-DGVVVPPFEEGEIVVKGP--NVTKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 482 VYGDTDRFRhtywEHIQP---KEGQYLYFagdgarrDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVV 558
Cdd:PRK03640 346 YLNREDATR----ETFQDgwfKTGDIGYL-------DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6647434 559 GRPDELTGEAIFAFVSLEGnaEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQ 632
Cdd:PRK03640 415 GVPDDKWGQVPVAFVVKSG--EVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-629 |
1.37e-38 |
|
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: 146.09 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 260 SEDMLFILYTSGSTGKPKGVVHTTGGyNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVmyegVP 339
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV----LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 RPS---NPGC---FWDVIERYGVNIFYTAPTAIRAFIrmgeAVPNARDLSSLRLLGTVGEPINPEAwmwYHRVIGGGKCP 413
Cdd:cd05944 76 GPAgyrNPGLfdnFWKLVERYRITSLSTVPTVYAALL----QVPVNADISSLRFAMSGAAPLPVEL---RARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 IVDTWWQTETGGIMLTPLPGAiPTKPGSCTKPFPGIVAEIVDLDGN-----PVESDQGGFLVIKQPwpsmirDVYGDtdr 488
Cdd:cd05944 149 VVEGYGLTEATCLVAVNPPDG-PKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGP------GVFGG--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 489 frHTYWEHIQPKEGQYLYF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGE 567
Cdd:cd05944 219 --YLYTEGNKNAFVADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGE 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 568 AIFAFVSLEGNAEPS-EELKKDLVKHVTEEigaIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:cd05944 297 LPVAYVQLKPGAVVEeEELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
110-625 |
2.81e-38 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 147.82 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadggfrkdkaialkqevDKALEHGAPsvenvivvqrTKADVTMTAGRDhwwhelqPQQSAHCPAEPIDSEDMLFILYT 269
Cdd:cd12116 89 LT-----------------DDALPDRLP----------AGLPVLLLALAA-------AAAAPAAPRTPVSPDDLAYVIYT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGGY-NLYTHMTTKwiFDLKDTDVYWCTADVGW-ITGHSyiVYGPLSNGATTVMyegVPRP--SNPG 345
Cdd:cd12116 135 SGSTGRPKGVVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVI---APREtqRDPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 346 CFWDVIERYGVNIFYTAPTAIRAF----------IRM---GEAVPnaRDLSSlRLLGTVGEPINpeawmwyhrVIGggkc 412
Cdd:cd12116 208 ALARLIEAHSITVMQATPATWRMLldagwqgragLTAlcgGEALP--PDLAA-RLLSRVGSLWN---------LYG---- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 413 PIVDTWWQTETggiMLTPLPGAIPTkpgscTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwPSMIRDVYGDTD----R 488
Cdd:cd12116 272 PTETTIWSTAA---RVTAAAGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYIGG--DGVAQGYLGRPAltaeR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 489 FRHtyweHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGeA 568
Cdd:cd12116 342 FVP----DPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDR-R 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 569 IFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd12116 417 LVAYVVLKAGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
99-626 |
4.62e-38 |
|
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: 146.74 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 99 KAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALR 178
Cdd:cd17649 3 AVALVFGDQS-----LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 179 DRLVDAEAKLVITADggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqPQQSAhcpaepi 258
Cdd:cd17649 78 YMLEDSGAGLLLTHH-----------------------------------------------------PRQLA------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 dsedmlFILYTSGSTGKPKGVVHTTGGynLYTHM-TTKWIFDLKDTDVYWCTADVGWITGHSYiVYGPLSNGATTVMyEG 337
Cdd:cd17649 98 ------YVIYTSGSTGTPKGVAVSHGP--LAAHCqATAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGACVVL-RP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 VPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPnARDLSSLRLLGTVGEPINPEAWmwyhRVIGGGKCPIVDT 417
Cdd:cd17649 168 DELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG-DGRPPSLRLYIFGGEALSPELL----RRWLKAPVRLFNA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 418 WWQTETggiMLTPL-----------PGAIPTKpgsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGDT 486
Cdd:cd17649 243 YGPTEA---TVTPLvwkceagaaraGASMPIG-----RPLGGRSAYILDADLNPVPVGVTGELYIGGE--GLARGYLGRP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 487 DRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELtG 566
Cdd:cd17649 313 ELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 567 EAIFAFVSLEGnAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd17649 392 KQLVAYVVLRA-AAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-629 |
4.74e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 148.77 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADG 194
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gFRKDKAIALKQEVDKALEHGA---------PSVENVIVVQRTKADvTMTAgrdhwWHELQPQQSAHCPAE------PID 259
Cdd:PRK12583 127 -FKTSDYHAMLQELLPGLAEGQpgalacerlPELRGVVSLAPAPPP-GFLA-----WHELQARGETVSREAlaerqaSLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 260 SEDMLFILYTSGSTGKPKGVVHTTggYNLythMTTKWI----FDLKDTDV-------YWCTADVgwitghsYIVYGPLSN 328
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKGATLSH--HNI---LNNGYFvaesLGLTEHDRlcvpvplYHCFGMV-------LANLGCMTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 329 GATTVMyegvprpsnPGCFWD------VIERYGVNIFYTAPTAiraFIRMGEAVPNAR-DLSSLRLLGTVGEPINPEAwm 401
Cdd:PRK12583 268 GACLVY---------PNEAFDplatlqAVEEERCTALYGVPTM---FIAELDHPQRGNfDLSSLRTGIMAGAPCPIEV-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 402 wYHRVIGGGKCP-IVDTWWQTETGGI-MLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMI 479
Cdd:PRK12583 334 -MRRVMDEMHMAeVQIAYGMTETSPVsLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGY--SVM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 480 RDVYGDTDRFRhtywEHIQpKEGqYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVG 559
Cdd:PRK12583 411 KGYWNNPEATA----ESID-EDG-WMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 560 RPDELTGEAIFAFVSLEGNAEPSEELKKDLVKhvtEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK12583 484 VPDEKYGEEIVAWVRLHPGHAASEEELREFCK---ARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
87-631 |
1.78e-37 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 146.66 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 87 CLDRHltTWRRNKAAIIwEGEPGdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHS 166
Cdd:PLN02246 29 CFERL--SEFSDRPCLI-DGATG--RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 167 VVFGGFSAEALRDRLVDAEAKLVITadggfrkdkaiaLKQEVDKALEHGAPsvENVIVVqrtkadvTMTAGRD---HWWH 243
Cdd:PLN02246 104 TANPFYTPAEIAKQAKASGAKLIIT------------QSCYVDKLKGLAED--DGVTVV-------TIDDPPEgclHFSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 244 ELQPQQSAhCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGY-------------NLYTHmttkwifdlkDTDVYWCTA 310
Cdd:PLN02246 163 LTQADENE-LPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLvtsvaqqvdgenpNLYFH----------SDDVILCVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 311 DVGWITGHSYIVYGPLSNGATTVmyegVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGT 390
Cdd:PLN02246 232 PMFHIYSLNSVLLCGLRVGAAIL----IMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVV--EKYDLSSIRMVLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 391 VGEPIN-----------PEAwmwyhrVIGGGkcpivdtWWQTETGGIMLTPLPGA---IPTKPGSCtkpfpGIV---AE- 452
Cdd:PLN02246 306 GAAPLGkeledafraklPNA------VLGQG-------YGMTEAGPVLAMCLAFAkepFPVKSGSC-----GTVvrnAEl 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 453 -IVDLD-GNPVESDQGGFLVIK--QPWPSMIRDVYG-----DTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVM 523
Cdd:PLN02246 368 kIVDPEtGASLPRNQPGEICIRgpQIMKGYLNDPEAtantiDKDGWLHT----------------GDIGYIDDDDELFIV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 524 GRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARP 603
Cdd:PLN02246 432 DRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRI 508
|
570 580
....*....|....*....|....*....
gi 6647434 604 AEIRFTDVLPKTRSGKIMRRLLRS-LASG 631
Cdd:PLN02246 509 HKVFFVDSIPKAPSGKILRKDLRAkLAAG 537
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
115-633 |
9.35e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 143.79 E-value: 9.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITadg 194
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gfrkdkaialkqevDKALEHGAPSVENVIVvqrtkadvtmtagrdhwwheLQPQQSAHCPA--EPIDSEDMLFILYTSGS 272
Cdd:PRK09088 101 --------------DDAVAAGRTDVEDLAA--------------------FIASADALEPAdtPSIPPERVSLILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVV-------HTTGGYNLYTHMTTKWIFdLKDTDVYWCtadVGWITGhsyiVYGPLSNGATTVMYEGVPRPSNPG 345
Cdd:PRK09088 147 SGQPKGVMlsernlqQTAHNFGVLGRVDAHSSF-LCDAPMFHI---IGLITS----VRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 346 CFWDviERYGVNIFYTAPTAIRAFIRMGEAVPNArdLSSLRLLGTVGEPINPEAWMWYhrvIGGGkCPIVDTWWQTETGG 425
Cdd:PRK09088 219 RLGD--PALGITHYFCVPQMAQAFRAQPGFDAAA--LRHLTALFTGGAPHAAEDILGW---LDDG-IPMVDGFGMSEAGT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 426 IMLTPL-PGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQP--WPSMIRDVYGDTDRFRHTYWehiqpkeg 502
Cdd:PRK09088 291 VFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnlSPGYWRRPQATARAFTGDGW-------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 503 qylYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLegnAEPS 582
Cdd:PRK09088 363 ---FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVP---ADGA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6647434 583 EELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS-LASGQE 633
Cdd:PRK09088 437 PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDaLAAGRK 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
114-625 |
4.37e-36 |
|
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: 141.30 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITad 193
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepiDSEDMLFILYTSGST 273
Cdd:cd12115 103 -----------------------------------------------------------------DPDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGgyNLYTHM-----------------TTKWIFDLKdtdvywctadvgwitghSYIVYGPLSNGATTVMYE 336
Cdd:cd12115 118 GRPKGVAIEHR--NAAAFLqwaaaafsaeelagvlaSTSICFDLS-----------------VFELFGPLATGGKVVLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 337 GVPR-PSNPGcfwdvieRYGVNIFYTAPTAIRAFIRMGeAVPnardlSSLRLLGTVGEPINPEAwmwYHRVIG--GGKC- 412
Cdd:cd12115 179 NVLAlPDLPA-------AAEVTLINTVPSAAAELLRHD-ALP-----ASVRVVNLAGEPLPRDL---VQRLYArlQVERv 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 413 -----PIVDTWWQTetggimLTPLPGAIPTKPgSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGD-- 485
Cdd:cd12115 243 vnlygPSEDTTYST------VAPVPPGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGA--GVARGYLGRpg 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 --TDRFRHtywehIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDE 563
Cdd:cd12115 314 ltAERFLP-----DPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6647434 564 LTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd12115 389 AGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
99-627 |
3.25e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 139.83 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 99 KAAIIWegePGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALR 178
Cdd:PRK13391 13 KPAVIM---ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 179 DRLVDAEAKLVITAdggfrkdkaiALKQEVDKALEHGAPSVENVIVVQRTKAdvtmtagRDHWwhELQPQQSAHCPAEPI 258
Cdd:PRK13391 90 YIVDDSGARALITS----------AAKLDVARALLKQCPGVRHRLVLDGDGE-------LEGF--VGYAEAVAGLPATPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSE----DMLfilYTSGSTGKPKGV---------VHTTGgynlYTHMTTK-WIFDlKDTdVYWCTADVgWITGHSYIVYG 324
Cdd:PRK13391 151 ADEslgtDML---YSSGTTGRPKGIkrplpeqppDTPLP----LTAFLQRlWGFR-SDM-VYLSPAPL-YHSAPQRAVML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 325 PLSNGATTVMYEGVprpsNPGCFWDVIERYGVNIFYTAPTAiraFIRM---GEAVPNARDLSSLRLLGTVGEPINPE--- 398
Cdd:PRK13391 221 VIRLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTM---FSRMlklPEEVRDKYDLSSLEVAIHAAAPCPPQvke 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 399 ---AWmWyhrvigggkCPIVDTWW-QTETGGIMLTPLPGAIpTKPGSCTKPFPGIVaEIVDLDGNPVESDQGGFLVIKQP 474
Cdd:PRK13391 294 qmiDW-W---------GPIIHEYYaATEGLGFTACDSEEWL-AHPGTVGRAMFGDL-HILDDDGAELPPGEPGTIWFEGG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 475 WPSMIRDVYGDTDRFRHTY--WEHIqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV 552
Cdd:PRK13391 362 RPFEYLNDPAKTAEARHPDgtWSTV-----------GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 553 AEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:PRK13391 431 ADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
114-626 |
5.29e-35 |
|
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: 137.48 E-value: 5.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvvfggfsaealrdrlvdaeaklvitad 193
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenVIVVQRTKadvtMTAgrdhwwHELQPQ-QSAHcpaepIDSEDMLFILYTSGS 272
Cdd:cd05912 52 ----------------------------EAVLLNTR----LTP------NELAFQlKDSD-----VKLDDIATIMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVVHTTGgyNLYTHMT-TKWIFDLKDTDVYWCTADVGWITGHSYIVYGpLSNGATTVMYEGVprpsNPGCFWDVI 351
Cdd:cd05912 89 TGKPKGVQQTFG--NHWWSAIgSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLI 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 352 ERYGVNIFYTAPTAIRAFI-RMGEAVPNardlsSLR--LLGtvGEPINP---EawmwyhrvigggKC-----PIVDTWWQ 420
Cdd:cd05912 162 NSGKVTIISVVPTMLQRLLeILGEGYPN-----NLRciLLG--GGPAPKpllE------------QCkekgiPVYQSYGM 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 421 TETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESdqgGFLVIKQPwpsMIRDVY-GDTDRFRHTYwehiqp 499
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEV---GEILLKGP---NVTKGYlNRPDATEESF------ 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 500 kEGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGna 579
Cdd:cd05912 291 -ENGWFK-TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER-- 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 6647434 580 EPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05912 367 PISEE---ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
114-625 |
1.16e-34 |
|
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: 138.03 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GG-------FRKDKAIALKQEVD-KALEHGAPSVEnvivvqrtkadvtmtagrdhwwhelqpqqsahcpAEPIDSEDMLF 265
Cdd:cd05923 109 DAqvmdaifQSGVRVLALSDLVGlGEPESAGPLIE----------------------------------DPPREPEQPAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ILYTSGSTGKPKGVV-------------HTTGGYNLYTHMTTKWIFDLKDTdvywctadvgwiTGHSYIVYGPLSNGATT 332
Cdd:cd05923 155 VFYTSGTTGLPKGAVipqraaesrvlfmSTQAGLRHGRHNVVLGLMPLYHV------------IGFFAVLVAALALDGTY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 333 VmyegVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPnaRDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkc 412
Cdd:cd05923 223 V----VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAG--LKLSSLRHVTFAGATMPDAVLERVNQHLPG--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 413 PIVDTWWQTETGGIMLTPLPgaiptKPGSCTKPfpGIVAE--IVDLDGNPVES----DQGGFLVikqpwpsmirDVYGDT 486
Cdd:cd05923 294 EKVNIYGTTEAMNSLYMRDA-----RTGTEMRP--GFFSEvrIVRIGGSPDEAlangEEGELIV----------AAAADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 487 dRFRHtYWEHIQP-----KEGQYlyFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRP 561
Cdd:cd05923 357 -AFTG-YLNQPEAtakklQDGWY--RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 562 DELTGEAIFAFVSL-EGNaePSEELKKDLVKhvTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd05923 433 DERWGQSVTACVVPrEGT--LSADELDQFCR--ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
96-623 |
2.93e-34 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 138.31 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAE 175
Cdd:COG1022 23 RFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 176 ALRDRLVDAEAKLVITADggfrkdkaialKQEVDKALEHGA--PSVENVIVVQrtkADVTMTAGRDHWWHELQPQQSAHC 253
Cdd:COG1022 103 EVAYILNDSGAKVLFVED-----------QEQLDKLLEVRDelPSLRHIVVLD---PRGLRDDPRLLSLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 254 PAEPIDS-------EDMLFILYTSGSTGKPKGVVHTTGG--YNLYTHMTtkwIFDLKDTDVY-----WCtadvgWITGHS 319
Cdd:COG1022 169 DPAELEArraavkpDDLATIIYTSGTTGRPKGVMLTHRNllSNARALLE---RLPLGPGDRTlsflpLA-----HVFERT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 320 YIVYGpLSNGAT-------------------TVMYeGVPRpsnpgcFWDVI---------ERYGV--NIFYTA-PTAIRA 368
Cdd:COG1022 241 VSYYA-LAAGATvafaespdtlaedlrevkpTFML-AVPR------VWEKVyagiqakaeEAGGLkrKLFRWAlAVGRRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 369 FIRM--GEAVPNARDL----------SSLR-LLG-------TVGEPINPEAWMWYHrVIGggkCPIVDTWWQTETGGIML 428
Cdd:COG1022 313 ARARlaGKSPSLLLRLkhaladklvfSKLReALGgrlrfavSGGAALGPELARFFR-ALG---IPVLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 429 TPLPGAIptKPGSCTKPFPGIVAEIVDlDG---------------NPVESDQggflVIkqpwpsmirdvygDTDRFRHTy 493
Cdd:COG1022 389 VNRPGDN--RIGTVGPPLPGVEVKIAE-DGeilvrgpnvmkgyykNPEATAE----AF-------------DADGWLHT- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 494 wehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGhrlGTM----EIESALVSHPLVAEAAVVGR--------- 560
Cdd:COG1022 448 ---------------GDIGELDEDGFLRITGRKKDLIVTSG---GKNvapqPIENALKASPLIEQAVVVGDgrpflaali 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 561 -PDEltgEAIFAFVSLEG-NAEPSEEL--KKDLVKHVTEEIGAI----ARPAEI-RFTdVLPK---------TRSGKIMR 622
Cdd:COG1022 510 vPDF---EALGEWAEENGlPYTSYAELaqDPEVRALIQEEVDRAnaglSRAEQIkRFR-LLPKeftiengelTPTLKLKR 585
|
.
gi 6647434 623 R 623
Cdd:COG1022 586 K 586
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
96-628 |
5.68e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 136.60 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRNKAAIIWE-GEpgdsriITYAQLHREVCQFANALKSLGVQKGDRVAI----YLPMIpeaaITMLACSRIGAPHSVVFG 170
Cdd:PRK07788 62 APDRAALIDErGT------LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGARIILLNT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 171 GFSAEALRDRLVDAEAKLVITADggfrkdkaialkqEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQS 250
Cdd:PRK07788 132 GFSGPQLAEVAAREGVKALVYDD-------------EFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 251 AHcPAEPIDSEDMLFILyTSGSTGKPKGVVHTT-------GGynLYTHMTtkwifdLKDTDVYWCTADVGWITGHSYIVY 323
Cdd:PRK07788 199 TA-PLPKPPKPGGIVIL-TSGTTGTPKGAPRPEpsplaplAG--LLSRVP------FRAGETTLLPAPMFHATGWAHLTL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 GpLSNGATTVMyegvPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWY 403
Cdd:PRK07788 269 A-MALGSTVVL----RRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 HRVIGggkcPIV-DTWWQTETGgIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGG--Flvikqpwpsmir 480
Cdd:PRK07788 344 LEAFG----PVLyNLYGSTEVA-FATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGriF------------ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 dVYGDTDRFRHTYWEHIQPKEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGR 560
Cdd:PRK07788 407 -VGNGFPFEGYTDGRDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 561 PDELTGEAIFAFVSLEGNAEPSEELKKDLVKhvteeiGAIAR---PAEIRFTDVLPKTRSGKIMRRLLRSL 628
Cdd:PRK07788 484 DDEEFGQRLRAFVVKAPGAALDEDAIKDYVR------DNLARykvPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
96-625 |
5.55e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 133.06 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRNKAAIIwegepGDSRIITYAQLHREVCQFANALK-SLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvvfggfSA 174
Cdd:PRK06839 15 HPDRIAII-----TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVEC---------IA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 175 EALRDRLVDAEAKLVITaDGGFRKdkaialkQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHwwhelqpqqsAHCP 254
Cdd:PRK06839 81 VPLNIRLTENELIFQLK-DSGTTV-------LFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDR----------KIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 AEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVm 334
Cdd:PRK06839 143 FVEKNESASFIICYTSGTTGKPKGAVLTQENM-FWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 yegVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIrmgEAVPNAR-DLSSLRLLGTVGEPInPEAWMWYHRVIGggkCP 413
Cdd:PRK06839 221 ---VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALI---NCSKFETtNLQSVRWFYNGGAPC-PEELMREFIDRG---FL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 IVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmirDVYGDtdrfrhtY 493
Cdd:PRK06839 291 FGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP------NVMKE-------Y 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 494 WEhiQPKEGQ------YLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGE 567
Cdd:PRK06839 358 WN--RPDATEetiqdgWLC-TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 568 AIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK06839 435 IPIAFIVKKSSSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
260-619 |
6.55e-33 |
|
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: 130.19 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 260 SEDMLFILYTSGSTGKPKGVVHTTGGYNLyTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEG-- 337
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIFR-MLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 -------VPRPS-NPGCFWDVIERYGVNifyTAPTAIRAFIR-MGEAV--PNARDLSSLRLLGTVGEPINPEA-----WM 401
Cdd:cd05924 81 lggqtvvLPDDRfDPEEVWRTIEKHKVT---SMTIVGDAMARpLIDALrdAGPYDLSSLFAISSGGALLSPEVkqgllEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 402 WYHRVigggkcpIVDTWWQTETGGIMlTPLPGAIPTKPGSCTKPFPGIVaeIVDLDGNPVESDQGGFLVIKQpwpsmiRD 481
Cdd:cd05924 158 VPNIT-------LVDAFGSSETGFTG-SGHSAGSGPETGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIAR------RG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 482 V-----YGDTDRFRHTYWEhiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAA 556
Cdd:cd05924 222 HiplgyYGDEAKTAETFPE----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 557 VVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGK 619
Cdd:cd05924 298 VVGRPDERWGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
114-625 |
1.50e-32 |
|
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: 131.24 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GGFRKDKAIALKQEVDKALEHGAPSVenvivvqrtkadvtmtagrdhwwhelqpqqsahcPAEPIDSEDMLFILYTSGST 273
Cdd:cd12114 93 PDAQLDVAVFDVLILDLDALAAPAPP----------------------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGG-YNLYTHMTTKWIFDLKDTdvywctadVGWITGHS-----YIVYGPLSNGATTVMyegvPRP---SNP 344
Cdd:cd12114 139 GTPKGVMISHRAaLNTILDINRRFAVGPDDR--------VLALSSLSfdlsvYDIFGALSAGATLVL----PDEarrRDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 345 GCFWDVIERYGVNIFYTAPtairAFIRM--GEAVPNARDLSSLRLLGTVGE-----------PINPEAwmwyhRVIG-GG 410
Cdd:cd12114 207 AHWAELIERHGVTLWNSVP----ALLEMllDVLEAAQALLPSLRLVLLSGDwipldlparlrALAPDA-----RLISlGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 411 KcpivdtwwqTEtGGIMLTPLP-GAIPTKPGSCT--KPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwPSMIRDVYGDTD 487
Cdd:cd12114 278 A---------TE-ASIWSIYHPiDEVPPDWRSIPygRPLANQRYRVLDPRGRDCPDWVPGELWIGG--RGVALGYLGDPE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 488 RFRHTYWEHiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRpDELTGE 567
Cdd:cd12114 346 LTAARFVTH---PDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGK 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 568 AIFAFVSLEGNAEP--SEELKKDLVKHVTeeigAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd12114 422 RLAAFVVPDNDGTPiaPDALRAFLAQTLP----AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
98-626 |
2.65e-32 |
|
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: 130.88 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWegepGDSRIiTYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEaaitMLACSrIGAPHSvvfgGFSAEAL 177
Cdd:cd12118 19 DRTSIVY----GDRRY-TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPA----MYELH-FGVPMA----GAVLNAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLvDAEAKLVItadggfrkdkaialkqevdkaLEHGAPSVenVIVVQRTKADVTMTAGRDhwWHELQPqqsahcpaeP 257
Cdd:cd12118 85 NTRL-DAEEIAFI---------------------LRHSEAKV--LFVDREFEYEDLLAEGDP--DFEWIP---------P 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYThMTTKWIFDLKDTDVYWCTADV----GWItghsyIVYGPLSNGATTV 333
Cdd:cd12118 130 ADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNA-LANILEWEMKQHPVYLWTLPMfhcnGWC-----FPWTVAAVGGTNV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 334 MYEGVprpsNPGCFWDVIERYGVNIFYTAPTAIRAFIrmgeavpNARDLSSLRLLGTVgepinpeawmwyhRVIGGGKCP 413
Cdd:cd12118 204 CLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLA-------NAPPSDARPLPHRV-------------HVMTAGAPP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 IVDTWWQTETGGIMLTPLPGAIPTKPgsctkpfPGIVAEIVD-LDGNPVE------SDQGGFLVIKQPW----PSMIRDV 482
Cdd:cd12118 260 PAAVLAKMEELGFDVTHVYGLTETYG-------PATVCAWKPeWDELPTEerarlkARQGVRYVGLEEVdvldPETMKPV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 YGDTDR-----FR-HT----YWEHiqPK------EGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESAL 546
Cdd:cd12118 333 PRDGKTigeivFRgNIvmkgYLKN--PEataeafRGGWFH-SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 547 VSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDvLPKTRSGKIMRRLLR 626
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
99-628 |
5.65e-32 |
|
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: 130.82 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 99 KAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGvQKGDRVAIYLPMIPEAAITMLACSRIGA---PHSVVFGGFSAE 175
Cdd:cd05931 10 PAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAiavPLPPPTPGRHAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 176 ALRDRLVDAEAKLVITADggfrkdkaiALKQEVDKALEHGAPSVENVIVVqrtkADVTMTAGRDHWwhelqpqqsahcPA 255
Cdd:cd05931 89 RLAAILADAGPRVVLTTA---------AALAAVRAFAASRPAAGTPRLLV----VDLLPDTSAADW------------PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 256 EPIDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTH---MTTKWIFDLKDTDVYW--CTADVGWITGhsyiVYGPLSNGA 330
Cdd:cd05931 144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHR--NLLANvrqIRRAYGLDPGDVVVSWlpLYHDMGLIGG----LLTPLYSGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 TTVMYEG---VPRPSnpgcFW-DVIERYGVNIFYtAPT-----AIRafiRMGEAVPNARDLSSLRLLGTVGEPINPEAwm 401
Cdd:cd05931 218 PSVLMSPaafLRRPL----RWlRLISRYRATISA-APNfaydlCVR---RVRDEDLEGLDLSSWRVALNGAEPVRPAT-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 402 wYHR-----------------------------VIGGGKCPIVDTWWQTETGGimlTPLPGAIPTKPG----SCTKPFPG 448
Cdd:cd05931 288 -LRRfaeafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAG---RAVAVAADDPAArelvSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 449 IVAEIVDLDGNPVESDQGgflvIKQPW---PSMIRDVYGDTDRFRHTYWEHIQPKEGQYLYfAGD-GARRdkDGYFWVMG 524
Cdd:cd05931 364 QEVRIVDPETGRELPDGE----VGEIWvrgPSVASGYWGRPEATAETFGALAATDEGGWLR-TGDlGFLH--DGELYITG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 525 RVDDVINVSGHRLGTMEIE-SALVSHPLVAE--AAVVGRPDElTGEAIFAFVSLEGNAEPSE--ELKKDLVKHVTEEIGa 599
Cdd:cd05931 437 RLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcVAAFSVPDD-GEERLVVVAEVERGADPADlaAIAAAIRAAVAREHG- 514
|
570 580 590
....*....|....*....|....*....|.
gi 6647434 600 iARPAEIRF--TDVLPKTRSGKIMRRLLRSL 628
Cdd:cd05931 515 -VAPADVVLvrPGSIPRTSSGKIQRRACRAA 544
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
110-625 |
1.33e-31 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 127.97 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelQPqqsahcpaepidsEDMLFILYT 269
Cdd:cd17650 89 LT------------------------------------------------------QP-------------EDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTtggYNLYTHMTTKW--IFDLKDTDVYWCTadvgwITGHSYIVYG-----PLSNGATTVMyegVPRPS 342
Cdd:cd17650 102 SGTTGKPKGVMVE---HRNVAHAAHAWrrEYELDSFPVRLLQ-----MASFSFDVFAgdfarSLLNGGTLVI---CPDEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 343 --NPGCFWDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLRLL--GTVGEPINPEAWMwYHRVigGGKCPIVDTW 418
Cdd:cd17650 171 klDPAALYDLILKSRITLMESTPALIRPV--MAYVYRNGLDLSAMRLLivGSDGCKAQDFKTL-AARF--GQGMRIINSY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTETGgIMLTPLPGAIPTKPGSCT----KPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGDTDRFRHTYW 494
Cdd:cd17650 246 GVTEAT-IDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRPELTAERFV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 EHiqPKE-GQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDElTGEAifafv 573
Cdd:cd17650 323 EN--PFApGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEA----- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6647434 574 SLEGNAEPSEELK-KDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17650 395 RLCAYVVAAATLNtAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
541-619 |
1.36e-31 |
|
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: 117.26 E-value: 1.36e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6647434 541 EIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPseeLKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGK 619
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
250-627 |
1.85e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.18 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 250 SAHCPAEPiDSEDMLFILYTSGSTGKPKGVVhttggynLYTHMTTKWIFDLKDTdVYWCTADV-----------GWITGh 318
Cdd:PRK07787 118 SWHRYPEP-DPDAPALIVYTSGTTGPPKGVV-------LSRRAIAADLDALAEA-WQWTADDVlvhglplfhvhGLVLG- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 319 syiVYGPLSNGATtVMYEGVPRPsnpgcfwdviERY------GVNIFYTAPTAiraFIRMGEAVPNARDLSSLRLL--GT 390
Cdd:PRK07787 188 ---VLGPLRIGNR-FVHTGRPTP----------EAYaqalseGGTLYFGVPTV---WSRIAADPEAARALRGARLLvsGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 391 VGEPInPEawmwYHRVIGGGKCPIVDTWWQTETggIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQG--GF 468
Cdd:PRK07787 251 AALPV-PV----FDRLAALTGHRPVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 469 LVIKQPW--------PSMIRDVYGDTDRFRhtywehiqpkegqylyfAGDGARRDKDGYFWVMGRVD-DVINVSGHRLGT 539
Cdd:PRK07787 324 LQVRGPTlfdgylnrPDATAAAFTADGWFR-----------------TGDVAVVDPDGMHRIVGREStDLIKSGGYRIGA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 540 MEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSleGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGK 619
Cdd:PRK07787 387 GEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAAD---ELIDFVAQQLSVHKRPREVRFVDALPRNAMGK 461
|
....*...
gi 6647434 620 IMRRLLRS 627
Cdd:PRK07787 462 VLKKQLLS 469
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
113-627 |
2.77e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 128.34 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 113 IITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDrlVDAEAKLVITa 192
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE--VVTREGVDTV- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 193 dggFRKDKAIALkqeVDKALEhGAPSVENVIVVQRTKADVTMTAGRDhwwhelqpqqsAHCPAEPIDS-EDMLFILYTSG 271
Cdd:PRK13382 145 ---IYDEEFSAT---VDRALA-DCPQATRIVAWTDEDHDLTVEVLIA-----------AHAGQRPEPTgRKGRVILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 272 STGKPKGVVHTTGGynlyTHMTTKWIFD---LKDTDVYWCTADVGWITGHSYIVYGpLSNGATTVMYegvpRPSNPGCFW 348
Cdd:PRK13382 207 TTGTPKGARRSGPG----GIGTLKAILDrtpWRAEEPTVIVAPMFHAWGFSQLVLA-ASLACTIVTR----RRFDPEATL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkcPIVDTWWQTETGGIMl 428
Cdd:PRK13382 278 DLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNATEAGMIA- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 429 TPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwpSMIRDVY--GDTDRFRhtywehiqpkEGqyLY 506
Cdd:PRK13382 354 TATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRN---DTQFDGYtsGSTKDFH----------DG--FM 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 507 FAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElk 586
Cdd:PRK13382 419 ASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE-- 496
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 6647434 587 kDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:PRK13382 497 -TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
96-626 |
3.17e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 128.24 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRN--KAAIIWegepGDsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGA---------- 163
Cdd:PRK07470 18 RRFpdRIALVW----GD-RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAvwvptnfrqt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 164 PHSVVFGGFSAEAlrdrlvdaeaKLVItADGGFRkdkaialkqEVDKALEHGAPSVENVIVVQRTKADVTMTAG-RDHWW 242
Cdd:PRK07470 93 PDEVAYLAEASGA----------RAMI-CHADFP---------EHAAAVRAASPDLTHVVAIGGARAGLDYEALvARHLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 243 HELQPQQsahcpaepIDSEDMLFILYTSGSTGKPKGVVHTTG--GYNLYTHMttkwifdlkdtdvywctADVGWITGHS- 319
Cdd:PRK07470 153 ARVANAA--------VDHDDPCWFFFTSGTTGRPKAAVLTHGqmAFVITNHL-----------------ADLMPGTTEQd 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 320 -YIVYGPLSNGA------------TTVMYEGvpRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRmGEAVpNARDLSSLR 386
Cdd:PRK07470 208 aSLVVAPLSHGAgihqlcqvargaATVLLPS--ERFDPAEVWALVERHRVTNLFTVPTILKMLVE-HPAV-DRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 387 LLGTVGEPINPEAWMWYHRVIGGgkcPIVDTWWQTE-TGGImlTPLPGAI-------PTKPGSCTKPFPGIVAEIVDLDG 458
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGK---VLVQYFGLGEvTGNI--TVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 459 NPVESDQGGFLVIKQP--WPSMIRDVYGDTDRFRHTyWEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHR 536
Cdd:PRK07470 359 RELPPGETGEICVIGPavFAGYYNNPEANAKAFRDG-WFR-----------TGDLGHLDARGFLYITGRASDMYISGGSN 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 537 LGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTeeiGAIAR---PAEIRFTDVLP 613
Cdd:PRK07470 427 VYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLD---GKVARyklPKRFFFWDALP 500
|
570
....*....|...
gi 6647434 614 KTRSGKIMRRLLR 626
Cdd:PRK07470 501 KSGYGKITKKMVR 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
109-623 |
4.44e-31 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 126.56 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITADGgfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidsEDMLFILY 268
Cdd:cd05907 81 LFVEDP------------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGGY--NLYTHMTTkwiFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPRPSnpgc 346
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNIlsNALALAER---LPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 347 fwDVIERYGVNIFYTAPT---AIRAFIRMgEAVPNARD-------LSSLRLLGTVGEPINPEAWMWYHRvIGggkCPIVD 416
Cdd:cd05907 168 --DDLSEVRPTVFLAVPRvweKVYAAIKV-KAVPGLKRklfdlavGGRLRFAASGGAPLPAELLHFFRA-LG---IPVYE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 417 TWWQTETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDlDGNpvesdqggfLVIKQPwpSMIRDVYG---------DTD 487
Cdd:cd05907 241 GYGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIAD-DGE---------ILVRGP--NVMLGYYKnpeataealDAD 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 488 RFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVI-NVSGHRLGTMEIESALVSHPLVAEAAVVGR------ 560
Cdd:cd05907 307 GWLHT----------------GDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDgrpflv 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 561 ----PDEltgEAIFAFVSLEGNAEPS-EELKKD--LVKHVTEEIGAI----ARPAEIR-FTdVLPK---------TRSGK 619
Cdd:cd05907 371 alivPDP---EALEAWAEEHGIAYTDvAELAANpaVRAEIEAAVEAAnarlSRYEQIKkFL-LLPEpftiengelTPTLK 446
|
....
gi 6647434 620 IMRR 623
Cdd:cd05907 447 LKRP 450
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
107-626 |
6.15e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.79 E-value: 6.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 107 EPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVFGGFSAEALRDRLVD--- 183
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIKKqae 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 184 -AEAKLVITADGGFRKDKAIALKqevdkalehgapsvenVIVVQRTKADVTMTagrdhwWHEL---QPQQSAHCPAEPID 259
Cdd:PLN02330 125 aAGAKLIVTNDTNYGKVKGLGLP----------------VIVLGEEKIEGAVN------WKELleaADRAGDTSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 260 SEDMLFILYTSGSTGKPKGVVHTTggYNLYTHMTTKwIFDLKdTDVYWCTADVGWIT-----GHSYIVYGPLSNGATTVm 334
Cdd:PLN02330 183 QTDLCALPFSSGTTGISKGVMLTH--RNLVANLCSS-LFSVG-PEMIGQVVTLGLIPffhiyGITGICCATLRNKGKVV- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 yegvprpsnpgcfwdVIERYGVNIFYTA------------PTAIRAFIRmgEAVPNARDLSSLRL--LGTVGEPINPEAW 400
Cdd:PLN02330 258 ---------------VMSRFELRTFLNAlitqevsfapivPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 401 MWYHRVIGGGKcpIVDTWWQTETGGIMLT---PLPGAIPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPwp 476
Cdd:PLN02330 321 TAFEAKFPGVQ--VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQ-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 SMIRDVYGDTDRFRHTY----WEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV 552
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIdedgWLH-----------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6647434 553 AEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PLN02330 466 EDAAVVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
96-626 |
7.30e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.91 E-value: 7.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRNKAAIiwegEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVF----GG 171
Cdd:PRK07514 15 DRDAPFI----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 172 FSAEALRDRLVDAEAKLVITADGGFRKDKAIALKqevdkaleHGAPSVEnvivvqrtkadvTMTAGRDHWWHELQPQQSA 251
Cdd:PRK07514 87 YTLAELDYFIGDAEPALVVCDPANFAWLSKIAAA--------AGAPHVE------------TLDADGTGSLLEAAAAAPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 252 HCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTTkwifdLKDtdvYWctadvGWITG----HSYIVY---- 323
Cdd:PRK07514 147 DFETVPRGADDLAAILYTSGTTGRSKGAMLSHG--NLLSNALT-----LVD---YW-----RFTPDdvliHALPIFhthg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 ------GPLSNGATTVMyegVPR--PSnpgcfwDVIERY-------GVNIFYTAPTAIRAFIRmgEAVpnardlSSLRLL 388
Cdd:PRK07514 212 lfvatnVALLAGASMIF---LPKfdPD------AVLALMpratvmmGVPTFYTRLLQEPRLTR--EAA------AHMRLF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 389 GTVGEPINPEAWM-WYHRViggGKcPIVDTWWQTETGgiMLT--PLPGAipTKPGSCTKPFPGIVAEIVDLD-GNPVESD 464
Cdd:PRK07514 275 ISGSAPLLAETHReFQERT---GH-AILERYGMTETN--MNTsnPYDGE--RRAGTVGFPLPGVSLRVTDPEtGAELPPG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 465 QGGFLVIKQPwpsmirDVYGDtdrfrhtYWeHIQPKEGQYL----YF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGT 539
Cdd:PRK07514 347 EIGMIEVKGP------NVFKG-------YW-RMPEKTAEEFradgFFiTGDLGKIDERGYVHIVGRGKDLIISGGYNVYP 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 540 MEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKhvteeiGAIAR---PAEIRFTDVLPKTR 616
Cdd:PRK07514 413 KEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK------GRLARfkqPKRVFFVDELPRNT 486
|
570
....*....|
gi 6647434 617 SGKIMRRLLR 626
Cdd:PRK07514 487 MGKVQKNLLR 496
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
110-626 |
9.30e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 126.74 E-value: 9.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYL----PMIpEAAitmLACSRIGAPHSVVFGGFSAEALRDRLVDAE 185
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMrndfAFF-EAA---YAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 186 AK-LVITADggfrkdkaiaLKQEVDKALEHG-----APSVENVIVVQRTKAD-VTMTAGRDHWWHELQPQQSAHCPAEPI 258
Cdd:PRK12406 84 ARvLIAHAD----------LLHGLASALPAGvtvlsVPTPPEIAAAYRISPAlLTPPAGAIDWEGWLAQQEPYDGPPVPQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSEdmlfILYTSGSTGKPKGVVHT--TGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSY-IVYGPLsnGATTVMy 335
Cdd:PRK12406 154 PQS----MIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYgLRAGRL--GGVLVL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 egVPRpSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRllgtvgepinpeawmwyHRVIGGGKCP-- 413
Cdd:PRK12406 227 --QPR-FDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLR-----------------HVIHAAAPCPad 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 ----IVDtWW---------QTETGGIMLTPLPGAIpTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmir 480
Cdd:PRK12406 287 vkraMIE-WWgpviyeyygSTESGAVTFATSEDAL-SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA------ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 dvyGDTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGR 560
Cdd:PRK12406 359 ---GNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGI 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 561 PDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK12406 436 PDAEFGEALMAVVEPQPGATLDEA---DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
88-630 |
1.18e-30 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 126.64 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTwrrNKAAIIwEGEpgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIG-APHS 166
Cdd:PRK10946 31 LTRHAAS---DAIAVI-CGE----RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGvAPVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 167 VVFGGFSAEaLRDRLVDAEAKLVItADGG---FRKDKAIalkqevdKALEHGAPSVENVIVvqrtkADVTMTAGRDHWwh 243
Cdd:PRK10946 103 ALFSHQRSE-LNAYASQIEPALLI-ADRQhalFSDDDFL-------NTLVAEHSSLRVVLL-----LNDDGEHSLDDA-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 244 eLQpQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADvgwiTGHSYivy 323
Cdd:PRK10946 167 -IN-HPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDY-YYSVRRSVEICGFTPQTRYLCALP----AAHNY--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 gPLSN-GATTVMYEG-----VPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINP 397
Cdd:PRK10946 237 -PMSSpGALGVFLAGgtvvlAPDPSATLCF-PLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 398 EAWMWYHRVIGggkCPIVDTWWQTEtGGIMLTPL---PGAIPTKPGSCTKPFPGIvaEIVDLDGNPVESDQGGFLvikqp 474
Cdd:PRK10946 315 TLARRIPAELG---CQLQQVFGMAE-GLVNYTRLddsDERIFTTQGRPMSPDDEV--WVADADGNPLPQGEVGRL----- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 475 wpsMIRDVYgdtdRFRHTYW--EHIQP---KEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSH 549
Cdd:PRK10946 384 ---MTRGPY----TFRGYYKspQHNASafdANG--FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRH 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 550 PLVAEAAVVGRPDELTGEAIFAFVSlegnaePSEELKK-DLVKHVTEEigAIAR---PAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK10946 455 PAVIHAALVSMEDELMGEKSCAFLV------VKEPLKAvQLRRFLREQ--GIAEfklPDRVECVDSLPLTAVGKVDKKQL 526
|
....*
gi 6647434 626 RSLAS 630
Cdd:PRK10946 527 RQWLA 531
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
114-629 |
1.44e-30 |
|
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: 125.91 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSlGVQKGDRVAIYLPMIPEAAITMLACSRIG-APhsvVFGGFSA--EALRDRLVDAEAKLVI 190
Cdd:cd05909 8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGkVP---VMLNYTAglRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TAdggfrkdkaialKQEVDKALEHGAPSVE---NVIVVQRTKADVTmtagrdhWWHELQPQQSAHCPAE---------PI 258
Cdd:cd05909 84 TS------------KQFIEKLKLHHLFDVEydaRIVYLEDLRAKIS-------KADKCKAFLAGKFPPKwllrifgvaPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSEDMLFILYTSGSTGKPKGVVHTTggYNLYTH-MTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYeg 337
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSH--KNLLANvEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 vPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGeavpNARDLSSLRLLGTVGEPINPEAW-MWYHRViggGKcPIVD 416
Cdd:cd05909 221 -PNPLDYKKIPELIYDKKATILLGTPTFLRGYARAA----HPEDFSSLRLVVAGAEKLKDTLRqEFQEKF---GI-RILE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 417 TWWQTETGGIMLTPLPGAiPTKPGSCTKPFPGIVAEIVDLDGN-PVESDQGGFLVIKQPwpsMIRDVYGDTDrfrhtywE 495
Cdd:cd05909 292 GYGTTECSPVISVNTPQS-PNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGP---NVMLGYLNEP-------E 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 496 HIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSH-PLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:cd05909 361 LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 575 LEgNAEPSEelkkdLVKHVTE-EIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:cd05909 441 TT-DTDPSS-----LNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-625 |
2.49e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 128.54 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVFGGFSAEALRDRLV----DAE 185
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG----AYVPLDPEYPRERLAymmeDSG 4648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 186 AKLVITadggfrkdkaialkqevDKALEHGAPSVENV--IVVQRTkadvtmtagrDHWwhelqPQQSAHCPAEPIDSEDM 263
Cdd:PRK12316 4649 AALLLT-----------------QSHLLQRLPIPDGLasLALDRD----------EDW-----EGFPAHDPAVRLHPDNL 4696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 264 LFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKwifdlkdtdVYWCTAD--VGWITGHSYIV-----YGPLSNGATTVMYE 336
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGE---------RYELTPDdrVLQFMSFSFDGsheglYHPLINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 337 gvPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIrmgEAVPNARDLSSLRLLGTVGEPINP----EAW-----MWYHRVI 407
Cdd:PRK12316 4768 --DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLA---EHAERDGEPPSLRVYCFGGEAVAQasydLAWralkpVYLFNGY 4842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 GGGKCPIVDTWWQTETGGImltPLPGAIPTKpgsctKPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQPWPS 477
Cdd:PRK12316 4843 GPTETTVTVLLWKARDGDA---CGAAYMPIG-----TPLGNRSGYVLDGQLNPLPVGVAGELYLggegvargylERPALT 4914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 478 MIRDVygdTDRFrhtywehiqPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAV 557
Cdd:PRK12316 4915 AERFV---PDPF---------GAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 558 VGRPDElTGEAIFAFV---------SLEGNAEPSEELKKDLVKHVTEEIgaiaRPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12316 4983 IAQEGA-VGKQLVGYVvpqdpaladADEAQAELRDELKAALRERLPEYM----VPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
114-628 |
4.81e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 124.95 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANAL-KSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITA 192
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 193 dggfrkdkaialKQEVDKALEHGAPsvenVIVVQRTkADVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGS 272
Cdd:PLN02574 147 ------------PENVEKLSPLGVP----VIGVPEN-YDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVVHTTGgyNLYTHMTTKWIFDLKD------TDVYWCTADVGWITGHSYIVYGPLSNGATTVmyegVPRPSNPGC 346
Cdd:PLN02574 210 TGASKGVVLTHR--NLIAMVELFVRFEASQyeypgsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIV----VMRRFDASD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 347 FWDVIERYGVNIFYTAPTAIRAFIRMGEAVpNARDLSSLRLLGTVGEPINPEAWMWYHRVIgggkcPIVD---TWWQTET 423
Cdd:PLN02574 284 MVKVIDRFKVTHFPVVPPILMALTKKAKGV-CGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-----PHVDfiqGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 424 GGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPW-------PSMIRDVYGDTDRFRHTywe 495
Cdd:PLN02574 358 TAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWStGCLLPPGNCGELWIQGPGvmkgylnNPKATQSTIDKDGWLRT--- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 496 hiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL 575
Cdd:PLN02574 435 -------------GDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6647434 576 EGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSL 628
Cdd:PLN02574 502 RQGSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
96-626 |
4.91e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.23 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 96 RRN--KAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYlpMIPEAAIT--MLACSRIGAPHSVVFGG 171
Cdd:PRK06145 13 RRTpdRAALVYRDQE-----ISYAEFHQRILQAAGMLHARGIGQGDVVALL--MKNSAAFLelAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 172 FSAEALRDRLVDAEAKLVItadggfrkdkaialkqeVDKALEHGAPSVENVIVV-QRTKADVTMTAgrdhwwhelQPQQS 250
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETPKIVIdAAAQADSRRLA---------QGGLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 251 AhCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGgynlythmttkwifdlkdtDVYWCTAD----VGWITGHSYIVYGPL 326
Cdd:PRK06145 140 I-PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLVVGPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 SN-GA-----TTVMYEG----VPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEavPNARDLSSLRLLGTVGEPIN 396
Cdd:PRK06145 200 YHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPD--RDRFDLDSLAWCIGGGEKTP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 397 PEAWMWYHRVIGGGKcpIVDTWWQTET-GGIMLTPlPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPw 475
Cdd:PRK06145 278 ESRIRDFTRVFTRAR--YIDAYGLTETcSGDTLME-AGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 476 psmirdvygdtdRFRHTYWEhiQPKEGQYLYF-----AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHP 550
Cdd:PRK06145 354 ------------KVTKGYWK--DPEKTAEAFYgdwfrSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELP 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 551 LVAEAAVVGRPDELTGEAIFAFVSLegNAEPSEELKKdLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK06145 420 EVAEAAVIGVHDDRWGERITAVVVL--NPGATLTLEA-LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
173-627 |
1.05e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 123.64 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 173 SAEALRDRLVDAEAKLVITadggfrKDKAIALKQEVDkalehgaPSVEnVIVVQRtkadvtmtagrDHWWHELQPQQSAH 252
Cdd:PRK07867 89 RGAALARDIAHADCQLVLT------ESAHAELLDGLD-------PGVR-VINVDS-----------PAWADELAAHRDAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 253 CPAEPIDSEDMLFILYTSGSTGKPKGVVHTTG-----GYNLYTHmttkwiFDLKDTDVYWCTAD--------VGWITGhs 319
Cdd:PRK07867 144 PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVMLAQR------FGLGPDDVCYVSMPlfhsnavmAGWAVA-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 320 yivygpLSNGATTVMyegvPRPSNPGCFWDVIERYGVNIFYTAPTAIrAFIRMGEAVPNARDlSSLRLL-GTVGEPINPE 398
Cdd:PRK07867 216 ------LAAGASIAL----RRKFSASGFLPDVRRYGATYANYVGKPL-SYVLATPERPDDAD-NPLRIVyGNEGAPGDIA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 399 AwmwYHRVIGggkCPIVDTWWQTEtGGIMLTPLPGaipTKPGSCTKPFPGIvaEIVDLDGN----PVESDQGGFLVIKQP 474
Cdd:PRK07867 284 R---FARRFG---CVVVDGFGSTE-GGVAITRTPD---TPPGALGPLPPGV--AIVDPDTGtecpPAEDADGRLLNADEA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 475 WPSMI------------RDVYGDTDRFRH-TYWehiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTME 541
Cdd:PRK07867 352 IGELVntagpggfegyyNDPEADAERMRGgVYW-------------SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAP 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 542 IESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAE-PSEELKKDLvkHVTEEIGAIARPAEIRFTDVLPKTRSGKI 620
Cdd:PRK07867 419 IERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKV 496
|
....*..
gi 6647434 621 MRRLLRS 627
Cdd:PRK07867 497 LKRQLSA 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-625 |
1.21e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.04 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 21 FSERAYVRSGREYEQLYSRAASNPEKFWGELAEQELHwfkKWDQVL-DWQPPFAKWFVGGQLnisHNCLDRHLTTwRRNK 99
Cdd:PRK12467 3039 FDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAH---ERRQVLhAWNATAAAYPSERLV---HQLIEAQVAR-TPEA 3111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 100 AAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRD 179
Cdd:PRK12467 3112 PALVFGD-----QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 180 RLVDAEAKLVITadggfrkdkaialKQEVdkaLEH-GAPSVENVIVVQRtkadvtmtagrDHWWHElqpqqSAHCPAEPI 258
Cdd:PRK12467 3187 MIEDSGVKLLLT-------------QAHL---LEQlPAPAGDTALTLDR-----------LDLNGY-----SENNPSTRV 3234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHmttkWIFDLKDTDVywcTADVGWITGHSYIV-----YGPLSNGATTV 333
Cdd:PRK12467 3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLC----WIAEAYELDA---NDRVLLFMSFSFDGaqerfLWTLICGGCLV 3307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 334 MYEGVPRpsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEavpnARDLSSLRLLGTVGEPINPEAWMWYHRVI------ 407
Cdd:PRK12467 3308 VRDNDLW--DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFEQVKRKLkprglt 3381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 ---GGGKCPIVDTWWQTETGGImltPLPGAIPTKpgsctKPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQP 474
Cdd:PRK12467 3382 ngyGPTEAVVTVTLWKCGGDAV---CEAPYAPIG-----RPVAGRSIYVLDGQLNPVPVGVAGELYIggvglargyhQRP 3453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 475 WPSMIRDVygdTDRFRHTywehiqpkeGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAE 554
Cdd:PRK12467 3454 SLTAERFV---ADPFSGS---------GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 555 AAVVGRPDElTGEAIFAFVSLEgnaEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12467 3522 AVVLARDGA-GGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
114-628 |
3.47e-29 |
|
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: 122.25 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIG---APHSVVFggfSAEALRDRLVDAEAKLVI 190
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGvgvAPTNDIY---NERELDHSLNISKPTIVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADGGFrkDKAIALKQEVdkalehgaPSVENVIVVQrTKADVTMTAGRDHWWHELQP---QQSAHCPAEPIDSEDMLFIL 267
Cdd:cd17642 122 CSKKGL--QKVLNVQKKL--------KIIKTIIILD-SKEDYKGYQCLYTFITQNLPpgfNEYDFKPPSFDRDEQVALIM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVvhttggynLYTHMTTKWIFDLKDTDVYWC-----TADVGWITGHS----YIVYGPLSNGATTVMyegV 338
Cdd:cd17642 191 NSSGSTGLPKGV--------QLTHKNIVARFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRVVL---M 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 339 PRPSNPgCFWDVIERYGVNIFYTAPTaIRAFIRMGEAVpNARDLSSLRLLGTVGEPINPEAWMWYHRVIgggKCPIV-DT 417
Cdd:cd17642 260 YKFEEE-LFLRSLQDYKVQSALLVPT-LFAFFAKSTLV-DKYDLSNLHEIASGGAPLSKEVGEAVAKRF---KLPGIrQG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 418 WWQTE-TGGIMLTPlpgAIPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQPwpsMI-RDVYGDTDRFRHtyw 494
Cdd:cd17642 334 YGLTEtTSAILITP---EGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGP---MImKGYVNNPEATKA--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 ehIQPKEGqYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:cd17642 405 --LIDKDG-WLH-SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 575 LEGNAEPSEelkKDLVKHVTEEIGAIAR-PAEIRFTDVLPKTRSGKIMRRLLRSL 628
Cdd:cd17642 481 LEAGKTMTE---KEVMDYVASQVSTAKRlRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
98-626 |
3.98e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 121.65 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIwEGEPGDSriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRigaphsvvfGGFSAEAL 177
Cdd:PRK13390 12 DRPAVI-VAETGEQ--VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALR---------SGLYITAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVItADGGFRKDKAIALKQEVdkALEHGAPsvenvivvqrtkADVTMT-AGRDHWWHELQPQQSAHCP-- 254
Cdd:PRK13390 80 NHHLTAPEADYIV-GDSGARVLVASAALDGL--AAKVGAD------------LPLRLSfGGEIDGFGSFEAALAGAGPrl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 255 -AEPIDSedmlFILYTSGSTGKPKGVVHTTGGYNLYTH-----MTTKWIFDLKDTDVYWCTADVGwitgHSyivyGPL-- 326
Cdd:PRK13390 145 tEQPCGA----VMLYSSGTTGFPKGIQPDLPGRDVDAPgdpivAIARAFYDISESDIYYSSAPIY----HA----APLrw 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 -----SNGATTVMYEGVPRPSNPGcfwdVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLR--LLGTVGEPINPEA 399
Cdd:PRK13390 213 csmvhALGGTVVLAKRFDAQATLG----HVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRavIHAAAPCPVDVKH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 400 WM--WyhrvIGggkcPIVDTWWQ-TETGGIMLTPLPGAIpTKPGSCTKPFPGIVaEIVDLDGNPVESDQGGflvikqpwp 476
Cdd:PRK13390 289 AMidW----LG----PIVYEYYSsTEAHGMTFIDSPDWL-AHPGSVGRSVLGDL-HICDDDGNELPAGRIG--------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 smirDVYGDTDRFRHTYweHIQPK---EGQ-----YLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVS 548
Cdd:PRK13390 350 ----TVYFERDRLPFRY--LNDPEktaAAQhpahpFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTM 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 549 HPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK13390 424 HPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
114-625 |
4.29e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 124.68 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GGFRKdkaIALKQEVDK-ALEHGAPSVENvivvqrtkadvtmtagrdhwwhelqpqQSAHCPAEPIDSEDMLFILYTSGS 272
Cdd:PRK12316 617 HLGRK---LPLAAGVQVlDLDRPAAWLEG---------------------------YSEENPGTELNPENLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVVHTTGGY-NLYTHMTTKWIFDLKDT--DVYWCTADVGwitghSYIVYGPLSNGATTVM-YEGVPRpsNPGCFW 348
Cdd:PRK12316 667 TGKPKGAGNRHRALsNRLCWMQQAYGLGVGDTvlQKTPFSFDVS-----VWEFFWPLMSGARLVVaAPGDHR--DPAKLV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAFIRmGEAVPnarDLSSLRLLGTVGEPI------NPEAWMWYHRVI---GGGKCPIVDTWW 419
Cdd:PRK12316 740 ELINREGVDTLHFVPSMLQAFLQ-DEDVA---SCTSLRRIVCSGEALpadaqeQVFAKLPQAGLYnlyGPTEAAIDVTHW 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 420 Q-TETGGimltplpGAIPTKpgsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwPSMIRDVYG----DTDRFRHTYW 494
Cdd:PRK12316 816 TcVEEGG-------DSVPIG-----RPIANLACYILDANLEPVPVGVLGELYLAG--RGLARGYHGrpglTAERFVPSPF 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 ehiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGrpdeLTGEAIFAFVS 574
Cdd:PRK12316 882 -----VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVV 952
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 6647434 575 LEgnaEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12316 953 LE---SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
115-626 |
4.60e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 121.78 E-value: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVItADG 194
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF-APT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 GFRK----DKAIALKQEVdkalehgaPSVENVIVVQRTkADVTMTAGRDHWWHELQPQQSAhcpaEPIDSEDMLFILYTS 270
Cdd:PRK06087 130 LFKQtrpvDLILPLQNQL--------PQLQQIVGVDKL-APATSSLSLSQIIADYEPLTTA----ITTHGDELAAVLFTS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 271 GSTGKPKGVVHTTG-------GYNLYTHMTTKwifdlkdtDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVprpsN 343
Cdd:PRK06087 197 GTEGLPKGVMLTHNnilaserAYCARLNLTWQ--------DVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF----T 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 344 PGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNarDLSSLRLLGTVGEPInPEAwmwyhrvigggkcpIVDTWWQTet 423
Cdd:PRK06087 265 PDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPA--DLSALRFFLCGGTTI-PKK--------------VARECQQR-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 424 gGIMLTPLPGA---IP---TKPGSCTK--------PFPGIVAEIVDLDGNPV-------ESDQGgflvikqpwPSMIRDV 482
Cdd:PRK06087 326 -GIKLLSVYGStesSPhavVNLDDPLSrfmhtdgyAAAGVEIKVVDEARKTLppgcegeEASRG---------PNVFMGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 YGDTDRFRHTYWEhiqpkEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:PRK06087 396 LDEPELTARALDE-----EG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 563 ELTGEAIFAFVSLEGNaEPSEELkKDLVKHV-TEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK06087 469 ERLGERSCAYVVLKAP-HHSLTL-EEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
88-629 |
4.78e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 121.77 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLttwRRNKAAIIWEGEPgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSV 167
Cdd:PRK06164 16 LDAHA---RARPDAVALIDED---RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFGGFSAEALRDRLVDAEAKLVITADgGFRKDKAIALKQEVDKALEHGAPSvenVIVVQRTKADVTMTAGRDhwWHELQP 247
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWP-GFKGIDFAAILAAVPPDALPPLRA---IAVVDDAADATPAPAPGA--RVQLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 QQSAHCPA---EPIDSEDMLFILY-TSGSTGKPKGVVHTTGGYNLYTHMTTKwIFDLKDTDVYWCTADVGWITGHSYIVy 323
Cdd:PRK06164 164 LPDPAPPAaagERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 GPLSNGATTVMYEgvprpsnpgcfwdvierygvnIFYTAPTAIR--------------AFIRMGEAVPNARDLSSLRLLG 389
Cdd:PRK06164 242 GALAGGAPLVCEP---------------------VFDAARTARAlrrhrvthtfgndeMLRRILDTAGERADFPSARLFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 390 TVG-EPINPE--AWMWYHRVigggkcPIVDTWWQTETGGIML---TPLPGAIPTKPGScTKPFPGIVAEIVD-LDGNPVE 462
Cdd:PRK06164 301 FASfAPALGElaALARARGV------PLTGLYGSSEVQALVAlqpATDPVSVRIEGGG-RPASPEARVRARDpQDGALLP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 463 SDQGGFLVIKQpwPSMIRDVYGDTDRFRhtywEHIQPkEGqylYF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTME 541
Cdd:PRK06164 374 DGESGEIEIRA--PSLMRGYLDNPDATA----RALTD-DG---YFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 542 IESALVSHPLVAEAAVVGRpdELTGEAI-FAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSG-- 618
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGA--TRDGKTVpVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAng 518
|
570
....*....|..
gi 6647434 619 -KIMRRLLRSLA 629
Cdd:PRK06164 519 aKIQKHRLREMA 530
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
98-633 |
1.02e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 120.27 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEgepgdSRIITYAQLHREVCQFANALKSLGvQKGDRVAIYLPMIPE-----AAITMLACsrIGAPHSVvfgGF 172
Cdd:PRK07638 16 NKIAIKEN-----DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEflqlfAGAAMAGW--TCVPLDI---KW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 173 SAEALRDRLVDAEAKLVITADggFRKDKAIalkqEVDKAlehgapsvenVIVVQRTKADVTMTAGRdhwwhelqpqqsah 252
Cdd:PRK07638 85 KQDELKERLAISNADMIVTER--YKLNDLP----DEEGR----------VIEIDEWKRMIEKYLPT-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 253 cPAEPIDSEDMLFIL-YTSGSTGKPKGvvhttggynlYTHMTTKWI--FDLKDTDVYWCTADVGWITG---HSYIVYGPL 326
Cdd:PRK07638 135 -YAPIENVQNAPFYMgFTSGSTGKPKA----------FLRAQQSWLhsFDCNVHDFHMKREDSVLIAGtlvHSLFLYGAI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 SN---GATTVMYegvpRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMgEAVPNARDlsslrllgtvgepinpeawmwy 403
Cdd:PRK07638 204 STlyvGQTVHLM----RKFIPNQVLDKLETENISVMYTVPTMLESLYKE-NRVIENKM---------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 hRVIGGGkcpivdTWWQTETGGIMLTPLPGA-----------------IPT----KPGSCTKPFPGIVAEIVDLDGNPVE 462
Cdd:PRK07638 257 -KIISSG------AKWEAEAKEKIKNIFPYAklyefygaselsfvtalVDEeserRPNSVGRPFHNVQVRICNEAGEEVQ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 463 SDQGGFLVIKQPWPSMirdvygdtdRFRHTYWEHIQPKEGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEI 542
Cdd:PRK07638 330 KGEIGTVYVKSPQFFM---------GYIIGGVLARELNADGWMT-VRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEI 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 543 ESALVSHPLVAEAAVVGRPDELTGEAIFAFVslEGNAEpseelKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMR 622
Cdd:PRK07638 400 ESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSAT-----KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
570
....*....|.
gi 6647434 623 RLLRSLASGQE 633
Cdd:PRK07638 473 MEAKSWIENQE 483
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
112-626 |
1.48e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 120.49 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphSVVFGG--FSAEALRDRLVDAEAKLV 189
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA--VVVEHNplYTAHELEHPFEDHGARVA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADggfrkdKAIALKQEV--DKALEHgAPSVeNVI----VVQRT----------KADVTMTAGRDHW--WHELQ----- 246
Cdd:PRK05605 134 IVWD------KVAPTVERLrrTTPLET-IVSV-NMIaampLLQRLalrlpipalrKARAALTGPAPGTvpWETLVdaaig 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 247 -PQQSAHCPAepIDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTH--MTTKWIFDLKDTDvywctadvgwitghsYIVY 323
Cdd:PRK05605 206 gDGSDVSHPR--PTPDDVALILYTSGTTGKPKGAQLTHR--NLFANaaQGKAWVPGLGDGP---------------ERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 GPL----------------SNGATTVMYegvPRPSNPgCFWDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLR- 386
Cdd:PRK05605 267 AALpmfhaygltlcltlavSIGGELVLL---PAPDID-LILDAMKKHPPTWLPGVPPLYEKI--AEAAEERGVDLSGVRn 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 387 -LLGTVGEPINP-EAWmwyHRVIGGgkcPIVDTWWQTETGGIML-TPLPGAipTKPGSCTKPFPGIVAEIVDLDgNPVES 463
Cdd:PRK05605 341 aFSGAMALPVSTvELW---EKLTGG---LLVEGYGLTETSPIIVgNPMSDD--RRPGYVGVPFPDTEVRIVDPE-DPDET 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 464 ---DQGGFLVIKQPwpsmirdvygdtDRFrHTYWEhiQPKEGQYL-----YFAGDGARRDKDGYFWVMGRVDDVINVSGH 535
Cdd:PRK05605 412 mpdGEEGELLVRGP------------QVF-KGYWN--RPEETAKSfldgwFRTGDVVVMEEDGFIRIVDRIKELIITGGF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 536 RLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDlvkHVTEEIGAIARPAEIRFTDVLPKT 615
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRA---YCREHLTRYKVPRRFYHVDELPRD 553
|
570
....*....|.
gi 6647434 616 RSGKIMRRLLR 626
Cdd:PRK05605 554 QLGKVRRREVR 564
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
254-626 |
2.79e-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: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 254 PAEPIDSE----DMLfilYTSGSTGKPKGVV--HTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYiVYGPLS 327
Cdd:cd05929 117 PETPIEDEaagwKML---YSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRW-SMTALF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 328 NGATTVMYEGVprpsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINP---EAWM-WY 403
Cdd:cd05929 193 MGGTLVLMEKF----DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 HRVI--------GGGKCPIVDTWWQTEtggimltplpgaiptkPGSCTKPFPGIVaEIVDLDGNPVESDQGGFLVIKQPW 475
Cdd:cd05929 269 GPIIweyyggteGQGLTIINGEEWLTH----------------PGSVGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 476 PSmirdvygdtDRFRHTYWEHIQPKEGQYLYFaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEA 555
Cdd:cd05929 332 GF---------EYTNDPEKTAAARNEGGWSTL-GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDA 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 556 AVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05929 402 AVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
112-629 |
1.28e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 117.67 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFAN-ALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVI 190
Cdd:PRK08751 49 KTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADG-GFRKDKAIA---LKQEVDKALEH--GAP--SVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAH-CPAEPIDSE 261
Cdd:PRK08751 129 VIDNfGTTVQQVIAdtpVKQVITTGLGDmlGFPkaALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHsMPTLQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 262 DMLFILYTSGSTGKPKGVVHTTggYNLYTHM--TTKWifdLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEG-- 337
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTH--RNLVANMqqAHQW---LAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGcn 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 --VPRPSNPGCFWDVIERY------GVNIFYTAPTAIRAFIRMgeavpnarDLSSLRLLGTVGEPINPEAWMWYHRVIGg 409
Cdd:PRK08751 284 hlISNPRDMPGFVKELKKTrftaftGVNTLFNGLLNTPGFDQI--------DFSSLKMTLGGGMAVQRSVAERWKQVTG- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 410 gkCPIVDTWWQTETG-GIMLTPLpgAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmirdvygdtdR 488
Cdd:PRK08751 355 --LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP-------------Q 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 489 FRHTYWEhiQPKEGQYLYFA------GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:PRK08751 418 VMKGYWK--RPEETAKVMDAdgwlhtGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPD 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6647434 563 ELTGEAIFAFVSLEGNAEPSEELKkdlvKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK08751 496 EKSGEIVKVVIVKKDPALTAEDVK----AHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
104-645 |
1.33e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 118.60 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 104 WEGEPG--DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGaphsvvFGGFSA--EALRD 179
Cdd:PRK06060 19 WYDRPAfyAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG------VMAFLAnpELHRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 180 RLV----DAEAKLVITaDGGFRkdkaialkqevdkalEHGAPSveNVIVVQRTKADVTMTAGRDHwwhelqpqqsahcpa 255
Cdd:PRK06060 93 DHAlaarNTEPALVVT-SDALR---------------DRFQPS--RVAEAAELMSEAARVAPGGY--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 256 EPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMY 335
Cdd:PRK06060 140 EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVIN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 egvPRPSNPGCFWDVIERYGVNIFYTAPTAiraFIRMGEAVpNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkCPIV 415
Cdd:PRK06060 220 ---SAPVTPEAAAILSARFGPSVLYGVPNF---FARVIDSC-SPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPIL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETGGIMLTPlpGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmirdvygdtdRFRHTYWE 495
Cdd:PRK06060 291 DGIGSTEVGQTFVSN--RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGP-------------AIAKGYWN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 496 HIQP--KEGQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGrPDELTGEAIF-AF 572
Cdd:PRK06060 356 RPDSpvANEGWLD-TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA-VRESTGASTLqAF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 573 VSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS---------LASGQEISGDTSTLED 643
Cdd:PRK06060 434 LVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKqsptkpiweLSLTEPGSGVRAQRDD 513
|
..
gi 6647434 644 RT 645
Cdd:PRK06060 514 LS 515
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-625 |
2.40e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.12 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 15 FDPPTEFSERAYV-RSGREYEQLYSRAASNPEKFWGELA---EQELHWFKKWDQVLdwQPPFAKWFVGGqlnishncLDR 90
Cdd:PRK05691 1070 FDYAAELFDAATIeRLAEHFLALLEQVCEDPQRALGDVQlldAAERAQLAQWGQAP--CAPAQAWLPEL--------LNE 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 91 H--LTTWRRnkaAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVV 168
Cdd:PRK05691 1140 QarQTPERI---ALVWDGGS-----LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 169 FGGFSAEALRDRLVDAEAKLVITadggfrkdkaialkqevDKALEHGAPSVENVIVVQRTKADVtmtagrDHWwhelqpq 248
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELLLT-----------------QSHLLERLPQAEGVSAIALDSLHL------DSW------- 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 249 qSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHmttkWI---FDLKDTDVYWCTADVGWITGhSYIVYGP 325
Cdd:PRK05691 1262 -PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ----WMqatYALDDSDVLMQKAPISFDVS-VWECFWP 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 326 LSNGATTVMyEGVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMgeavPNARDLSSLRLLGTVGEPINPE------- 398
Cdd:PRK05691 1336 LITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE----PLAAACTSLRRLFSGGEALPAElrnrvlq 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 399 --AWMWYHRVIGGGKCPIVDTWWQTETGGIMLTPLpgaiptkpgscTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwP 476
Cdd:PRK05691 1411 rlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIGG--A 1477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 SMIRDVYG----DTDRFRhtywehIQP--KEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHP 550
Cdd:PRK05691 1478 GLARGYLGrpalTAERFV------PDPlgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQP 1551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 551 LVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLvkhvTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK05691 1552 GVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAAL----AAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
262-622 |
2.55e-27 |
|
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: 113.13 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 262 DMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWITGhsyivygplSNGATTVMYEG---- 337
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNL-IAANLQLIHAMGLTEADVYLNMLPLFHIAG---------LNLALATFHAGganv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 VPRPSNPGCFWDVIERYGVNIFYTAPtAIRAFIrMGEAVPNARDLSSLRLLGTVGEPINPEAWmwyHRVIGGgkcpivdT 417
Cdd:cd17637 71 VMEKFDPAEALELIEEEKVTLMGSFP-PILSNL-LDAAEKSGVDLSSLRHVLGLDAPETIQRF---EETTGA-------T 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 418 WW----QTETGGIMLTplpGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsMIrdvygdtdrFrHTY 493
Cdd:cd17637 139 FWslygQTETSGLVTL---SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGP---LV---------F-QGY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 494 WEhiQPKEGQYLY-----FAGDGARRDKDGYFWVMGRV--DDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTG 566
Cdd:cd17637 203 WN--LPELTAYTFrngwhHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 567 EAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMR 622
Cdd:cd17637 281 EGIKAVCVLKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-629 |
2.75e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 116.45 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADG 194
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gFRKDKAIALKQEVD---KALEHGA------PSVENVIVVQRTK-------ADVTMTAGR--DHWWHELQPQQSAHcpaE 256
Cdd:PRK08315 125 -FKDSDYVAMLYELApelATCEPGQlqsarlPELRRVIFLGDEKhpgmlnfDELLALGRAvdDAELAARQATLDPD---D 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 257 PIDsedmlfILYTSGSTGKPKGVVHT-----TGGYNLYTHMttkwifDLKDTD-------VYWCtadVGWITGhsyiVYG 324
Cdd:PRK08315 201 PIN------IQYTSGTTGFPKGATLThrnilNNGYFIGEAM------KLTEEDrlcipvpLYHC---FGMVLG----NLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 325 PLSNGATTVMyegvPRPS-NPGCFWDVIER------YGVnifytaPTAiraFIRMGEaVPN--ARDLSSLRllgtVGepi 395
Cdd:PRK08315 262 CVTHGATMVY----PGEGfDPLATLAAVEEerctalYGV------PTM---FIAELD-HPDfaRFDLSSLR----TG--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 396 npeawmwyhrVIGGGKCPI------VD---------TWWQTETGgimltplPGAIPTKPGS-----CT---KPFPGIVAE 452
Cdd:PRK08315 321 ----------IMAGSPCPIevmkrvIDkmhmsevtiAYGMTETS-------PVSTQTRTDDplekrVTtvgRALPHLEVK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 453 IVDLD-GNPVE-SDQG-----GFLVIKQPW--PSMIRDVYgDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVM 523
Cdd:PRK08315 384 IVDPEtGETVPrGEQGelctrGYSVMKGYWndPEKTAEAI-DADGWMHT----------------GDLAVMDEEGYVNIV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 524 GRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKhvteeiGAIAR- 602
Cdd:PRK08315 447 GRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCR------GKIAHy 520
|
570 580
....*....|....*....|....*....
gi 6647434 603 --PAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK08315 521 kiPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-625 |
2.92e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.52 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PRK12316 2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadggfrkdkaialkqevDKALEHGAPSVENVIVVQRTkadvtmtagRDHWWHElQPQqsaHCPAEPIDSEDMLFILYT 269
Cdd:PRK12316 2105 LT-----------------QRHLLERLPLPAGVARLPLD---------RDAEWAD-YPD---TAPAVQLAGENLAYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGVVHTTGGYNLYTHMTTKWiFDLKDTDVYWCTADVGWITGHSYIvYGPLSNGATTVMYEGVPRpsNPGCFWD 349
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQW-FHPLLNGARVLIRDDELW--DPEQLYD 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 350 VIERYGVNIFYTAPTAIRAFIRMGEavpNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKcpIVDTWWQTETggiMLT 429
Cdd:PRK12316 2231 EMERHGVTILDFPPVYLQQLAEHAE---RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVT 2302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 430 PL--------PGAIPTKPgsCTKPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQPWPSMIRDVygdTDRFRH 491
Cdd:PRK12316 2303 PLlwkcrpqdPCGAAYVP--IGRALGNRRAYILDADLNLLAPGMAGELYLggeglargylNRPGLTAERFV---PDPFSA 2377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 492 TywehiqpkeGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRpDELTGEAIFA 571
Cdd:PRK12316 2378 S---------GERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVA 2447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6647434 572 FVSLEgnaEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12316 2448 YVVPD---DAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
262-622 |
4.26e-27 |
|
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: 112.11 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 262 DMLFILYTSGSTGKPKGvvhttggynlYTHMTTKWI--FDLKDTDVYWCTADvgwitghSYIVYGPLS-----NGATTVM 334
Cdd:cd17633 1 NPFYIGFTSGTTGLPKA----------YYRSERSWIesFVCNEDLFNISGED-------AILAPGPLShslflYGAISAL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 YEG----VPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVpnardlSSLRLLGTVGEPINPEAwmwyHRVIGGG 410
Cdd:cd17633 64 YLGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE------SKIKSIFSSGQKLFEST----KKKLKNI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 411 --KCPIVDTWWQTETGGImlTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVesdqgGFLVIKQPwpsMIRDVYGDTDR 488
Cdd:cd17633 134 fpKANLIEFYGTSELSFI--TYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSE---MVFSGYVRGGF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 489 FRHTYWehiqpkegqylYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEA 568
Cdd:cd17633 204 SNPDGW-----------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 6647434 569 IFAFVSleGNAEPSEELKKDLVKHVTEEigaiARPAEIRFTDVLPKTRSGKIMR 622
Cdd:cd17633 273 AVALYS--GDKLTYKQLKRFLKQKLSRY----EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
242-627 |
4.62e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 115.89 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 242 WHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTG-----GYNLythmTTKwiFDLKDTDVYWCTADVGwit 316
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGrlafaGRAL----TER--FGLTRDDVCYVSMPLF--- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 317 gHSYIVY---GP-LSNGATTVMyegVPRPSNPGcFWDVIERYGVNIFYTAPTAIrAFIRmgeAVPNARDLSSLRLLGTVG 392
Cdd:PRK13388 202 -HSNAVMagwAPaVASGAAVAL---PAKFSASG-FLDDVRRYGATYFNYVGKPL-AYIL---ATPERPDDADNPLRVAFG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 393 EPINPEAWMWYHRVIGggkCPIVDTWWQTEtGGIMLTPLPGaipTKPGSCTKPFPGIVaeIVDLDG-------------- 458
Cdd:PRK13388 273 NEASPRDIAEFSRRFG---CQVEDGYGSSE-GAVIVVREPG---TPPGSIGRGAPGVA--IYNPETltecavarfdahga 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 459 --NPVESDqgGFLVIKQPwPSMIRDVYGD----TDRFRH-TYWehiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVIN 531
Cdd:PRK13388 344 llNADEAI--GELVNTAG-AGFFEGYYNNpeatAERMRHgMYW-------------SGDLAYRDADGWIYFAGRTADWMR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 532 VSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL-EGNAEPSEELKKDLvkHVTEEIGAIARPAEIRFTD 610
Cdd:PRK13388 408 VDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLrDGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAA 485
|
410
....*....|....*..
gi 6647434 611 VLPKTRSGKIMRRLLRS 627
Cdd:PRK13388 486 DLPSTATNKVLKRELIA 502
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
114-626 |
9.12e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 115.12 E-value: 9.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GgFrkdkAIALKQEVDKAlehgapSVENVIV-----------------VQRTKADV-------------TMTAGRDHwwh 243
Cdd:PRK07059 129 N-F----ATTVQQVLAKT------AVKHVVVasmgdllgfkghivnfvVRRVKKMVpawslpghvrfndALAEGARQ--- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 244 ELQPQQSAHCpaepidseDMLFILYTSGSTGKPKGVVHTTGgyNLYTHM--TTKWI---FDLK---DTDVYWCTADVGWI 315
Cdd:PRK07059 195 TFKPVKLGPD--------DVAFLQYTGGTTGVSKGATLLHR--NIVANVlqMEAWLqpaFEKKprpDQLNFVCALPLYHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 316 TGHSYIVYGPLSNGATTVMyegVPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFirMGEAVPNARDLSSLRL-LG---TV 391
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNAL--LNNPDFDKLDFSKLIVaNGggmAV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 392 GEPInpeAWMWYHRVigggKCPIVDTWWQTETGGImLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVI 471
Cdd:PRK07059 340 QRPV---AERWLEMT----GCPITEGYGLSETSPV-ATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 472 KQPwpsmirdvygdtdRFRHTYWEhiQPKEGQYLYFA------GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESA 545
Cdd:PRK07059 412 RGP-------------QVMAGYWN--RPDETAKVMTAdgffrtGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 546 LVSHPLVAEAAVVGRPDELTGEAIFAFVsLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK07059 477 VASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEE---DVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
.
gi 6647434 626 R 626
Cdd:PRK07059 553 R 553
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
33-87 |
1.08e-26 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 102.55 E-value: 1.08e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 33 YEQLYSRAASNPEKFWGELAEqELHWFKKWDQVLDW-QPPFAKWFVGGQLNISHNC 87
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAK-ELDWFKPFDKVLDGsNGPFAKWFVGGKLNVCYNC 55
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
265-629 |
2.33e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 110.11 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 265 FILYTSGSTGKPKGVVHTtggynLYTH----MTTKWIFDLKDTDVYWCTADVGWITGHsYIVYGPLSNGATTVMYEGVpr 340
Cdd:cd17630 4 TVILTSGSTGTPKAVVHT-----AANLlasaAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 341 psnpgcfWDVIERYGVNIFYTA---PTAIRafiRMGEAVPNARDLSSLR--LLGtvGEPINPE-AWMWYHRVIgggkcPI 414
Cdd:cd17630 76 -------QALAEDLAPPGVTHVslvPTQLQ---RLLDSGQGPAALKSLRavLLG--GAPIPPElLERAADRGI-----PL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 415 VDTWWQTETGG-IMLTPLPGaipTKPGSCTKPFPGIVAEIVDldgnpvesdqGGFLVIKQPWPSMIRDVYGDTDRFRHTY 493
Cdd:cd17630 139 YTTYGMTETASqVATKRPDG---FGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 494 WEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFV 573
Cdd:cd17630 206 WFT-----------TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 574 SLEGNAEPSEelkkdLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:cd17630 275 VGRGPADPAE-----LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
113-626 |
2.38e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 113.61 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 113 IITYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAK-LVI 190
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 191 TADggFrkdkAIALKQEVDKAlehgapSVENVI------------------VVQRTKADV-------------TMTAGRD 239
Cdd:PRK08974 128 VSN--F----AHTLEKVVFKT------PVKHVIltrmgdqlstakgtlvnfVVKYIKRLVpkyhlpdaisfrsALHKGRR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 240 HWWheLQPQqsahcpaepIDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTH-MTTKWIFD--LKDtdvywctadvgwit 316
Cdd:PRK08974 196 MQY--VKPE---------LVPEDLAFLQYTGGTTGVAKGAMLTHR--NMLANlEQAKAAYGplLHP-------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 317 GHSYIVYG-PLSN-GATTVmyegvprpsNPGCFwdvIERYGVNIFYTAPTAIRAFIRMGEAVP-----------NAR--- 380
Cdd:PRK08974 249 GKELVVTAlPLYHiFALTV---------NCLLF---IELGGQNLLITNPRDIPGFVKELKKYPftaitgvntlfNALlnn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 381 ------DLSSLRLlgtvgepinpeawmwyhrVIGGGKcPI---VDTWWQTETG-----GIMLT---PLPGAIPTK----P 439
Cdd:PRK08974 317 eefqelDFSSLKL------------------SVGGGM-AVqqaVAERWVKLTGqylleGYGLTecsPLVSVNPYDldyyS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 440 GSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsmirdvygdtdRFRHTYWEhiQP-------KEGqylYFA-GDG 511
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGP-------------QVMLGYWQ--RPeatdeviKDG---WLAtGDI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 512 ARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVK 591
Cdd:PRK08974 440 AVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRR 519
|
570 580 590
....*....|....*....|....*....|....*
gi 6647434 592 HVTeeigAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK08974 520 HLT----GYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
110-623 |
7.15e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 111.90 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRI-ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:PRK05852 39 ADRIaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 V-ITADGGFRKDKA------IALKQEVDKALEHGAPSVenvivvqrtkaDVTMTAgrdhwwhELQPQQSAHCPAEPIDSe 261
Cdd:PRK05852 119 VlIDADGPHDRAEPttrwwpLTVNVGGDSGPSGGTLSV-----------HLDAAT-------EPTPATSTPEGLRPDDA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 262 dmlFILYTSGSTGKPKGVVHTTGGYNLYTH-MTTKWIFDLKDTDVywctADVGWITGHSYI--VYGPLSNGATtVMYEGV 338
Cdd:PRK05852 180 ---MIMFTGGTTGLPKMVPWTHANIASSVRaIITGYRLSPRDATV----AVMPLYHGHGLIaaLLATLASGGA-VLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 339 PRPSnPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGgkcPIVDTW 418
Cdd:PRK05852 252 GRFS-AHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTET---------GGIMLTPLPGAIPTKPGSCTkpfpGIVAEIVDLDGNPVESDQGGflvikQPW---PSMIRDVYGD- 485
Cdd:PRK05852 328 GMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAVG-----EVWlrgTTVVRGYLGDp 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 -------TDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVV 558
Cdd:PRK05852 399 titaanfTDGWLRT----------------GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVF 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 559 GRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRR 623
Cdd:PRK05852 463 GVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-626 |
1.12e-25 |
|
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: 108.90 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHT-----TGGYNLYTHMttkwifDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMy 335
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFIGERL------GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 egvPRPS-NPGCFWDVIERYGVNIFYTAPTAiraFIRM-GEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKCP 413
Cdd:cd05917 75 ---PSPSfDPLAVLEAIEKEKCTALHGVPTM---FIAElEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 IVdtWWQTETGGIMLTPLPGA-IPTKPGSCTKPFPGIVAEIVDLDGNPVES--DQG-----GFLVIKQPW--PSMIRDVY 483
Cdd:cd05917 149 IA--YGMTETSPVSTQTRTDDsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvgVPGelcirGYSVMKGYWndPEKTAEAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 484 gDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDE 563
Cdd:cd05917 227 -DGDGWLHT----------------GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 564 LTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05917 290 RYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
112-626 |
1.44e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 111.39 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSL-GVQKGDRVAIYLPMIPEAAITMLACSRIGAphsVVFGG---FSAEALRDRLVDAEAK 187
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL---IVVNTnplYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 188 -LVITADGGFRKDKAI-------ALKQEV------------DKALEHGAPSVENVIVVQRTKADVTMTAGRDhwwhelQP 247
Cdd:PRK05677 125 aLVCLANMAHLAEKVLpktgvkhVIVTEVadmlpplkrlliNAVVKHVKKMVPAYHLPQAVKFNDALAKGAG------QP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 QQSAHCpaepiDSEDMLFILYTSGSTGKPKGVVHTTggYNLYTHMTTkwifdlkdtdvywCTADVGWITGH-SYIVYGPL 326
Cdd:PRK05677 199 VTEANP-----QADDVAVLQYTGGTTGVAKGAMLTH--RNLVANMLQ-------------CRALMGSNLNEgCEILIAPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 327 S----------------NGATTVMyegVPRPSNPGCFWDVIERY------GVNIFYTAPTAIRAFIRMgeavpnarDLSS 384
Cdd:PRK05677 259 PlyhiyaftfhcmammlIGNHNIL---ISNPRDLPAMVKELGKWkfsgfvGLNTLFVALCNNEAFRKL--------DFSA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 385 LRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDLDGNPVESD 464
Cdd:PRK05677 328 LKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTETSPVVSVNPSQAI--QVGTIGIPVPSTLCKVIDDDGNELPLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 465 QGGFLVIKQPwpsmirdvygdtdRFRHTYWEhiQPKEGQYLYFA------GDGARRDKDGYFWVMGRVDDVINVSGHRLG 538
Cdd:PRK05677 403 EVGELCVKGP-------------QVMKGYWQ--RPEATDEILDSdgwlktGDIALIQEDGYMRIVDRKKDMILVSGFNVY 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 539 TMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSlegnAEPSEELKKDLVK-HVTEEIGAIARPAEIRFTDVLPKTRS 617
Cdd:PRK05677 468 PNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVV----VKPGETLTKEQVMeHMRANLTGYKVPKAVEFRDELPTTNV 543
|
....*....
gi 6647434 618 GKIMRRLLR 626
Cdd:PRK05677 544 GKILRRELR 552
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
110-625 |
1.96e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITAdggfrkdkaialkqevdkalEHGAPSVEnvivvqrTKADVTM--TAGRDHWWHelqpQQSAHCPAEPIDSEDMLFIL 267
Cdd:PRK12467 614 LTQ--------------------SHLLAQLP-------VPAGLRSlcLDEPADLLC----GYSGHNPEVALDPDNLAYVI 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVVHTTGGYNLYTHMTTKWiFDLkdtdvywcTADVGWITGHSY-------IVYGPLSNGATTVMyegVPR 340
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGALANYVCVIAER-LQL--------AADDSMLMVSTFafdlgvtELFGALASGATLHL---LPP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 341 PS--NPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPnardLSSLRLLGTVGEPINPEAWMWYHRVigGGKCPIVDTW 418
Cdd:PRK12467 731 DCarDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL----PRPQRALVCGGEALQVDLLARVRAL--GPGARLINHY 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTETG-GIMLTPLPG-AIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQPWPSMIRDVygdT 486
Cdd:PRK12467 805 GPTETTvGVSTYELSDeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIggaglargyhRRPALTAERFV---P 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 487 DRFrhtywehiqPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDElTG 566
Cdd:PRK12467 882 DPF---------GADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AG 951
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 567 EAIFAFV----SLEG--NAEPSEELKKDLVKHVTEEIgaiaRPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12467 952 LQLVAYLvpaaVADGaeHQATRDELKAQLRQVLPDYM----VPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
261-622 |
4.01e-25 |
|
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: 106.96 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVPR 340
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 341 PSnpgcFWDVIERYGVNIFYTAPTAIRAFIRMGEAVpnARDLSSLRLLGTVGE-PINPEAwmwyhRVI-GGGKCPIVDTW 418
Cdd:cd17635 81 KS----LFKILTTNAVTTTCLVPTLLSKLVSELKSA--NATVPSLRLIGYGGSrAIAADV-----RFIeATGLTNTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 419 WQTETGGIMLTPLpGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWpsmirdvygdtdrFRHTYWEHIQ 498
Cdd:cd17635 150 GLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-------------NMLGYWNNPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 499 PKE----GQYLYfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:cd17635 216 RTAevliDGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6647434 575 LEGnaEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMR 622
Cdd:cd17635 295 ASA--ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
88-633 |
4.84e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 109.71 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 88 LDRHLTTWRRNKAAIIWEGEPGDSRIiTYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSV 167
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDGTSAL-RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 168 VFGGFSAeALRDRLVD-AEAKLVITADGGfrkdkaiALKQEVDKALEHGAPSVEnvivvqrtkadVTMTAGRDHWWHELQ 246
Cdd:PRK05857 96 ADGNLPI-AAIERFCQiTDPAAALVAPGS-------KMASSAVPEALHSIPVIA-----------VDIAAVTRESEHSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 247 pqqSAHCPAEP-IDSEDMLFILYTSGSTGKPKGVvhttggynLYTHMTTKWIFD-LKDTDVYWctadVGWITGHSyiVYG 324
Cdd:PRK05857 157 ---AASLAGNAdQGSEDPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW----VTWVVGET--TYS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 325 PLSngATTV----------MYEG--VPRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIrmGEAVPNARDLSSLRLLGTVG 392
Cdd:PRK05857 220 PLP--ATHIgglwwiltclMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLV--SELKSANATVPSLRLVGYGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 393 -EPINPEAwmwyhRVIGGGKCPIVDTWWQTETGGIMLtplpgAIPTKPGSCTK--------PFPGIVAEIVDLDG-NPVE 462
Cdd:PRK05857 296 sRAIAADV-----RFIEATGVRTAQVYGLSETGCTAL-----CLPTDDGSIVKieagavgrPYPGVDVYLAATDGiGPTA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 463 SDQG-----GFLVIKQPwPSMIrdvygdtdrfrhTYWEHIQpKEGQYL----YFAGDGARRDKDGYFWVMGRVDDVINVS 533
Cdd:PRK05857 366 PGAGpsasfGTLWIKSP-ANML------------GYWNNPE-RTAEVLidgwVNTGDLLERREDGFFYIKGRSSEMIICG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 534 GHRLGTMEIESALVSHPLVAEAAVVGRPDE----LTGEAIFAFVSLEGNAepSEELKKDLVKHVTEEIGAIARPAEIRFT 609
Cdd:PRK05857 432 GVNIAPDEVDRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELDESA--ARALKHTIAARFRRESEPMARPSTIVIV 509
|
570 580
....*....|....*....|....
gi 6647434 610 DVLPKTRSGKIMRRLLRSLASGQE 633
Cdd:PRK05857 510 TDIPRTQSGKVMRASLAAAATADK 533
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
111-629 |
7.30e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 108.88 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 111 SRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEaaitMLAC----SRIGAPHSVVFGGFSAEALRDRLVDAEA 186
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA----MVEAhfgvPMAGAVLNTLNTRLDAASIAFMLRHGEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 187 KLVITaDGGFRkdkaiALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAepiDSEDMLFI 266
Cdd:PRK08162 117 KVLIV-DTEFA-----EVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLPA---DEWDAIAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 267 LYTSGSTGKPKGVV-HTTGGY-NLYTHMTTkwiFDLKDTDVY-W------CTadvGWitGHSYIVygpLSNGATTVMYeg 337
Cdd:PRK08162 188 NYTSGTTGNPKGVVyHHRGAYlNALSNILA---WGMPKHPVYlWtlpmfhCN---GW--CFPWTV---AARAGTNVCL-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 vpRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIrmgeavpNARDlsSLRllgtvgEPINpeawmwyHRVIG--GGKCPIV 415
Cdd:PRK08162 255 --RKVDPKLIFDLIREHGVTHYCGAPIVLSALI-------NAPA--EWR------AGID-------HPVHAmvAGAAPPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETGGIMLTPLPGAIPT-KPGS-CTK---------------------PFPgIVAEIVDLD---GNPVESD---QG 466
Cdd:PRK08162 311 AVIAKMEEIGFDLTHVYGLTETyGPATvCAWqpewdalplderaqlkarqgvRYP-LQEGVTVLDpdtMQPVPADgetIG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 467 -----GFLVIKqpwpSMIRDVYGDTDRFRHTyWEHiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTME 541
Cdd:PRK08162 390 eimfrGNIVMK----GYLKNPKATEEAFAGG-WFH-----------TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 542 IESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDvLPKTRSGKIM 621
Cdd:PRK08162 454 VEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQ 529
|
....*...
gi 6647434 622 RRLLRSLA 629
Cdd:PRK08162 530 KFVLREQA 537
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-625 |
7.37e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.20 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 21 FSERAYVRSGREYEQLYSRAASNPEKFWGELAEQELHwfkkwdqvlDWQPPFAKWFVGGQLNISHNCLDRHL--TTWRRN 98
Cdd:PRK12316 3001 FDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAE---------ERGQLLEAWNATAAEYPLERGVHRLFeeQVERTP 3071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 99 KAAIIWEGEpgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALR 178
Cdd:PRK12316 3072 DAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA 3147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 179 DRLVDAEAKLVITAdggfrkdkaialkqevdkalEH-GAPSVENVIVVQRTKADvtmtagrdhwwhelqPQQSAHCPAEP 257
Cdd:PRK12316 3148 YMLEDSGAQLLLSQ--------------------SHlRLPLAQGVQVLDLDRGD---------------ENYAEANPAIR 3192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDSEDMLFILYTSGSTGKPKGVVHTTGGYNlythMTTKWIFDLKDTDVYWCTADVGWIT--GHSYIVYGPLSNGATTVMy 335
Cdd:PRK12316 3193 TMPENLAYVIYTSGSTGKPKGVGIRHSALS----NHLCWMQQAYGLGVGDRVLQFTTFSfdVFVEELFWPLMSGARVVL- 3267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 EGVPRPSNPGCFWDVIERYGVNIfytaPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAwmwYHRVIGGGkcPIV 415
Cdd:PRK12316 3268 AGPEDWRDPALLVELINSEGVDV----LHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADL---QQQVFAGL--PLY 3338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETGgIMLTPLPGAIPTKPGS-CTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQpwpSMIRDVYGDTDRFRHTYW 494
Cdd:PRK12316 3339 NLYGPTEAT-ITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVGALGELYLGG---EGLARGYHNRPGLTAERF 3414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 EHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVgrpdELTGEAIFAFVS 574
Cdd:PRK12316 3415 VPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVV 3490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 6647434 575 LEgnaEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK12316 3491 PE---DEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-644 |
9.33e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.64 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 111 SRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVFGGFSAEALRDRLV----DAEA 186
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG----AYVPLDPEYPRERLAymieDSGI 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 187 KLVITADggfrkdkaiALKQEVdkALEHGAPSVEnvivvqrtkadvtMTAGRDhwWHELQPQQSahcPAEPIDSEDMLFI 266
Cdd:PRK12467 1673 ELLLTQS---------HLQARL--PLPDGLRSLV-------------LDQEDD--WLEGYSDSN---PAVNLAPQNLAYV 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 267 LYTSGSTGKPKGVVHTTGGYNLYTHMTTKWiFDLkdtdvywCTADVgWITGHSYI-------VYGPLSNGATTVmyegVP 339
Cdd:PRK12467 1724 IYTSGSTGRPKGAGNRHGALVNRLCATQEA-YQL-------SAADV-VLQFTSFAfdvsvweLFWPLINGARLV----IA 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 RPS---NPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARdlsSLRLLGTVGEPINPEAW-MWYHRViggGKCPIV 415
Cdd:PRK12467 1791 PPGahrDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPL---SLRRVVCGGEALEVEALrPWLERL---PDTGLF 1864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETG-GIMLTPLPGAIPTKPGSCT--KPFPGIVAEIVDLDGNPVESDQGGFLVI----------KQPWPSMIRDV 482
Cdd:PRK12467 1865 NLYGPTETAvDVTHWTCRRKDLEGRDSVPigQPIANLSTYILDASLNPVPIGVAGELYLggvglargylNRPALTAERFV 1944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 483 ygdTDRFrhtywehiqPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRpD 562
Cdd:PRK12467 1945 ---ADPF---------GTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-D 2011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 563 ELTGEAIFAFV-----SLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSL---ASGQEI 634
Cdd:PRK12467 2012 GANGKQLVAYVvptdpGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPdasELQQAY 2091
|
570
....*....|
gi 6647434 635 SGDTSTLEDR 644
Cdd:PRK12467 2092 VAPQSELEQR 2101
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
114-629 |
2.59e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 107.60 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsVVFGG---FSAEALRDRLVDAEAKLV 189
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGL---IVVNTnplYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGgFRKdkaiaLKQEV--DKALEH--------GAPSVENVIV---VQRTKADV-------------TMTAGRDHwwh 243
Cdd:PRK12492 127 VYLNM-FGK-----LVQEVlpDTGIEYlieakmgdLLPAAKGWLVntvVDKVKKMVpayhlpqavpfkqALRQGRGL--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 244 ELQPQQSAHcpaepidsEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTtkwifdlkdtDVYWCTADVGwITGHSYIVY 323
Cdd:PRK12492 198 SLKPVPVGL--------DDIAVLQYTGGTTGLAKGAMLTHG--NLVANML----------QVRACLSQLG-PDGQPLMKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 GPLSNGATTVMYEGVPRPSNPGCfwdVIERYGVNIFYTAPTAIRAFIR--------------------MGEAVPNARDLS 383
Cdd:PRK12492 257 GQEVMIAPLPLYHIYAFTANCMC---MMVSGNHNVLITNPRDIPGFIKelgkwrfsallglntlfvalMDHPGFKDLDFS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 384 SLRLLGTVGEPI---NPEAWmwyHRVIGggkCPIVDTWWQTETGGIMLTPlPGAIPTKPGSCTKPFPGIVAEIVDLDGNP 460
Cdd:PRK12492 334 ALKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTETSPVASTN-PYGELARLGTVGIPVPGTALKVIDDDGNE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 461 VESDQGGFLVIKQPwpsmirdvygdtdRFRHTYWEhiQPK------EGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSG 534
Cdd:PRK12492 407 LPLGERGELCIKGP-------------QVMKGYWQ--QPEataealDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 535 HRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKkdlvKHVTEEIGAIARPAEIRFTDVLPK 614
Cdd:PRK12492 472 FNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELK----AYCKENFTGYKVPKHIVLRDSLPM 547
|
570
....*....|....*
gi 6647434 615 TRSGKIMRRLLRSLA 629
Cdd:PRK12492 548 TPVGKILRRELRDIA 562
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
98-625 |
4.85e-24 |
|
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: 105.87 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:cd17655 12 DHTAVVFEDQT-----LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITadggfrkdkaialkQEVDKALEHGAPSVENvivvqrtkadvtmtagrdhwwheLQPQQSAHCPAE- 256
Cdd:cd17655 87 QYILEDSGADILLT--------------QSHLQPPIAFIGLIDL-----------------------LDEDTIYHEESEn 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 257 ---PIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDV-----YWCTADVGWItghsyivYGPLSN 328
Cdd:cd17655 130 lepVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRValfasISFDASVTEI-------FASLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 329 GATTVMYEGVPRpSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGeavpnARDLSSLRLLGTVGEPINPE-AWMWYHRVi 407
Cdd:cd17655 203 GNTLYIVRKETV-LDGQALTQYIRQNRITIIDLTPAHLKLLDAAD-----DSEGLSLKHLIVGGEALSTElAKKIIELF- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 gGGKCPIVDTWWQTETG-GIMLTPL-PGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKqpwpsmirdvyGD 485
Cdd:cd17655 276 -GTNPTITNAYGPTETTvDASIYQYePETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIG-----------GE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 TdrFRHTYWEHiqP---KE---------GQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVA 553
Cdd:cd17655 344 G--VARGYLNR--PeltAEkfvddpfvpGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIK 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6647434 554 EAAVVGRPDELTGEAIFAFVSLEGNAePSEELKKDLVKHVTEEIgaIarPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17655 420 EAVVIARKDEQGQNYLCAYIVSEKEL-PVAQLREFLARELPDYM--I--PSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
83-630 |
8.52e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 105.32 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 83 ISHNCLDRhlttwrRNKAAI-IWEGEpgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLAcsri 161
Cdd:cd05918 5 IEERARSQ------PDAPAVcAWDGS------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLA---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 162 gaphsvvfggfsaealrdrlvdaeaklVITADGGFrkdkaialkqeVdkALEHGAPSVENVIVVQRTKADVTMTAgrdhw 241
Cdd:cd05918 69 ---------------------------VLKAGGAF-----------V--PLDPSHPLQRLQEILQDTGAKVVLTS----- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 242 whelqpqqsahcpaepiDSEDMLFILYTSGSTGKPKGVV--H---TTG----GYNLYTHMTTKWI------FDLkdtdvy 306
Cdd:cd05918 104 -----------------SPSDAAYVIFTSGSTGKPKGVVieHralSTSalahGRALGLTSESRVLqfasytFDV------ 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 307 wCTADVgwitghsyivYGPLSNGATTVmyegVP----RPSNPGcfwDVIERYGVN-IFYTaPTAIRAFirmgeavpNARD 381
Cdd:cd05918 161 -SILEI----------FTTLAAGGCLC----IPseedRLNDLA---GFINRLRVTwAFLT-PSVARLL--------DPED 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 382 LSSLRLLGTVGEPINPEawmwyhrvigggkcpIVDTWWQ----------TETGGIMLTPLPGAiPTKPGSCTKPFPGiVA 451
Cdd:cd05918 214 VPSLRTLVLGGEALTQS---------------DVDTWADrvrlinaygpAECTIAATVSPVVP-STDPRNIGRPLGA-TC 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 452 EIVDLDGN--PVESDQGGFLVIKQPwpSMIRDVYGDTDR-----FRHTYW-EHIQPKEGQYLYFAGDGARRDKDGYFWVM 523
Cdd:cd05918 277 WVVDPDNHdrLVPIGAVGELLIEGP--ILARGYLNDPEKtaaafIEDPAWlKQEGSGRGRRLYRTGDLVRYNPDGSLEYV 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 524 GRVDDVINVSGHR--LGtmEIESALVSHP---LVAEAAVVGRPDELTGEAIFAFVSLEG-----------NAEPSEELKk 587
Cdd:cd05918 355 GRKDTQVKIRGQRveLG--EIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQLVAFVVLDGsssgsgdgdslFLEPSDEFR- 431
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 6647434 588 DLVKHVTEEI-GAIAR---PAEIRFTDVLPKTRSGKIMRRLLRSLAS 630
Cdd:cd05918 432 ALVAELRSKLrQRLPSymvPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
99-626 |
2.01e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 104.44 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 99 KAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALR 178
Cdd:cd05915 10 RKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 179 DRLVDAEAKLVItadggfrkdkaialkqeVDKalEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPI 258
Cdd:cd05915 90 YILNHAEDKVLL-----------------FDP--NLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSEDMLFILYTSGSTGKPKGVVHT-TGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEg 337
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 338 vprPSNPGCFWDVIERYGVNIFYTAPTAIrafirmgEAVPNARDlsSLRllgtvgepinpEAWMWYHRVIGGGKCP---- 413
Cdd:cd05915 230 ---RLDPASLVELFDGEGVTFTAGVPTVW-------LALADYLE--STG-----------HRLKTLRRLVVGGSAAprsl 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 414 ----------IVDTWWQTETGGI----MLTPLPGAIPTKPGSCTKPFPGI--VAEIVD-LDGNPVESDQGGflvikqpwp 476
Cdd:cd05915 287 iarfermgveVRQGYGLTETSPVvvqnFVKSHLESLSEEEKLTLKAKTGLpiPLVRLRvADEEGRPVPKDG--------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 SMIRDVYGDTDRFRHTYWEHIQPKEGQYL----YFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV 552
Cdd:cd05915 358 KALGEVQLKGPWITGGYYGNEEATRSALTpdgfFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 553 AEAAVVGRPDELTGEAIFAFVSLEgNAEPSEElkkDLVKHVTEEIGAIAR-PAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:cd05915 438 KEAAVVAIPHPKWQERPLAVVVPR-GEKPTPE---ELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
114-627 |
4.12e-23 |
|
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: 102.39 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 GGfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidsEDMLFILYTSGST 273
Cdd:cd17653 103 SP-----------------------------------------------------------------DDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHT---------TGGYNLYT--HMTTKWIFDLKdtdvYWCTADVgwitghsyiVYGPLSNGATTVMYEgvprPS 342
Cdd:cd17653 118 GIPKGVMVPhrgvlnyvsQPPARLDVgpGSRVAQVLSIA----FDACIGE---------IFSTLCNGGTLVLAD----PS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 343 NPgcFWDVIERygVNIFYTAPTAIrafirmgeAVPNARDLSSLRLLGTVGEPINPeawmwyhrvigggkcPIVDTWWQ-- 420
Cdd:cd17653 181 DP--FAHVART--VDALMSTPSIL--------STLSPQDFPNLKTIFLGGEAVPP---------------SLLDRWSPgr 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 421 --------TETGGIMLTP--LPGaiptKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGD----T 486
Cdd:cd17653 234 rlynaygpTECTISSTMTelLPG----QPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGV--QVARGYLGNpaltA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 487 DRFRHTYWEHiqpkeGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIES-ALVSHPLVAEAAVVgrpdeLT 565
Cdd:cd17653 308 SKFVPDPFWP-----GSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-----VV 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6647434 566 GEAIFAFVSLEGNAEpsEELKKDLVKHVTeeigAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:cd17653 378 NGRLVAFVTPETVDV--DGLRSELAKHLP----SYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
101-625 |
2.81e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 100.20 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 101 AIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDR 180
Cdd:cd17644 18 AVVFEDQQ-----LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 181 LVDAEAKLVITadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelQPqqsahcpaepids 260
Cdd:cd17644 93 LEDAQISVLLT------------------------------------------------------QP------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKwIFDLKDTDVYWCTADVGWITGHSYIvYGPLSNGATTVMYEGVPR 340
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK-EYGITSSDRVLQFASIAFDVAAEEI-YVTLLSGATLVLRPEEMR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 341 PSNPGcFWDVIERYGVNIFYTAPTAIRAFIRmgEAVPNARDL-SSLRLLGTVGEPINPEAW-MW---------YHRVIGG 409
Cdd:cd17644 184 SSLED-FVQYIQQWQLTVLSLPPAYWHLLVL--ELLLSTIDLpSSLRLVIVGGEAVQPELVrQWqknvgnfiqLINVYGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 410 GKCPIVDTWWQtetggimLTPLPGAIPTKPgSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIkqpwpSMIRDVYGDTDRF 489
Cdd:cd17644 261 TEATIAATVCR-------LTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHI-----GGVGLARGYLNRP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 490 RHTYWEHIQ----PKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELT 565
Cdd:cd17644 328 ELTAEKFIShpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPG 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 566 GEAIFAFVSLEGNAEPSEE-----LKKDLVKHVTeeigaiarPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17644 408 NKRLVAYIVPHYEESPSTVelrqfLKAKLPDYMI--------PSAFVVLEELPLTPNGKIDRRAL 464
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
114-625 |
1.04e-21 |
|
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: 98.67 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAD 193
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidSEDMLFILYTSGST 273
Cdd:cd05914 88 ------------------------------------------------------------------EDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTtgGYNLYTHMT-TKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTV--------------MYE-- 336
Cdd:cd05914 102 GNSKGVMLT--YRNIVSNVDgVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVfldkipsakiialaFAQvt 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 337 ---GVPRPsnpgcfWDVIERYGVNIFYTAPTAIRAFIRMgeAVPNARDLSSL-------------RLLGTVGEPINPEAW 400
Cdd:cd05914 180 ptlGVPVP------LVIEKIFKMDIIPKLTLKKFKFKLA--KKINNRKIRKLafkkvheafggniKEFVIGGAKINPDVE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 401 MWYHRVigggKCPIVDTWWQTETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDLDGNPVEsdqgGFLVIKQPwpSMIR 480
Cdd:cd05914 252 EFLRTI----GFPYTIGYGMTETAPIISYSPPNRI--RLGSAGKVIDGVEVRIDSPDPATGE----GEIIVRGP--NVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 DVYG---------DTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVI-NVSGHRLGTMEIESALVSHP 550
Cdd:cd05914 320 GYYKnpeataeafDKDGWFHT----------------GDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMP 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 551 LVAEAAVVGRPDELTGEAI----FAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIR-FTDVLPKTRSGKIMRRLL 625
Cdd:cd05914 384 FVLESLVVVQEKKLVALAYidpdFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKKISKVKiVKEEFEKTPKGKIKRFLY 463
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
98-626 |
1.16e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 99.56 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:PRK08279 52 DRPALLFED-----QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITADggfrkdkaiALKQEVDKALEHGAPSVENVIVVQRTKADVtmtagrdHWWHELQpQQSAHCPAEP 257
Cdd:PRK08279 127 AHSLNLVDAKHLIVGE---------ELVEAFEEARADLARPPRLWVAGGDTLDDP-------EGYEDLA-AAAAGAPTTN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDS------EDMLFILYTSGSTGKPKGVVhttggynlYTHMttKW---------IFDLKDTDVYWCT--------ADVGW 314
Cdd:PRK08279 190 PASrsgvtaKDTAFYIYTSGTTGLPKAAV--------MSHM--RWlkamggfggLLRLTPDDVLYCClplyhntgGTVAW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 315 ITGhsyivygpLSNGATTVMyegvpRP----SNpgcFWDVIERYGvnifytaptaIRAFIRMGE---------AVPNARD 381
Cdd:PRK08279 260 SSV--------LAAGATLAL-----RRkfsaSR---FWDDVRRYR----------ATAFQYIGElcryllnqpPKPTDRD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 382 lSSLRLLgtVGEPINPEAWMWYHRVIGGGKcpIVDTWWQTEtGGIMLTPL---PGAIPTKPGSCTKPFpgivaEIVDLD- 457
Cdd:PRK08279 314 -HRLRLM--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASE-GNVGFINVfnfDGTVGRVPLWLAHPY-----AIVKYDv 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 458 --GNPVESDQG----------GFLV--IKQPWP------------SMIRDVYGDTDR-FRhtywehiqpkegqylyfAGD 510
Cdd:PRK08279 383 dtGEPVRDADGrcikvkpgevGLLIgrITDRGPfdgytdpeasekKILRDVFKKGDAwFN-----------------TGD 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 511 GARRDKDGYFWVMGRVDDVI-----NVSghrlgTMEIESALVSHPLVAEAAVVGRPDELT-GEAIFAFVSLEGNAEPseE 584
Cdd:PRK08279 446 LMRDDGFGHAQFVDRLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEVPGTdGRAGMAAIVLADGAEF--D 518
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 6647434 585 LKKdLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK08279 519 LAA-LAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLR 559
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
112-625 |
4.81e-21 |
|
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: 96.17 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIT 191
Cdd:cd17652 11 ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 adggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelQPQQSAhcpaepidsedmlFILYTSG 271
Cdd:cd17652 91 ------------------------------------------------------TPDNLA-------------YVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 272 STGKPKGVVHT-TGGYNLYTHMTTKwiFDLKDTDVYWCTADVGWITGHSYIVYGPLSnGATTVMyegVPR-PSNPGC-FW 348
Cdd:cd17652 104 STGRPKGVVVThRGLANLAAAQIAA--FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVL---APAeELLPGEpLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 349 DVIERYGVNIFYTAPTAIRAfirmgeaVPnARDLSSLRLLGTVGEPINPE---AWMWYHRVIGGgkcpivdtWWQTET-- 423
Cdd:cd17652 178 DLLREHRITHVTLPPAALAA-------LP-PDDLPDLRTLVVAGEACPAElvdRWAPGRRMINA--------YGPTETtv 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 424 GGIMLTPLPGAIPTKPGsctKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGDTDRFRHTYWEHIQPKEGQ 503
Cdd:cd17652 242 CATMAGPLPGGGVPPIG---RPVPGTRVYVLDARLRPVPPGVPGELYIAGA--GLARGYLNRPGLTAERFVADPFGAPGS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 504 YLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSE 583
Cdd:cd17652 317 RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 6647434 584 E-----LKKDLVKHVTeeigaiarPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17652 397 AelrahLAERLPGYMV--------PAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
102-631 |
2.51e-20 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 95.04 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 102 IIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACsrigaphsvVFGGF-----SAEA 176
Cdd:cd05906 28 ITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFvpaplTVPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 177 LRDRLVDAEAKL-----------VITADggfrkdkaiALKQEVDKALEHGAPSVENVIVVQRTKAdvtmtAGRDHWWHEL 245
Cdd:cd05906 99 TYDEPNARLRKLrhiwqllgspvVLTDA---------ELVAEFAGLETLSGLPGIRVLSIEELLD-----TAADHDLPQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 246 QPqqsahcpaepidsEDMLFILYTSGSTGKPKGVVHTTGgyNLyTHMT--TKWIFDLKDTDVY--WCTAD-VGWITgHSY 320
Cdd:cd05906 165 RP-------------DDLALLMLTSGSTGFPKAVPLTHR--NI-LARSagKIQHNGLTPQDVFlnWVPLDhVGGLV-ELH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 IVygPLSNGATTVMyegVPRP---SNPGCFWDVIERYGVNIFYtAP----TAIRAFIRMGEAVPnaRDLSSLRLLGTVGE 393
Cdd:cd05906 228 LR--AVYLGCQQVH---VPTEeilADPLRWLDLIDRYRVTITW-APnfafALLNDLLEEIEDGT--WDLSSLRYLVNAGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 394 PINPEAWMWYHRVIGGGKCP---IVDTWWQTETG-GIMLTPLPGAIPTKPG----SCTKPFPGIVAEIVDLDGNPVESDQ 465
Cdd:cd05906 300 AVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 466 GGFLVIKQpwPSMIRDVYGDTD----RFRHTYWehiqpkegqylYFAGDGARRDkDGYFWVMGRVDDVINVSGHRLGTME 541
Cdd:cd05906 380 VGRLQVRG--PVVTKGYYNNPEanaeAFTEDGW-----------FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 542 IESAL-----VSHPLVAEAAVVGRPDELTGEAIFaFVSLEGNAEPSEELKKDLVKHVTEEIGaIARPAEIRF-TDVLPKT 615
Cdd:cd05906 446 IEAAVeevpgVEPSFTAAFAVRDPGAETEELAIF-FVPEYDLQDALSETLRAIRSVVSREVG-VSPAYLIPLpKEEIPKT 523
|
570
....*....|....*..
gi 6647434 616 RSGKIMR-RLLRSLASG 631
Cdd:cd05906 524 SLGKIQRsKLKAAFEAG 540
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
97-632 |
3.14e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 94.85 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 97 RNKAAIIWEGEpgDSRIITYAQLHREVCQFANALK-SLGVQKGDRVAIYLPMIPEAAITMLACSRIGAphsvVFGGFSAE 175
Cdd:PRK05620 24 GDTTVTTWGGA--EQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGA----VFNPLNKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 176 ALRDRLV----DAEAKlVITADGgfrkdkaiALKQEVDKALEHgAPSVENVIVVQRTKADVTMTAGRDHW----WHELQP 247
Cdd:PRK05620 98 LMNDQIVhiinHAEDE-VIVADP--------RLAEQLGEILKE-CPCVRAVVFIGPSDADSAAAHMPEGIkvysYEALLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 QQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTggYNLYTHMttkwiFDLKDTD---------------VY----WC 308
Cdd:PRK05620 168 GRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSH--RSLYLQS-----LSLRTTDslavthgesflccvpIYhvlsWG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 309 TADVGWITGHSYIVYGPLSNGAT--TVMYEGVPRPSnpgcfwdvierYGVnifytaPTA-IRAFIRMGEAVPNARDLSSL 385
Cdd:PRK05620 241 VPLAAFMSGTPLVFPGPDLSAPTlaKIIATAMPRVA-----------HGV------PTLwIQLMVHYLKNPPERMSLQEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 386 RLLGTVGEPINPEAWMWYHRVigggkcPIVDTWWQTETGGIMLTPLP-----GAIPTKPGSCTKPFP-GIVAEIVDlDGN 459
Cdd:PRK05620 304 YVGGSAVPPILIKAWEERYGV------DVVHVWGMTETSPVGTVARPpsgvsGEARWAYRVSQGRFPaSLEYRIVN-DGQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 460 PVESD--QGGFLVIKQPW--PSMIRDVYGDTDRFRHTYWEHiqPKEGQYLYFAGDGARR-------DKDGYFWVMGRVDD 528
Cdd:PRK05620 377 VMESTdrNEGEIQVRGNWvtASYYHSPTEEGGGAASTFRGE--DVEDANDRFTADGWLRtgdvgsvTRDGFLTIHDRARD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 529 VINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRF 608
Cdd:PRK05620 455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTF 534
|
570 580
....*....|....*....|....*
gi 6647434 609 TDVLPKTRSGKIMRRLLRS-LASGQ 632
Cdd:PRK05620 535 VDEIDKTSVGKFDKKDLRQhLADGD 559
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
517-632 |
3.22e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 89.72 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 517 DGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVslEGNAEPSEELkKDLVKHVTEE 596
Cdd:PRK07824 246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV--VGDGGPAPTL-EALRAHVART 322
|
90 100 110
....*....|....*....|....*....|....*.
gi 6647434 597 IGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQ 632
Cdd:PRK07824 323 LDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
266-622 |
4.47e-19 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 88.71 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ILYTSGSTGKPKGVvhttggynLYTHMTTKWIFdlkdtdVYWCtaDVGWIT-GHSYIVYGP--------------LSNGA 330
Cdd:cd17638 5 IMFTSGTTGRSKGV--------MCAHRQTLRAA------AAWA--DCADLTeDDRYLIINPffhtfgykagivacLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 TTVmyegvprpsnPGCFWDV------IERYGVNIFYTAPTAIRAFIrmgeAVPNAR--DLSSLRLLGTVGEPINPEAWMW 402
Cdd:cd17638 69 TVV----------PVAVFDVdaileaIERERITVLPGPPTLFQSLL----DHPGRKkfDLSSLRAAVTGAATVPVELVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 403 YHRVIGGGKcpIVDTWWQTETGGIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDlDGNPV---ESDQGGFLVIKQPWPSMI 479
Cdd:cd17638 135 MRSELGFET--VLTAYGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLvrgYNVMQGYLDDPEATAEAI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 480 rdvygDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVG 559
Cdd:cd17638 212 -----DADGWLHT----------------GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6647434 560 RPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMR 622
Cdd:cd17638 271 VPDERMGEVGKAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
98-631 |
5.06e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 91.23 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWegepGDSRIiTYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:PLN03102 29 NRTSIIY----GKTRF-TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITaDGGFRkdkaiALKQEVDKALEhGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEP 257
Cdd:PLN03102 104 AAILRHAKPKILFV-DRSFE-----PLAREVLHLLS-SEDSNLNLPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 I------DSEDMLFILYTSGSTGKPKGVVHTTGGYNLYT-HMTTKWifDLKDTDVYWCTADVGWITGHSYiVYGPLSNGA 330
Cdd:PLN03102 177 ArmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTlSAIIGW--EMGTCPVYLWTLPMFHCNGWTF-TWGTAARGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 TTVMYEGVPRPSnpgcFWDVIERYGVNIFYTAPTAIRaFIRMGEAVPNARDLSSLRLLgTVGEP-----INPEAWMWYHR 405
Cdd:PLN03102 254 TSVCMRHVTAPE----IYKNIEMHNVTHMCCVPTVFN-ILLKGNSLDLSPRSGPVHVL-TGGSPppaalVKKVQRLGFQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 406 VIGGGKC----PIVDTWWQTETGgimltplpgAIPTKPGSCTKPFPGI-VAEIVDLD--------GNPVESDQGGFLVIK 472
Cdd:PLN03102 328 MHAYGLTeatgPVLFCEWQDEWN---------RLPENQQMELKARQGVsILGLADVDvknketqeSVPRDGKTMGEIVIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 473 QP--WPSMIRDVYGDTDRFRHTYWEhiqpkegqylyfAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHP 550
Cdd:PLN03102 399 GSsiMKGYLKNPKATSEAFKHGWLN------------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 551 LVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEEL-------KKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRR 623
Cdd:PLN03102 467 KVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKP 546
|
....*...
gi 6647434 624 LLRSLASG 631
Cdd:PLN03102 547 KLRDIAKG 554
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
97-625 |
5.44e-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: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 97 RNKAAIIWegepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEA 176
Cdd:cd17641 2 REKDFGIW-------QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 177 LRDRLVDAEAKLVITADggfrkdkaialKQEVDKALEHGA--PSVENVIVVQ----RTKADvtmtaGRDHWWHELQPQQS 250
Cdd:cd17641 75 VAYLLNYTGARVVIAED-----------EEQVDKLLEIADriPSVRYVIYCDprgmRKYDD-----PRLISFEDVVALGR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 251 AHCPAEP---------IDSEDMLFILYTSGSTGKPKGVVHTTGgyNLYTHMTTKWIFD-LKDTDVYWCTADVGWITGHSY 320
Cdd:cd17641 139 ALDRRDPglyerevaaGKGEDVAVLCTTSGTTGKPKLAMLSHG--NFLGHCAAYLAADpLGPGDEYVSVLPLPWIGEQMY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 IVYGPLSNG--------ATTVM-----------------YEGV-----PRPSNPGCFWDVIERYGVNIFYTAPTAIRAFI 370
Cdd:cd17641 217 SVGQALVCGfivnfpeePETMMedlreigptfvllpprvWEGIaadvrARMMDATPFKRFMFELGMKLGLRALDRGKRGR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 371 RMGEAVPNA------------RD---LSSLRLLGTVGEPINPEAWMWYHrVIGggkCPIVDTWWQTETGGIMLTPLPGAI 435
Cdd:cd17641 297 PVSLWLRLAswladallfrplRDrlgFSRLRSAATGGAALGPDTFRFFH-AIG---VPLKQLYGQTELAGAYTVHRDGDV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 436 PtkPGSCTKPFPGivAEI-VDLDGNPVESDQGGFL-VIKQPWPSMIRDvygDTDRFRHTywehiqpkegqylyfaGDGAR 513
Cdd:cd17641 373 D--PDTVGVPFPG--TEVrIDEVGEILVRSPGVFVgYYKNPEATAEDF---DEDGWLHT----------------GDAGY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 514 RDKDGYFWVMGRVDDVINVS-GHRLGTMEIESALVSHPLVAEAAVVG--RP----------------DELTGEAIFAFVS 574
Cdd:cd17641 430 FKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGagRPyltaficidyaivgkwAEQRGIAFTTYTD 509
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 575 LEGNAEPSEELKKDlVKHVTEEigaIARPAEIRFTDVLPK---------TRSGKIMRRLL 625
Cdd:cd17641 510 LASRPEVYELIRKE-VEKVNAS---LPEAQRIRRFLLLYKeldaddgelTRTRKVRRGVI 565
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
115-629 |
6.92e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 90.67 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIP---EA------AITMLACS--RIGAPHSVVFGGFS-AEALrdrLV 182
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPamyEAhfgvpmAGAVVNCVniRLNAPTIAFLLEHSkSEVV---MV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 183 D------AEAKLVITAD---GGFRKDKAIALKQE------VDKALEHGAPSVENVIvvqrtkadvtMTAGRDHWWhelqp 247
Cdd:PLN02479 124 DqefftlAEEALKILAEkkkSSFKPPLLIVIGDPtcdpksLQYALGKGAIEYEKFL----------ETGDPEFAW----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 248 qqsahcpAEPIDSEDMLFILYTSGSTGKPKGVV-HTTGGYNLytHMTTKWIFDLKDTDVY-----------WC-TADVGW 314
Cdd:PLN02479 189 -------KPPADEWQSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYlwtlpmfhcngWCfTWTLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 315 ITGHSYIvygpLSNGATTVMYEGvprpsnpgcfwdvIERYGVNIFYTAPTAIRAFIR-----------------MGEAVP 377
Cdd:PLN02479 260 LCGTNIC----LRQVTAKAIYSA-------------IANYGVTHFCAAPVVLNTIVNapksetilplprvvhvmTAGAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 378 NARDLSSLRLLG-----TVG--EPINPE---AWM--WyhrviggGKCPIVDTWWQTETGGIMLTPLPGAIPTKPGScTKP 445
Cdd:PLN02479 323 PPSVLFAMSEKGfrvthTYGlsETYGPStvcAWKpeW-------DSLPPEEQARLNARQGVRYIGLEGLDVVDTKT-MKP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 446 FPG---IVAEIVdLDGNPVesdQGGFLviKQPwpsmirdvYGDTDRFRHTyWEHiqpkegqylyfAGDGARRDKDGYFWV 522
Cdd:PLN02479 395 VPAdgkTMGEIV-MRGNMV---MKGYL--KNP--------KANEEAFANG-WFH-----------SGDLGVKHPDGYIEI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 523 MGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEE--LKKDLVKHVTEEIGAI 600
Cdd:PLN02479 449 KDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAY 528
|
570 580
....*....|....*....|....*....
gi 6647434 601 ARPAEIRFTDvLPKTRSGKIMRRLLRSLA 629
Cdd:PLN02479 529 WVPKSVVFGP-LPKTATGKIQKHVLRAKA 556
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
114-559 |
7.32e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.34 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITad 193
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaIALKQEVDKALEHGAPSVENVIVVqrtkadvtmtaGRDHWW------HELQPQQSAHCPAEPIDSEDMLFIL 267
Cdd:PRK09274 120 --------IPKAHLARRLFGWGKPSVRRLVTV-----------GGRLLWggttlaTLLRDGAAAPFPMADLAPDDMAAIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVVhttggynlYTH-MTTKWIFDLKDtdvywctaDVGWITG----HSYIVYG--PLSNGATTVmyegVP- 339
Cdd:PRK09274 181 FTSGSTGTPKGVV--------YTHgMFEAQIEALRE--------DYGIEPGeidlPTFPLFAlfGPALGMTSV----IPd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 ----RPS--NPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGTVGEPINPEAWMWYHRVI------ 407
Cdd:PRK09274 241 mdptRPAtvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLRRVISAGAPVPIAVIERFRAMLppdaei 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 ----GGGKC-PIV---------DTWWQTETGGimltplpgaiptkpGSCT-KPFPGIVAEIVDLDGNPVES--------- 463
Cdd:PRK09274 319 ltpyGATEAlPISsiesreilfATRAATDNGA--------------GICVgRPVDGVEVRIIAISDAPIPEwddalrlat 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 464 DQGGFLVIKQPwpsMIRDVYgdTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIE 543
Cdd:PRK09274 385 GEIGEIVVAGP---MVTRSY--YNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCE 459
|
490
....*....|....*.
gi 6647434 544 SALVSHPLVAEAAVVG 559
Cdd:PRK09274 460 RIFNTHPGVKRSALVG 475
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
115-589 |
1.88e-18 |
|
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: 89.06 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITAdg 194
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gfrkdkaialKQEVDKALEHGAPsvENVIVVQRTKADvtmtAGRDHW-WHELQPQQSAHCPAEPIDSEDMLFILYTSGST 273
Cdd:cd05932 86 ----------KLDDWKAMAPGVP--EGLISISLPPPS----AANCQYqWDDLIAQHPPLEERPTRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTtggYNLYTHMTTKWI--FDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYE--------------- 336
Cdd:cd05932 150 GQPKGVMLT---FGSFAWAAQAGIehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqrarpt 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 337 ---GVPRpsnpgcFW-----DVIERYGV---NIFYTAPTaIRAFIRmgEAVPNARDLSSLRLLGTVGEPINPEAWMWYHR 405
Cdd:cd05932 227 lffSVPR------LWtkfqqGVQDKIPQqklNLLLKIPV-VNSLVK--RKVLKGLGLDQCRLAGCGSAPVPPALLEWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 406 VigggKCPIVDTWWQTETGGIMLTPLPGAipTKPGSCTKPFPGIVAEIVDlDGNpVESDQGGFLVIKQPWPSMIRDVYgD 485
Cdd:cd05932 298 L----GLNILEAYGMTENFAYSHLNYPGR--DKIGTVGNAGPGVEVRISE-DGE-ILVRSPALMMGYYKDPEATAEAF-T 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 TDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVS-GHRLGTMEIESALVSHPLVAEAAVVGrpDEL 564
Cdd:cd05932 369 ADGFLRT----------------GDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG--SGL 430
|
490 500
....*....|....*....|....*
gi 6647434 565 TGEAIFAFVSLEGNAEPSEELKKDL 589
Cdd:cd05932 431 PAPLALVVLSEEARLRADAFARAEL 455
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-625 |
1.79e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.02 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADG 194
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 gfrkdkaialkqevDKALEHGAPSVEnvivvqrtkadvtmTAGRDHWWheLQPQQSAHCPAEPidsEDMLFILYTSGSTG 274
Cdd:PRK10252 565 --------------QLPRFADVPDLT--------------SLCYNAPL--APQGAAPLQLSQP---HHTAYIIFTSGSTG 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 275 KPKGVV--HTTGGYNLythmttKWIFD---LKDTDVYW----CTADVG-----WitghsyivygPLSNGATTVMYE-GVP 339
Cdd:PRK10252 612 RPKGVMvgQTAIVNRL------LWMQNhypLTADDVVLqktpCSFDVSvweffW----------PFIAGAKLVMAEpEAH 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 RpsNPGCFWDVIERYGVNIFYTAPTAIRAFIrmGEAVPNA--RDLSSLRLLGTVGEPINPEAWMWYHRVIG-------GG 410
Cdd:PRK10252 676 R--DPLAMQQFFAEYGVTTTHFVPSMLAAFV--ASLTPEGarQSCASLRQVFCSGEALPADLCREWQQLTGaplhnlyGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 411 KCPIVD-TWWqtETGGIMLTPLPGA-IPTKpgsctkpFP----GIvaEIVDLDGNPVesdqggflvikqPwPSMIRDVYG 484
Cdd:PRK10252 752 TEAAVDvSWY--PAFGEELAAVRGSsVPIG-------YPvwntGL--RILDARMRPV------------P-PGVAGDLYL 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 485 DTDRFRHTYweHIQPK------------EGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV 552
Cdd:PRK10252 808 TGIQLAQGY--LGRPDltasrfiadpfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDV 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 553 AEA---AVVGRPDELTG---EAIFAFVSlegnAEPSEELKKDLVK-HVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK10252 886 EQAvthACVINQAAATGgdaRQLVGYLV----SQSGLPLDTSALQaQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
109-610 |
1.86e-17 |
|
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: 85.73 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITaDGgfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepiDSEDMLFILY 268
Cdd:cd17639 81 IFT-DG----------------------------------------------------------------KPDDLACIMY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 269 TSGSTGKPKGVVHTTGgyNLYTHMTT--KWIFD-LKDTDVYW----------------CTADVGWI------TGHSYIVY 323
Cdd:cd17639 96 TSGSTGNPKGVMLTHG--NLVAGIAGlgDRVPElLGPDDRYLaylplahifelaaenvCLYRGGTIgygsprTLTDKSKR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 324 GP---LSNGATTVMYeGVPRpsnpgcFWDVIeRYGVN------------IFYTAPTAIRAFIRMGEAVP--------NAR 380
Cdd:cd17639 174 GCkgdLTEFKPTLMV-GVPA------IWDTI-RKGVLaklnpmgglkrtLFWTAYQSKLKALKEGPGTPlldelvfkKVR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 381 DL--SSLRLLGTVGEPINPEAwmwyHRVIGGGKCPIVDTWWQTETGGIMLTPLPGAIPTkpGSCTKPFPGIVAEIVDLDG 458
Cdd:cd17639 246 AAlgGRLRYMLSGGAPLSADT----QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLET--GRVGPPLPCCEIKLVDWEE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 459 NPVESDQG---GFLVIKQPW--------PSMIRDVYgDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVD 527
Cdd:cd17639 320 GGYSTDKPpprGEILIRGPNvfkgyyknPEKTKEAF-DGDGWFHT----------------GDIGEFHPDGTLKIIDRKK 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 528 D-VINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDE-------LTGEAI---FAFVSLEGNAEPSEELK-KDLVKHVTE 595
Cdd:cd17639 383 DlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKsypvaivVPNEKHltkLAEKHGVINSEWEELCEdKKLQKAVLK 462
|
570 580
....*....|....*....|....
gi 6647434 596 EIGAIAR---------PAEIRFTD 610
Cdd:cd17639 463 SLAETARaaglekfeiPQGVVLLD 486
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
112-629 |
6.25e-17 |
|
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: 83.94 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 112 RIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIt 191
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 adggfrkdkaialkqeVDKAlehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepidsedmlFILYTSG 271
Cdd:cd05940 81 ----------------VDAA-----------------------------------------------------LYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 272 STGKPKGVVHTTGGYNLYTHMTTKWIFdLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVpRPSNpgcFWDVI 351
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSGG-ALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKF-SASN---FWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 352 ERYGVNIF-YtaptairafirMGE---------AVPNARDlSSLRLLgtVGEPINPEAWMWYHRVIGGGKcpIVDTWWQT 421
Cdd:cd05940 167 RKYQATIFqY-----------IGElcryllnqpPKPTERK-HKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAAT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 422 E--TGGIMLTPLPGAIPTKPGSCTKPFPgivAEIVDLD---GNPVESDQG----------GFLV--IKQPWP-------- 476
Cdd:cd05940 231 EgnSGFINFFGKPGAIGRNPSLLRKVAP---LALVKYDlesGEPIRDAEGrcikvprgepGLLIsrINPLEPfdgytdpa 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 ----SMIRDVYGDTDRFRHTywehiqpkegqylyfaGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV 552
Cdd:cd05940 308 atekKILRDVFKKGDAWFNT----------------GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGV 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 553 AEAAVVGRPDELT-GEAIFAFVSLEGNAEpsEELKKdLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:cd05940 372 EEANVYGVQVPGTdGRAGMAAIVLQPNEE--FDLSA-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
98-625 |
6.66e-17 |
|
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: 84.06 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:cd17656 3 DAVAVVFENQK-----LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITADggfrkdkaialkqevdkalEHGAPSVENVIVVQRTKADVTmtagrdhwwhelqpQQSAHCPAEP 257
Cdd:cd17656 78 IYIMLDSGVRVVLTQR-------------------HLKSKLSFNKSTILLEDPSIS--------------QEDTSNIDYI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDSEDMLFILYTSGSTGKPKGVV--HTTGgYNLYTHMTTKWIFDLKDTDVYW--CTADVgwitghSY--IVYGPLSNGAT 331
Cdd:cd17656 125 NNSDDLLYIIYTSGTTGKPKGVQleHKNM-VNLLHFEREKTNINFSDKVLQFatCSFDV------CYqeIFSTLLSGGTL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 332 TVMYEGVPRPSNPgcFWDVIERYGVNIFYTaPTAIRAFI-RMGEAVPNARDlsSLRLLGTVGEPI---NPEAWMWY---- 403
Cdd:cd17656 198 YIIREETKRDVEQ--LFDLVKRHNIEVVFL-PVAFLKFIfSEREFINRFPT--CVKHIITAGEQLvitNEFKEMLHehnv 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 --HRVIGGGKCPIVDTWWQTETGGIMLTPLPGaiptKPGSCTKPFpgivaeIVDLDGNPVESDQGGFLVIKQPwpSMIRD 481
Cdd:cd17656 273 hlHNHYGPSETHVVTTYTINPEAEIPELPPIG----KPISNTWIY------ILDQEQQLQPQGIVGELYISGA--SVARG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 482 vYGDTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRP 561
Cdd:cd17656 341 -YLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6647434 562 DELTGEAIFAFVSLEgNAEPSEELKKDLVKHVTEEIgaiaRPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17656 420 DDKGEKYLCAYFVME-QELNISQLREYLAKQLPEYM----IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
115-626 |
5.92e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.87 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITaDG 194
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 GFrkdkaIALKQEVDKALehgaPSVENVIVVqrtkadvtmtAGRDHwwhelQPQQS---AHCPAEPIDSEDMLF------ 265
Cdd:PRK06018 120 TF-----VPILEKIADKL----PSVERYVVL----------TDAAH-----MPQTTlknAVAYEEWIAEADGDFawktfd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ------ILYTSGSTGKPKGVVHTTGGYNLYTHMTT-KWIFDLKDTDVYWCTADV----GWITGHSyivyGPlSNGATTVM 334
Cdd:PRK06018 176 entaagMCYTSGTTGDPKGVLYSHRSNVLHALMANnGDALGTSAADTMLPVVPLfhanSWGIAFS----AP-SMGTKLVM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 yegvprpsnPGCFWDVIERYGV----NIFYTA--PTAIRAFIRMGEAvpNARDLSSLRLLgtvgepinpeawmwyhrVIG 408
Cdd:PRK06018 251 ---------PGAKLDGASVYELldteKVTFTAgvPTVWLMLLQYMEK--EGLKLPHLKMV-----------------VCG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 409 GGKCP-------------IVDTWWQTETGGI-MLTPLPGAIPTKPGSC------TKPFP--GIVAEIVDLDGNPVESDQG 466
Cdd:PRK06018 303 GSAMPrsmikafedmgveVRHAWGMTEMSPLgTLAALKPPFSKLPGDArldvlqKQGYPpfGVEMKITDDAGKELPWDGK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 467 GFLVIKQPWPSMIRDVYGDTDrfrhtyweHIQPKEGqylYF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESA 545
Cdd:PRK06018 383 TFGRLKVRGPAVAAAYYRVDG--------EILDDDG---FFdTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 546 LVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK06018 452 AVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATRE---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
.
gi 6647434 626 R 626
Cdd:PRK06018 529 R 529
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-559 |
9.30e-15 |
|
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: 77.12 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 256 EPIDSEDMLfILYTSGSTGKPKGVVhttggynlYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSnGATTVMY 335
Cdd:cd05910 81 IPKADEPAA-ILFTSGSTGTPKGVV--------YRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPAL-GLTSVIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 336 EGVP-RPS--NPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvpNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGkC 412
Cdd:cd05910 151 DMDPtRPAraDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKMLSDE-A 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 413 PIVDTWWQTET------GGIMLTPLPGAIPTK-PGSCT-KPFPGIVAEIVDLDGNPVESDQG---------GFLVIKQPw 475
Cdd:cd05910 228 EILTPYGATEAlpvssiGSRELLATTTAATSGgAGTCVgRPIPGVRVRIIEIDDEPIAEWDDtlelprgeiGEITVTGP- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 476 psMIRDVYgdTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEA 555
Cdd:cd05910 307 --TVTPTY--VNRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
....
gi 6647434 556 AVVG 559
Cdd:cd05910 383 ALVG 386
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
100-627 |
1.49e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.57 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 100 AAIIWEGEPG---DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEA 176
Cdd:PRK13383 44 TAARWPGRTAiidDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 177 LRDRLvDAEAKLVITADGGFrkdkaialkqevdkaLEHGAPSVENVIVVqrtkaDVTMTAGRDhwwhelqpqqsahCPAE 256
Cdd:PRK13383 124 LAAAL-RAHHISTVVADNEF---------------AERIAGADDAVAVI-----DPATAGAEE-------------SGGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 257 PIDSEDMLFILYTSGSTGKPKGVVHTTGgynlYTHMTTKWIFDLKDTDVYwctadvgwiTGHSYIVYGPLSNG------A 330
Cdd:PRK13383 170 PAVAAPGRIVLLTSGTTGKPKGVPRAPQ----LRSAVGVWVTILDRTRLR---------TGSRISVAMPMFHGlglgmlM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 TTVMYEGV---PRPSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVI 407
Cdd:PRK13383 237 LTIALGGTvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 408 GGgkcPIVDTWWQTETG-GIMLTPlpGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVikqpwpsmirdVYGDT 486
Cdd:PRK13383 317 GD---ILYNGYGSTEVGiGALATP--ADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIF-----------VGGEL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 487 DRFRHTYWEHIQPKEGqyLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTG 566
Cdd:PRK13383 381 AGTRYTDGGGKAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFG 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 567 EAIFAFVSLEGNAEPSEELKKDLVKhvtEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRS 627
Cdd:PRK13383 459 HRLAAFVVLHPGSGVDAAQLRDYLK---DRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
115-626 |
5.37e-14 |
|
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: 74.78 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVItad 193
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 194 ggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepIDSEDMLFILYTSGST 273
Cdd:cd05937 84 ----------------------------------------------------------------VDPDDPAILIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTG----GYNLYTHmttkwIFDLKDTD-VYWCTA---DVGWITGHSYIvygpLSNGATTVMyegvPRPSNPG 345
Cdd:cd05937 100 GLPKAAAISWRrtlvTSNLLSH-----DLNLKNGDrTYTCMPlyhGTAAFLGACNC----LMSGGTLAL----SRKFSAS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 346 CFWDVIERYGVNIFYTAPTAIRAFIrmgeAVPNARDLSSLRLLGTVGEPINPEAW------------------------M 401
Cdd:cd05937 167 QFWKDVRDSGATIIQYVGELCRYLL----STPPSPYDRDHKVRVAWGNGLRPDIWerfrerfnvpeigefyaategvfaL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 402 WYHRV--IGGGKCPIVDTWWQ-------------TETGGIMLTPlpgaiptKPGSCTKPFPGIVAE-IVDLDGNPVESDQ 465
Cdd:cd05937 243 TNHNVgdFGAGAIGHHGLIRRwkfenqvvlvkmdPETDDPIRDP-------KTGFCVRAPVGEPGEmLGRVPFKNREAFQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 466 GGFLVIKQPWPSMIRDVYgdtdrfrhtywehiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESA 545
Cdd:cd05937 316 GYLHNEDATESKLVRDVF----------------RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 546 LVSHPLVAEAAVVG-RPDELTGEAIFAFVSLEGNA-EPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRR 623
Cdd:cd05937 380 LGAHPDIAEANVYGvKVPGHDGRAGCAAITLEESSaVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKG 459
|
...
gi 6647434 624 LLR 626
Cdd:cd05937 460 VLR 462
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
126-629 |
7.41e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 75.35 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 126 FANALKSLgVQKGDRVAIYLPMIPEAAITMLACSRIGAphSVVFGGFSA--EALRDRLVDAEAKLVITADGGFRKdkaIA 203
Cdd:PRK08633 654 LARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGK--VPVNLNYTAseAALKSAIEQAQIKTVITSRKFLEK---LK 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 204 LKQEVDKALEH-GAPSVENvIVVQRTKAD--VTMTAGRdhwwheLQPQ---QSAHCPaePIDSEDMLFILYTSGSTGKPK 277
Cdd:PRK08633 728 NKGFDLELPENvKVIYLED-LKAKISKVDklTALLAAR------LLPArllKRLYGP--TFKPDDTATIIFSSGSEGEPK 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 278 GVVHTtgGYNLythMTT----KWIFDLKDTDVywctadvgwITG-----HS--YIV--YGPLSNGATTVMyegVPRPSNP 344
Cdd:PRK08633 799 GVMLS--HHNI---LSNieqiSDVFNLRNDDV---------ILSslpffHSfgLTVtlWLPLLEGIKVVY---HPDPTDA 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 345 GCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPnaRDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETG 424
Cdd:PRK08633 862 LGIAKLVAKHRATILLGTPTFLRLYLRNKKLHP--LMFASLRLVVAGAEKLKPEVADAFEEKFG---IRILEGYGATETS 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 425 GIMLTPLPGA--------IPTKPGSCTKPFPGIVAEIVDLD-GNPVESDQGGFLVIKQpwPSMIRDVYGDTDRFRhtywE 495
Cdd:PRK08633 937 PVASVNLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGG--PQVMKGYLGDPEKTA----E 1010
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 496 HIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHrlgtmeiesaLVSHPLVAEA------------AVVGRPDE 563
Cdd:PRK08633 1011 VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGE----------MVPLGAVEEElakalggeevvfAVTAVPDE 1080
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 564 LTGEAIFAFVSLEgnAEPSEELKKDLVKhvtEEIGAIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:PRK08633 1081 KKGEKLVVLHTCG--AEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
110-284 |
9.65e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 74.63 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadGGFRKDKAIALkqeVDKALEHGAPsvenVIVVQRTKADVTMTAGRDHWWHEL----QPQQSAHCPAEPIDSEDMLF 265
Cdd:PTZ00216 198 VC--NGKNVPNLLRL---MKSGGMPNTT----IIYLDSLPASVDTEGCRLVAWTDVvakgHSAGSHHPLNIPENNDDLAL 268
|
170
....*....|....*....
gi 6647434 266 ILYTSGSTGKPKGVVHTTG 284
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHG 287
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
109-306 |
1.34e-13 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 74.00 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKL 188
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 189 VITADGGFRKDKAIALKQEvdkalehgapSVENVIVVQRTKADVTMT-AGRDHWWHELQPQ-----QSAHCPAEPIDSED 262
Cdd:PLN02387 182 VICDSKQLKKLIDISSQLE----------TVKRVIYMDDEGVDSDSSlSGSSNWTVSSFSEveklgKENPVDPDLPSPND 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6647434 263 MLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVY 306
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
98-625 |
1.66e-13 |
|
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: 72.97 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 98 NKAAIIWEGEPgdsriITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEAL 177
Cdd:cd17645 13 DHVAVVDRGQS-----LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 178 RDRLVDAEAKLVITadggfrkdkaialkqevdkalehgapsvenvivvqrtkadvtmtagrdhwwhelqpqqsahcpaep 257
Cdd:cd17645 88 AYMLADSSAKILLT------------------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 iDSEDMLFILYTSGSTGKPKGVV---HTTGGYNLYTHMTtkwiFDLKDTDVYWCTADVGWiTGHSYIVYGPLSNGATTVM 334
Cdd:cd17645 102 -NPDDLAYVIYTSGSTGLPKGVMiehHNLVNLCEWHRPY----FGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALHV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 335 YEGVPRpSNPGCFWDVIERYGVNIFYTAPTAIRAFIRMgeavpnarDLSSLRLLGTVGEPINpeawmwyhrVIGGGKCPI 414
Cdd:cd17645 176 VPSERR-LDLDALNDYFNQEGITISFLPTGAAEQFMQL--------DNQSLRVLLTGGDKLK---------KIERKGYKL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 415 VDTWWQTETGgIMLTPLPGAIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpSMIRDVYGDTDRFRHTYW 494
Cdd:cd17645 238 VNNYGPTENT-VVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNRPELTAEKFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 EHIQPKeGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:cd17645 315 VHPFVP-GERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6647434 575 LEGNAEPSE---ELKKDLVKHVTeeigaiarPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:cd17645 394 APEEIPHEElreWLKNDLPDYMI--------PTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
113-559 |
1.68e-13 |
|
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: 73.16 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 113 IITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIta 192
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 193 dggfrkdkaialkqevdkalehgapsVENvivvqrtkadvtmtagrdhwwhelqpqqsahcpaepiDSEDMLFILYTSGS 272
Cdd:cd17640 83 --------------------------VEN-------------------------------------DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 273 TGKPKGVVHTTGgyNLYTHMTTKW-IFDLKDTDVYWCTADVgWitgHSY---IVYGPLSNGA----TTV----------- 333
Cdd:cd17640 100 TGNPKGVMLTHA--NLLHQIRSLSdIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCsqayTSIrtlkddlkrvk 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 334 --MYEGVPRpsnpgcFWDVIeRYGVNIFYTAPTAIRAFIrmgeavpnardLSSLRLLGTVGEPINpeawmwyhrviGGGK 411
Cdd:cd17640 174 phYIVSVPR------LWESL-YSGIQKQVSKSSPIKQFL-----------FLFFLSGGIFKFGIS-----------GGGA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 412 CPI-VDTWWQ------------TETGGIMLTPLPGAIptKPGSCTKPFPGIVAEIVDLDGN-PVESDQGGFLVIKQpwPS 477
Cdd:cd17640 225 LPPhVDTFFEaigievlngyglTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRG--PQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 478 MIRDVYGDTDRFRhtywEHIQPkEGqylYF-AGDGARRDKDGYFWVMGRVDDVINVS-GHRLGTMEIESALVSHPLVAEA 555
Cdd:cd17640 301 VMKGYYKNPEATS----KVLDS-DG---WFnTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQI 372
|
....
gi 6647434 556 AVVG 559
Cdd:cd17640 373 MVVG 376
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
109-626 |
1.82e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 73.20 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGVQKGDRVAiylpmipeaaitMLACSriGAPHSVVFGGFSA-----EALRDRLV- 182
Cdd:PRK07008 35 GDIHRYTYRDCERRAKQLAQALAALGVEPGDRVG------------TLAWN--GYRHLEAYYGVSGsgavcHTINPRLFp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 183 DAEAKLVITADggfrkDKAIALKQEVDKALEHGAPSVENVivvqrtKADVTMTaGRDHW---------WHELQPQQSAHC 253
Cdd:PRK07008 101 EQIAYIVNHAE-----DRYVLFDLTFLPLVDALAPQCPNV------KGWVAMT-DAAHLpagstpllcYETLVGAQDGDY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 254 PAEPIDSEDMLFILYTSGSTGKPKGVvhttggynLYTHM-TTKWIFDLKDTDVYWCTA-DV-----------GWITGHSy 320
Cdd:PRK07008 169 DWPRFDENQASSLCYTSGTTGNPKGA--------LYSHRsTVLHAYGAALPDAMGLSArDAvlpvvpmfhvnAWGLPYS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 ivyGPLsNGATTVMyegvPRPSNPG-CFWDVIERYGVNIFYTAPTAIRAFIrmGEAVPNARDLSSLRllgtvgepinpea 399
Cdd:PRK07008 240 ---APL-TGAKLVL----PGPDLDGkSLYELIEAERVTFSAGVPTVWLGLL--NHMREAGLRFSTLR------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 400 wmwyHRVIGGGKCP--------------IVDTWWQTEtggimLTPL-------------PG----AIPTKPGsctKPFPG 448
Cdd:PRK07008 297 ----RTVIGGSACPpamirtfedeygveVIHAWGMTE-----MSPLgtlcklkwkhsqlPLdeqrKLLEKQG---RVIYG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 449 IVAEIVDLDGNPVESDQGGF--LVIKQPWpsMIRDVYGDTDRFRHTYWEHiqpkegqylyfAGDGARRDKDGYFWVMGRV 526
Cdd:PRK07008 365 VDMKIVGDDGRELPWDGKAFgdLQVRGPW--VIDRYFRGDASPLVDGWFP-----------TGDVATIDADGFMQITDRS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 527 DDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkDLVKHVTeeiGAIAR---P 603
Cdd:PRK07008 432 KDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTRE---ELLAFYE---GKVAKwwiP 505
|
570 580
....*....|....*....|...
gi 6647434 604 AEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PRK07008 506 DDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
87-626 |
1.94e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 73.29 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 87 CLDRhLTTWRRNKAAIIWEGepgdsRIITYAQLHREVCQFANALKSLGVQKGDRVAI-------YLPMipeaaitMLACS 159
Cdd:PLN02860 12 CLTR-LATLRGNAVVTISGN-----RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIaalnsdlYLEW-------LLAVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 160 RIGAPHSVVFGGFSAEALRDRLVDAEAKLVITaDGGfrkdkaiaLKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGR- 238
Cdd:PLN02860 79 CAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT-DET--------CSSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSf 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 239 ---DHWW-HELQPQQSAHCPAepidSEDMLFILYTSGSTGKPKGVV--HTTggynLYTHMTTKW-IFDLKDTDVYWCTAD 311
Cdd:PLN02860 150 lttEMLKqRALGTTELDYAWA----PDDAVLICFTSGTTGRPKGVTisHSA----LIVQSLAKIaIVGYGEDDVYLHTAP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 312 VGWITGhsyivygpLSNGATTVMYEG----VPRPSNPGCFwDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARDLSSLRL 387
Cdd:PLN02860 222 LCHIGG--------LSSALAMLMVGAchvlLPKFDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 388 L----GTVGEPINPEAWMWYHRVigggkcPIVDTWWQTETGGIMlTPLPGAIPTKPGSctKPFPGIVAEIVDLDGNPves 463
Cdd:PLN02860 293 IlnggGSLSSRLLPDAKKLFPNA------KLFSAYGMTEACSSL-TFMTLHDPTLESP--KQTLQTVNQTKSSSVHQ--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 464 dQGGFLV----------IKQPWPSMIRDVYGDTDRFRHTYWEHI------QPKEGqYLYfAGDGARRDKDGYFWVMGRVD 527
Cdd:PLN02860 361 -PQGVCVgkpaphvelkIGLDESSRVGRILTRGPHVMLGYWGQNsetasvLSNDG-WLD-TGDIGWIDKAGNLWLIGRSN 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 528 DVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSL----------EGNAEPSEELKKDLVKHVTEEI 597
Cdd:PLN02860 438 DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrdgwiwsdneKENAKKNLTLSSETLRHHCREK 517
|
570 580 590
....*....|....*....|....*....|...
gi 6647434 598 G----AIARpAEIRFTDVLPKTRSGKIMRRLLR 626
Cdd:PLN02860 518 NlsrfKIPK-LFVQWRKPFPLTTTGKIRRDEVR 549
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
259-624 |
2.11e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 72.82 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSEDMLFILYTSGSTGKPKGV-VHTTGGYNLYTHMTTKWIFDLKDTDVywctadvgwITGHSYIVYGP--------LSNG 329
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVlVEHGSVVNLRTSLSERYFGRDNGDEA---------VLFFSNYVFDFfveqmtlaLLNG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 330 ATTVMYEGVPRpSNPGCFWDVIERYGVNIFYTAPTAIRAFirmgeavpNARDLSSLRLLGTVGEPINPEAwmwYHRVIGG 409
Cdd:cd17648 163 QKLVVPPDEMR-FDPDRFYAYINREKVTYLSGTPSVLQQY--------DLARLPHLKRVDAAGEEFTAPV---FEKLRSR 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 410 GKCPIVDTWWQTETGGIML-TPLPGAIPTKpGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPWPS---MIRDVYgD 485
Cdd:cd17648 231 FAGLIINAYGPTETTVTNHkRFFPGDQRFD-KSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVArgyLNRPEL-T 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 486 TDRF-RHTYWEHIQPKEGQY--LYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPD 562
Cdd:cd17648 309 AERFlPNPFQTEQERARGRNarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKED 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6647434 563 ELTGEAIFA------FVSLEGNAEPSeelkkDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKI-MRRL 624
Cdd:cd17648 389 ASQAQSRIQkylvgyYLPEPGHVPES-----DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
261-632 |
5.41e-13 |
|
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: 71.75 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGVVHTTggYNLYTHM-----TTKWifDLKDTDVYW--CTADVGWITGHsyivYGPLSNGATTV 333
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTH--ENLVHNMfailnSTEW--KTKDRILSWmpLTHDMGLIAFH----LAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 334 MY---EGVPRPSNpgcfW-DVIERYGVNIFYTAPTAIRAFI-RMGEAVPNARDLSSLRLLGTVGEPINPE---AWMWYHR 405
Cdd:cd05908 178 LMptrLFIRRPIL----WlKKASEHKATIVSSPNFGYKYFLkTLKPEKANDWDLSSIRMILNGAEPIDYElchEFLDHMS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 406 VIGGGKCPIVDTWWQTE-TGGIMLTPLpgAIPTKPGSCTKPFPGIVAEIVDLDgnpvESDQGGFLVIKQPWP---SMIRD 481
Cdd:cd05908 254 KYGLKRNAILPVYGLAEaSVGASLPKA--QSPFKTITLGRRHVTHGEPEPEVD----KKDSECLTFVEVGKPideTDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 482 VYGDTDRFRHTYWEHIQ-------------PKEGQYLyFAGDGARRDKD------GYFWVMGRVDDVINVSGHRLGTMEI 542
Cdd:cd05908 328 CDEDNKILPDGYIGHIQirgknvtpgyynnPEATAKV-FTDDGWLKTGDlgfirnGRLVITGREKDIIFVNGQNVYPHDI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 543 ESALVSHP--LVAEAAVVGRPDELT-GEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIG-AIARPAEIRftdVLPKTRSG 618
Cdd:cd05908 407 ERIAEELEgvELGRVVACGVNNSNTrNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwQINEVLPIR---RIPKTTSG 483
|
410
....*....|....*
gi 6647434 619 KIMR-RLLRSLASGQ 632
Cdd:cd05908 484 KVKRyELAQRYQSGE 498
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
110-625 |
5.49e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PRK05691 2210 AGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLL 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITadggfrkdkaialkqevDKALehgapsvenvivvqrTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDS----EDMLF 265
Cdd:PRK05691 2290 LS-----------------DRAL---------------FEALGELPAGVARWCLEDDAAALAAYSDAPLPFlslpQHQAY 2337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 266 ILYTSGSTGKPKGVVHTTGGYNLYTHMTTKwIFDLKDTDV----YWCTADVGwitghSYIVYGPLSNGATTVMyegvpRP 341
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDCelhfYSINFDAA-----SERLLVPLLCGARVVL-----RA 2406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 342 SNPgcfWDV------IERYGVNIFYTAPTAIRafiRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIGGGKcpIV 415
Cdd:PRK05691 2407 QGQ---WGAeeicqlIREQQVSILGFTPSYGS---QLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL--FF 2478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 416 DTWWQTETggiMLTPLPGAIPT--KPGSCTKPFPGIV----AEIVDLDGNPVESDQGGFLVI----------KQPWPSMI 479
Cdd:PRK05691 2479 NAYGPTET---VVMPLACLAPEqlEEGAASVPIGRVVgarvAYILDADLALVPQGATGELYVggaglaqgyhDRPGLTAE 2555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 480 RDVygdTDRFRHtywehiqpkEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVG 559
Cdd:PRK05691 2556 RFV---ADPFAA---------DGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6647434 560 RpDELTGEAIFAFVS---LEGNAEPSEELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK05691 2624 L-DTPSGKQLAGYLVsavAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
242-637 |
5.68e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.89 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 242 WHELQPQQSA-HCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSY 320
Cdd:PRK05691 3849 WEEVQAGEVAsHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGM-LNNQLSKVPYLALSEADVIAQTASQSFDISVWQ 3927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 321 IVYGPLSNGATTVMYEGVPRpsNPGCFWDVIERYGVNIFYTAPTAIRafirmGEAVPNARDLSSLRLLGTVGEPINPE-A 399
Cdd:PRK05691 3928 FLAAPLFGARVEIVPNAIAH--DPQGLLAHVQAQGITVLESVPSLIQ-----GMLAEDRQALDGLRWMLPTGEAMPPElA 4000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 400 WMWYHRVIGGGkcpIVDTWwqtetggimltplpgaiptKPGSCTKP---FPgivaeiVDLdgnpvESDQGGFLVIKQPWP 476
Cdd:PRK05691 4001 RQWLQRYPQIG---LVNAY-------------------GPAECSDDvafFR------VDL-----ASTRGSYLPIGSPTD 4047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 S---------------------------MIRDVYGDTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDV 529
Cdd:PRK05691 4048 NnrlylldealelvplgavgelcvagtgVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 530 INVSGHRLGTMEIESALVSHPLVAEAAvVGRPDELTGEAIFAF-VSLEGNAEPSEELKKdLVKHVTEEIGAIARPAEIRF 608
Cdd:PRK05691 4128 VKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYlVPHQTVLAQGALLER-IKQRLRAELPDYMVPLHWLW 4205
|
410 420
....*....|....*....|....*....
gi 6647434 609 TDVLPKTRSGKIMRRLLRSLASGQEISGD 637
Cdd:PRK05691 4206 LDRLPLNANGKLDRKALPALDIGQLQSQA 4234
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
359-618 |
1.06e-12 |
|
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: 69.64 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 359 FYTAPT--AIRAFIRMGeavpnARDLSSLRLLGTVGE---PINPEAWMWYHRVIGGGkcpivdtwwQTETGGimLTPLPG 433
Cdd:cd17636 93 FLLPPTidQIVELNADG-----LYDLSSLRSSPAAPEwndMATVDTSPWGRKPGGYG---------QTEVMG--LATFAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 434 AIPTKPGSCTKPFPGIVAEIVDLDGNPVESDQGGFLVIKQPwpsMIRDVYGDTD-----RFRHTYWEhiqpkegqylyfA 508
Cdd:cd17636 157 LGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGP---TVMAGYWNRPevnarRTRGGWHH------------T 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 509 GDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAEPSEElkkD 588
Cdd:cd17636 222 NDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEA---E 298
|
250 260 270
....*....|....*....|....*....|
gi 6647434 589 LVKHVTEEIGAIARPAEIRFTDVLPKTRSG 618
Cdd:cd17636 299 LIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
131-635 |
2.25e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.12 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 131 KSLGV--------QKGDRVAIylpMIPEAAITMLAC------SRIGAPHSVVFGgfsAEALRDRLVDAEAKLVITADGGF 196
Cdd:PRK08043 240 KTLFVgrilekysVEGERIGL---MLPNATISAAVIfgaslrRRIPAMMNYTAG---VKGLTSAITAAEIKTIFTSRQFL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 197 RKDKAIALKQEVDKAlehgapsveNVIVVQRTKADVTMTAGRDHWWHELQPQQsAHCPAEPidsEDMLFILYTSGSTGKP 276
Cdd:PRK08043 314 DKGKLWHLPEQLTQV---------RWVYLEDLKDDVTTADKLWIFAHLLMPRL-AQVKQQP---EDAALILFTSGSEGHP 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 277 KGVVHTTGGYnLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYegvPRPSN----PGCFWDvie 352
Cdd:PRK08043 381 KGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PSPLHyrivPELVYD--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 353 RYGVNIFYTApTAIRAFIRMGeavpNARDLSSLRLLGTVGEPINPEAWMWYHRVIGggkCPIVDTWWQTETGGIMLTPLP 432
Cdd:PRK08043 454 RNCTVLFGTS-TFLGNYARFA----NPYDFARLRYVVAGAEKLQESTKQLWQDKFG---LRILEGYGVTECAPVVSINVP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 433 GAipTKPGSCTKPFPGIVAEIVDLDGnpveSDQGGFLVIKQPwpsMIRDVY---GDTDRFRHTYWEHIQPKEGQYLYFAG 509
Cdd:PRK08043 526 MA--AKPGTVGRILPGMDARLLSVPG----IEQGGRLQLKGP---NIMNGYlrvEKPGVLEVPTAENARGEMERGWYDTG 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 510 DGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIES-ALVSHPLVAEAAVVgRPDELTGEAIFAFVSlegnaepSEELKKD 588
Cdd:PRK08043 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEALVLFTT-------DSELTRE 668
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6647434 589 LVKHVTEEIGA--IARPAEIRFTDVLPKTRSGKIMRRLLRSLASGQEIS 635
Cdd:PRK08043 669 KLQQYAREHGVpeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQH 717
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
495-625 |
2.72e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.91 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 495 EHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVS 574
Cdd:PRK08308 282 EEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6647434 575 LEGNAEPsEELKKDLVKHvteeIGAIARPAEIRFTDVLPKTRSGKIMRRLL 625
Cdd:PRK08308 362 SHEEIDP-VQLREWCIQH----LAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
138-633 |
9.38e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.45 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 138 GDRVAIYLPMIPEAAITMLACSRIGAPHSVVfgGFSA--EALRDRLVDAEAKLVITADGGFRKDKAialkQEVDKALEHG 215
Cdd:PRK06814 682 GENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSAgiANILSACKAAQVKTVLTSRAFIEKARL----GPLIEALEFG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 216 ApsveNVIVVQRTKADVTmtagrdhWWHELQPQQSAHCPAEPI---DSEDMLFILYTSGSTGKPKGVV--HTtggyNLYT 290
Cdd:PRK06814 756 I----RIIYLEDVRAQIG-------LADKIKGLLAGRFPLVYFcnrDPDDPAVILFTSGSEGTPKGVVlsHR----NLLA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 291 HM---TTKwiFDLKDTDVYWCTADVgwitGHSYIVYG----PLSNGATTVMYegvPRPSNPGCFWDVIerYGVN--IFYT 361
Cdd:PRK06814 821 NRaqvAAR--IDFSPEDKVFNALPV----FHSFGLTGglvlPLLSGVKVFLY---PSPLHYRIIPELI--YDTNatILFG 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 362 APTAIRAFIRMGeavpNARDLSSLRLLGTVGEPINPEA---WMWYHRVigggkcPIVDTWWQTETGGI--MLTPLpgaiP 436
Cdd:PRK06814 890 TDTFLNGYARYA----HPYDFRSLRYVFAGAEKVKEETrqtWMEKFGI------RILEGYGVTETAPViaLNTPM----H 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 437 TKPGSCTKPFPGIVAEIVdldgnPVES-DQGGFLVIKQPwpsMIRDVYGDTDRFRhtyweHIQPKEGQYlYFAGDGARRD 515
Cdd:PRK06814 956 NKAGTVGRLLPGIEYRLE-----PVPGiDEGGRLFVRGP---NVMLGYLRAENPG-----VLEPPADGW-YDTGDIVTID 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 516 KDGYFWVMGRVDDVINVSGhrlgtmEIESALVSHPLVAEA------AVVGRPDELTGEAIFAFVSLEGNAepseelKKDL 589
Cdd:PRK06814 1022 EEGFITIKGRAKRFAKIAG------EMISLAAVEELAAELwpdalhAAVSIPDARKGERIILLTTASDAT------RAAF 1089
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6647434 590 VKHVtEEIGA--IARPAEIRFTDVLPKTRSGKI----MRRLLRSLASGQE 633
Cdd:PRK06814 1090 LAHA-KAAGAseLMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPE 1138
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
106-628 |
2.37e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.56 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 106 GEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIyLPMIPE-------------AAITMLAcsrigAPHSVVFGGF 172
Cdd:PRK07768 22 GEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVeiaptaqglwmrgASLTMLH-----QPTPRTDLAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 173 SAEALRDRLVDAEAKLVITADggfrkdkaialkqevdkALEHGAPSVENVIVVQRTKADVTmtagrdhwwhelqpqqsAH 252
Cdd:PRK07768 96 WAEDTLRVIGMIGAKAVVVGE-----------------PFLAAAPVLEEKGIRVLTVADLL-----------------AA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 253 CPAEPIDS-EDMLFIL-YTSGSTGKPKGVVHTTGgyNLYTH---MTTKWIFDLkDTDVYwctadVGWItghsyivygPLS 327
Cdd:PRK07768 142 DPIDPVETgEDDLALMqLTSGSTGSPKAVQITHG--NLYANaeaMFVAAEFDV-ETDVM-----VSWL---------PLF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 328 N-----GATTV-MYEGVP----RP----SNPGCFWDVIERYGVNIfytapTAIRAFI------RMGEAVPNAR-DLSSLR 386
Cdd:PRK07768 205 HdmgmvGFLTVpMYFGAElvkvTPmdflRDPLLWAELISKYRGTM-----TAAPNFAyallarRLRRQAKPGAfDLSSLR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 387 LLGTVGEPINPEAwmwYHRVIGGGK------CPIVDTWWQTET----------GGI--------MLTPLPGAIPTKPG-- 440
Cdd:PRK07768 280 FALNGAEPIDPAD---VEDLLDAGArfglrpEAILPAYGMAEAtlavsfspcgAGLvvdevdadLLAALRRAVPATKGnt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 441 ----SCTKPFPGIVAEIVDLDGNPVESDQGGflVIKQPWPSMIRDvYGDTDRFRHTywehiQPKEGqyLYFAGDGARRDK 516
Cdd:PRK07768 357 rrlaTLGPPLPGLEVRVVDEDGQVLPPRGVG--VIELRGESVTPG-YLTMDGFIPA-----QDADG--WLDTGDLGYLTE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 517 DGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLV-AEAAVVGRPDELTGEAIFAfVSLEGNAEPSEELKKDLVKHVTE 595
Cdd:PRK07768 427 EGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVAVRLDAGHSREGFA-VAVESNAFEDPAEVRRIRHQVAH 505
|
570 580 590
....*....|....*....|....*....|....*..
gi 6647434 596 EIGAI--ARPAEIRFTDV--LPKTRSGKIMRRLLRSL 628
Cdd:PRK07768 506 EVVAEvgVRPRNVVVLGPgsIPKTPSGKLRRANAAEL 542
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
261-620 |
8.45e-11 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 64.42 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILYTSGSTGKPKGV-VHTTGGYNLYTHMTTKwiFDLKDTDVYWCTadvgwitghSYIVYGP--------LSNGAT 331
Cdd:cd17654 118 ECLAYVIHTSGTTGTPKIVaVPHKCILPNIQHFRSL--FNITSEDILFLT---------SPLTFDPsvveiflsLSSGAT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 332 TVMYEGVPRpSNPGCFWDVI-ERYGVNIFYTAPTAIRAFirmGEAVPNARDLS---SLRLLGTVGE--PINPEAWMWYHR 405
Cdd:cd17654 187 LLIVPTSVK-VLPSKLADILfKRHRITVLQATPTLFRRF---GSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWRGK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 406 vigGGKCPIVDTWWQTETGGIMLT--------PLPGaiptkpGSctkPFPGIVAEIVDLDGNPVE-SDQGGflvikqpwp 476
Cdd:cd17654 263 ---GNRTRIFNIYGITEVSCWALAykvpeedsPVQL------GS---PLLGTVIEVRDQNGSEGTgQVFLG--------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 477 SMIRDVYGDTdrfrhtywEHIQPKeGQyLYFAGDGARRDKDGYFWVmGRVDDVINVSGHRLGTMEIESALVSHpLVAEAA 556
Cdd:cd17654 322 GLNRVCILDD--------EVTVPK-GT-MRATGDFVTVKDGELFFL-GRKDSQIKRRGKRINLDLIQQVIESC-LGVESC 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6647434 557 VVGRPDEltgEAIFAFVSLEGNaepSEELKKDLVKHVTEeigAIARPAEIRFTDVLPKTRSGKI 620
Cdd:cd17654 390 AVTLSDQ---QRLIAFIVGESS---SSRIHKELQLTLLS---SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
114-625 |
3.12e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.99 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGapHSVVFGGFSAEAlrDRLVD----AEAKLV 189
Cdd:PRK04813 28 LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSSPA--ERIEMiievAKPSLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGgfrkdkaiaLKQEVDKALEHGAPSVENVIvvqRTKADVTMTAgrdhwwhelqpqqsahcpaePIDSEDMLFILYT 269
Cdd:PRK04813 104 IATEE---------LPLEILGIPVITLDELKDIF---ATGNPYDFDH--------------------AVKGDDNYYIIFT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 270 SGSTGKPKGV--VHTtggyNLYTHmtTKWI-------------------FDLKDTDVYWCtadvgwitghsyivygpLSN 328
Cdd:PRK04813 152 SGTTGKPKGVqiSHD----NLVSF--TNWMledfalpegpqflnqapysFDLSVMDLYPT-----------------LAS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 329 GATTVMyegVPRP--SNPGCFWDVIERYGVNIFYTAPTairaFIRMGEAVP--NARDLSSLRLLGTVGEPI-NPEAWMWY 403
Cdd:PRK04813 209 GGTLVA---LPKDmtANFKQLFETLPQLPINVWVSTPS----FADMCLLDPsfNEEHLPNLTHFLFCGEELpHKTAKKLL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 404 HRVigggkcP---IVDTWWQTET----GGIMLT--------PLPGAIpTKPGSCTKpfpgivaeIVDLDGNPVESDQGGF 468
Cdd:PRK04813 282 ERF------PsatIYNTYGPTEAtvavTSIEITdemldqykRLPIGY-AKPDSPLL--------IIDEEGTKLPDGEQGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 469 LVIKQPwpSMIRDVYGDTDRFRHTYWEHiqpkEGQYLYFAGDGARRDkDGYFWVMGRVDDVINVSGHRLGTMEIESALVS 548
Cdd:PRK04813 347 IVISGP--SVSKGYLNNPEKTAEAFFTF----DGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 549 HPLVAEAAVV-----GRPDELTGEAIFAFVSLEGNAEPSEELKKDLVKHVTEEIgaIarPAEIRFTDVLPKTRSGKIMRR 623
Cdd:PRK04813 420 SSYVESAVVVpynkdHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYM--I--PRKFIYRDSLPLTPNGKIDRK 495
|
..
gi 6647434 624 LL 625
Cdd:PRK04813 496 AL 497
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
89-449 |
7.10e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 61.99 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 89 DRHLTTWRRNKAAI----IW----EGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSR 160
Cdd:PRK12582 48 PRSIPHLLAKWAAEapdrPWlaqrEPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 161 IG---APHSVVFGGFSAEALRDR-LVDAEAKLVITADGGFRKDKAIAlkqevdkALEHGAPSVenvIVVQRTKADVTMTA 236
Cdd:PRK12582 128 AGvpaAPVSPAYSLMSHDHAKLKhLFDLVKPRVVFAQSGAPFARALA-------ALDLLDVTV---VHVTGPGEGIASIA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 237 GRDhwWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTD----VYWctadV 312
Cdd:PRK12582 198 FAD--LAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvsLDW----M 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 313 GW--ITGHSYIVYGPLSNGATTVMYEGVPRpsnPGCFWDVIErygvNIFYTAPTAI----RAFIRMGEAVPNARDL---- 382
Cdd:PRK12582 272 PWnhTMGGNANFNGLLWGGGTLYIDDGKPL---PGMFEETIR----NLREISPTVYgnvpAGYAMLAEAMEKDDALrrsf 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6647434 383 -SSLRLLGTVGEPINPEAW--MWYHRV-IGGGKCPIVDTWWQTETGGIMLTplPGAIPTKPGSCTKPFPGI 449
Cdd:PRK12582 345 fKNLRLMAYGGATLSDDLYerMQALAVrTTGHRIPFYTGYGATETAPTTTG--THWDTERVGLIGLPLPGV 413
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
109-456 |
1.09e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 61.46 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 109 GDSRIITYAQLHREVCQFANALKSLGV--QKGDRVAIYLPMIPEAAITMLACSRigapHSVV----FGGFSAEALRDRLV 182
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYA----YSLVtvplYDTLGPEAIEYILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 183 DAEAKLVItADGGFrkdKAIALKQEVDKalehgapsvenvivvqrtkadvtmtaGRDhwwhelqpqqsAHCPAEPIDSED 262
Cdd:cd05927 77 HAEISIVF-CDAGV---KVYSLEEFEKL--------------------------GKK-----------NKVPPPPPKPED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 263 MLFILYTSGSTGKPKGVVHT-------TGGYNLYTHMTTKwifdLKDTDVYWC---TAdvgwitgHSY---IVYGPLSNG 329
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLThgnivsnVAGVFKILEILNK----INPTDVYISylpLA-------HIFervVEALFLYHG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 330 ATTVMYEG-------------------VPRPSN---PGCFWDVIERYGV--NIFYTAPTAIRAFIRMGEAVPN------- 378
Cdd:cd05927 185 AKIGFYSGdirlllddikalkptvfpgVPRVLNriyDKIFNKVQAKGPLkrKLFNFALNYKLAELRSGVVRASpfwdklv 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 379 -----ARDLSSLRLLGTVGEPINPEAwMWYHRVIGGgkCPIVDTWWQTET-GGIMLTpLPGAipTKPGSCTKPFPGIVAE 452
Cdd:cd05927 265 fnkikQALGGNVRLMLTGSAPLSPEV-LEFLRVALG--CPVLEGYGQTECtAGATLT-LPGD--TSVGHVGGPLPCAEVK 338
|
....
gi 6647434 453 IVDL 456
Cdd:cd05927 339 LVDV 342
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
105-284 |
1.82e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 60.63 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 105 EGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDA 184
Cdd:PLN02861 69 DSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 185 EAKLVITADggfRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKAD---VTMTAgrdhwWHELQPQQSAHCPAEPIDSE 261
Cdd:PLN02861 149 EVSIAFVQE---SKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEelgVSCFS-----WEEFSLMGSLDCELPPKQKT 220
|
170 180
....*....|....*....|...
gi 6647434 262 DMLFILYTSGSTGKPKGVVHTTG 284
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNR 243
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
114-282 |
2.30e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.16 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 114 ITYAQLHREVCQFANALKSLG-VQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLvITA 192
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL-LAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 193 DggfrkdkAIALKQEVDKALEHGAPSvenVIVVQRTKADVTMTA-------------GRDHWWHELQPQQSAHCPAEPID 259
Cdd:cd17632 147 S-------AEHLDLAVEAVLEGGTPP---RLVVFDHRPEVDAHRaalesarerlaavGIPVTTLTLIAVRGRDLPPAPLF 216
|
170 180
....*....|....*....|....*...
gi 6647434 260 SED-----MLFILYTSGSTGKPKGVVHT 282
Cdd:cd17632 217 RPEpdddpLALLIYTSGSTGTPKGAMYT 244
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
89-282 |
3.37e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 59.83 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 89 DRHLTTWRRnkaaiIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSrigaPHSVV 168
Cdd:PLN02430 57 DNKMLGWRR-----IVDGKVGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACA----AHSLI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 169 ----FGGFSAEALrDRLVD-AEAKLVitadggFRKDKaialkqEVDKALEHGAPSvenvivVQRTKADVTMTAGRD---- 239
Cdd:PLN02430 128 cvplYDTLGPGAV-DYIVDhAEIDFV------FVQDK------KIKELLEPDCKS------AKRLKAIVSFTSVTEeesd 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6647434 240 ---------HWWHEL----QPQQSAHCPAEPIdseDMLFILYTSGSTGKPKGVVHT 282
Cdd:PLN02430 189 kasqigvktYSWIDFlhmgKENPSETNPPKPL---DICTIMYTSGTSGDPKGVVLT 241
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
103-348 |
9.73e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 58.49 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 103 IWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLV 182
Cdd:PLN02614 69 IVDGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIIS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 183 DAEAKLVitadggFRKDKAIAlkqEVDKALEHGAPSVENVIV---VQRTKADVTMTAGR-DHWWHELQPQQSAHCPAEPI 258
Cdd:PLN02614 149 HSEVSIV------FVEEKKIS---ELFKTCPNSTEYMKTVVSfggVSREQKEEAETFGLvIYAWDEFLKLGEGKQYDLPI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 259 DSE-DMLFILYTSGSTGKPKGVVHTTGGynlYTHMTTKWIFDLKDTDVYWCTADVgwitghsYIVYGPLSNGATTVMYEG 337
Cdd:PLN02614 220 KKKsDICTIMYTSGTTGDPKGVMISNES---IVTLIAGVIRLLKSANAALTVKDV-------YLSYLPLAHIFDRVIEEC 289
|
250
....*....|.
gi 6647434 338 VPRPSNPGCFW 348
Cdd:PLN02614 290 FIQHGAAIGFW 300
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
493-629 |
2.14e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.93 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 493 YWEHIqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAF 572
Cdd:PRK07445 315 YYPQI--LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI 392
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6647434 573 VSLEgNAEPSEELKKDLVKHvteEIGAIARPAE-IRFTDvLPKTRSGKIMRRLLRSLA 629
Cdd:PRK07445 393 YVPK-DPSISLEELKTAIKD---QLSPFKQPKHwIPVPQ-LPRNPQGKINRQQLQQIA 445
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
115-629 |
5.20e-08 |
|
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: 55.89 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 115 TYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGaphsvvfggfsaealrdrlvdaeaklVITADG 194
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIG--------------------------VETALI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 195 GFRkdkaiaLKQEvdkALEHgapsvenVIVVQRTKADVTmtagrDHWwHELQPQQSAHCPAEPI-DSEDMLFILYTSGST 273
Cdd:cd05939 59 NSN------LRLE---SLLH-------CITVSKAKALIF-----NLL-DPLLTQSSTEPPSQDDvNFRDKLFYIYTSGTT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 274 GKPKGVVHTTGGYnLYTHMTTKWIFDLKDTDV-YWC-----TAdvGWITGhsyiVYGPLSNGATTVMYEGVpRPSNpgcF 347
Cdd:cd05939 117 GLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVvYDClplyhSA--GGIMG----VGQALLHGSTVVIRKKF-SASN---F 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 348 WDVIERYGVnifyTAPTAIRAFIRMGEAVPNARDLSSLRLLGTVGEPINPEAWMWYHRVIG-----------GGKCPIVD 416
Cdd:cd05939 186 WDDCVKYNC----TIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGipqigefygatEGNSSLVN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 417 TWWQTETGGIMLTPLPGAIP---------------TKPGSCTKPFPG----IVAEIVDldGNPVeSDQGGFLVIKQPWPS 477
Cdd:cd05939 262 IDNHVGACGFNSRILPSVYPirlikvdedtgelirDSDGLCIPCQPGepglLVGKIIQ--NDPL-RRFDGYVNEGATNKK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 478 MIRDVYgdtdrfrhtywehiqpKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIEsALVSHPL-VAEAA 556
Cdd:cd05939 339 IARDVF----------------KKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVE-GILSNVLgLEDVV 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6647434 557 VVG-RPDELTGEA-IFAFVSLEGNAEPsEELKKDLVKHVTEeigaIARPAEIRFTDVLPKTRSGKIMRRLLRSLA 629
Cdd:cd05939 402 VYGvEVPGVEGRAgMAAIVDPERKVDL-DRFSAVLAKSLPP----YARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
110-603 |
5.57e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 52.80 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPhSVVF--GGFSAEALRdrLVDAEak 187
Cdd:PRK07868 469 DGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV-AVLMppDTDLAAAVR--LGGVT-- 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 188 lVITADGGfRKDKAIALKQEV-------DKALEhgAPSVENVIVVQRTKADVTMTAGrdhwWHELQPQQSahcpaepids 260
Cdd:PRK07868 544 -EIITDPT-NLEAARQLPGRVlvlgggeSRDLD--LPDDADVIDMEKIDPDAVELPG----WYRPNPGLA---------- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 261 EDMLFILY-TSGSTGKPKGVvhTTGGYNLyTHMTTKWIFDLKDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGVp 339
Cdd:PRK07868 606 RDLAFIAFsTAGGELVAKQI--TNYRWAL-SAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL- 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 340 rpsNPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAVPNARdlSSLRLLGTVGEPinpeAWMWyHRVIGGGKCPIVDTWW 419
Cdd:PRK07868 682 ---DPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGN--HPVRLFIGSGMP----TGLW-ERVVEAFAPAHVVEFF 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 420 QTETGGIMLTPLPGAiptKPGSCTKPFPGIV-AEIVDLD---GNPVESDQG----------GFLVIKQPWP-----SMIR 480
Cdd:PRK07868 752 ATTDGQAVLANVSGA---KIGSKGRPLPGAGrVELAAYDpehDLILEDDRGfvrraevnevGVLLARARGPidptaSVKR 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 DVYGDTDRFRHTywehiqpkegQYLYfagdgaRRDKDGYFWVMGRVDDVINVSGHRLGTMEIESAL-------------- 546
Cdd:PRK07868 829 GVFAPADTWIST----------EYLF------RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALgriggvdlavtygv 892
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6647434 547 -VSHPLVAEAAVVGRPdeltGEAIFAFVSLEGNAEPSEELKKDLVKHVTE-EIGAIARP 603
Cdd:PRK07868 893 eVGGRQLAVAAVTLRP----GAAITAADLTEALASLPVGLGPDIVHVVPEiPLSATYRP 947
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
105-282 |
5.67e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 52.79 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 105 EGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDA 184
Cdd:PLN02736 70 DGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 185 E-AKLVITADG-----GFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHwwhelqPQqsAHCPAEPi 258
Cdd:PLN02736 150 EvAAIFCVPQTlntllSCLSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSS------PQ--PFRPPKP- 220
|
170 180
....*....|....*....|....
gi 6647434 259 dsEDMLFILYTSGSTGKPKGVVHT 282
Cdd:PLN02736 221 --EDVATICYTSGTTGTPKGVVLT 242
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
113-625 |
7.25e-07 |
|
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: 52.29 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 113 IITYAQLHREVCQFANALKS-LGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVIT 191
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 192 AdggfrkdkaialkQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCP----AEPIDSEDMLFIl 267
Cdd:cd05938 85 A-------------PELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPaslrAHVTIKSPALYI- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 268 YTSGSTGKPKGVVHTTggYNLYTHMTTKWIFDLKDTDVYWCTADV----GWITGhsyiVYGPLSNGATTVMyegvpRPS- 342
Cdd:cd05938 151 YTSGTTGLPKAARISH--LRVLQCSGFLSLCGVTADDVIYITLPLyhssGFLLG----IGGCIELGATCVL-----KPKf 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 343 NPGCFWDVIERYGVNIFYTAPTAIRAFIRMGEAvPNARDlSSLRLlgTVGEPINPEAWMWYHRVIggGKCPIVDTWWQTE 422
Cdd:cd05938 220 SASQFWDDCRKHNVTVIQYIGELLRYLCNQPQS-PNDRD-HKVRL--AIGNGLRADVWREFLRRF--GPIRIREFYGSTE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 423 --TGGIMLTPLPGAIPTkpGSCTK----PFpgivaEIVDLD---GNPVESDQG----------GFLVIK----QPW---- 475
Cdd:cd05938 294 gnIGFFNYTGKIGAVGR--VSYLYkllfPF-----ELIKFDvekEEPVRDAQGfcipvakgepGLLVAKitqqSPFlgya 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 476 -------PSMIRDVY--GDtdrfrhtywehiqpkegqyLYF-AGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESA 545
Cdd:cd05938 367 gdkeqteKKLLRDVFkkGD-------------------VYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 546 LVSHPLVAEAAVVGRPDE-LTGEAIFAFVSLegnaEPSEELK-KDLVKHVTEEIGAIARPAEIRFTDVLPKTRSGKIMRR 623
Cdd:cd05938 428 LGLLDFLQEVNVYGVTVPgHEGRIGMAAVKL----KPGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKV 503
|
..
gi 6647434 624 LL 625
Cdd:cd05938 504 RL 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
106-631 |
8.24e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 106 GEPGDSRIITYAQLHREVCQFANALKSLGvQKGDRVAIYLPMIPEAAITMLACSRIGAphsVVFGGFSAEALR----DRL 181
Cdd:PRK05691 33 DDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGV---IAVPAYPPESARrhhqERL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 182 V----DAEAKLVITaDGGFRKdkaiALkQEVDKALEHGAPSVENVIVVQRTKADVtmtagrdhwWHElqPQqsahcpaep 257
Cdd:PRK05691 109 LsiiaDAEPRLLLT-VADLRD----SL-LQMEELAAANAPELLCVDTLDPALAEA---------WQE--PA--------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 258 IDSEDMLFILYTSGSTGKPKGVVHTTGgyNLythMTTKWI------FDLKDTDVYwctadVGWIT-GHSYIVYGPLSNGa 330
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGVQVSHG--NL---VANEQLirhgfgIDLNPDDVI-----VSWLPlYHDMGLIGGLLQP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 331 ttvMYEGVP-RPSNPGCF------W-DVIERYGVNIFYTAPTAIRAFI-RMGEAVPNARDLSSLRLLGTVGEPI------ 395
Cdd:PRK05691 232 ---IFSGVPcVLMSPAYFlerplrWlEAISEYGGTISGGPDFAYRLCSeRVSESALERLDLSRWRVAYSGSEPIrqdsle 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 396 -----------NPEAWMWYHRV------IGGGKcpivdtwwqtETGGIMLTPLPG----AIPTKPG------SCTKPFPG 448
Cdd:PRK05691 309 rfaekfaacgfDPDSFFASYGLaeatlfVSGGR----------RGQGIPALELDAealaRNRAEPGtgsvlmSCGRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 449 IVAEIVDldgnPVESDQGGFLVIKQPW---PSMIRDVYGDTDRFRHTYWEHiqpkEGQYLYFAGD-GARRdkDGYFWVMG 524
Cdd:PRK05691 379 HAVLIVD----PQSLEVLGDNRVGEIWasgPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDlGFLR--DGELFVTG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 525 RVDDVINVSGHRL------GTMEIESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEgNAEPSEELKKDLVKHVTEEIG 598
Cdd:PRK05691 449 RLKDMLIVRGHNLypqdieKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAAEISRSVQ-KILPPQALIKSIRQAVAEACQ 527
|
570 580 590
....*....|....*....|....*....|....
gi 6647434 599 AIARPAEIRFTDVLPKTRSGKIMRRLLRS-LASG 631
Cdd:PRK05691 528 EAPSVVLLLNPGALPKTSSGKLQRSACRLrLADG 561
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
481-620 |
6.98e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.97 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 481 DVYGDTDRFRHTYWEHIQPKEGQYLYFAGDGARRDKDGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVGR 560
Cdd:cd17647 349 DHWNYLDKDNNEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 561 PDELTGEAIFAFVSLEGNAEPSE------------------------ELKKDLVKHVTEEIGAIARPAEIRFTDVLPKTR 616
Cdd:cd17647 429 RDKDEEPTLVSYIVPRFDKPDDEsfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNP 508
|
....
gi 6647434 617 SGKI 620
Cdd:cd17647 509 NGKV 512
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
542-653 |
2.49e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 40.52 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 542 IESALVSHPLVAEAAVVGRPDELTGEAIFAFVSLEGNAepseeLKKDLVKHVTEEIGAIArPAEIRFTDVLPKTRSGKIM 621
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELPA-----DEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....
gi 6647434 622 RRLLRSLASGQ--EISGDTSTLEDRTVLDKLREG 653
Cdd:PRK09188 319 DDILRLIAMNQidELDDLLREPEIRGLVEAIAAH 352
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
517-624 |
4.12e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 40.13 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 517 DGYFWVMGRVDDVINVSGHRLGTMEIESALVSHPLVAEAAVVG--------RPdeltGEAIFAfvSLEGNAEPSEelKKD 588
Cdd:PRK05851 408 DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgtgegsaRP----GLVIAA--EFRGPDEAGA--RSE 479
|
90 100 110
....*....|....*....|....*....|....*...
gi 6647434 589 LVKHVTEEIGAIarPAEIRFTD--VLPKTRSGKiMRRL 624
Cdd:PRK05851 480 VVQRVASECGVV--PSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
110-282 |
7.79e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 39.08 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 110 DSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLV 189
Cdd:PRK09029 25 NDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6647434 190 ITADGgfrkDKAIALKQEVDKALEHGAPSVEnvivvqrtkadvtmtagrdhwWhelQPQQSAhcpaepidseDMLFilyT 269
Cdd:PRK09029 105 LVLEG----ENTFSALTSLHLQLVEGAHAVA---------------------W---QPQRLA----------TMTL---T 143
|
170
....*....|...
gi 6647434 270 SGSTGKPKGVVHT 282
Cdd:PRK09029 144 SGSTGLPKAAVHT 156
|
|
| |
