|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1-600 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1201.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDEsDAPFYKWFDDGELNASYNCLDRHVEAGnGQRVAVIFEADD-GTVTRVTYAELLARVSRFANALKKRGI 79
Cdd:PRK00174 43 WFKPFDTVLDW-NAPFIKWFEDGELNVSYNCLDRHLKTR-GDKVAIIWEGDDpGDSRKITYRELHREVCRFANALKSLGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 80 AKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMg 159
Cdd:PRK00174 121 KKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALAN- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 gCEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTM 239
Cdd:PRK00174 200 -CPSVEKVIVVRRTGGDVDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 240 KWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE 319
Cdd:PRK00174 279 KYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 320 AddkvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIM 399
Cdd:PRK00174 359 E----HPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 400 AAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGGrlYLAGDGTVRDKDtGYFTIMGRIDDVLNV 479
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGM--YFTGDGARRDED-GYYWITGRVDDVLNV 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 480 SGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWVGKQIGPIAKPKDIRFG 559
Cdd:PRK00174 512 SGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE---LRKELRNWVRKEIGPIAKPDVIQFA 588
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1860891105 560 DNLPKTRSGKIMRRLLRSLAKGEAITQDTSTLENPAILDQL 600
Cdd:PRK00174 589 PGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1-600 |
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: 1060.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNCLDRHVEAgNGQRVAVIFEADD-GTVTRVTYAELLARVSRFANALKKRGI 79
Cdd:TIGR02188 32 WFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWEGDEpGEVRKITYRELHREVCRFANVLKSLGV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 80 AKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMG 159
Cdd:TIGR02188 111 KKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKC 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 GCeAVKSVIVYRRTGGKID-WHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQT 238
Cdd:TIGR02188 191 PV-SVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 239 MKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAA 318
Cdd:TIGR02188 270 MKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 319 EAddkvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGI 398
Cdd:TIGR02188 350 DE----WVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVP-NGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVL 477
Cdd:TIGR02188 426 EPAVVDEEGNPVEgPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPG--YYFTGDGARRDKD-GYIWITGRVDDVI 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 478 NVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWVGKQIGPIAKPKDIR 557
Cdd:TIGR02188 503 NVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE---LRKELRKHVRKEIGPIAKPDKIR 579
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1860891105 558 FGDNLPKTRSGKIMRRLLRSLAKGEA-ITQDTSTLENPAILDQL 600
Cdd:TIGR02188 580 FVPGLPKTRSGKIMRRLLRKIAAGEAeILGDTSTLEDPSVVEEL 623
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1-593 |
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: 1050.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDES-DAPFYKWFDDGELNASYNCLDRHVEAgNGQRVAVIFEADDGTVTR-VTYAELLARVSRFANALKKRG 78
Cdd:cd05966 27 WFKPWDKVLDWSkGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDEPDQSRtITYRELLREVCRFANVLKSLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 79 IAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAm 158
Cdd:cd05966 106 VKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALE- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 159 gGCEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQT 238
Cdd:cd05966 185 -KCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 239 MKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAA 318
Cdd:cd05966 264 FKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 319 EAddkvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGI 398
Cdd:cd05966 344 DE----WVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVLN 478
Cdd:cd05966 420 EPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPG--YYFTGDGARRDED-GYYWITGRVDDVIN 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 479 VSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRpegEEAAALAKTLRDWVGKQIGPIAKPKDIRF 558
Cdd:cd05966 497 VSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGE---EPSDELRKELRKHVRKEIGPIATPDKIQF 573
|
570 580 590
....*....|....*....|....*....|....*
gi 1860891105 559 GDNLPKTRSGKIMRRLLRSLAKGEAITQDTSTLEN 593
Cdd:cd05966 574 VPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
18-600 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 893.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 18 KWFDDGELNASYNCLDRHVEaGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIV 97
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 98 AMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAmgGCEAVKSVIVYRRTGGKI 177
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE--ELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 178 DWHAgrDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADI 257
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 258 GWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkvHPKSYDLSSLRII 337
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDE----PLKKYDLSSLRLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 338 GTVGEPINPEAWMWYHKHVGqerCPIVDTWWQTETGGHMITPLPGaTPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGI 417
Cdd:COG0365 312 GSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 418 LVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHE 497
Cdd:COG0365 388 LVIKGPWPGMFRGYWNDPERYRETYFGRFPG--WYRTGDGARRDED-GYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 498 LVAEAAVVGRPDDTTGEAVVAFVVLKrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLK---PGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
570 580
....*....|....*....|...
gi 1860891105 578 LAKGEAItQDTSTLENPAILDQL 600
Cdd:COG0365 542 IAEGRPL-GDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1-571 |
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: 672.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKV---LDESDAPFYKWFDDGELNASYNCLDRHVEaGNGQRVAVIFEADDGTVTR-VTYAELLARVSRFANALKK 76
Cdd:cd17634 25 WITPYQKVkntSFAPGAPSIKWFEDATLNLAANALDRHLR-ENGDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTLLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 77 RGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAV 156
Cdd:cd17634 104 LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 157 AMGGcEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAA 236
Cdd:cd17634 184 NPNV-TSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 237 QTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLik 316
Cdd:cd17634 263 TTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRAL-- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 317 AAEADDKVhpKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLP 396
Cdd:cd17634 341 MAAGDDAI--EGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 397 GIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDV 476
Cdd:cd17634 419 GVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKG--MYFSGDGARRDED-GYYWITGRSDDV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 477 LNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEAAALAKTLRDWVGKQIGPIAKPKDI 556
Cdd:cd17634 496 INVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVL---NHGVEPSPELYAELRNWVRKEIGPLATPDVV 572
|
570
....*....|....*
gi 1860891105 557 RFGDNLPKTRSGKIM 571
Cdd:cd17634 573 HWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
18-600 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 645.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 18 KWFDDGELNASYNCLDRHVEAGNGQRVAVIFEADD-GTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGI 96
Cdd:PLN02654 80 EWFKGGKTNICYNCLDRNVEAGNGDKIAIYWEGNEpGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 97 VAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEA--------VAMGGCEAVKSVI 168
Cdd:PLN02654 160 IAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAAldesakngVSVGICLTYENQL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 169 VYRRTGGKidWHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPD 248
Cdd:PLN02654 240 AMKREDTK--WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 249 DVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaDDKVHPKS 328
Cdd:PLN02654 318 DVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMR----DGDEYVTR 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 329 YDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQ 408
Cdd:PLN02654 394 HSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGK 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 409 DVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTME 488
Cdd:PLN02654 474 EIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAG--YYFSGDGCSRDKD-GYYWLTGRVDDVINVSGHRIGTAE 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 489 IESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSG 568
Cdd:PLN02654 551 VESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE---LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSG 627
|
570 580 590
....*....|....*....|....*....|...
gi 1860891105 569 KIMRRLLRSLAKGEAIT-QDTSTLENPAILDQL 600
Cdd:PLN02654 628 KIMRRILRKIASRQLDElGDTSTLADPGVVDQL 660
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1-600 |
0e+00 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 645.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNCLDRHVEAGNGQRVAVIFE-ADDGTVTRVTYAELLARVSRFANALKKRGI 79
Cdd:cd05967 25 WFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDsPVTGTERTYTYAELLDEVSRLAGVLRKLGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 80 AKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMG 159
Cdd:cd05967 105 VKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 GCEAVKsVIVYRRTGGKID-WHAGRDL-WMHELADAESDTCAPewVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQ 237
Cdd:cd05967 185 GHKPHH-VLVLNRPQVPADlTKPGRDLdWSELLAKAEPVDCVP--VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 238 TMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPT-WPDAGRFWKMIGDHKVTVFYTAPTAIRSlIK 316
Cdd:cd05967 262 SMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRA-IR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 317 AAEADDKvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGGHMITPLPG--ATPTVPGSCTLP 394
Cdd:cd05967 341 KEDPDGK-YIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 395 LPGIMAAVVDETGQDVPNGQGGILVVKRPW-PAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRI 473
Cdd:cd05967 417 VPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDED-GYLFIMGRT 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 474 DDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaALAKTLRDWVGKQIGPIAKP 553
Cdd:cd05967 494 DDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAE--ELEKELVALVREQIGPVAAF 571
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1860891105 554 KDIRFGDNLPKTRSGKIMRRLLRSLAKGEAITqDTSTLENPAILDQL 600
Cdd:cd05967 572 RLVIFVKRLPKTRSGKILRRTLRKIADGEDYT-IPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1-600 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 597.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNCLDRHVEAGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIA 80
Cdd:PRK10524 28 WQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 81 KGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMGG 160
Cdd:PRK10524 108 RGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 161 CEAVKSVIVYRRTgGKIDWHAGRDLWMHELADAESDTCAP-EWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTM 239
Cdd:PRK10524 188 HKPRHVLLVDRGL-APMARVAGRDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 240 KWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE 319
Cdd:PRK10524 267 DTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 320 AddkvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGGHMITPLPG--ATPTVPGSCTLPLPG 397
Cdd:PRK10524 347 A----LLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 398 IMAAVVDE-TGQDVPNGQGGILVVKRPW-PAMIRTIWGDPERFRKSYYpEELGGRLYLAGDGTVRDKDtGYFTIMGRIDD 475
Cdd:PRK10524 420 YNVKLLNEvTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYW-SLFGRQVYSTFDWGIRDAD-GYYFILGRTDD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 476 VLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSR--PEGEEAAALAKTLRDWVGKQIGPIAKP 553
Cdd:PRK10524 498 VINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDslADREARLALEKEIMALVDSQLGAVARP 577
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1860891105 554 KDIRFGDNLPKTRSGKIMRRLLRSLAKGEAiTQDTSTLENPAILDQL 600
Cdd:PRK10524 578 ARVWFVSALPKTRSGKLLRRAIQAIAEGRD-PGDLTTIEDPAALQQI 623
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
19-592 |
1.30e-178 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 517.14 E-value: 1.30e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 19 WFDDGELNASYNCLDRHVEAGNGQRVAVIFEaDDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVA 98
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGRKDKVALRYL-DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 99 MQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARggktlplKSIADEAvamggcEAVKSVIVYRRTGGKID 178
Cdd:PRK04319 115 LLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL------PSLKHVLLVGEDVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 179 whagRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLwAAQTMKWTFDWKPDDVFWCTADIG 258
Cdd:PRK04319 182 ----GTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ-HYQTGKYVLDLHEDDVYWCTADPG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 259 WVTGHTYITYGPLACGGTQVVFEGVPtwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAeaDDKVhpKSYDLSSLRIIG 338
Cdd:PRK04319 257 WVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAG--DDLV--KKYDLSSLRHIL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 339 TVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGGHMITPLPgATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGIL 418
Cdd:PRK04319 330 SVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 419 VVKRPWPAMIRTIWGDPERFRKSYypeeLGGrLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHEL 498
Cdd:PRK04319 406 AIKKGWPSMMRGIWNNPEKYESYF----AGD-WYVSGDSAYMDED-GYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 499 VAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEAA-ALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK04319 480 VAEAGVIGKPDPVRGEIIKAFVALR----PGYEPSeELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
570
....*....|....*....
gi 1860891105 578 ----LAKGeaitqDTSTLE 592
Cdd:PRK04319 556 welgLPEG-----DLSTME 569
|
|
| propion_prpE |
TIGR02316 |
propionate--CoA ligase; This family contains one of three readily separable clades of proteins ... |
1-600 |
6.55e-171 |
|
propionate--CoA ligase; This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate.
Pssm-ID: 131369 [Multi-domain] Cd Length: 628 Bit Score: 499.82 E-value: 6.55e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNCLDRHVEAGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIA 80
Cdd:TIGR02316 27 WQTPPQRILDYSNPPFARWFAGGRTNLCHNALDRHLDERGEQLALVTVSSETGQERTLTYRQLHREVNVFASALRALGVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 81 KGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMGG 160
Cdd:TIGR02316 107 RGDRVLIYMPMIAEAVFAMLACARIGAIHSVVFGGFASHSLALRIDDATPKLIVSADAGMRGGKVIPYKPLLDAAIAEAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 161 CEAvKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTCAP-EWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTM 239
Cdd:TIGR02316 187 HPP-PHVLLVDRGLAPMRLIPGRDVDYAALRTQHEDAQVPvEWLESNEPSYILYTSGTTGKPKGVQRDVGGYAVALALSM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 240 KWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE 319
Cdd:TIGR02316 266 WAIFGIRAGQVMFSASDVGWVVGHSYIVYAPLLAGAATVLYEGLPTNPDPGVWWSIVERYGVRTMFSAPTAIRVLKKQDA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 320 ADDKVHpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGGHMITPLPGATPTVP--GSCTLPLPG 397
Cdd:TIGR02316 346 AWLRKH----DLSSLHWLFLAGEPLDEPTAHWITDGLGK---PVIDNYWQTETGWPVLAIMPGLDLKPVklGSPGLPMYG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 398 IMAAVVDE-TGQDVPNGQGGILVVKRPW-PAMIRTIWGDPERFRKSYYpEELGGRLYLAGDGTVRDKDtGYFTIMGRIDD 475
Cdd:TIGR02316 419 YHLRVLDEaTGRPCGPNEKGVLTVVPPLpPGCLSTVWGDDARFLKTYW-SHFKRPLYSSFDWGIRDED-GYTFILGRTDD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 476 VLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAA--ALAKTLRDWVGKQIGPIAKP 553
Cdd:TIGR02316 497 VINVAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKESDSAGDAHDphAVETGMMDCVVRQLGAVARP 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1860891105 554 KDIRFGDNLPKTRSGKIMRRLLRSLAKGEAiTQDTSTLENPAILDQL 600
Cdd:TIGR02316 577 ARVYFVAALPKTRSGKLLRRSIQALAEGRD-PGDLTTIDDPGALEQV 622
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-594 |
2.73e-168 |
|
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: 492.39 E-value: 2.73e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLD-ESDAPFYKWFDDGELNASYNCLDRHVeAGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGI 79
Cdd:cd05968 35 WYEPPYQTLDlSGGKPWAAWFVGGRMNIVEQLLDKWL-ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 80 AKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMg 159
Cdd:cd05968 114 GKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQ- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 gCEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDtcAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTM 239
Cdd:cd05968 193 -CPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGD--GAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 240 KWTFDWKPDD-VFWCTaDIGWVTGhTYITYGPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAA 318
Cdd:cd05968 270 YFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 319 EADDKVHpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQERCPIVDTWWQTETGGHMITPLPgATPTVPGSCTLPLPGI 398
Cdd:cd05968 348 DAPVNAH----DLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVPnGQGGILVVKRPWPAMIRTIWGDPERFRKSYYPEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVLN 478
Cdd:cd05968 423 KADVLDESGKPAR-PEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDN--VWVHGDFAYYDEE-GYFYILGRSDDTIN 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 479 VSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRF 558
Cdd:cd05968 499 VAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL---KPGVTPTEALAEELMERVADELGKPLSPERILF 575
|
570 580 590
....*....|....*....|....*....|....*.
gi 1860891105 559 GDNLPKTRSGKIMRRLLRSLAKGEAITqDTSTLENP 594
Cdd:cd05968 576 VKDLPKTRNAKVMRRVIRAAYLGKELG-DLSSLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
59-579 |
1.88e-138 |
|
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: 409.97 E-value: 1.88e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADE 138
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 139 qarggktlplksiadeavamggceavksviVYRRTGgkidwhagrdlwmheladaesdtcapewvgAEHPLFILYTSGST 218
Cdd:cd05969 82 ------------------------------LYERTD------------------------------PEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 219 GKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPtwpDAGRFWKMIGD 298
Cdd:cd05969 102 GTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 299 HKVTVFYTAPTAIRSLIKAAEAddkvHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGGHMIT 378
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDE----LARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV---PIHDTWWQTETGSIMIA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 379 PLPGaTPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSYypeeLGGrLYLAGDGT 458
Cdd:cd05969 251 NYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSF----IDG-WYLTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 459 VRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKT 538
Cdd:cd05969 325 YRDED-GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE---LKEE 400
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1860891105 539 LRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd05969 401 IINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
58-576 |
2.10e-110 |
|
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: 337.39 E-value: 2.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTad 137
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvGAEHPLFILYTSGS 217
Cdd:cd05972 79 ------------------------------------------------------------------DAEDPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTwpDAGRFWKMIG 297
Cdd:cd05972 93 TGLPKGVLH-THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 298 DHKVTVFYTAPTAIRSLIKaaeaddkVHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGgHMI 377
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIK-------QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGL---PIRDGYGQTETG-LTV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 378 TPLPGaTPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSyypeeLGGRLYLAGDG 457
Cdd:cd05972 239 GNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEAS-----IRGDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 458 TVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAK 537
Cdd:cd05972 313 AYRDED-GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEE---LAE 388
|
490 500 510
....*....|....*....|....*....|....*....
gi 1860891105 538 TLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05972 389 ELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
32-480 |
2.22e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 331.97 E-value: 2.22e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVeAGNGQRVAVifeaDDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:pfam00501 1 LERQA-ARTPDKTAL----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTADEqarggktLPLKSIADeavAMGGCEAVKSVIVYRRTGGKIDWHAGrdlwmHELA 191
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA-------LKLEELLE---ALGKLEVVKLVLVLDRDPVLKEEPLP-----EEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTgGYLLWAAQTMKWTFDWK----PDDVFWCTADIGWVTGHTYIT 267
Cdd:pfam00501 141 PADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVRPRGfglgPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 YGPLACGGTQVVFEGVPTwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEaddkvhPKSYDLSSLRIIGTVGEPINPE 347
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGA------PKRALLSSLRLVLSGGAPLPPE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 348 AWMWYHKHVGqerCPIVDTWWQTETGGHMITPLPGATP-TVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPWp 425
Cdd:pfam00501 293 LARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPG- 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 426 aMIRTIWGDPERFRKSYYPEelggRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVS 480
Cdd:pfam00501 369 -VMKGYLNDPELTAEAFDED----GWYRTGDLGRRDED-GYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
32-583 |
3.28e-108 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 332.55 E-value: 3.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:COG0318 5 LRRAAAR-HPDRPALVFGG-----RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTAdeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmhela 191
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 daesdtcapewvgaehplFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPL 271
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 272 ACGGTQVVfegVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVGEPINPEAWMW 351
Cdd:COG0318 165 LAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPEFAR------YDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 352 YHKHVGqerCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWpaMIRTI 431
Cdd:COG0318 235 FEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 WGDPERFRKSyypeeLGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDT 511
Cdd:COG0318 310 WNDPEATAEA-----FRDGWLRTGDLGRLDED-GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEK 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 512 TGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGEA 583
Cdd:COG0318 384 WGERVVAFVVLR------PGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-599 |
1.77e-98 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 313.66 E-value: 1.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNCLdRHveaGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIA 80
Cdd:PRK03584 62 GSTPYTVVLAGRRMPGARWFPGARLNYAENLL-RH---RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 81 KGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKS-IADEAVAMG 159
Cdd:PRK03584 138 PGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAkVAELRAALP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 GCEAVksVIV-YRRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQT 238
Cdd:PRK03584 218 SLEHV--VVVpYLGPAAAAAALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 239 MKWTFDWKPDD-VFWCTAdIGW------VTGhtyitygpLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAI 311
Cdd:PRK03584 296 LGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 312 RSLIKAaeaddKVHP-KSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercpivDTWWQTETGGHMI-TPLPGATPTVP- 388
Cdd:PRK03584 367 DACEKA-----GLVPgETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGTDIcSCFVGGNPLLPv 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 389 --GSCTLPLPGIMAAVVDETGQDVpNGQGGILVVKRPWPAMIRTIWGDP--ERFRKSY---YPEelggrLYLAGDgTVRD 461
Cdd:PRK03584 436 yrGEIQCRGLGMAVEAWDEDGRPV-VGEVGELVCTKPFPSMPLGFWNDPdgSRYRDAYfdtFPG-----VWRHGD-WIEI 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 462 KDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEE-AAALAKTLR 540
Cdd:PRK03584 509 TEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA----EGVTlDDALRARIR 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 541 DWVGKQIGPIAKPKDIRFGDNLPKTRSGKIM----RRLLRslakGEAITQ--DTSTLENPAILDQ 599
Cdd:PRK03584 585 TTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLH----GRPVKKavNRDALANPEALDW 645
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1-598 |
9.02e-97 |
|
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: 308.43 E-value: 9.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLDESD-APFYKWFDDGELNASYNCLdRHveaGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGI 79
Cdd:cd05943 45 GSKPYDVVVVSGRiMPGARWFPGARLNYAENLL-RH---ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 80 AKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAmG 159
Cdd:cd05943 121 KPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVK-G 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 160 GCEAVKSVIV-YRRTGGKIDW--HAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAA 236
Cdd:cd05943 200 LPSLLAVVVVpYTVAAGQPDLskIAKALTLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 237 QTMKWTFDWKPDDVFWCTADIGWVTGHTYITYgpLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIK 316
Cdd:cd05943 280 KEHILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 317 AaeaddKVHP-KSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercpivDTWWQTETGG-HMITPLPGATPTVP---GSC 391
Cdd:cd05943 358 A-----GLKPaETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGGtDIISCFVGGNPLLPvyrGEI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 392 TLPLPGIMAAVVDETGQDVPnGQGGILVVKRPWPAMIRTIWGDPE--RFRKSYYpEELGGrLYLAGDGTVRDKDTGYfTI 469
Cdd:cd05943 427 QCRGLGMAVEAFDEEGKPVW-GEKGELVCTKPFPSMPVGFWNDPDgsRYRAAYF-AKYPG-VWAHGDWIEITPRGGV-VI 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 470 MGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEAAALAKTLRDWVGKQIGP 549
Cdd:cd05943 503 LGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKL---REGVELDDELRKRIRSTIRSALSP 579
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1860891105 550 IAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGEAITQdTSTLENPAILD 598
Cdd:cd05943 580 RHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKN-AGALANPESLD 627
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-571 |
4.32e-96 |
|
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: 297.27 E-value: 4.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 207 HPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVtGHTYITYGPLACGGTQVVFEGvptw 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN-LLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 287 PDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIVDT 366
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAG------YDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 367 WWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAmiRTIWGDPERFRksyypEE 446
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVM--KGYWNNPEATA-----AV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 447 LGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsr 526
Cdd:cd04433 219 DEDGWYRTGDLGRLDED-GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR--- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1860891105 527 pegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIM 571
Cdd:cd04433 295 ---PGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
59-576 |
2.79e-84 |
|
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: 270.16 E-value: 2.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADE 138
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 139 QarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwMHELADAesdtcapewvgaehPLFILYTSGST 218
Cdd:cd05973 82 N-----------------------------------------------RHKLDSD--------------PFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 219 GKPKGVQHSTGGYLLWAAQtMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAgrfWKMIGD 298
Cdd:cd05973 101 GLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 299 HKVTVFYTAPTAIRSLIkAAEADDKVHPKSydlsSLRIIGTVGEPINPEAWMWYHKHVGqerCPIVDTWWQTETGGHMIT 378
Cdd:cd05973 177 LGVTNLAGSPTAYRLLM-AAGAEVPARPKG----RLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLAN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 379 PLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVV-KRPWPAMirtiWgdperFRKSYYPEE--LGGRLYLAG 455
Cdd:cd05973 249 HHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSPLM----W-----FRGYQLPDTpaIDGGYYLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 456 DgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEAAAL 535
Cdd:cd05973 320 D-TVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVL---RGGHEGTPAL 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1860891105 536 AKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05973 396 ADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-577 |
1.85e-79 |
|
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: 257.75 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 52 DGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAV 131
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 132 ALVTadeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmhelaDAESDtcapewvgaehPLFI 211
Cdd:cd05971 81 ALVT--------------------------------------------------------DGSDD-----------PALI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 212 LYTSGSTGKPKGVQHSTGgYLLWAAQTMKWTFDWKP--DDVFWCTADIGWVtghtyitygplacGGTQVVF-----EGVP 284
Cdd:cd05971 94 IYTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWI-------------GGLLDVLlpslyFGVP 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 ------TWPDAGRFWKMIGDHKVTVFYTAPTAIRsLIKAAEAddkvhPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQ 358
Cdd:cd05971 160 vlahrmTKFDPKAALDLMSRYGVTTAFLPPTALK-MMRQQGE-----QLKHAQVKLRAIATGGESLGEELLGWAREQFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 359 ErcpIVDTWWQTEtGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERF 438
Cdd:cd05971 234 E---VNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSAT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 439 RKSYypeelGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVA 518
Cdd:cd05971 310 EKKM-----AGDWLLTGDLGRKDSD-GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKA 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 519 FVVLkrsRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:cd05971 384 FVVL---NPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
32-576 |
7.73e-79 |
|
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: 258.07 E-value: 7.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAGNGQRVAVIfeaddGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:cd05959 9 VDLNLNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTADEqarggktlplksIADEAVAMGG--CEAVKSVIVYRRTGGKidwhAGRdLWMHE 189
Cdd:cd05959 84 VNTLLTPDDYAYYLEDSRARVVVVSGE------------LAPVLAAALTksEHTLVVLIVSGGAGPE----AGA-LLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 190 LADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHsTGGYLLWAAQTM-KWTFDWKPDDVFWCTADIGWVTGHTYITY 268
Cdd:cd05959 147 LVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVH-LHADIYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 269 GPLACGGTQVVFEGVPTwPDagRFWKMIGDHKVTVFYTAPTAIRSLIKAAEaddkvhPKSYDLSSLRIIGTVGEPINPEA 348
Cdd:cd05959 226 FPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFFGVPTLYAAMLAAPN------LPSRDLSSLRLCVSAGEALPAEV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 349 WMWYHKHVGQErcpIVDTWWQTETGGHMITPLPGATPtvPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMI 428
Cdd:cd05959 297 GERWKARFGLD---ILDGIGSTEMLHIFLSNRPGRVR--YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 429 rtIWGDPERFRKSYYpeelgGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRP 508
Cdd:cd05959 372 --YWNNRDKTRDTFQ-----GEWTRTGDKYVRDDD-GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVE 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 509 DDTTGEAVVAFVVLkrsRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05959 444 DEDGLTKPKAFVVL---RPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
29-577 |
4.06e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 245.87 E-value: 4.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 29 YNCLDRHVEAgNGQRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGA- 107
Cdd:PRK06187 9 GRILRHGARK-HPDKEAVYFDGR-----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 108 THSVvfggfsakslNERLVDvGAVALVTADEQAR----GGKTLPL-KSIADEavamggCEAVKSVIVYrrTGGKIDWHAG 182
Cdd:PRK06187 83 LHPI----------NIRLKP-EEIAYILNDAEDRvvlvDSEFVPLlAAILPQ------LPTVRTVIVE--GDGPAAPLAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 183 RDLWMHELADAESDTcaPEWVGA-EHPLF-ILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWtFDWKPDDVF--------- 251
Cdd:PRK06187 144 EVGEYEELLAAASDT--FDFPDIdENDAAaMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAW-LKLSRDDVYlvivpmfhv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 252 --WctadiGWvtghtyiTYGPLACGGTQVV---FegvptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhp 326
Cdd:PRK06187 221 haW-----GL-------PYLALMAGAKQVIprrF-------DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYF---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 327 ksYDLSSLR--IIGtvGEPInPEAWMwyhkHVGQER--CPIVDTWWQTETGGHM-ITPLPGATP---TVPGSCTLPLPGI 398
Cdd:PRK06187 278 --VDFSSLRlvIYG--GAAL-PPALL----REFKEKfgIDLVQGYGMTETSPVVsVLPPEDQLPgqwTKRRSAGRPLPGV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVPNGQG--GILVVKRPWpaMIRTIWGDPERFRKSYYpeelGGRLyLAGDGTVRDKDtGYFTIMGRIDDV 476
Cdd:PRK06187 349 EARIVDDDGDELPPDGGevGEIIVRGPW--LMQGYWNRPEATAETID----GGWL-HTGDVGYIDED-GYLYITDRIKDV 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 477 LNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKDI 556
Cdd:PRK06187 421 IISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK----PGATLD--AKELRAFLRGRLAKFKLPKRI 494
|
570 580
....*....|....*....|.
gi 1860891105 557 RFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK06187 495 AFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
43-572 |
1.16e-72 |
|
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: 239.43 E-value: 1.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVvfggfsaksLN 122
Cdd:cd17631 11 RTALVFGG-----RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---------LN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLvdvgavalvTADEQArggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmHELADAESDtcapew 202
Cdd:cd17631 77 FRL---------TPPEVA-----------------------------------------------YILADSGAK------ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 VGAEHPLFILYTSGSTGKPKGVQHSTGGyllWAAQTMKWTFDWK--PDDVFWCTADIGWVTGHTYITYGPLACGGTQVVF 280
Cdd:cd17631 95 VLFDDLALLMYTSGTTGRPKGAMLTHRN---LLWNAVNALAALDlgPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EGvptwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVGEPInPEAWmwyhKHVGQER 360
Cdd:cd17631 172 RK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFAT------TDLSSLRAVIYGGAPM-PERL----LRALQAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 -CPIVDTWWQTETGGhMITPL-PGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERF 438
Cdd:cd17631 237 gVKFVQGYGMTETSP-GVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVMAGYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 439 RKSyypeeLGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVA 518
Cdd:cd17631 314 AAA-----FRDGWFHTGDLGRLDED-GYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVA 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 519 FVVLKRSRPEGEEaaalakTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:cd17631 388 VVVPRPGAELDED------ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
51-577 |
2.48e-69 |
|
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: 233.51 E-value: 2.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 51 DDGTVTRVTYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGathSVVFGG---FSAKSLNERLV 126
Cdd:cd05928 35 GKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTG---LVFIPGtiqLTAKDILYRLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 127 DVGAVALVTADEQARGgktlpLKSIADEavamggCEAVKSVIVYRrtggkidwHAGRDLWMH--ELADAESDTCAPEWVG 204
Cdd:cd05928 112 ASKAKCIVTSDELAPE-----VDSVASE------CPSLKTKLLVS--------EKSRDGWLNfkELLNEASTEHHCVETG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEgVP 284
Cdd:cd05928 173 SQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHH-LP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 TWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaDDKvhpKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQErcpIV 364
Cdd:cd05928 252 RF-DPLVILKTLSSYPITTFCGAPTVYRMLVQ----QDL---SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 365 DTWWQTETGghMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVK----RPWpAMIRTIWGDPERFRK 440
Cdd:cd05928 321 EGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpiRPF-GLFSGYVDNPEKTAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 SyypeeLGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFV 520
Cdd:cd05928 398 T-----IRGDFYLTGDRGIMDED-GYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFV 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 521 VL----KRSRPEgeeaaALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:cd05928 472 VLapqfLSHDPE-----QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1-575 |
3.35e-69 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 236.18 E-value: 3.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 1 WHTPFTKVLdESDAPFYKWFDDGELNASYNCLDRHVE-AGNGQRVAVIFEAD--DGTVtRVTYAELLARVSRFANALKKR 77
Cdd:PTZ00237 35 WDKMYDKVY-SGDEIYPDWFKGGELNTCYNVLDIHVKnPLKRDQDALIYECPylKKTI-KLTYYQLYEKVCEFSRVLLNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 78 GIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVA 157
Cdd:PTZ00237 113 NISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 158 MGGCEAVKSVIVYRRtggkiDWHAGRDL--------------WMHELADAESDTCAP--EWVGAE--HPLFILYTSGSTG 219
Cdd:PTZ00237 193 LSTFKPSNVITLFRN-----DITSESDLkkietiptipntlsWYDEIKKIKENNQSPfyEYVPVEssHPLYILYTSGTTG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 220 KPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQVVFEGVPTWPDAGR--FWKMIG 297
Cdd:PTZ00237 268 NSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHIEddLWNTIE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 298 DHKVTVFYTAPTAIRSLIKAAEADDKVHPKsYDLSSLRIIGTVGEPIN---PEawmwYHKHVGQERCPIVdtWWQTETGg 374
Cdd:PTZ00237 347 KHKVTHTLTLPKTIRYLIKTDPEATIIRSK-YDLSNLKEIWCGGEVIEesiPE----YIENKLKIKSSRG--YGQTEIG- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 375 hmITPLPG-ATPTVP-GSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWP-AMIRTIWGDPERFRK--SYYPEelgg 449
Cdd:PTZ00237 419 --ITYLYCyGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFATTFYKNDEKFKQlfSKFPG---- 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 450 rLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEG 529
Cdd:PTZ00237 493 -YYNSGDLGFKDEN-GYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQ 570
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1860891105 530 E-EAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PTZ00237 571 SiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
38-576 |
1.05e-68 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 230.14 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 38 AGNGQRVAVIFeadDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVfggfs 117
Cdd:cd05936 10 RRFPDKTALIF---MGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV--VV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 118 akSLNerlvdvgavALVTADEqarggktlpLKSIADEAVAmggceavKSVIVyrrtggkidwhagrdlwMHELADA-ESD 196
Cdd:cd05936 78 --PLN---------PLYTPRE---------LEHILNDSGA-------KALIV-----------------AVSFTDLlAAG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 197 TCAPEWVG--AEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWK-PDDVFWCTADIGWVTGHTYITYGPLAC 273
Cdd:cd05936 114 APLGERVAltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLeGDDVVLAALPLFHVFGLTVALLLPLAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 274 GGTQVVfegVPTwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEaddkvhPKSYDLSSLRIIGTVGEPINPEAWMWYH 353
Cdd:cd05936 194 GATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE------FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 KHVGqerCPIVDTWWQTETG--GHmITPLPGatPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTI 431
Cdd:cd05936 264 ELTG---VPIVEGYGLTETSpvVA-VNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 WGDPE----RFRksyypeelGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGR 507
Cdd:cd05936 336 WNRPEetaeAFV--------DGWLR-TGDIGYMDED-GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 508 PDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05936 406 PDPYSGEAVKAFVVLK------EGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
26-577 |
1.34e-66 |
|
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: 226.61 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 26 NASYNCLDRHVEAgNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARI 105
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 106 GATHSVVFGGFSAKSLNERLVDVGAVALVTADEQArggktlpLKSIADEAVAMGGCEAVKSVIVYRRTGGKIDWHAgrdl 185
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN-------IPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRK---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 186 wmhELADAESDTCAPE---WVGAEHPLFILYTSGSTGKPKGVQHSTGgYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTG 262
Cdd:cd05970 165 ---LIKNASPDFERPTansYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 263 HTYITYGPLACGGTQVVFegvptwpDAGRF-----WKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpksYDLSSLRII 337
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVY-------DYDKFdpkalLEKLSKYGVTTFCAPPTIYRFLIREDLSR-------YDLSSLRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 338 GTVGEPINPEAWMWYHKHVGQErcpIVDTWWQTETGGHMITpLPGATPTvPGSCTLPLPGIMAAVVDETGQDVPNGQGGI 417
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEPK-PGSMGKPAPGYEIDLIDREGRSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 418 LVvkrpwpamIRTIWGDPERFRKSYY------PEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIES 491
Cdd:cd05970 382 IV--------IRTSKGKPVGLFGGYYkdaektAEVWHDGYYHTGDAAWMDED-GYLWFVGRTDDLIKSSGYRIGPFEVES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 492 ALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIM 571
Cdd:cd05970 453 ALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE---LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIR 529
|
....*.
gi 1860891105 572 RRLLRS 577
Cdd:cd05970 530 RVEIRE 535
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
58-576 |
3.48e-66 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 222.72 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsvvfggfsAKSLNERLVDvGAVALVTAD 137
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI---------AVVINPLLHP-DDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQARggktlpLKSIADEAVAmggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvgaehplFILYTSGS 217
Cdd:cd05919 81 CEAR------LVVTSADDIA----------------------------------------------------YLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADI--GWVTGHTYItyGPLACGGTQVVFegvPTWPDAGRFWKM 295
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLN---PGWPTAERVLAT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 296 IGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIVDTWWQTETGGH 375
Cdd:cd05919 178 LARFRPTVLYGVPTFYANLLDSCAGS------PDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 376 MITPLPGATPtvPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYypeeLGGRLYlAG 455
Cdd:cd05919 249 FLSNRPGAWR--LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP--SAAVGYWNNPEKSRATF----NGGWYR-TG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 456 DGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrPEGEEAAAL 535
Cdd:cd05919 320 DKFCRDAD-GWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLK---SPAAPQESL 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1860891105 536 AKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05919 396 ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-598 |
4.44e-65 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 225.14 E-value: 4.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 3 TPFTKVLDESDAPFYKWFDDGELNASYNCLdRHVEAGNgqrvAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKG 82
Cdd:TIGR01217 65 TPCARVVDDRTMPGAQWFPGARLNYAENLL-RAAGTEP----ALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 83 DRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMGGCE 162
Cdd:TIGR01217 140 DRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 163 AVKSVIVYRRTGGKID-WHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKW 241
Cdd:TIGR01217 220 RAVVHIPYLGPRETEApKIDGALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 242 TFDWKPDDVFWCTADIGWVTGHTYITygPLACGGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAead 321
Cdd:TIGR01217 300 HCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAG--- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 322 dkVHP-KSYDLSSLRIIGTVGEPINPEAWMWYHkhvgqeRCPIVDTWWQTETGG-HMITPLPGATPTVP---GSCTLPLP 396
Cdd:TIGR01217 375 --VHPaRTHDLSALQCVASTGSPLPPDGFRWVY------DEIKADVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 397 GIMAAVVDETGQDVpNGQGGILVVKRPWPAMIRTIWGDPE--RFRKSYYPEELGgrLYLAGDgTVRDKDTGYFTIMGRID 474
Cdd:TIGR01217 447 GTAVQSWDPEGKPV-TGEVGELVCTNPMPSMPIRFWNDPDgsKYRDAYFDTYPG--VWRHGD-WITLTPRGGIVIHGRSD 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 475 DVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRpegEEAAALAKTLRDWVGKQIGPIAKPK 554
Cdd:TIGR01217 523 STLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGA---TLDDALLDRIKRTIRAGLSPRHVPD 599
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1860891105 555 DIRFGDNLPKTRSGKIMRRLLRSLAKGEAItQDTSTLENPAILD 598
Cdd:TIGR01217 600 EIIEVPGIPHTLTGKRVEVAVKRVLQGTPV-DNPGAIDNPELLD 642
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
51-571 |
2.07e-63 |
|
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: 216.70 E-value: 2.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 51 DDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGA 130
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 131 -VALVTADEQARggktlpLKSIADEavamggCEAVKSVIVyrrTGGKIDWHAGR-DLWMHELADAESDTCAPEWVGAEHP 208
Cdd:cd05911 84 kVIFTDPDGLEK------VKEAAKE------LGPKDKIIV---LDDKPDGVLSIeDLLSPTLGEEDEDLPPPLKDGKDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 209 LFILYTSGSTGKPKGVQHSTGGYLLWAAQT-MKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLaCGGTQVVFEGvptwP 287
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNLIANLSQVqTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPK----F 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPINPEAwmwyhkhvgQERCP----- 362
Cdd:cd05911 224 DSELFLDLIEKYKITFLYLVPPIAAALAKSPLLD------KYDLSSLRVILSGGAPLSKEL---------QELLAkrfpn 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 363 --IVDTWWQTETGGhMITPLPGaTPTVPGSCTLPLPGIMAAVVDETGQDV--PNGQGGILV---------VKRPwPAMIR 429
Cdd:cd05911 289 atIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSlgPNEPGEICVrgpqvmkgyYNNP-EATKE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 430 TIwgDPERFRKSyypeelggrlylaGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPD 509
Cdd:cd05911 366 TF--DEDGWLHT-------------GDIGYFDED-GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPD 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860891105 510 DTTGEAVVAFVVLKrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKD-IRFGDNLPKTRSGKIM 571
Cdd:cd05911 430 EVSGELPRAYVVRK----PGEKLT--EKEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
55-576 |
6.18e-63 |
|
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: 213.31 E-value: 6.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 55 VTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAthsvvfggfSAKSLNERLVdvgavalv 134
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGA---------VLVPINTALR-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 135 tADEqarggktlpLKSIADEAvamgGCEAVksvIVyrrtggkidwhagrdlwmheladaesDTCApewvgaehplfILYT 214
Cdd:cd05934 64 -GDE---------LAYIIDHS----GAQLV---VV--------------------------DPAS-----------ILYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 215 SGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfegVPTWpDAGRFWK 294
Cdd:cd05934 90 SGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRFWS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 295 MIGDHKVTVFYTAPTAIRSLIKAAE-ADDKVHPksydlssLRIIGtvGEPINPEAWMWYHKHVGqerCPIVDTWWQTETG 373
Cdd:cd05934 165 DVRRYGATVTNYLGAMLSYLLAQPPsPDDRAHR-------LRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETI 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 374 GHMITPLPGatPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVK--RPWpAMIRTIWGDPERFRKSyypeeLGGRL 451
Cdd:cd05934 233 VGVIGPRDE--PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglRGW-GFFKGYYNMPEATAEA-----MRNGW 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 YLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEE 531
Cdd:cd05934 305 FHTGDLGYRDAD-GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1860891105 532 AaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05934 384 E------LFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
41-576 |
2.16e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 211.69 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVfggfsakS 120
Cdd:PRK07656 19 GDKEAYVFGD-----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV--VV-------P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNER---------LVDVGAVALVTADEqarggkTLPLksiaDEAvAMGGCEAVKSVIVYRrTGGKIDWHAGRDLWMHELA 191
Cdd:PRK07656 85 LNTRytadeaayiLARGDAKALFVLGL------FLGV----DYS-ATTRLPALEHVVICE-TEEDDPHTEKMKTFTDFLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDTCAPEwVGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDD----------VFWCTAdiGWVT 261
Cdd:PRK07656 153 AGDPAERAPE-VDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDrylaanpffhVFGYKA--GVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 262 ghtyitygPLACGGT---QVVFegvptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIG 338
Cdd:PRK07656 229 --------PLMRGATilpLPVF-------DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA------EDLSSLRLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 339 TVGEPINPEAWMWYHKHVGqerCPIVDTWWQ-TETGGHM-ITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGG 416
Cdd:PRK07656 288 TGAASMPVALLERFESELG---VDIVLTGYGlSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 417 ILVVKRPwPAMirtiwgdperfrKSYY--PEE------LGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTME 488
Cdd:PRK07656 365 ELLVRGP-NVM------------KGYYddPEAtaaaidADGWLH-TGDLGRLDEE-GYLYIVDRKKDMFIVGGFNVYPAE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 489 IESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSrpegeeAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSG 568
Cdd:PRK07656 430 VEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------AELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATG 503
|
....*...
gi 1860891105 569 KIMRRLLR 576
Cdd:PRK07656 504 KVLKRALR 511
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
43-583 |
2.15e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 206.71 E-value: 2.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:PRK08316 27 KTALVFGD-----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTADEqarggktlpLKSIADEAVAMGGCEAVKSVIVYRRTGgkidwHAGRDLWMHELADAESDTCAPEW 202
Cdd:PRK08316 102 YILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGRE-----APGGWLDFADWAEAGSVAEPDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 VGAEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDV-------FWCTADigwvtgHTYItyGP-LACG 274
Cdd:PRK08316 168 LADDDLAQILYTSGTESLPKGAMLTHRA-LIAEYVSCIVAGDMSADDIplhalplYHCAQL------DVFL--GPyLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVFEGvptwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIiGTVGEPINPEAWMwyhk 354
Cdd:PRK08316 239 ATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPDFD------TRDLSSLRK-GYYGASIMPVEVL---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 355 HVGQERCPIVDTW---WQTEtgghmITPL-----PGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwPA 426
Cdd:PRK08316 304 KELRERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP-QL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 427 MIrTIWGDPER----FRksyypeelGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEA 502
Cdd:PRK08316 378 ML-GYWDDPEKtaeaFR--------GGWFH-SGDLGVMDEE-GYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 503 AVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGE 582
Cdd:PRK08316 447 AVIGLPDPKWIEAVTAVVVPK------AGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
.
gi 1860891105 583 A 583
Cdd:PRK08316 521 F 521
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
52-576 |
4.52e-59 |
|
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: 205.24 E-value: 4.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 52 DGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAV 131
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 132 ALVTADEQ----ARGGKTLPLkSIADEAVAMGGCEAVKSVivyrrtggkidwhagrdlwmHELADAESDTCAPEWVGAEH 207
Cdd:cd05926 89 LVLTPKGElgpaSRAASKLGL-AILELALDVGVLIRAPSA--------------------ESLSNLLADKKNAKSEGVPL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 P---LFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfegvP 284
Cdd:cd05926 148 PddlALILHTSGTTGRPKGVP-LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL----P 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 TWPDAGRFWKMIGDHKVTvFYTA-PTAIRSLIKAAEADdKVHPKSydlsSLRIIGTVGEPINPEawmwyHKHVGQER--C 361
Cdd:cd05926 223 PRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNRPEPN-PESPPP----KLRFIRSCSASLPPA-----VLEALEATfgA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 362 PIVDTWWQTETGgHMIT--PLPgATPTVPGSCTLPLpGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFR 439
Cdd:cd05926 292 PVLEAYGMTEAA-HQMTsnPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNPEANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 440 KSYYPEelggRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAF 519
Cdd:cd05926 367 EAAFKD----GWFRTGDLGYLDAD-GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 520 VVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05926 442 VVLR------EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
57-576 |
5.07e-59 |
|
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: 203.48 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALK-KRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsvvfggfsakslnerlvdvgAVAlvt 135
Cdd:cd05958 10 EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI---------------------AVA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 adeqarggkTLPLKSIADEAVAMGGCEAVKSVIVYRRTggkidwhagrdlwmheladAESDTCapewvgaehplFILYTS 215
Cdd:cd05958 66 ---------TMPLLRPKELAYILDKARITVALCAHALT-------------------ASDDIC-----------ILAFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 216 GSTGKPKGVQHSTGGYLL----WAAQTMKWTfdwkPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGvpTWPDagR 291
Cdd:cd05958 107 GTTGAPKATMHFHRDPLAsadrYAVNVLRLR----EDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE--ATPD--L 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 292 FWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIVDTWWQTE 371
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP------DLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGHMITPLPGATPtvPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpamirTI-WGDPERFRKSYYPeelGGR 450
Cdd:cd05958 250 MFHIFISARPGDAR--PGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGcRYLADKRQRTYVQ---GGW 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 451 LYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGE 530
Cdd:cd05958 319 NI-TGDTYSRDPD-GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVL---RPGVI 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1860891105 531 EAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05958 394 PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
42-575 |
2.79e-58 |
|
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: 201.60 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHsvvfggfsaksl 121
Cdd:cd05930 2 DAVAVVDGD-----QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAY------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 nerlvdvgaVALVTADEQARggktlpLKSIADEAvamggceAVKSVIVyrrtggkidwhagrdlwmheladaesdtcape 201
Cdd:cd05930 65 ---------VPLDPSYPAER------LAYILEDS-------GAKLVLT-------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wvGAEHPLFILYTSGSTGKPKGVQHSTGG---YLLWAAQTmkwtFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQV 278
Cdd:cd05930 91 --DPDDLAYVIYTSGSTGKPKGVMVEHRGlvnLLLWMQEA----YPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 279 VfegVP--TWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksydLSSLRIIGTVGEPINPEAW-MWYHKH 355
Cdd:cd05930 164 V---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA--------LPSLRLVLVGGEALPPDLVrRWRELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 356 vgqERCPIVDTWWQTETGG----HMITPLPGATPTVP-GsctLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRT 430
Cdd:cd05930 233 ---PGARLVNLYGPTEATVdatyYRVPPDDEEDGRVPiG---RPIPNTRVYVLDENLRPVPPGVPGELYIGGA--GLARG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 431 IWGDPE----RFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHR--LGtmEIESALVSHELVAEAAV 504
Cdd:cd05930 305 YLNRPEltaeRFVPN--PFGPGERMYRTGD-LVRWLPDGNLEFLGRIDDQVKIRGYRieLG--EIEAALLAHPGVREAAV 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 505 VGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05930 380 VAREDGDGEKRLVAYVVPD------EGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
43-575 |
4.36e-54 |
|
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: 192.06 E-value: 4.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIfeaDDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:cd05904 21 RPALI---DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTAdeqargGKTLP-LKSIADEAVAMGGCEAVKsvivyrrtggkidWHAGRDLwmheLADAESDTCAPE 201
Cdd:cd05904 98 KQVKDSGAKLAFTT------AELAEkLASLALPVVLLDSAEFDS-------------LSFSDLL----FEADEAEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wVGAEHPLFILYTSGSTGKPKGVQHSTGGYL-LWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVF 280
Cdd:cd05904 155 -IKQDDVAALLYSSGTTGRSKGVMLTHRNLIaMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVGEPINPEawmwyHKHVGQER 360
Cdd:cd05904 234 PRF----DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDK------YDLSSLRQIMSGAAPLGKE-----LIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 CPIVDT---WWQTETGG--HMiTPLPGATPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRpwPAMIRTIWGD 434
Cdd:cd05904 299 FPNVDLgqgYGMTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG--PSIMKGYLNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PERFRKSYYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGE 514
Cdd:cd05904 376 PEATAATIDKE---GWLH-TGDLCYIDED-GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGE 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 515 AVVAFVVLKRSRPEGEeaaalaKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05904 451 VPMAFVVRKPGSSLTE------DEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
42-575 |
5.78e-54 |
|
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: 190.21 E-value: 5.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:cd17643 2 EAVAVVDEDR-----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTAdeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcape 201
Cdd:cd17643 77 AFILADSGPSLLLTD----------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wvgAEHPLFILYTSGSTGKPKGVQ--HSTGGYLLWAAQtmkWTFDWKPDDVfwctadigWVTGHTYI-------TYGPLA 272
Cdd:cd17643 92 ---PDDLAYVIYTSGSTGRPKGVVvsHANVLALFAATQ---RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 273 CGGTQVVfegVPTW----PDAgrFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINPeA 348
Cdd:cd17643 158 HGGRLVV---VPYEvarsPED--FARLLRDEGVTVLNQTPSAFYQLVEAADRDGR------DPLALRYVIFGGEALEA-A 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 349 WM--WYhKHVGQERCPIVDTWWQTETGGHM----ITP--LPGATPTVPGSctlPLPGIMAAVVDETGQDVPNGQGGILVV 420
Cdd:cd17643 226 MLrpWA-GRFGLDRPQLVNMYGITETTVHVtfrpLDAadLPAAAASPIGR---PLPGLRVYVLDADGRPVPPGVVGELYV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 421 KRPWPAmiRTIWGDP----ERFRKSYYPEElGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSH 496
Cdd:cd17643 302 SGAGVA--RGYLGRPeltaERFVANPFGGP-GSRMYRTGD-LARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 497 ELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17643 378 PSVRDAAVIVREDEPGDTRLVAYVVAD------DGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
57-575 |
2.83e-53 |
|
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: 187.69 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTA 136
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEQarggktlplksiadEAVAMggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvgaehplfILYTSG 216
Cdd:cd05935 81 SEL--------------DDLAL----------------------------------------------------IPYTSG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGGYLLWAAQTMKWtFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfegVPTWpDAGRFWKMI 296
Cdd:cd05935 95 TTGLPKGCMHTHFSAAANALQSAVW-TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL---MARW-DRETALELI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 297 GDHKVTVFYTAPTAIRSLIKAAEAddkvhpKSYDLSSLRIIGTVGEPInPEAwmwyhkhVGQ---ERCPI--VDTWWQTE 371
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLLATPEF------KTRDLSSLKVLTGGGAPM-PPA-------VAEkllKLTGLrfVEGYGLTE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TgghmITPLPGATPTVPGSCTLPLP--GIMAAVVD-ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYYpeELG 448
Cdd:cd05935 236 T----MSQTHTNPPLRPKLQCLGIP*fGVDARVIDiETGRELPPNEVGEIVVRGP--QIFKGYWNRPEETEESFI--EIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 449 GRLYL-AGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrp 527
Cdd:cd05935 308 GRRFFrTGDLGYMDEE-GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR---- 382
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1860891105 528 EGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05935 383 PEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
56-583 |
5.88e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 187.09 E-value: 5.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALK-KRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALV 134
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 135 TADEqarggktlplksIADEAVAMGGCEAVKSVIVYRRTGGkidwhagrdlwmhelADAESDTCAPEWVGAEHPLFIL-- 212
Cdd:PRK08314 114 VGSE------------LAPKVAPAVGNLRLRHVIVAQYSDY---------------LPAEPEIAVPAWLRAEPPLQALap 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 213 ------------------------------YTSGSTGKPKG-------VQHSTGGYLLWAAQTmkwtfdwkPDDVFWCTA 255
Cdd:PRK08314 167 ggvvawkealaaglappphtagpddlavlpYTSGTTGVPKGcmhthrtVMANAVGSVLWSNST--------PESVVLAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 256 DIGWVTGHTYITYGPLACGGTQVVfegVPTWpD---AGRfwkMIGDHKVTVFYTAPTAIRSLIkaaeADDKVHpkSYDLS 332
Cdd:PRK08314 239 PLFHVTGMVHSMNAPIYAGATVVL---MPRW-DreaAAR---LIERYRVTHWTNIPTMVVDFL----ASPGLA--ERDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 333 SLRIIGTVGEPInPEAwmwyhkhVGQ---ERC--PIVDTWWQTETGGHMITPLPGAtptvPGSCTL--PLPGIMAAVVD- 404
Cdd:PRK08314 306 SLRYIGGGGAAM-PEA-------VAErlkELTglDYVEGYGLTETMAQTHSNPPDR----PKLQCLgiPTFGVDARVIDp 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 405 ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYYpeELGGRLYL-AGDGTVRDKDtGYFTIMGRIDDVLNVSGHR 483
Cdd:PRK08314 374 ETLEELPPGEVGEIVVHGP--QVFKGYWNRPEATAEAFI--EIDGKRFFrTGDLGRMDEE-GYFFITDRLKRMINASGFK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 484 LGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLK---RSRPEGEEaaalaktLRDWVGKQIGPIAKPKDIRFGD 560
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRpeaRGKTTEEE-------IIAWAREHMAAYKYPRIVEFVD 521
|
570 580
....*....|....*....|...
gi 1860891105 561 NLPKTRSGKIMRRLLRSLAKGEA 583
Cdd:PRK08314 522 SLPKSGSGKILWRQLQEQEKARA 544
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
58-579 |
3.18e-49 |
|
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: 176.99 E-value: 3.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAthsvvfggfsakslnerlVDVGAVALVTAD 137
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA------------------VVIPATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQ----ARGGKTLplkSIADEAVAmggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvgAEHPLFILY 213
Cdd:cd05974 63 DLrdrvDRGGAVY---AAVDENTH-----------------------------------------------ADDPMLLYF 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 214 TSGSTGKPKGVQHSTGGYLLWAAQTMKWtFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEgvPTWPDAGRFW 293
Cdd:cd05974 93 TSGTTSKPKLVEHTHRSYPVGHLSTMYW-IGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFN--YARFDAKRVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 294 KMIGDHKVTVFYTAPTAIRSLIKAAEADDKVhpksydlsSLRIIGTVGEPINPEAWMWYHKHVGQErcpIVDTWWQTETG 373
Cdd:cd05974 170 AALVRYGVTTLCAPPTVWRMLIQQDLASFDV--------KLREVVGAGEPLNPEVIEQVRRAWGLT---IRDGYGQTETT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 374 GhMITPLPGaTPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGI-LVVKRPWPAMiRTIWGDPERFRksyypEELGGRLY 452
Cdd:cd05974 239 A-LVGNSPG-QPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALdLGDTRPVGLM-KGYAGDPDKTA-----HAMRGGYY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 453 LAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEA 532
Cdd:cd05974 311 RTGDIAMRDED-GYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVL---RAGYEPS 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1860891105 533 AALAKTLRDWVGKQIGPIAKPKDIRFGDnLPKTRSGKIMRRLLRSLA 579
Cdd:cd05974 387 PETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
2-577 |
3.41e-48 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 179.50 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 2 HTPFTKVLDESDA--PFYKWFDDGELNASYNCLDRHVEAgNGQRVAVIF--EADDGT-VTRVTYAELLARVSRFANALKK 76
Cdd:PLN03052 149 SVPPRCILDTSDEsnPGGQWLPGAVLNVAECCLTPKPSK-TDDSIAIIWrdEGSDDLpVNRMTLSELRSQVSRVANALDA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 77 RGIAKGDRVVIYMPMSIEGIVAMQACarIGATHSVVF--GGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADE 154
Cdd:PLN03052 228 LGFEKGDAIAIDMPMNVHAVIIYLAI--ILAGCVVVSiaDSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 155 AVAmggceavKSVIVYRRTGGKIDWH-AGRDL-WMHELADAESDTCAPEWVGAEHPL----FILYTSGSTGKPKGV---Q 225
Cdd:PLN03052 306 AKA-------PKAIVLPADGKSVRVKlREGDMsWDDFLARANGLRRPDEYKAVEQPVeaftNILFSSGTTGEPKAIpwtQ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 226 HSTggyLLWAAQTmkWT-FDWKPDDVF-WCTaDIGWVTGHtYITYGPLACGGTQVVFEGVPTWPDAGRFwkmIGDHKVTV 303
Cdd:PLN03052 379 LTP---LRAAADA--WAhLDIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTM 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 304 FYTAPtairSLIKAAEADDKVHpkSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQErcPIVDTWWQTETGGHMITplpGA 383
Cdd:PLN03052 449 LGTVP----SIVKTWKNTNCMA--GLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTELGGGFVT---GS 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 384 --TPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVkrpwpAMIRTIWGDPERF-----RKSYY---PEELGGRLYL 453
Cdd:PLN03052 518 llQPQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGEL-----ALFPLMFGASSTLlnadhYKVYFkgmPVFNGKILRR 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 454 AGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESAL-VSHELVAEAAVVGRPDDTTG-EAVVAFVVLKRSRPEGEE 531
Cdd:PLN03052 593 HGDIFERTSG-GYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPD 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1860891105 532 AAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:PLN03052 672 LNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
32-541 |
7.03e-48 |
|
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: 180.82 E-value: 7.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHsv 111
Cdd:COG1020 482 FEAQAAR-TPDAVAVVFGD-----QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY-- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 vfggfsakslnerlvdvgaVALVTADEQARggktlpLKSIADEAvamggceAVKSVIVYRRTGGKIDWHAGRDLWMHELA 191
Cdd:COG1020 554 -------------------VPLDPAYPAER------LAYMLEDA-------GARLVLTQSALAARLPELGVPVLALDALA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDTCAPEW-VGAEHPLFILYTSGSTGKPKGVQHSTGG---YLLWAAQTmkwtFDWKPDDVF-WCTA---DIGwvtgh 263
Cdd:COG1020 602 LAAEPATNPPVpVTPDDLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRR----YGLGPGDRVlQFASlsfDAS----- 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 264 TYITYGPLACGGTQVVFEgvPTW-PDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpksydLSSLRIIGTVGE 342
Cdd:COG1020 673 VWEIFGALLSGATLVLAP--PEArRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA---------LPSLRLVLVGGE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 343 PINPEAW-MWYHKHVGqerCPIVDTWWQTETG----GHMITPLPGATPTVP-GSctlPLPGIMAAVVDETGQDVPNGQ-- 414
Cdd:COG1020 742 ALPPELVrRWRARLPG---ARLVNLYGPTETTvdstYYEVTPPDADGGSVPiGR---PIANTRVYVLDAHLQPVPVGVpg 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 415 ----GGILVvkrpwpAmiRTIWGDP----ERFRKSYYPEElGGRLYLAGD-------GTVRdkdtgyftIMGRIDDVLNV 479
Cdd:COG1020 816 elyiGGAGL------A--RGYLNRPeltaERFVADPFGFP-GARLYRTGDlarwlpdGNLE--------FLGRADDQVKI 878
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 480 SGHR--LGtmEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAALAKTLRD 541
Cdd:COG1020 879 RGFRieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLL 940
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
42-575 |
8.24e-48 |
|
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: 173.20 E-value: 8.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVifeadDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:cd05945 6 DRPAV-----VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 nERLVDVGAVALVTADEqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmHELAdaesdtcape 201
Cdd:cd05945 81 -REILDAAKPALLIADG-------------------------------------------------DDNA---------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wvgaehplFILYTSGSTGKPKGVQHSTGG---YLLWAAQTmkwtFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQV 278
Cdd:cd05945 101 --------YIIFTSGSTGRPKGVQISHDNlvsFTNWMLSD----FPLGPGDVFLNQAPFSFDLSVMDL-YPALASGATLV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 279 VfegVP----TWPdaGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydlsSLRIIGTVGEPI-NPEAWMWyh 353
Cdd:cd05945 168 P---VPrdatADP--KQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLP------SLRHFLFCGEVLpHKTARAL-- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 khvgQER---CPIVDTWWQTET----GGHMITPLPGAT-PTVP-GSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPw 424
Cdd:cd05945 235 ----QQRfpdARIYNTYGPTEAtvavTYIEVTPEVLDGyDRLPiGY---AKPGAKLVILDEDGRPVPPGEKGELVISGP- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 pAMIRTIWGDPERFRKSYYPEElGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd05945 307 -SVSKGYLNNPEKTAAAFFPDE-GQRAYRTGD-LVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 505 VGRPDDTTGEAVVAFVVlkrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05945 384 VPKYKGEKVTELIAFVV-----PKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
32-580 |
4.81e-47 |
|
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: 173.02 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIfeadDGTvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsV 111
Cdd:COG1021 31 LRRRAER-HPDRIAVV----DGE-RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VF----------GGFSAKSlnerlvdvGAVALVTADeQARGGKTLPLksiADEAVAmgGCEAVKSVIVYRRTGGKIDWha 181
Cdd:COG1021 103 VFalpahrraeiSHFAEQS--------EAVAYIIPD-RHRGFDYRAL---ARELQA--EVPSLRHVLVVGDAGEFTSL-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 182 grDLWMHELADAESDTCAPEWVGaehplFILYTSGSTGKPKGVQHSTGGYLLWA---AQTMKWTfdwkPDDVFWCTADIg 258
Cdd:COG1021 167 --DALLAAPADLSEPRPDPDDVA-----FFQLSGGTTGLPKLIPRTHDDYLYSVrasAEICGLD----ADTVYLAALPA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 259 wvtGHTYitygPLAC---------GGTqVVFEGVptwPDAGRFWKMIGDHKVTVfyTA--PTAIRSLIKAAEADDkvhpk 327
Cdd:COG1021 235 ---AHNF----PLSSpgvlgvlyaGGT-VVLAPD---PSPDTAFPLIERERVTV--TAlvPPLALLWLDAAERSR----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 328 sYDLSSLRIIGTVGEPINPEAwmwyhkhvgQERcpivdtwwqtetgghmITPLPGATP---------------------T 386
Cdd:COG1021 297 -YDLSSLRVLQVGGAKLSPEL---------ARR----------------VRPALGCTLqqvfgmaeglvnytrlddpeeV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 387 VPGSCTLPL-PGIMAAVVDETGQDVPNGQGGILVVKRPWpaMIRTIWGDPERFRKSYYPEelGgrLYLAGDGTVRDKDtG 465
Cdd:COG1021 351 ILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPY--TIRGYYRAPEHNARAFTPD--G--FYRTGDLVRRTPD-G 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 466 YFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPegeEAAALAKTLRDWvGk 545
Cdd:COG1021 424 YLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPL---TLAELRRFLRER-G- 498
|
570 580 590
....*....|....*....|....*....|....*...
gi 1860891105 546 qigpIAK---PKDIRFGDNLPKTRSGKIMRRLLRSLAK 580
Cdd:COG1021 499 ----LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
59-504 |
1.14e-46 |
|
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: 169.37 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EqarggktlplksIADEAVAMGGCEavksvivyrrtggkidwHAGRDLWMHELADAESDTCAPEWVGAEHPLFILYTSGS 217
Cdd:TIGR01733 81 A------------LASRLAGLVLPV-----------------ILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGG---YLLWAAQtmkwTFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQVVFEGVPTWPDAGRFWK 294
Cdd:TIGR01733 132 TGRPKGVVVTHRSlvnLLAWLAR----RYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEERDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 295 MIGDHKVTVFYTAPTAIRSLIKAAEAddkvhpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQERcpIVDTWWQTETGG 374
Cdd:TIGR01733 207 LIAEHPVTVLNLTPSLLALLAAALPP---------ALASLRLVILGGEALTPALVDRWRARGPGAR--LINLYGPTETTV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 375 H-MITPLPGATPTVPGSCTL--PLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAmiRTIWGDP----ERFRKSYYPEEL 447
Cdd:TIGR01733 276 WsTATLVDPDDAPRESPVPIgrPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVA--RGYLNRPeltaERFVPDPFAGGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 448 GGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHR--LGtmEIESALVSHELVAEAAV 504
Cdd:TIGR01733 354 GARLYRTGDLVRYLPD-GNLEFLGRIDDQVKIRGYRieLG--EIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
41-575 |
2.60e-46 |
|
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: 170.07 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKS 120
Cdd:cd12117 11 PDAVAVVYGD-----RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMGGCEAVKSVivyrrtggkidwhagrdlwmheladaesdtcap 200
Cdd:cd12117 86 LAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVP--------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 ewVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDwkPDDVFWCTADIGWvTGHTYITYGPLACGGTQVVF 280
Cdd:cd12117 133 --VSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLG--PDDRVLQTSPLAF-DASTFEIWGALLNGARLVLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 E-GVPTwpDAGRFWKMIGDHKVTV-FYTAPTaIRSLikaaeADDkvHPKSydLSSLRIIGTVGEPINPeawmwyhKHVGQ 358
Cdd:cd12117 208 PkGTLL--DPDALGALIAEEGVTVlWLTAAL-FNQL-----ADE--DPEC--FAGLRELLTGGEVVSP-------PHVRR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 359 --ERCP---IVDTWWQTETGG----HMITPLPGATPTVP-GSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAmi 428
Cdd:cd12117 269 vlAACPglrLVNGYGPTENTTfttsHVVTELDEVAGSIPiGR---PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLA-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 429 RTIWGDP----ERFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd12117 344 LGYLNRPaltaERFVAD--PFGPGERLYRTGD-LARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 505 VGRPDDTTGEAVVAFVVLKRSRPEGEeaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd12117 421 VVREDAGGDKRLVAYVVAEGALDAAE--------LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
42-575 |
1.45e-45 |
|
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: 167.11 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHsvvfggfsaksl 121
Cdd:cd12115 14 DAIALVCGDE-----SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAY------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 nerlvdvgaVALVTADEQARggktlpLKSIADEAvamgGCEAVksvivyrrtggkidwhagrdlwmheladaesdtcape 201
Cdd:cd12115 77 ---------VPLDPAYPPER------LRFILEDA----QARLV------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAEHPLFILYTSGSTGKPKGV---QHSTGGYLLWAAQTmkwtfdwkpddvfwCTAD-IGWVTGHTYITY--------G 269
Cdd:cd12115 101 LTDPDDLAYVIYTSGSTGRPKGVaieHRNAAAFLQWAAAA--------------FSAEeLAGVLASTSICFdlsvfelfG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 270 PLACGGTQVVFEGVPTWPDAGRfwkmigDHKVTVFYTAPTAIRSLIKAaeadDKVHPksydlsSLRIIGTVGEPINPEAW 349
Cdd:cd12115 167 PLATGGKVVLADNVLALPDLPA------AAEVTLINTVPSAAAELLRH----DALPA------SVRVVNLAGEPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 350 MWYHKHVGQERC-----PIVDTWWQTetgGHMITPLPGATPTVpGSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPW 424
Cdd:cd12115 231 QRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEVSI-GR---PLANTQAYVLDRALQPVPLGVPGELYIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 PAmiRTIWGDP----ERFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVA 500
Cdd:cd12115 304 VA--RGYLGRPgltaERFLPD--PFGPGARLYRTGD-LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 501 EAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd12115 379 EAVVVAIGDAAGERRLVAYIVAEPGAAGLVED------LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
34-576 |
1.99e-44 |
|
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: 164.82 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 34 RHVEAgNGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVF 113
Cdd:cd17651 3 RQAAR-TPDAPALVAEG-----RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 GGFSAKSLNERLVDVGAVALVTADEQArggktlPLKSIADEAVAmggceavksvivyrrtggkidwhagRDLWMHELADA 193
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPALA------GELAVELVAVT-------------------------LLDQPGAAAGA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 194 ESDTCAPewVGAEHPLFILYTSGSTGKPKGV--QHST-GGYLLW------------AAQTMKWTFDWKPDDVFwctadig 258
Cdd:cd17651 126 DAEPDPA--LDADDLAYVIYTSGSTGRPKGVvmPHRSlANLVAWqarasslgpgarTLQFAGLGFDVSVQEIF------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 259 wvtghtyityGPLACGGTQVVFEgvPTW-PDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydlsSLRII 337
Cdd:cd17651 197 ----------STLCAGATLVLPP--EEVrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLA------ALRYL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 338 GTVGEP-INPEAWMWYHKHVGQERcpIVDTWWQTET---GGHMITPLPGATPTVPgSCTLPLPGIMAAVVDETGQDVPNG 413
Cdd:cd17651 259 LTGGEQlVLTEDLREFCAGLPGLR--LHNHYGPTEThvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVLDAALRPVPPG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 414 QGGILVVKRPWPAmiRTIWGDP----ERFrkSYYPEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEI 489
Cdd:cd17651 336 VPGELYIGGAGLA--RGYLNRPeltaERF--VPDPFVPGARMYRTGDLARWLPD-GELEFLGRADDQVKIRGFRIELGEI 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 490 ESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsrpeGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGK 569
Cdd:cd17651 411 EAALARHPGVREAVVLAREDRPGEKRLVAYVVG------DPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGK 484
|
....*..
gi 1860891105 570 IMRRLLR 576
Cdd:cd17651 485 LDRRALP 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
42-577 |
3.40e-44 |
|
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: 163.23 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIfeaDDGTvtRVTYAELLARVSRFANAL-KKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsvvfggfsaks 120
Cdd:cd05941 1 DRIAIV---DDGD--SITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 lnerlvdvgAVALVTADEQArggktlplksiadeavamggcEAVksvivyrrtggkidwhagrdlwmHELADAESDtcap 200
Cdd:cd05941 64 ---------AVPLNPSYPLA---------------------ELE-----------------------YVITDSEPS---- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 EWVgaeHPLFILYTSGSTGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTqVVF 280
Cdd:cd05941 87 LVL---DPALILYTSGTTGRPKGVVL-THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGAS-VEF 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EGVPtwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPK--SYDLSSLRIIGTVGEPINP---EAWMWYHKH 355
Cdd:cd05941 162 LPKF---DPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFarAAAAERLRLMVSGSAALPVptlEEWEAITGH 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 356 VGQERcpivdtWWQTETGGHMITPLPGatPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPwpAMIRTIWGD 434
Cdd:cd05941 239 TLLER------YGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGP--SVFKEYWNK 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PERFRKSYypeeLGGRLYLAGDGTVRDKDtGYFTIMGRI-DDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:cd05941 309 PEATKEEF----TDDGWFKTGDLGVVDED-GYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWG 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 514 EAVVAFVVlkrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:cd05941 384 ERVVAVVV-----LRAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
42-576 |
5.67e-44 |
|
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: 162.92 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHsvvfggfsaksl 121
Cdd:cd17649 2 DAVALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAY------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 nerlvdvgavalvtadeqarggktLPLKsiadeavamggceavksvivyrrtggkIDWHAGRDLWMheLADAESdtcapE 201
Cdd:cd17649 65 ------------------------VPLD---------------------------PEYPAERLRYM--LEDSGA-----G 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAEHP---LFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKwTFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTqV 278
Cdd:cd17649 87 LLLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE-RYGLTPGDRELQFASFNFDGAHEQL-LPPLICGAC-V 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 279 VFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPKSydlssLRIIGTVGEPINPE-AWMWyhkhvG 357
Cdd:cd17649 164 VLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-----LRLYIFGGEALSPElLRRW-----L 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 358 QERCPIVDTWWQTETgghMITPL-----PGAT---PTVP-GSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMI 428
Cdd:cd17649 234 KAPVRLFNAYGPTEA---TVTPLvwkceAGAAragASMPiGR---PLGGRSAYILDADLNPVPVGVTGELYIGGE--GLA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 429 RTIWGDP----ERFRKSYYPEElGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd17649 306 RGYLGRPeltaERFVPDPFGAP-GSRLYRTGD-LARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAV 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 505 VGRPDDtTGEAVVAFVVLKrsrpEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd17649 384 VALDGA-GGKQLVAYVVLR----AAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
32-584 |
6.70e-44 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 164.46 E-value: 6.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTA------DEQARGGKTLPLKSIADEAVAMGGCEAVKsvivYRRTGGKIDWHAGRDl 185
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPktfrgfDHAAMARRLRPELPALRHVVVVGGDGADS----FEALLITPAWEQEPD- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 186 wmhelADAESDTCAPewvGAEHPLFILYTSGSTGKPKGVQHSTGgyLLWA-----AQTMkwtfDWKPDDVFWCTADIGWV 260
Cdd:PRK13295 185 -----APAILARLRP---GPDDVTQLIYTSGTTGEPKGVMHTAN--TLMAnivpyAERL----GLGADDVILMASPMAHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 261 TGHTYITYGPLACGGTQVVFEgvpTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTV 340
Cdd:PRK13295 251 TGFMYGLMMPVMLGATAVLQD---IW-DPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGR------PVSSLRTFLCA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 341 GEPINPEAwmwyhkhVGQER----CPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGG 416
Cdd:PRK13295 321 GAPIPGAL-------VERARaalgAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 417 ILVV----------KRP-WPAMIRTIWGDPerfrksyypeelGGRLYLAGDGTVRdkdtgyftIMGRIDDVLNVSGHRLG 485
Cdd:PRK13295 394 RLQVrgcsnfggylKRPqLNGTDADGWFDT------------GDLARIDADGYIR--------ISGRSKDVIIRGGENIP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 486 TMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAaalaktLRDWVGKQigPIAK---PKDIRFGDNL 562
Cdd:PRK13295 454 VVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEE------MVEFLKAQ--KVAKqyiPERLVVRDAL 525
|
570 580
....*....|....*....|..
gi 1860891105 563 PKTRSGKIMRRLLRSLAKGEAI 584
Cdd:PRK13295 526 PRTPSGKIQKFRLREMLRGEDA 547
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
41-575 |
1.09e-43 |
|
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: 162.83 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKS 120
Cdd:cd17646 12 PDAPAVVDEG-----RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLVDVGA-VALVTADEQARGGKTLPLKSIADEAVAmggceavksvivyrrtggkidwhagrdlwmheladAESDTCA 199
Cdd:cd17646 87 LAYMLADAGPaVVLTTADLAARLPAGGDVALLGDEALA-----------------------------------APPATPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 200 PEWVGAEHPLFILYTSGSTGKPKGV---QHSTGGYLLWaaqtMKWTFDWKPDDVFWCTADIGW-VTGhtYITYGPLACGG 275
Cdd:cd17646 132 LVPPRPDNLAYVIYTSGSTGRPKGVmvtHAGIVNRLLW----MQDEYPLGPGDRVLQKTPLSFdVSV--WELFWPLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 276 TQVVFEgvptwP----DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksydLSSLRIIGTVGEPINPEAWMW 351
Cdd:cd17646 206 RLVVAR-----PgghrDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGS--------CASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 352 YHKHVGqerCPIVDTWWQTETG----GHMITPlPGATPTVP-GSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPA 426
Cdd:cd17646 273 FLALPG---AELHNLYGPTEAAidvtHWPVRG-PAETPSVPiGR---PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 427 miRTIWGDP----ERFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEA 502
Cdd:cd17646 346 --RGYLGRPaltaERFVPD--PFGPGSRMYRTGD-LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHA 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860891105 503 AVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17646 421 VVVARAAPAGAARLVGYVVPAAGAAGPDTAA-----LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
45-576 |
1.49e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 162.77 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 45 AVIFeADDGTVtrVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNER 124
Cdd:PRK08276 2 AVIM-APSGEV--VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 125 LVDVGAVALVTadeQARGGKTlplksiADEAVAmggcEAVKSVIVYRRTGGKIDwhaGRDLWmHELADAESDT-CAPEWV 203
Cdd:PRK08276 79 VDDSGAKVLIV---SAALADT------AAELAA----ELPAGVPLLLVVAGPVP---GFRSY-EEALAAQPDTpIADETA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 204 GAEhplfILYTSGSTGKPKGVQHS-TGGYLLWAAQTMKW----TFDWKPDDVFWCTADIgwvtGHTyityGPL------- 271
Cdd:PRK08276 142 GAD----MLYSSGTTGRPKGIKRPlPGLDPDEAPGMMLAllgfGMYGGPDSVYLSPAPL----YHT----APLrfgmsal 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 272 ACGGTQVVFEGvptWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkVHpKSYDLSSLRIIGTVGEPINPE---- 347
Cdd:PRK08276 210 ALGGTVVVMEK---F-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEE---VR-ARYDVSSLRVAIHAAAPCPVEvkra 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 348 --AWmWyhkhvGqercPIVD-TWWQTEtgGHMITPlpgATP----TVPGSCTLPLPGIMaAVVDETGQDVPNGQGGILVV 420
Cdd:PRK08276 282 miDW-W-----G----PIIHeYYASSE--GGGVTV---ITSedwlAHPGSVGKAVLGEV-RILDEDGNELPPGEIGTVYF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 421 KRPWPAMirTIWGDPERFRKSYYPEelggRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVA 500
Cdd:PRK08276 346 EMDGYPF--EYHNDPEKTAAARNPH----GWVTVGDVGYLDED-GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVA 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 501 EAAVVGRPDDTTGEAVVAFVvlkRSRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK08276 419 DVAVFGVPDEEMGERVKAVV---QPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
38-579 |
4.85e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 163.59 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 38 AGNGQRVAVIF---EADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQAcariGATHSVVF- 113
Cdd:PRK07529 36 ARHPDAPALSFlldADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 --GGFSAKSLNERLVDVGAVALVTAdeqarggKTLPLKSIADEAVAM-GGCEAVKSVIVY---RRTGGKIDW-------- 179
Cdd:PRK07529 112 inPLLEPEQIAELLRAAGAKVLVTL-------GPFPGTDIWQKVAEVlAALPELRTVVEVdlaRYLPGPKRLavplirrk 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 180 HAGRDLWMHELADAESDTC--APEWVGAEHPLFILYTSGSTGKPKGVQHSTGG--YLLWAAQTmkwTFDWKPDDVFWCTA 255
Cdd:PRK07529 185 AHARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevANAWLGAL---LLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 256 DIGWVTGHTYITYGPLACGGtQVVFEGVPTWPDAG---RFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddkVHPKSYDLS 332
Cdd:PRK07529 262 PLFHVNALLVTGLAPLARGA-HVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALLQ-------VPVDGHDIS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 333 SLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTE-TGGHMITPLPGatPTVPGSCTLPLPG--IMAAVVDETG-- 407
Cdd:PRK07529 334 SLRYALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYqrVRVVILDDAGry 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 408 -QDVPNGQGGILVVKRPwpamirTIWG---DPERFRKSYypeeLGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHR 483
Cdd:PRK07529 409 lRDCAVDEVGVLCIAGP------NVFSgylEAAHNKGLW----LEDGWLNTGDLGRIDAD-GYFWLTGRAKDLIIRGGHN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 484 LGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIG-PIAKPKDIRFGDNL 562
Cdd:PRK07529 478 IDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLK------PGASATEAELLAFARDHIAeRAAVPKHVRILDAL 551
|
570
....*....|....*..
gi 1860891105 563 PKTRSGKIMRRLLRSLA 579
Cdd:PRK07529 552 PKTAVGKIFKPALRRDA 568
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
56-577 |
2.49e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 159.77 E-value: 2.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQAC----ARIGATHSVvfggfsaKSLNER---LVDV 128
Cdd:PRK06188 36 TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAqlagLRRTALHPL-------GSLDDHayvLEDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 129 GAVALVTADEQarggktlplksIADEAVAMG-GCEAVKSVIVYRRTGGkidwhaGRDLWmhelADAESDTCAPEWVGAEH 207
Cdd:PRK06188 109 GISTLIVDPAP-----------FVERALALLaRVPSLKHVLTLGPVPD------GVDLL----AAAAKFGPAPLVAAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 P--LFILYTSGSTGKPKGVQHSTGGYLLwAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYItygP-LACGGTQVVFEGVp 284
Cdd:PRK06188 168 PdiAGLAYTGGTTGKPKGVMGTHRSIAT-MAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL---PtLLRGGTVIVLAKF- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 twpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINP----EAwmwyHKHVGqer 360
Cdd:PRK06188 243 ---DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTR------DLSSLETVYYGASPMSPvrlaEA----IERFG--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 cPI-VDTWWQTETGgHMITPLP-----GATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGD 434
Cdd:PRK06188 307 -PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMDGYWNR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PER----FRksyypeelGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDD 510
Cdd:PRK06188 383 PEEtaeaFR--------DGWLH-TGDVAREDED-GFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 511 TTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK06188 453 KWGEAVTAVVVLR------PGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
34-582 |
8.37e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 159.05 E-value: 8.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 34 RHVEAGNGQRVAVIFEaddGTVTrvTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVF 113
Cdd:PRK06178 40 RAWARERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 GGFSAKSLNERLVDVGAVALVTAD------EQARGGktLPLKSIADEAVA-MggCEAVKSVIVYRRTGGKIDWHAGrdlw 186
Cdd:PRK06178 115 PLFREHELSYELNDAGAEVLLALDqlapvvEQVRAE--TSLRHVIVTSLAdV--LPAEPTLPLPDSLRAPRLAAAG---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 187 MHELADAESDTCAP---EWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGH 263
Cdd:PRK06178 187 AIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 264 TYITYGPLACGGTQVVfegVPTWpDAGRFWKMIGDHKVTVfytaptAIRSLIKAAEADDKVHPKSYDLSSLRIIGTVG-- 341
Cdd:PRK06178 267 NFGLLFPLFSGATLVL---LARW-DAVAFMAAVERYRVTR------TVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfv 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 342 EPINPEawmwYHKHvgqercpivdtwWQTETGGHMITPLPGATPT-------------------VPGSCTLPLPGIMAAV 402
Cdd:PRK06178 337 KKLNPD----YRQR------------WRALTGSVLAEAAWGMTEThtcdtftagfqdddfdllsQPVFVGLPVPGTEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 403 VD-ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRksyypEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSG 481
Cdd:PRK06178 401 CDfETGELLPLGAEGEIVVRTP--SLLKGYWNKPEATA-----EALRDGWLHTGDIGKIDEQ-GFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 482 HRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsRPEGEEAAAlakTLRDWVGKQIGPIAKPkDIRFGDN 561
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQL---KPGADLTAA---ALQAWCRENMAVYKVP-EIRIVDA 545
|
570 580
....*....|....*....|.
gi 1860891105 562 LPKTRSGKIMRRLLRSLAKGE 582
Cdd:PRK06178 546 LPMTATGKVRKQDLQALAEEL 566
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-576 |
3.12e-41 |
|
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: 155.29 E-value: 3.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 65 ARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFggfsaKSLNERLVDvGAVALVTADEQARggK 144
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVF-----VPLNPTLKE-SVLRYLVADAGGR--I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 145 TLPLKSIADEAVamggceavKSVIVYRRTGGKID----WHAGRDLWMHELADaesdtcapewvgaEHPLFILYTSGSTGK 220
Cdd:cd05922 73 VLADAGAADRLR--------DALPASPDPGTVLDadgiRAARASAPAHEVSH-------------EDLALLLYTSGSTGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 221 PKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGhTYITYGPLACGGTQVVFE-GVPtwPDAgrFWKMIGDH 299
Cdd:cd05922 132 PKLVRLSHQN-LLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNdGVL--DDA--FWEDLREH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 300 KVTVFYTAPTAIRSLIKAAEADDKvhpksydLSSLRIIGTVGEPINPEAWMWY-HKHVGQErcpIVDTWWQTETGGHMIT 378
Cdd:cd05922 206 GATGLAGVPSTYAMLTRLGFDPAK-------LPSLRYLTQAGGRLPQETIARLrELLPGAQ---VYVMYGQTEATRRMTY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 379 PLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMirTIWGDPERFRKsyyPEELGGRLYlAGDGT 458
Cdd:cd05922 276 LPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMK--GYWNDPPYRRK---EGRGGGVLH-TGDLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 459 VRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDtTGEAVVAFVVlkrsRPEGEEAAALAKT 538
Cdd:cd05922 350 RRDED-GFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVT----APDKIDPKDVLRS 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 1860891105 539 LRdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05922 424 LA----ERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
43-578 |
1.04e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 152.77 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIfeADDGTVTrvtYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:PRK07788 65 RAALI--DERGTLT---YAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTADEQArggktlPLKSIADEAvaMGGCEAvksvIVYRRTGGKIDWHAGRDLwmHELADAESDTCAPEW 202
Cdd:PRK07788 140 EVAAREGVKALVYDDEFT------DLLSALPPD--LGRLRA----WGGNPDDDEPSGSTDETL--DDLIAGSSTAPLPKP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 vgAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTfDWKPDDVFWCTADIGWVTGHTYITYGpLACGGTQVV--- 279
Cdd:PRK07788 206 --PKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV-PFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrr 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 280 FegvptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIkaaEADDKVHPKsYDLSSLRIIGTVGEPINPEAWMWYHKHVGqe 359
Cdd:PRK07788 282 F-------DPEATLEDIAKHKATALVVVPVMLSRIL---DLGPEVLAK-YDTSSLKIIFVSGSALSPELATRALEAFG-- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 360 rcPIV-DTWWQTETGGHMItplpgATP----TVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGD 434
Cdd:PRK07788 349 --PVLyNLYGSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PERFrksyypeelggrlylagDGTVRDKDTGYFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRP 508
Cdd:PRK07788 422 KQII-----------------DGLLSSGDVGYFDedgllfVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 509 DDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:PRK07788 485 DEEFGQRLRAFVVKA------PGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
43-575 |
1.20e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 151.29 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVifEADDGTVTrvtYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:cd12116 3 ATAV--RDDDRSLS---YAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTADEQARGGktlplksiadeavamggceavksvivyrrtggkidwHAGRDLWMH-ELADAESDTCAPE 201
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRL------------------------------------PAGLPVLLLaLAAAAAAPAAPRT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDvfwctadiGWVTGHTY---IT----YGPLACG 274
Cdd:cd12116 122 PVSPDDLAYVIYTSGSTGRPKGVVVSHRN-LVNFLHSMRERLGLGPGD--------RLLAVTTYafdISllelLLPLLAG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVFEGvPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpksydLSSLRII-GtvGEPINP------- 346
Cdd:cd12116 193 ARVVIAPR-ETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQG---------RAGLTALcG--GEALPPdlaarll 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 347 ----EAWMWYhkhvGqercPIVDTWWQTetgghmITPLPGATPTVPGSctLPLPGIMAAVVDETGQDVPNGQGGILVVKR 422
Cdd:cd12116 261 srvgSLWNLY----G----PTETTIWST------AARVTAAAGPIPIG--RPLANTQVYVLDAALRPVPPGVPGELYIGG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 423 PwpAMIRTIWGDP----ERFRKSYYPEElGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHEL 498
Cdd:cd12116 325 D--GVAQGYLGRPaltaERFVPDPFAGP-GSRLYRTGDLVRRRAD-GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPG 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 499 VAEAAVVGRPDDTTGeAVVAFVVLKRSRPEGEEA--AALAKTLRDWVgkqigpiaKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd12116 401 VAQAAVVVREDGGDR-RLVAYVVLKAGAAPDAAAlrAHLRATLPAYM--------VPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
35-569 |
1.69e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 151.96 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 35 HVEAGNGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFG 114
Cdd:PRK07798 11 AVADAVPDRVALVCGD-----RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 115 GFSAKSLNERLVDVGAVALVTADEQA-RGGKTLP-------LKSIADEAVAMGGCEAVksvivyrrtggkidwhagrdlw 186
Cdd:PRK07798 86 RYVEDELRYLLDDSDAVALVYEREFApRVAEVLPrlpklrtLVVVEDGSGNDLLPGAV---------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 187 mhELADAESDTCAPEWVGAEHP--LFILYTSGSTGKPKGV---QH-----STGGYLLWAAQTMKwtfdwKPDDVfwcTAD 256
Cdd:PRK07798 144 --DYEDALAAGSPERDFGERSPddLYLLYTGGTTGMPKGVmwrQEdifrvLLGGRDFATGEPIE-----DEEEL---AKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 257 IGWVTGHTYITYGPLACGGTQ------------VVFEGVPTWpDAGRFWKMIGDHKVTVFYTAPTAI-RSLIKAAEAddk 323
Cdd:PRK07798 214 AAAGPGMRRFPAPPLMHGAGQwaafaalfsgqtVVLLPDVRF-DADEVWRTIEREKVNVITIVGDAMaRPLLDALEA--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 324 vhPKSYDLSSLRIIGTVGEPINPEawmwyHKHVGQERCP---IVDTWWQTETG-GHMITPLPGATPTVPGSCTlplPGIM 399
Cdd:PRK07798 290 --RGPYDLSSLFAIASGGALFSPS-----VKEALLELLPnvvLTDSIGSSETGfGGSGTVAKGAVHTGGPRFT---IGPR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 400 AAVVDETGQDVPNGQGGILVVKRPWPAMIRtIWGDPERFRKSYyPEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNV 479
Cdd:PRK07798 360 TVVLDEDGNPVEPGSGEIGWIARRGHIPLG-YYKDPEKTAETF-PTIDGVRYAIPGDRARVEAD-GTITLLGRGSVCINT 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 480 SGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAfVVLKRSRPEGEEAAalaktLRDWVGKQIGPIAKPKDIRFG 559
Cdd:PRK07798 437 GGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVA-VVQLREGARPDLAE-----LRAHCRSSLAGYKVPRAIWFV 510
|
570
....*....|
gi 1860891105 560 DNLPKTRSGK 569
Cdd:PRK07798 511 DEVQRSPAGK 520
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
89-582 |
3.12e-39 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 150.74 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 89 MPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAmggceAVKSVI 168
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAP-----AKAIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 169 VYRRTGGKIDWHAGRDLWMHELADAESDTCA------PEWVGAEHPLFILYTSGSTGKPKGV--QHSTGgylLWAAQTMK 240
Cdd:PLN03051 76 PAAGEPVAVPLREQDLSWCDFLGVAAAQGSVggneysPVYAPVESVTNILFSSGTTGEPKAIpwTHLSP---LRCASDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 241 WTFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQVVFEGVPTWPDAGRFwkmIGDHKVTVFYTAPTAIRSLIKAAEA 320
Cdd:PLN03051 153 AHMDIQPGDVVCWPTNLGWMMGPWLL-YSAFLNGATLALYGGAPLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 321 DDKVHpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQERcPIVDTWWQTETGGHMI--TPLpgaTPTVPGSCTLPLPGI 398
Cdd:PLN03051 229 AMEGL----DWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLL---QPQAPGAFSTASLGT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVPNGQGGILVVKRPWPAMirtiwGDPERF-----RKSYYP-----EELGGRLYLAGDGTVRDKdTGYFT 468
Cdd:PLN03051 301 RFVLLNDNGVPYPDDQPCVGEVALAPPML-----GASDRLlnadhDKVYYKgmpmyGSKGMPLRRHGDIMKRTP-GGYFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 469 IMGRIDDVLNVSGHRLGTMEIESALV-SHELVAEAAVVG-RPDDTTGEAVVAFV---VLKRSRPEGEEaAALAKTLRDWV 543
Cdd:PLN03051 375 VQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGvAPPDGGPELLVIFLvlgEEKKGFDQARP-EALQKKFQEAI 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 1860891105 544 GKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGE 582
Cdd:PLN03051 454 QTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKE 492
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
58-577 |
4.56e-39 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 150.32 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQarggktlpLKSIADeavAMGGCEAVKSVIVYRRTGGKIDWHAGRDlwMHELADAES--DTCAPEWVGAEHPLFILYTS 215
Cdd:TIGR03098 106 ER--------LDLLHP---ALPGCHDLRTLIIVGDPAHASEGHPGEE--PASWPKLLAlgDADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 216 GSTGKPKGV--QHSTggylLWA-AQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGpLACGGTQVVFEGVpTWPDagrF 292
Cdd:TIGR03098 173 GSTGRPKGVvlSHRN----LVAgAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDYL-LPRD---V 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 293 WKMIGDHKVTVFYTAPTairslIKAAEADDKVHPKsyDLSSLRIIGTVGEPINPEAWMWYHKHVGQERcpIVDTWWQTET 372
Cdd:TIGR03098 244 LKALEKHGITGLAAVPP-----LWAQLAQLDWPES--AAPSLRYLTNSGGAMPRATLSRLRSFLPNAR--LFLMYGLTEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 373 GGHMITPlPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMirTIWGDPE----RFRKS--YYPE- 445
Cdd:TIGR03098 315 FRSTYLP-PEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAM--GYWNDPEktaeRFRPLppFPGEl 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 446 ELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVlkrs 525
Cdd:TIGR03098 392 HLPELAVWSGD-TVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVT---- 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 526 RPEGEEA--AALAKTLRdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:TIGR03098 467 PPGGEELdrAALLAECR----ARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-576 |
5.11e-39 |
|
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: 150.09 E-value: 5.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 34 RHVEAGNGQRVaVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAT-HSVv 112
Cdd:cd12119 3 EHAARLHGDRE-IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 113 fggfsakslNERL--------VDVGAVALVTADEQarggkTLPLKsiadEAVAmGGCEAVKSVIVYRRTGGKIDWHAGRD 184
Cdd:cd12119 81 ---------NPRLfpeqiayiINHAEDRVVFVDRD-----FLPLL----EAIA-PRLPTVEHVVVMTDDAAMPEPAGVGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 185 LWMHELADAESDTCapEWVGA-EH-PLFILYTSGSTGKPKGVQHSTGGYLLWA-AQTMKWTFDWKPDDVFWCTADI---- 257
Cdd:cd12119 142 LAYEELLAAESPEY--DWPDFdENtAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 258 GWVTGHTyityGPLAcgGTQVVFEGVptWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRII 337
Cdd:cd12119 220 AWGLPYA----AAMV--GAKLVLPGP--YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANG------RDLSSLRRV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 338 gTVGEPINPEAWM--WYHKHVgqercPIVDTWWQTETG--GHMITPLPGATPTVPG-------SCTLPLPGIMAAVVDET 406
Cdd:cd12119 286 -VIGGSAVPRSLIeaFEERGV-----RVIHAWGMTETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 407 GQDVP-NGQG-GILVVKRPWPAmirtiwgdperfrKSYYPEELGGRLYLA------GDGTVRDKDtGYFTIMGRIDDVLN 478
Cdd:cd12119 360 GRELPwDGKAvGELQVRGPWVT-------------KSYYKNDEESEALTEdgwlrtGDVATIDED-GYLTITDRSKDVIK 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 479 VSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRF 558
Cdd:cd12119 426 SGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK------EGATVTAEELLEFLADKVAKWWLPDDVVF 499
|
570
....*....|....*...
gi 1860891105 559 GDNLPKTRSGKIMRRLLR 576
Cdd:cd12119 500 VDEIPKTSTGKIDKKALR 517
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
32-588 |
7.05e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 150.29 E-value: 7.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:PRK06155 27 LARQAER-YPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAmggceavksvivyrRTGGKIDWHAGRDLWMHEL- 190
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVW--------------LLDAPASVSVPAGWSTAPLp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 191 ADAESDTCAPewVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTmkwtfdwkpddvfwcTADIGWVTGHTYITYGP 270
Cdd:PRK06155 167 PLDAPAPAAA--VQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNS---------------AEDLEIGADDVLYTTLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 271 L------------ACGGTQVVFEgvPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLI-KAAEADDKVHPksydlssLRII 337
Cdd:PRK06155 230 LfhtnalnaffqaLLAGATYVLE--PRF-SASGFWPAVRRHGATVTYLLGAMVSILLsQPARESDRAHR-------VRVA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 338 GTVGEPInpeawmwyHKHVG-QERC--PIVDTWWQTETGGHMITPLPGATPtvpGSCTLPLPGIMAAVVDETGQDVPNGQ 414
Cdd:PRK06155 300 LGPGVPA--------ALHAAfRERFgvDLLDGYGSTETNFVIAVTHGSQRP---GSMGRLAPGFEARVVDEHDQELPDGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 415 GGILVVKRPWP-AMIRTIWGDPERFRKSYYpeelggRLYL-AGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESA 492
Cdd:PRK06155 369 PGELLLRADEPfAFATGYFGMPEKTVEAWR------NLWFhTGDRVVRDAD-GWFRFVDRIKDAIRRRGENISSFEVEQV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 493 LVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEAAALAktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:PRK06155 442 LLSHPAVAAAAVFPVPSELGEDEVMAAVVLR----DGTALEPVA--LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQK 515
|
570
....*....|....*.
gi 1860891105 573 RLLRSlakgEAITQDT 588
Cdd:PRK06155 516 FVLRE----QGVTADT 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-576 |
1.31e-38 |
|
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: 147.53 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTA 136
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEqarggktlplksiadeavamggceavksvivYRRtggkidwhagrdlwmHELADAESDTCApewvgaehplfILYTSG 216
Cdd:cd05903 81 ER-------------------------------FRQ---------------FDPAAMPDAVAL-----------LLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGGYL-LWAAQTMKWTFDWKpdDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEgvpTWpDAGRFWKM 295
Cdd:cd05903 104 TTGEPKGVMHSHNTLSaSIRQYAERLGLGPG--DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IW-DPDKALAL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 296 IGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINP----EAWmwyhKHVGQERCPIvdtWWQTE 371
Cdd:cd05903 178 MREHGVTFMMGATPFLTDLLNAVEEAGE------PLSRLRTFVCGGATVPRslarRAA----ELLGAKVCSA---YGSTE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRksyypEELGGRL 451
Cdd:cd05903 245 CPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP--SVFLGYLDRPDLTA-----DAAPEGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 YLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKR-SRPEGE 530
Cdd:cd05903 318 FRTGDLARLDED-GYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgALLTFD 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1860891105 531 EAAALAKtlrdwvGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05903 397 ELVAYLD------RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
42-575 |
3.49e-38 |
|
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: 147.03 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIfeADDGTVTrvtYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:cd12114 2 DATAVI--CGDGTLT---YGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTADEQARGGKTLPLKSIADEAvamggceavksvivyrrtggkidwhagrdlwmhelADAESDTCAPE 201
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLD-----------------------------------ALAAPAPPPPV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAEHPLFILYTSGSTGKPKGVQHSTGGYL-LWAAQTMKWTFDwkPDDVFWCTA----DIGwvtghTYITYGPLACGGT 276
Cdd:cd12114 122 DVAPDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSslsfDLS-----VYDIFGALSAGAT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVfegvptwPDAGR-----FW-KMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINPEAWM 350
Cdd:cd12114 195 LVL-------PDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEAAQA------LLPSLRLVLLSGDWIPLDLPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 351 WYHKHVGQerCPIVDTWWQTETG----GHMITPLPGATPTVP-GsctLPLPGIMAAVVDETGQDVPNGqggilVVKRPW- 424
Cdd:cd12114 262 RLRALAPD--ARLISLGGATEASiwsiYHPIDEVPPDWRSIPyG---RPLANQRYRVLDPRGRDCPDW-----VPGELWi 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 --PAMIRTIWGDPERFRKSYYPEELGGRLYLAGD-GtvRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAE 501
Cdd:cd12114 332 ggRGVALGYLGDPELTAARFVTHPDGERLYRTGDlG--RYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 502 AAVVGRpDDTTGEAVVAFVVlkrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd12114 410 AVVVVL-GDPGGKRLAAFVV-----PDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
57-579 |
9.85e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 147.23 E-value: 9.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTA 136
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEQARGGKTLPLKSIADEaVAMGGCEA--------VKSVIVY--RRTGGKIDWHA----GRDLWMHELADAESDtcapew 202
Cdd:PRK12583 125 DAFKTSDYHAMLQELLPG-LAEGQPGAlacerlpeLRGVVSLapAPPPGFLAWHElqarGETVSREALAERQAS------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 VGAEHPLFILYTSGSTGKPKGVQHS-----TGGYLLwaAQTMKWTFDWK---PDDVFWCtadIGWVTGHtyitygpLAC- 273
Cdd:PRK12583 198 LDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFV--AESLGLTEHDRlcvPVPLYHC---FGMVLAN-------LGCm 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 274 -GGTQVVFEGVPTWPDAGrfWKMIGDHKVTVFYTAPTAIrslikAAEADdkvHP--KSYDLSSLRIIGTVGEPINPEAwm 350
Cdd:PRK12583 266 tVGACLVYPNEAFDPLAT--LQAVEEERCTALYGVPTMF-----IAELD---HPqrGNFDLSSLRTGIMAGAPCPIEV-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 351 wYHKHVGQERCP-IVDTWWQTETGGhmITPLPGATPTVPGSCTL---PLPGIMAAVVDETGQDVPNGQGGILVVkRPWPA 426
Cdd:PRK12583 334 -MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAADDLERRVETvgrTQPHLEVKVVDPDGATVPRGEIGELCT-RGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 427 MIrTIWGDPERFRKSYYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVG 506
Cdd:PRK12583 410 MK-GYWNNPEATAESIDED---GWMH-TGDLATMDEQ-GYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860891105 507 RPDDTTGEAVVAFVVLKRSRPEGEEaaalakTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:PRK12583 484 VPDEKYGEEIVAWVRLHPGHAASEE------ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
57-578 |
2.02e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 145.33 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSvvfggfsakSLNERLVDVGAVALVTA 136
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYV---------PLNWRLSASELDALLQD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEqarggktlPLKSIADEAVAMGGCEAVkSVIVYRrtgGKIDwhagrdlwMHELADAESdtcAPewvgAEHPLFILYTSG 216
Cdd:PRK09088 93 AE--------PRLLLGDDAVAAGRTDVE-DLAAFI---ASAD--------ALEPADTPS---IP----PERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVptwpDAGRFWKMI 296
Cdd:PRK09088 146 TSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF----EPKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 297 GDHK--VTVFYTAPTAIRSLikaaeaddKVHPkSYDLSSLR---IIGTVGEPINPEAWMWYHkhvgQERCPIVDTWWQTE 371
Cdd:PRK09088 221 GDPAlgITHYFCVPQMAQAF--------RAQP-GFDAAALRhltALFTGGAPHAAEDILGWL----DDGIPMVDGFGMSE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGHMITPL-PGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRpwPAMIRTIWGDPERFRKSYYPEElggr 450
Cdd:PRK09088 288 AGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG--PNLSPGYWRRPQATARAFTGDG---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 451 LYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegE 530
Cdd:PRK09088 362 WFRTGDIARRDAD-GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPA------D 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1860891105 531 EAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:PRK09088 435 GAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-577 |
2.56e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 145.22 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 53 GTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVA 132
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 133 LVTADEQArggktlplkSIADEAVAMggCEAVKSVIVYrrtgGKIDWHAGRDLWMHELADAESDTCAPEWVGAEhplfIL 212
Cdd:PRK13391 100 LITSAAKL---------DVARALLKQ--CPGVRHRLVL----DGDGELEGFVGYAEAVAGLPATPIADESLGTD----ML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 213 YTSGSTGKPKGV---------QHSTGgylLWAAQTMKWTFDwkPDDVFWCTADIgwvtGHTyityGPLA-------CGGT 276
Cdd:PRK13391 161 YSSGTTGRPKGIkrplpeqppDTPLP---LTAFLQRLWGFR--SDMVYLSPAPL----YHS----APQRavmlvirLGGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpKSYDLSSLRIIGTVGEPINPEawmwyhkhV 356
Cdd:PRK13391 228 VIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVR----DKYDLSSLEVAIHAAAPCPPQ--------V 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 GQErcpIVDtWWqtetgGHMITPLPGATPTV-------------PGSCTLPLPGIMaAVVDETGQDVPNGQGGilvvkrp 423
Cdd:PRK13391 292 KEQ---MID-WW-----GPIIHEYYAATEGLgftacdseewlahPGTVGRAMFGDL-HILDDDGAELPPGEPG------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 424 wpamirTIW----------GDPERFRKSYYPEelgGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESAL 493
Cdd:PRK13391 355 ------TIWfeggrpfeylNDPAKTAEARHPD---GTWSTVGDIGYVDED-GYLYLTDRAAFMIISGGVNIYPQEAENLL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 494 VSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRR 573
Cdd:PRK13391 425 ITHPKVADAAVFGVPNEDLGEEVKAVVQPV---DGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR 501
|
....
gi 1860891105 574 LLRS 577
Cdd:PRK13391 502 LLRD 505
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
56-575 |
1.95e-36 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 142.65 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVvfggfsaksLNERLVDVGAVALVT 135
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 ADEqARGGKTLPLKSIADEAVAMGGCEAVKSVIVyrrtggkidwhagrdlwmhELADAESDTCAPE--WVGAEHPLFILY 213
Cdd:cd05923 98 RGE-MTAAVIAVDAQVMDAIFQSGVRVLALSDLV-------------------GLGEPESAGPLIEdpPREPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 214 TSGSTGKPKGV---QHSTGGYLLWAAQTMKWTFDwkPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfegvPTWPDAG 290
Cdd:cd05923 158 TSGTTGLPKGAvipQRAAESRVLFMSTQAGLRHG--RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 291 RFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkvhpKSYDLSSLRIIGTVGEPINPEAWMWYHKHVgqeRCPIVDTWWQT 370
Cdd:cd05923 232 DALKLIEQERVTSLFATPTHLDALAAAAEF------AGLKLSSLRHVTFAGATMPDAVLERVNQHL---PGEKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 371 ETGGHMITPLPgatptVPGSCTLPlpGI-----MAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERFRKSyype 445
Cdd:cd05923 303 EAMNSLYMRDA-----RTGTEMRP--GFfsevrIVRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKK---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 446 eLGGRLYLAGDGTVRDkDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRS 525
Cdd:cd05923 372 -LQDGWYRTGDVGYVD-PSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1860891105 526 RPEGEEAAALAKTlrdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05923 450 TLSADELDQFCRA------SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
58-575 |
2.94e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 142.86 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 ---------EQARGGKTLPLKSIADeaVAMGGCEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHP 208
Cdd:PRK06710 130 lvfprvtnvQSATKIEHVIVTRIAD--FLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 209 LFIL-YTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKP-DDVFWCTADIGWVTGHTYITYGPLACGGTQVVfegVPTW 286
Cdd:PRK06710 208 LALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL---IPKF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 287 pDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkvhpKSYDLSSLRIIGTVGEPINPEAwmwyhkhvgQERcpivdt 366
Cdd:PRK06710 285 -DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLL------KEYDISSIRACISGSAPLPVEV---------QEK------ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 367 wWQTETGGHMITP--LPGATPT----------VPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPwpAMIRTIWG 433
Cdd:PRK06710 343 -FETVTGGKLVEGygLTESSPVthsnflwekrVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGP--QIMKGYWN 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 434 DPERFRKSYYpeelGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:PRK06710 420 KPEETAAVLQ----DGWLH-TGDVGYMDED-GFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRG 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 514 EAVVAFVVLKrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK06710 494 ETVKAFVVLK----EGTECS--EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
58-580 |
4.36e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 142.47 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 E-----QARGGKTlPLKSIAdeAVAMGGCEAVKSVIV---YRRTG---------GKIDWHAGrdlwmheLADAESDTCAP 200
Cdd:PRK07059 129 NfattvQQVLAKT-AVKHVV--VASMGDLLGFKGHIVnfvVRRVKkmvpawslpGHVRFNDA-------LAEGARQTFKP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 EWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKW---TFDWKPDD---VFWCTADIGWVTGHTYITYGPLACG 274
Cdd:PRK07059 199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWlqpAFEKKPRPdqlNFVCALPLYHIFALTVCGLLGMRTG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVfegVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdKVhpksyDLSSLRIIGTVGEPIN-PEAWMWYH 353
Cdd:PRK07059 279 GRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFD-KL-----DFSKLIVANGGGMAVQrPVAERWLE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 KhvgqERCPIVDTWWQTETGGhMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWG 433
Cdd:PRK07059 350 M----TGCPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP--QVMAGYWN 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 434 DPERFRKSYYPEELggrlYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:PRK07059 423 RPDETAKVMTADGF----FRTGDVGVMDER-GYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 514 EAVVAFVVLKRSRPEGEEAAALAKTlrdwvgkQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAK 580
Cdd:PRK07059 498 EAVKLFVVKKDPALTEEDVKAFCKE-------RLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
40-583 |
7.61e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.06 E-value: 7.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 40 NGQRVAVIFEaddGTVTrvTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVFGG--FS 117
Cdd:PRK05605 45 FGDRPALDFF---GATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV--VVEHNplYT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 118 AKSLNERLVDVGA-VALV---TADEQARGGKTLPLKSIAdeAVAMggCEA------------VKSVIVYRR--TG---GK 176
Cdd:PRK05605 118 AHELEHPFEDHGArVAIVwdkVAPTVERLRRTTPLETIV--SVNM--IAAmpllqrlalrlpIPALRKARAalTGpapGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 177 IDWHagrdlwmhELADA----ESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDD--- 249
Cdd:PRK05605 194 VPWE--------TLVDAaiggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPerv 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 250 -----VFwctadigwvtgHTY-----ITYGPLaCGGTQVVFegvPTwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE 319
Cdd:PRK05605 266 laalpMF-----------HAYgltlcLTLAVS-IGGELVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 320 ADDKvhpksyDLSSLR--IIGTVGEPInpeawmwyhkhvgqercPIVDTWwQTETGGHMI--------TPLPGATPTV-- 387
Cdd:PRK05605 330 ERGV------DLSGVRnaFSGAMALPV-----------------STVELW-EKLTGGLLVegygltetSPIIVGNPMSdd 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 388 --PGSCTLPLPGIMAAVVD--ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYYPEelggrLYLAGDGTVRDKD 463
Cdd:PRK05605 386 rrPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGP--QVFKGYWNRPEETAKSFLDG-----WFRTGDVVVMEED 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 464 tGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrsrpegEEAAAL-AKTLRDW 542
Cdd:PRK05605 459 -GFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL-------EPGAALdPEGLRAY 530
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1860891105 543 VGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS--LAKGEA 583
Cdd:PRK05605 531 CREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREelLEKLGA 573
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-575 |
7.72e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 144.71 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 40 NGQRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAK 119
Cdd:PRK12316 4564 TPDAVAVVFDEE-----KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE 4638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 120 SLNERLVDVGAVALVTadeQARGGKTLPlksIADEAVAMggceavksviVYRRTGgkiDWhAGRdlwmheladaeSDTCA 199
Cdd:PRK12316 4639 RLAYMMEDSGAALLLT---QSHLLQRLP---IPDGLASL----------ALDRDE---DW-EGF-----------PAHDP 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 200 PEWVGAEHPLFILYTSGSTGKPKGVQHSTG---GYLLWAAQTMKWTfdwkPDDVFWCTADIGWVTGHTYItYGPLACGGt 276
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGslvNHLHATGERYELT----PDDRVLQFMSFSFDGSHEGL-YHPLINGA- 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVFEGVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksyDLSSLRIIGTVGEPINPEA---WMWYH 353
Cdd:PRK12316 4762 SVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-------EPPSLRVYCFGGEAVAQASydlAWRAL 4833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 KHVGqercpIVDTWWQTETgghMITPLPGATP--TVPGSCTLP----LPGIMAAVVDETGQDVPNGQGGILVVKRPWPAm 427
Cdd:PRK12316 4834 KPVY-----LFNGYGPTET---TVTVLLWKARdgDACGAAYMPigtpLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVA- 4904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 428 iRTIWGDP----ERFRKSYYPEElGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAA 503
Cdd:PRK12316 4905 -RGYLERPaltaERFVPDPFGAP-GGRLYRTGDLARYRAD-GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4981
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 504 VVGRpDDTTGEAVVAFVVLKRSR--PEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK12316 4982 VIAQ-EGAVGKQLVGYVVPQDPAlaDADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
32-575 |
8.71e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 144.53 E-value: 8.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVeAGNGQRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:PRK12467 3101 IEAQV-ARTPEAPALVFGDQ-----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTadeQARGGKTLPLksiadeavamggcEAVKSVIVYRRTggkidwhagrDLWmhela 191
Cdd:PRK12467 3175 LDPEYPRERLAYMIEDSGVKLLLT---QAHLLEQLPA-------------PAGDTALTLDRL----------DLN----- 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 dAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGG---YLLWAAQT------------MKWTFDWKPDDVFWctad 256
Cdd:PRK12467 3224 -GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGAlanHLCWIAEAyeldandrvllfMSFSFDGAQERFLW---- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 257 igwvtghtyitygPLACGGTQVVFEGvPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpksyDLSSLRI 336
Cdd:PRK12467 3299 -------------TLICGGCLVVRDN-DLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGA--------DCASLDI 3355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 337 IGTVGEPINPEAWMWYHKHVGQeRCpIVDTWWQTETgghMITPLPGATP--TVPGSCTLP----LPGIMAAVVDETGQDV 410
Cdd:PRK12467 3356 YVFGGEAVPPAAFEQVKRKLKP-RG-LTNGYGPTEA---VVTVTLWKCGgdAVCEAPYAPigrpVAGRSIYVLDGQLNPV 3430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 411 PNGQGGILVVKRPWPAmiRTIWGDP----ERFRKSYYpEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGT 486
Cdd:PRK12467 3431 PVGVAGELYIGGVGLA--RGYHQRPsltaERFVADPF-SGSGGRLYRTGD-LARYRADGVIEYLGRIDHQVKIRGFRIEL 3506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 487 MEIESALVSHELVAEAAVVGRpDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTR 566
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPA------DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGP 3579
|
....*....
gi 1860891105 567 SGKIMRRLL 575
Cdd:PRK12467 3580 NGKVDRKAL 3588
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
41-576 |
1.14e-35 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 140.59 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVfggfsakS 120
Cdd:PRK08008 21 GHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI--MV-------P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLV---------DVGAVALVTADEqarggkTLPL-KSIADEAVAMggceaVKSVIVYRRTGGKIDwhaGRDLWMHEL 190
Cdd:PRK08008 92 INARLLreesawilqNSQASLLVTSAQ------FYPMyRQIQQEDATP-----LRHICLTRVALPADD---GVSSFTQLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 191 ADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDV-----------FWCTADIGw 259
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVV-ITHYNLRFAGYYSAWQCALRDDDVyltvmpafhidCQCTAAMA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 260 vtghtyitygPLACGGTQVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSL-IKAAEADDKVHpksydlsSLRIIg 338
Cdd:PRK08008 236 ----------AFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLmVQPPSANDRQH-------CLREV- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 339 tvgepinpeawMWYHKHVGQER--------CPIVDTWWQTETGGHMITPLPGATPTVPgSCTLPLPGIMAAVVDETGQDV 410
Cdd:PRK08008 294 -----------MFYLNLSDQEKdafeerfgVRLLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 411 PNGQGGILVVKR-PWPAMIRTIWGDPERFRKSYYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEI 489
Cdd:PRK08008 362 PAGEIGEICIKGvPGKTIFKEYYLDPKATAKVLEAD---GWLH-TGDTGYVDEE-GFFYFVDRRCNMIKRGGENVSCVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 490 ESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGE---EAAALAKTLRDWVGKQIgpiakPKDIRFGDNLPKTR 566
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN----EGEtlsEEEFFAFCEQNMAKFKV-----PSYLEIRKDLPRNC 507
|
570
....*....|
gi 1860891105 567 SGKIMRRLLR 576
Cdd:PRK08008 508 SGKIIKKNLK 517
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
32-575 |
1.83e-35 |
|
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: 139.38 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIfeaDDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsV 111
Cdd:cd05920 21 LARSAAR-HPDRIAVV---DGDR--RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSakslnERLVDVGAVAlvtadEQARggktlplksiadeavamggceaVKSVIVYRRTGGkidwHAGRDLwMHELA 191
Cdd:cd05920 93 VLALPS-----HRRSELSAFC-----AHAE----------------------AVAYIVPDRHAG----FDHRAL-ARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDtcapewvgaehPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWT-FDwkPDDVFWCTADIGwvtgHTYITYGP 270
Cdd:cd05920 136 ESIPE-----------VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCgLD--QDTVYLAVLPAA----HNFPLACP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 271 -----LACGGTQVVfegvPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkvhpKSYDLSSLRIIGTVGEPIN 345
Cdd:cd05920 199 gvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS------RRADLSSLRLLQVGGARLS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 346 PEAwmwyHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPL-PGIMAAVVDETGQDVPNGQGGILVVKRPW 424
Cdd:cd05920 269 PAL----ARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 paMIRTIWGDPERFRKSYYPEELggrlYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd05920 345 --TIRGYYRAPEHNARAFTPDGF----YRTGDLVRRTPD-GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 505 VGRPDDTTGEAVVAFVVLKRSRPegeEAAALAKTLRdwvGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd05920 418 VAMPDELLGERSCAFVVLRDPPP---SAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-575 |
8.00e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.63 E-value: 8.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 19 WFDDGELNASYNCLDRHVEAG---NGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEG 95
Cdd:PRK12316 500 WNATAAEYPLQRGVHRLFEEQverTPEAPALAFGE-----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 96 IVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTadeQARGGKTLPLKSIADeavamggceavksVIVYRRTGg 175
Cdd:PRK12316 575 VVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS---QSHLGRKLPLAAGVQ-------------VLDLDRPA- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 176 kidwhagrdLWMHELADAESDTCapewVGAEHPLFILYTSGSTGKPKGVQHSTGG---YLLWA------------AQTMK 240
Cdd:PRK12316 638 ---------AWLEGYSEENPGTE----LNPENLAYVIYTSGSTGKPKGAGNRHRAlsnRLCWMqqayglgvgdtvLQKTP 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 241 WTFDWKPDDVFWctadigwvtghtyitygPLACGGTQVVF-EGVPTWPDagRFWKMIGDHKVTVFYTAPTAIRSLIKAAE 319
Cdd:PRK12316 705 FSFDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDED 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 320 ADdkvhpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQERcpIVDTWWQTETGGHMI--TPLPGATPTVP-GSctlPLP 396
Cdd:PRK12316 766 VA--------SCTSLRRIVCSGEALPADAQEQVFAKLPQAG--LYNLYGPTEAAIDVThwTCVEEGGDSVPiGR---PIA 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 397 GIMAAVVDETGQDVPNGQGGILVVKRpwPAMIRTIWGDP----ERFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGR 472
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELYLAG--RGLARGYHGRPgltaERFVPS--PFVAGERMYRTGD-LARYRADGVIEYAGR 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 473 IDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGrpddTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAK 552
Cdd:PRK12316 908 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE------SEGGDWREALKAHLAASLPEYMV 977
|
570 580
....*....|....*....|...
gi 1860891105 553 PKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK12316 978 PAQWLALERLPLTPNGKLDRKAL 1000
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
41-578 |
1.14e-34 |
|
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: 138.14 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEADDGTVT-RVTYAELLARVSRFANALKKRGiAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVF---GGF 116
Cdd:cd05931 7 PDRPAYTFLDDEGGREeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPpptPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 117 SAKSLNERLVDVGAVALVTADEQArggktlplksiadeavamggcEAVKSVIVYRRTGGKiDWHAGRDLwmheLADAESD 196
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAAL---------------------AAVRAFAASRPAAGT-PRLLVVDL----LPDTSAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 197 TCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDD--VFW--CTADIGWVTGhtyITyGPLA 272
Cdd:cd05931 140 DWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDvvVSWlpLYHDMGLIGG---LL-TPLY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 273 CGGTqVVFegvpTWPDA-----GRFWKMIGDHKVTVFYtAPT-AIRSLIKAAEADDKvhpKSYDLSSLRIIGTVGEPINP 346
Cdd:cd05931 215 SGGP-SVL----MSPAAflrrpLRWLRLISRYRATISA-APNfAYDLCVRRVRDEDL---EGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 347 EAWMWYHK--------------------------HVGQERCPIVDTWWQTETGGHMITPLPGATPTVP-GSCTLPLPGIM 399
Cdd:cd05931 286 ATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARElVSCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 400 AAVVD-ETGQDVPNGQGGILVVKRpwPAMIRTIWGDPERFRKSYYPEE-LGGRLYLA-GD-GTVRDkdtGYFTIMGRIDD 475
Cdd:cd05931 366 VRIVDpETGRELPDGEVGEIWVRG--PSVASGYWGRPEATAETFGALAaTDEGGWLRtGDlGFLHD---GELYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 476 VLNVSGHRLGTMEIESALVSHELV---AEAAVVGRPDDTTGEAVVafVVLKRSRPEGEEAAALAKTLRDWVGKQIGpiAK 552
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERLVV--VAEVERGADPADLAAIAAAIRAAVAREHG--VA 516
|
570 580
....*....|....*....|....*...
gi 1860891105 553 PKDIRFG--DNLPKTRSGKIMRRLLRSL 578
Cdd:cd05931 517 PADVVLVrpGSIPRTSSGKIQRRACRAA 544
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
58-576 |
1.24e-34 |
|
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: 135.55 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVFggfsaksLNERLvdvgavalvTAD 137
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE--AVL-------LNTRL---------TPN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQArggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmHELADAESDTcapewvgaEHPLFILYTSGS 217
Cdd:cd05912 64 ELA-----------------------------------------------FQLKDSDVKL--------DDIATIMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGYLlWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGpLACGGTQVVFEGVptwpDAGRFWKMIG 297
Cdd:cd05912 89 TGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVLHLIN 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 298 DHKVTVFYTAPTAIRSLIKaaeaddkVHPKSYDlSSLRIIGTVGEPINPEAWmwyhkhvgqERC-----PIVDTWWQTET 372
Cdd:cd05912 163 SGKVTIISVVPTMLQRLLE-------ILGEGYP-NNLRCILLGGGPAPKPLL---------EQCkekgiPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 373 GGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQdvPNGQGGILVvKRPwpaMIRtiwgdperfrKSY-YPEELGGRL 451
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQP--PYEVGEILL-KGP---NVT----------KGYlNRPDATEES 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 YL-----AGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSR 526
Cdd:cd05912 290 FEngwfkTGDIGYLDEE-GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1860891105 527 PEGEEAAALAKTLrdwvgkqigpiAK---PKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05912 369 SEEELIAYCSEKL-----------AKykvPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
43-580 |
2.54e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 136.53 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEADDgtvtrVTYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGAThsvvfggfsAKSL 121
Cdd:PRK06839 18 RIAIITEEEE-----MTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI---------AVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDvGAVALVTADEQARggKTLPLKSIADEAVAMGGCEAVKSVIvyRRTGGKidwhagrdlwmhELADAESDTCAPE 201
Cdd:PRK06839 84 NIRLTE-NELIFQLKDSGTT--VLFVEKTFQNMALSMQKVSYVQRVI--SITSLK------------EIEDRKIDNFVEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wvGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfe 281
Cdd:PRK06839 147 --NESASFIICYTSGTTGKPKGAV-LTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 282 gvPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIkaaEADDKVHPksyDLSSLRIIGTVGEPInPEAWMwyhKHVGQERC 361
Cdd:PRK06839 222 --PRKFEPTKALSMIEKHKVTVVMGVPTIHQALI---NCSKFETT---NLQSVRWFYNGGAPC-PEELM---REFIDRGF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 362 PIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKS 441
Cdd:PRK06839 290 LFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVMKEYWNRPDATEET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 442 YYpeelGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVV 521
Cdd:PRK06839 368 IQ----DGWLC-TGDLARVDED-GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 522 LKRSrpegeeAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAK 580
Cdd:PRK06839 442 KKSS------SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
30-592 |
2.83e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 136.83 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 30 NCLDRHVEAGNGQrVAVIFEADDgtvtrVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATh 109
Cdd:PRK07786 21 NQLARHALMQPDA-PALRFLGNT-----TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 110 svvfggfsAKSLNERLVDvGAVALVTADEQARGGKTLPlkSIADEAVAMGGCEAVKSVIVYrrTGGKIDwhaGRDLWMHE 189
Cdd:PRK07786 94 --------AVPVNFRLTP-PEIAFLVSDCGAHVVVTEA--ALAPVATAVRDIVPLLSTVVV--AGGSSD---DSVLGYED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 190 LADAESDTCAPEWVGAEHPLFILYTSGSTGKPKG--VQHSTggyllWAAQTMKWTFDWK---PDDVFWCTADIGWVTGHT 264
Cdd:PRK07786 158 LLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGavLTHAN-----LTGQAMTCLRTNGadiNSDVGFVGVPLFHIAGIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 265 YITYGpLACGGTQVVFegvPTWP-DAGRFWKMIGDHKVTVFYTAPTAIrsliKAAEADDKVHPKsyDLSsLRIIGTVGEP 343
Cdd:PRK07786 233 SMLPG-LLLGAPTVIY---PLGAfDPGQLLDVLEAEKVTGIFLVPAQW----QAVCAEQQARPR--DLA-LRVLSWGAAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 344 IN-----------PEAwmwyhkhvgqercPIVDTWWQTET--------GGHMITPLpgatptvpGSCTLPLPGIMAAVVD 404
Cdd:PRK07786 302 ASdtllrqmaatfPEA-------------QILAAFGQTEMspvtcmllGEDAIRKL--------GSVGKVIPTVAARVVD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 405 ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERfrksyYPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRL 484
Cdd:PRK07786 361 ENMNDVPVGEVGEIVYRAP--TLMSGYWNNPEA-----TAEAFAGGWFHSGD-LVRQDEEGYVWVVDRKKDMIISGGENI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 485 GTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpeGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPK 564
Cdd:PRK07786 433 YCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVR-----NDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPR 507
|
570 580 590
....*....|....*....|....*....|....*
gi 1860891105 565 TRSGKIMRRLLR-------SLAKGEAITQDTSTLE 592
Cdd:PRK07786 508 NPAGKVLKTELRerygacvNVERRSASAGFTERRE 542
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
43-582 |
9.31e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.70 E-value: 9.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThsVVF--GGFSAKS 120
Cdd:PRK03640 18 RTAIEFEE-----KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLlnTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLVDVGAVALVTADEQARggKTLPLKSIADEAVAMGGCEAVKSvivyrrtggKIDWHagrdlwmheLADAESdtcap 200
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA--KLIPGISVKFAELMNGPKEEAEI---------QEEFD---------LDEVAT----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 ewvgaehplfILYTSGSTGKPKGVQHSTGGYLlWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTyITYGPLACGGTQVVF 280
Cdd:PRK03640 146 ----------IMYTSGTTGKPKGVIQTYGNHW-WSAVGSALNLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddKVHPKSYDlSSLRIIGTVGEPINPeawmwyhkhVGQER 360
Cdd:PRK03640 214 EKF----DAEKINKLLQTGGVTIISVVSTMLQRLLE------RLGEGTYP-SSFRCMLLGGGPAPK---------PLLEQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 C-----PIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKrpwPAMIRTIWGDP 435
Cdd:PRK03640 274 CkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDGVVVPPFEEGEIVVKG---PNVTKGYLNRE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 436 ERFRKS-----YYPEELGgrlYLagdgtvrDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDD 510
Cdd:PRK03640 351 DATRETfqdgwFKTGDIG---YL-------DEE-GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDD 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 511 TTGEAVVAFVVLKRSRPEGEeaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGE 582
Cdd:PRK03640 420 KWGQVPVAFVVKSGEVTEEE--------LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
38-577 |
2.70e-33 |
|
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: 133.95 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 38 AGNGQRVAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACarigathsvVFGGFS 117
Cdd:cd05906 20 AERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 118 AKSLnerlvdvgAVALVTADEQARGGKTLPLKSIADEAVAMGGCEAVKSVivyrRTGGKIDWHAGRD-LWMHELADAESD 196
Cdd:cd05906 91 PAPL--------TVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEF----AGLETLSGLPGIRvLSIEELLDTAAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 197 TCAPEwVGAEHPLFILYTSGSTGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDDVF--WCTADigWVTGHTYITYGPLACG 274
Cdd:cd05906 159 HDLPQ-SRPDDLALLMLTSGSTGFPKAVPL-THRNILARSAGKIQHNGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVvfeGVPT---WPDAGRFWKMIGDHKVTVFYtAPTAIRSLIkaAEADDKVHPKSYDLSSLRIIGTVGEPINPEAWMW 351
Cdd:cd05906 235 CQQV---HVPTeeiLADPLRWLDLIDRYRVTITW-APNFAFALL--NDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 352 Y----HKHVGQERCpIVDTWWQTETGGHMITPLPGATPTVPG-----SCTLPLPGIMAAVVDETGQDVPNGQGGILVVKR 422
Cdd:cd05906 309 LlrllEPYGLPPDA-IRPAFGMTETCSGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 423 pwPAMIRTIWGDPERFRKSYYPeelggrlylagDGTVRDKDTGY-----FTIMGRIDDVLNVSGHRLGTMEIESAL---- 493
Cdd:cd05906 388 --PVVTKGYYNNPEANAEAFTE-----------DGWFRTGDLGFldngnLTITGRTKDTIIVNGVNYYSHEIEAAVeevp 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 494 -VSHELVAEAAVvgRPDDT-TGEAVVAFVvlkrsrPEGEEAAALAKTL---RDWVGKQIG-------PIAKpkdirfgDN 561
Cdd:cd05906 455 gVEPSFTAAFAV--RDPGAeTEELAIFFV------PEYDLQDALSETLraiRSVVSREVGvspayliPLPK-------EE 519
|
570
....*....|....*.
gi 1860891105 562 LPKTRSGKIMRRLLRS 577
Cdd:cd05906 520 IPKTSLGKIQRSKLKA 535
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
34-576 |
3.17e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 133.63 E-value: 3.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 34 RHVEAGNGQRVAVIfeadDGTVTrVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVf 113
Cdd:PRK07470 14 RQAARRFPDRIALV----WGDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 ggfsakslNERLVDvGAVALVTADEQARGgkTLPLKSIADEAVAM-GGCEAVKSVIVYRRTGGKIDW------HAGRdlw 186
Cdd:PRK07470 88 --------NFRQTP-DEVAYLAEASGARA--MICHADFPEHAAAVrAASPDLTHVVAIGGARAGLDYealvarHLGA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 187 MHELADAESDTcapewvgaehPLFILYTSGSTGKPKG--VQHSTGGYLL--WAAQTMKWTfdwKPDDVFWCTADIGWVTG 262
Cdd:PRK07470 154 RVANAAVDHDD----------PCWFFFTSGTTGRPKAavLTHGQMAFVItnHLADLMPGT---TEQDASLVVAPLSHGAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 263 HTYITygPLACGGTQVVfegVPTWP-DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVG 341
Cdd:PRK07470 221 IHQLC--QVARGAATVL---LPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVD------RYDHSSLRYVIYAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 342 EPInpeaWMWYHKHVGQERCP-IVDTWWQTETGGHmITPLPGA------TPTVP-GSCTLPLPGIMAAVVDETGQDVPNG 413
Cdd:PRK07470 290 APM----YRADQKRALAKLGKvLVQYFGLGEVTGN-ITVLPPAlhdaedGPDARiGTCGFERTGMEVQIQDDEGRELPPG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 414 QGGILVVKRPwpAMIRTIWGDPERFRKSYYpeelggrlylagDGTVRDKDTGY------FTIMGRIDDVLNVSGHRLGTM 487
Cdd:PRK07470 365 ETGEICVIGP--AVFAGYYNNPEANAKAFR------------DGWFRTGDLGHldargfLYITGRASDMYISGGSNVYPR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 488 EIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRS 567
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAE------LLAWLDGKVARYKLPKRFFFWDALPKSGY 504
|
....*....
gi 1860891105 568 GKIMRRLLR 576
Cdd:PRK07470 505 GKITKKMVR 513
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-582 |
4.75e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 133.40 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAVIFEADDgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEgIVAMQ-ACARIGATHS 110
Cdd:PRK08315 22 LDRTAAR-YPDREALVYRDQG---LRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPE-WVLTQfATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 111 VVFGGFSAKSLNERLVDVGAVALVTAD-------------------EQARGG---KTLP-LKSIadeaVAMGGceavksv 167
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAADgfkdsdyvamlyelapelaTCEPGQlqsARLPeLRRV----IFLGD------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 168 ivyRRTGGKIDWHAGRDLWMHElADAESDTCAPEwVGAEHPLFILYTSGSTGKPKGVQHS-----TGGYllWAAQTMKWT 242
Cdd:PRK08315 166 ---EKHPGMLNFDELLALGRAV-DDAELAARQAT-LDPDDPINIQYTSGTTGFPKGATLThrnilNNGY--FIGEAMKLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 243 fdwkPDD-------VFWCtadIGWVTGHtyitygpLAC---GGTQV----VFegvptwpDAGRFWKMIGDHKVTVFYTAP 308
Cdd:PRK08315 239 ----EEDrlcipvpLYHC---FGMVLGN-------LACvthGATMVypgeGF-------DPLATLAAVEEERCTALYGVP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 309 TAirsLIkaAEADdkvHP--KSYDLSSLR--IIGtvGEPinpeawmwyhkhvgqerCPIvDTWWQTETGGHM--ITPLPG 382
Cdd:PRK08315 298 TM---FI--AELD---HPdfARFDLSSLRtgIMA--GSP-----------------CPI-EVMKRVIDKMHMseVTIAYG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 383 ATPTVPGSC-TLP--------------LPGIMAAVVD-ETGQDVPNGQGGILVVkRPWPAMiRTIWGDPERFRKSYYPEe 446
Cdd:PRK08315 350 MTETSPVSTqTRTddplekrvttvgraLPHLEVKIVDpETGETVPRGEQGELCT-RGYSVM-KGYWNDPEKTAEAIDAD- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 447 lgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsr 526
Cdd:PRK08315 427 --GWMH-TGDLAVMDEE-GYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILR--- 499
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 527 pEGEEAAALAktLRDWVgkqIGPIAK---PKDIRFGDNLPKTRSGKIMRRLLRSLAKGE 582
Cdd:PRK08315 500 -PGATLTEED--VRDFC---RGKIAHykiPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
32-579 |
1.63e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 131.79 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgngqRVAVIFEADDGTVtrVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:PRK06164 16 LDAHARA----RPDAVALIDEDRP--LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTADeqarGGKTLPLKSIADEaVAMGGCEAVKSVIVYRRTGGKIDWHA-GRDLWMHEL 190
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAA-VPPDALPPLRAIAVVDDAADATPAPApGARVQLFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 191 ADAESDTCAPEWVGAEHPLFILY-TSGSTGKPKGVQHSTGGYLLWAAQTMKwTFDWKPDDVFWCTADIGWVTGHTYITyG 269
Cdd:PRK06164 165 PDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTLL-G 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 270 PLACGGTQVVfegVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAeaddkvhPKSYDLSSLRIIGTVGepINPeAW 349
Cdd:PRK06164 243 ALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTA-------GERADFPSARLFGFAS--FAP-AL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 350 MWYHKHVGQERCPIVDTWWQTE-----TGGHMITP-----LPGATPTVpgsctlplPGIMAAVVD-ETGQDVPNGQGGIL 418
Cdd:PRK06164 309 GELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPAS--------PEARVRARDpQDGALLPDGESGEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 419 VVKRpwPAMIRTIWGDPERFRKSYYPeelggrlylagDGTVRDKDTGY------FTIMGRIDDVLNVSGHRLGTMEIESA 492
Cdd:PRK06164 381 EIRA--PSLMRGYLDNPDATARALTD-----------DGYFRTGDLGYtrgdgqFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 493 LVSHELVAEAAVVGRPDDTTGEAvVAFVVLKrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSG---K 569
Cdd:PRK06164 448 LEALPGVAAAQVVGATRDGKTVP-VAFVIPT----DGASPD--EAGLMAACREALAGFKVPARVQVVEAFPVTESAngaK 520
|
570
....*....|
gi 1860891105 570 IMRRLLRSLA 579
Cdd:PRK06164 521 IQKHRLREMA 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
41-576 |
4.46e-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: 129.73 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSvvfggfsakS 120
Cdd:cd12118 18 PDRTSIVYGD-----RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLN---------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLvDVGAVALVTADEQArggktlplksiadeavamggceavKSVIVYRRtggkidwHAGRDLwmheLADAESDtcaP 200
Cdd:cd12118 84 LNTRL-DAEEIAFILRHSEA------------------------KVLFVDRE-------FEYEDL----LAEGDPD---F 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 EWVGAE---HPLFILYTSGSTGKPKGVQHS-TGGYLlwAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYiTYGPLACGGT 276
Cdd:cd12118 125 EWIPPAdewDPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMFHCNGWCF-PWTVAAVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPKsydlsslRIIGTVGEPINPEAWMwyhKHV 356
Cdd:cd12118 202 NVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH-------RVHVMTAGAPPPAAVL---AKM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 GQERCPIVDTWWQTETGGhmitplPGAT-PTVPGSCTLPLP---GIMA------------AVVD-ETGQDVP-NGQ--GG 416
Cdd:cd12118 268 EELGFDVTHVYGLTETYG------PATVcAWKPEWDELPTEeraRLKArqgvryvgleevDVLDpETMKPVPrDGKtiGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 417 ILVVKRpwpAMIRTIWGDPERFRKSyypeeLGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSH 496
Cdd:cd12118 342 IVFRGN---IVMKGYLKNPEATAEA-----FRGGWFHSGDLAVIHPD-GYIEIKDRSKDIIISGGENISSVEVEGVLYKH 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 497 ELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEaaALAKTLRDWVGKQIGPIAKPKDIRFGDnLPKTRSGKIMRRLLR 576
Cdd:cd12118 413 PAVLEAAVVARPDEKWGEVPCAFVELK----EGAK--VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-579 |
2.94e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 124.90 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 213 YTSGSTGKPKGVQHSTGG--YLLWAAQTMKwtfDWKPDDVFWCTADIGWVTGHTYITYGPLACGGtQVVFEGVPTWPDAG 290
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNevYNAWMLALNS---LFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 291 ---RFWKMIGDHKVTVFYTAPTAIRSLIKAaeaddkvhPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIVDTW 367
Cdd:cd05944 85 lfdNFWKLVERYRITSLSTVPTVYAALLQV--------PVNADISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 368 WQTE-TGGHMITPlPGaTPTVPGSCTLPLPGIMAAVVDETG-----QDVPNGQGGILVVKRPwpamirTIWGDperfrks 441
Cdd:cd05944 154 GLTEaTCLVAVNP-PD-GPKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICVAGP------GVFGG------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 442 yYPEELGGRLYLAGDGTVRDKD------TGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEA 515
Cdd:cd05944 219 -YLYTEGNKNAFVADGWLNTGDlgrldaDGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGEL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 516 VVAFVVLKRSRPEGEEAaalaktLRDWVGKQIGP-IAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd05944 298 PVAYVQLKPGAVVEEEE------LLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
43-576 |
3.36e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.94 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIfeadDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:PRK06087 39 KIAVV----DNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTAdeqARGGKTLPLK---SIADEAVAMGGCEAVKsvivyrrtggKIDWHAGRDLWMHELADAESDTCA 199
Cdd:PRK06087 115 WVLNKCQAKMFFAP---TLFKQTRPVDlilPLQNQLPQLQQIVGVD----------KLAPATSSLSLSQIIADYEPLTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 200 PEwVGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVV 279
Cdd:PRK06087 182 IT-THGDELAAVLFTSGTEGLPKGVM-LTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 280 FEGVPtwPDAGrfWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPInPEAWMwyhKHVGQE 359
Cdd:PRK06087 260 LDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEKQ------PADLSALRFFLCGGTTI-PKKVA---RECQQR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 360 RCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFR 439
Cdd:PRK06087 326 GIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGP--NVFMGYLDEPELTA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 440 KSYypEELGgrLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAF 519
Cdd:PRK06087 404 RAL--DEEG--WYYSGDLCRMDEA-GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 520 VVLKRS--RPEGEEAAALAKTLRdwVGKQIgpiaKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK06087 479 VVLKAPhhSLTLEEVVAFFSRKR--VAKYK----YPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
488-569 |
7.55e-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: 114.95 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 488 EIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRS 567
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLK------PGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 1860891105 568 GK 569
Cdd:pfam13193 75 GK 76
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
31-581 |
7.62e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 126.63 E-value: 7.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 31 CLDRHVEAGNgqRVAVIfeadDGTVTRV-TYAE--LLARvsRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGA 107
Cdd:PLN02246 29 CFERLSEFSD--RPCLI----DGATGRVyTYADveLLSR--RVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 108 THSVVFGGFSAKSLNERLVDVGAVALVTadEQARGGKtlpLKSIADEavamggcEAVKSVIvyrrtggkIDWHAGRDLWM 187
Cdd:PLN02246 101 VTTTANPFYTPAEIAKQAKASGAKLIIT--QSCYVDK---LKGLAED-------DGVTVVT--------IDDPPEGCLHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 188 HELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKW---TFDWKPDDVFWCTADIGwvtgHT 264
Cdd:PLN02246 161 SELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpNLYFHSDDVILCVLPMF----HI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 265 YITYGPLACG---GTQVVFegVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVG 341
Cdd:PLN02246 237 YSLNSVLLCGlrvGAAILI--MPKF-EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEK------YDLSSIRMVLSGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 342 EPINPE---AWMwyhkhvgqERCP---IVDTWWQTETGGHMITPLPGA---TPTVPGSCTLPLPGIMAAVVD-ETGQDVP 411
Cdd:PLN02246 308 APLGKEledAFR--------AKLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSCGTVVRNAELKIVDpETGASLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 412 NGQGGILVVKRPwpAMIRTIWGDPERFRKSYYPEelgGRLYlAGDGTVRDKDTGYFtIMGRIDDVLNVSGHRLGTMEIES 491
Cdd:PLN02246 380 RNQPGEICIRGP--QIMKGYLNDPEATANTIDKD---GWLH-TGDIGYIDDDDELF-IVDRLKELIKYKGFQVAPAELEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 492 ALVSHELVAEAAVVGRPDDTTGEAVVAFVVlkrsRPEGEEAAalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIM 571
Cdd:PLN02246 453 LLISHPSIADAAVVPMKDEVAGEVPVAFVV----RSNGSEIT--EDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKIL 526
|
570
....*....|.
gi 1860891105 572 RRLLRS-LAKG 581
Cdd:PLN02246 527 RKDLRAkLAAG 537
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
43-575 |
1.09e-30 |
|
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: 125.52 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:cd17655 13 HTAVVFEDQ-----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTAdeqarggKTLPLKSIADEAVAMGGCEAVKSvivyrrtGGKIDWHAgrdlwmhelaDAESDTCApew 202
Cdd:cd17655 88 YILEDSGADILLTQ-------SHLQPPIAFIGLIDLLDEDTIYH-------EESENLEP----------VSKSDDLA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 vgaehplFILYTSGSTGKPKGV---QHSTGGYLLWAAQTM------------KWTFDWKPDDVFwctadigwvtghtyit 267
Cdd:cd17655 141 -------YVIYTSGSTGKPKGVmieHRGVVNLVEWANKVIyqgehlrvalfaSISFDASVTEIF---------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 yGPLACGGTQVVFEGVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLikaAEADDKVHPksydlsSLRIIGTVGEPINPE 347
Cdd:cd17655 198 -ASLLSGNTLYIVRKETVL-DGQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGL------SLKHLIVGGEALSTE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 348 -AWMWYHKHvgQERCPIVDTWWQTET----GGHMITPLPGATPTVP-GSctlPLPGIMAAVVDETGQDVPNGQGGILVVK 421
Cdd:cd17655 267 lAKKIIELF--GTNPTITNAYGPTETtvdaSIYQYEPETDQQVSVPiGK---PLGNTRIYILDQYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 422 RPWPAmiRTIWGDPERFRKSY--YPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELV 499
Cdd:cd17655 342 GEGVA--RGYLNRPELTAEKFvdDPFVPGERMYRTGD-LARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDI 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 500 AEAAVVGRPDDTTGEAVVAFVVLKRSRPegeeaaalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17655 419 KEAVVIARKDEQGQNYLCAYIVSEKELP--------VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-575 |
1.26e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.74 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 26 NASYNCLDRHVEAGNGQ---RVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQAC 102
Cdd:PRK12467 508 EYAPDCVHQLIEAQARQhpeRPALVFGEQ-----VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 103 ARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADEQARggkTLPLksiadeavamggCEAVKSvivyrrtggkIDWHAG 182
Cdd:PRK12467 583 LKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLA---QLPV------------PAGLRS----------LCLDEP 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 183 RDLWMHELADAESDTCAPEWVGaehplFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWtFDWKPDDVFWCTADIGWVTG 262
Cdd:PRK12467 638 ADLLCGYSGHNPEVALDPDNLA-----YVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 263 HTYItYGPLACGGTQVVFEGVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpksyDLSSLRIIGTVGE 342
Cdd:PRK12467 712 VTEL-FGALASGATLHLLPPDCAR-DAEAFAALMADQGVTVLKIVPSHLQALLQASRVA--------LPRPQRALVCGGE 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 343 PINPEAW-MWYHKHVGqerCPIVDTWWQTETGGHMITPLPGATPTVPGSCTL--PLPGIMAAVVDETGQDVPNGQGGILV 419
Cdd:PRK12467 782 ALQVDLLaRVRALGPG---ARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDHYLNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 420 VKRPWPAmiRTIWGDP----ERFRKSYYPEElGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVS 495
Cdd:PRK12467 859 IGGAGLA--RGYHRRPaltaERFVPDPFGAD-GGRLYRTGDLARYRAD-GVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 496 HELVAEAAVVGRPDDtTGEAVVAFVVLKRSrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK12467 935 QPGVREAVVLAQPGD-AGLQLVAYLVPAAV-ADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
36-576 |
1.36e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 125.76 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 36 VEAGNGQRVAVIFEADDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAthsvVF-- 113
Cdd:PRK07514 9 LRAAFADRDAPFIETPDGL--RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 --GGFSAKSLNERLVDVGAvALVTADEQARGGktlpLKSIADEAvamggceAVKSVivyrRTGGkidwhAGRDLWMHELA 191
Cdd:PRK07514 83 lnTAYTLAELDYFIGDAEP-ALVVCDPANFAW----LSKIAAAA-------GAPHV----ETLD-----ADGTGSLLEAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPL 271
Cdd:PRK07514 142 AAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 272 ACGGTQV------------------VFEGVPTwpdagrfwkmigdhkvtvFYTAPTAIRSLIKAAEAddkvhpksydlsS 333
Cdd:PRK07514 221 LAGASMIflpkfdpdavlalmpratVMMGVPT------------------FYTRLLQEPRLTREAAA------------H 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 334 LRIIGTVGEPINPE---AWmwyhkhvgQERC--PIVDTWWQTETGghMITPLPGATPTVPGSCTLPLPGIMAAVVD-ETG 407
Cdd:PRK07514 271 MRLFISGSAPLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDpETG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 408 QDVPNGQGGILVVKRPwpAMIRTIWGDPER----FRKSYYpeelggrlYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHR 483
Cdd:PRK07514 341 AELPPGEIGMIEVKGP--NVFKGYWRMPEKtaeeFRADGF--------FITGDLGKIDER-GYVHIVGRGKDLIISGGYN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 484 LGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAfVVLKRSRPEGEEAAALAkTLRdwvgkqiGPIAK---PKDIRFGD 560
Cdd:PRK07514 410 VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGAALDEAAILA-ALK-------GRLARfkqPKRVFFVD 480
|
570
....*....|....*.
gi 1860891105 561 NLPKTRSGKIMRRLLR 576
Cdd:PRK07514 481 ELPRNTMGKVQKNLLR 496
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
57-576 |
1.03e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 122.88 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVT- 135
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 AD--EQARGG-----KTLPLKSIADEAVAMGGCEAVKSVivyrrTGGKIDWhagrDLWmheLADAESDTCAPewvgAEHP 208
Cdd:PRK12406 91 ADllHGLASAlpagvTVLSVPTPPEIAAAYRISPALLTP-----PAGAIDW----EGW---LAQQEPYDGPP----VPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 209 LFILYTSGSTGKPKGVQHS--TGGYLLWAAQTMKWTFDWKPDDVFWCTadigwvtGHTYITyGPLACG------GTQVVF 280
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLT-------GPLYHS-APNAYGlragrlGGVLVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EgvPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkVHPKsYDLSSLRIIGTVGEPINPEawmwyhkhVGQEr 360
Cdd:PRK12406 227 Q--PRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEE---VRAK-YDVSSLRHVIHAAAPCPAD--------VKRA- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 cpIVDtWW---------QTETGghMITplpGATP----TVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAM 427
Cdd:PRK12406 291 --MIE-WWgpviyeyygSTESG--AVT---FATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 428 IrTIWGDPERFRKSyypeELGGrLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGR 507
Cdd:PRK12406 363 F-TYHNKPEKRAEI----DRGG-FITSGDVGYLDAD-GYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGI 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 508 PDDTTGEAVVAFVvlkRSRPEGE-EAAALAKTLRDWVGKqigpIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK12406 436 PDAEFGEALMAVV---EPQPGATlDEADIRAQLKARLAG----YKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-576 |
3.07e-29 |
|
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: 118.92 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 PLFILYTSGSTGKPKGV---QHS--TGGYLLwaAQTMKWTFDWK---PDDVFWCtadIGWVTGHtyitygpLAC--GGTQ 277
Cdd:cd05917 4 VINIQFTSGTTGSPKGAtltHHNivNNGYFI--GERLGLTEQDRlciPVPLFHC---FGSVLGV-------LACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 278 VVFEGvPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddkvHPK--SYDLSSLR--IIGtvGEPINPEAWMWYH 353
Cdd:cd05917 72 MVFPS-PSF-DPLAVLEAIEKEKCTALHGVPTMFIAELE--------HPDfdKFDLSSLRtgIMA--GAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 KHVGQERCPIVdtWWQTETGghmitplPGATPTVPG--------SCTLPLPGIMAAVVDETGQDVPN-GQGGILVVkRPW 424
Cdd:cd05917 140 EVMNMKDVTIA--YGMTETS-------PVSTQTRTDdsiekrvnTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCI-RGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 PAMiRTIWGDPERFRKSyypeELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd05917 210 SVM-KGYWNDPEKTAEA----IDGDGWLHTGDLAVMDED-GYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 505 VGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05917 284 VGVPDERYGEEVCAWIRLK------EGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
59-577 |
4.66e-29 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 121.40 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGIAKGDRVVIyMPMSIEGIV-AMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGI-MCRNHRGFVeALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EqarggktlpLKSIADEAVAmGGCEAVKSVivyrrtggkiDWHAGRDLWMHELADAESDTCAPEWVGaEHPLFILYTSGS 217
Cdd:PRK13382 149 E---------FSATVDRALA-DCPQATRIV----------AWTDEDHDLTVEVLIAAHAGQRPEPTG-RKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGYLLWAAQTMKWTfDWKPDDVFWCTADIGWVTGHTYITY-GPLACGG-TQVVFEgvptwPDAGrfWKM 295
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKAILDRT-PWRAEEPTVIVAPMFHAWGFSQLVLaASLACTIvTRRRFD-----PEAT--LDL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 296 IGDHKVTVFYTAPTAIRSLIkaaEADDKVHpKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTWWQTETGgh 375
Cdd:PRK13382 280 IDRHRATGLAVVPVMFDRIM---DLPAEVR-NRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNATEAG-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 376 MITPlpgATP----TVPGSCTLPLPGIMAAVVDETGQDVPNGQGGilvvkrpwpamirTIWGDPERFRKSYYPeelgGRL 451
Cdd:PRK13382 351 MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQDFREVPTGEVG-------------TIFVRNDTQFDGYTS----GST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 YLAGDGTVRDKDTGYFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrs 525
Cdd:PRK13382 411 KDFHDGFMASGDVGYLDengrlfVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK-- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 526 rpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK13382 489 ----PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
211-576 |
6.44e-29 |
|
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: 120.17 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWT--FDWKPDDVFWCTADIGWVTGHTYiTYGPLACGGTQVVFEGVptwpD 288
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAAlgFGPGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 289 AGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhPKSYDLSSLRIIGTVGEPINP---EAWM-W-----YHKHVGQE 359
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAV----RNAYDLSSLKRVIHAAAPCPPwvkEQWIdWggpiiWEYYGGTE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 360 R---CPIVDTWWQTetggHmitplpgatptvPGSCTLPLPGIMAaVVDETGQDVPNGQGGILVVKRPWP--AMIRTIWGD 434
Cdd:cd05929 281 GqglTIINGEEWLT----H------------PGSVGRAVLGKVH-ILDEDGNEVPPGEIGEVYFANGPGfeYTNDPEKTA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PERFRKSYypEELGGRLYLAGDGTVrdkdtgYFTimGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGE 514
Cdd:cd05929 344 AARNEGGW--STLGDVGYLDEDGYL------YLT--DRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQ 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 515 AVVAFVvlkRSRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05929 414 RVHAVV---QPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-575 |
7.59e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.14 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:PRK12316 2018 EAIAVVFGDQ-----HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERL 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVT-ADEQARggktLPLksiadeavamggceavksvivyrrTGGKIDWHAGRDLWMheladAESDTCAP 200
Cdd:PRK12316 2093 AYMLEDSGAALLLTqRHLLER----LPL------------------------PAGVARLPLDRDAEW-----ADYPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 EWVGAEHPL-FILYTSGSTGKPKGVQHSTG---GYLLWAAQT------------MKWTFDWKPDDVFWctadigwvtght 264
Cdd:PRK12316 2140 AVQLAGENLaYVIYTSGSTGLPKGVAVSHGalvAHCQAAGERyelspadcelqfMSFSFDGAHEQWFH------------ 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 265 yitygPLaCGGTQVVFEGVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvHPksydlSSLRIIGTVGEPI 344
Cdd:PRK12316 2208 -----PL-LNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG--RP-----PAVRVYCFGGEAV 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 345 NPEAWMWYHKHVGQERcpIVDTWWQTETgghMITPL--------PGATPTVP-GSctlPLPGIMAAVVDETGQDVPNGQG 415
Cdd:PRK12316 2274 PAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLlwkcrpqdPCGAAYVPiGR---ALGNRRAYILDADLNLLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 416 GILVVKRPWPAmiRTIWGDP----ERFRKSYYpEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIES 491
Cdd:PRK12316 2346 GELYLGGEGLA--RGYLNRPgltaERFVPDPF-SASGERLYRTGD-LARYRADGVVEYLGRIDHQVKIRGFRIELGEIEA 2421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 492 ALVSHELVAEAAVVGRpDDTTGEAVVAFVVlkrsrpeGEEAAA-LAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKI 570
Cdd:PRK12316 2422 RLQAHPAVREAVVVAQ-DGASGKQLVAYVV-------PDDAAEdLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
....*
gi 1860891105 571 MRRLL 575
Cdd:PRK12316 2494 DRKAL 2498
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
42-575 |
1.01e-28 |
|
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: 118.89 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:cd17652 2 DAPAVVFGDE-----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTAdeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcape 201
Cdd:cd17652 77 AYMLADARPALLLTT----------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 wvgAEHPLFILYTSGSTGKPKGV--QHsTGGYLLWAAQTMKwtFDWKPDDVFWCTADIGWVTGHTYITyGPLACGGTQVV 279
Cdd:cd17652 92 ---PDNLAYVIYTSGSTGRPKGVvvTH-RGLANLAAAQIAA--FDVGPGSRVLQFASPSFDASVWELL-MALLAGATLVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 280 FEGVPTWPDAGrFWKMIGDHKVTVFYTAPTAIRSLikaaEADDkvhpksydLSSLRIIGTVGEPINPEawmwyhkhvgqe 359
Cdd:cd17652 165 APAEELLPGEP-LADLLREHRITHVTLPPAALAAL----PPDD--------LPDLRTLVVAGEACPAE------------ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 360 rcpIVDTWWQ----------TET--GGHMITPLPGATPTVPGSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAM 427
Cdd:cd17652 220 ---LVDRWAPgrrminaygpTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARLRPVPPGVPGELYIAGA--GL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 428 IRTIWGDPERFRKSYYPE---ELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:cd17652 292 ARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRAD-GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 505 VGRPDDTTGEAVVAFVVlkrsrPEGEEAAAlAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17652 371 VVRDDRPGDKRLVAYVV-----PAPGAAPT-AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
58-576 |
1.83e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 119.22 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAthsvVFggfsaKSLNERLvDVGAVALVTAD 137
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA----VF-----LPINYRL-AADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQARggktlpLKSIADEAVAMGGCEAVKSVIvyrrtggkiDWHAGRDlwMHELAdAESDTCAPEWVGAEHPLF-ILYTSG 216
Cdd:PRK06145 98 AGAK------LLLVDEEFDAIVALETPKIVI---------DAAAQAD--SRRLA-QGGLEIPPQAAVAPTDLVrLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGgyllwaaqtmkwTFDWKPDDVfwcTADIGWVTGHTYITYGPL----ACG--GTQVVFEG----VPTW 286
Cdd:PRK06145 160 TTDRPKGVMHSYG------------NLHWKSIDH---VIALGLTASERLLVVGPLyhvgAFDlpGIAVLWVGgtlrIHRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 287 PDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPiNPEAWMWYHKHVGQeRCPIVDT 366
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD------RFDLDSLAWCIGGGEK-TPESRIRDFTRVFT-RARYIDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 367 WWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYYpee 446
Cdd:PRK06145 297 YGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFY--- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 447 lgGRLYLAGDGTVRDkDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsr 526
Cdd:PRK06145 372 --GDWFRSGDVGYLD-EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLN--- 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1860891105 527 pegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK06145 446 ---PGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
58-522 |
2.43e-28 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 118.08 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvgAEHPLFILYTSGS 217
Cdd:cd05907 86 -------------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTWPDAgrfwkmIG 297
Cdd:cd05907 99 TGRPKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDD------LS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 298 DHKVTVFYTAPTAIRSLIKAAEAdDKVHP---KSYDL---SSLRIIGTVGEPINPEAWMWYHKhVGqerCPIVDTWWQTE 371
Cdd:cd05907 172 EVRPTVFLAVPRVWEKVYAAIKV-KAVPGlkrKLFDLavgGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGHMITPLPGAtpTVPGSCTLPLPGIMAAVVDEtgqdvpngqgGILVVKRpwPAMIRTIWGDPERFRksyypEELGGRL 451
Cdd:cd05907 247 TSAVVTLNPPGD--NRIGTVGKPLPGVEVRIADD----------GEILVRG--PNVMLGYYKNPEATA-----EALDADG 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 452 YLA-GD-GTVrdKDTGYFTIMGRIDDVL-NVSGHRLGTMEIESALVSHELVAEAAVVG--RPddttgeAVVAFVVL 522
Cdd:cd05907 308 WLHtGDlGEI--DEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRP------FLVALIVP 375
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
44-575 |
4.10e-28 |
|
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: 117.57 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 44 VAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNE 123
Cdd:cd17650 4 IAVSDAT-----RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 124 RLVDVGAVALVTadeqarggktLPlksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewv 203
Cdd:cd17650 79 MLEDSGAKLLLT----------QP-------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 204 gaEHPLFILYTSGSTGKPKGV----QHSTGGYLLW------------AAQTMKWTFDwkpddVFwcTADIGWVtghtyit 267
Cdd:cd17650 93 --EDLAYVIYTSGTTGKPKGVmvehRNVAHAAHAWrreyeldsfpvrLLQMASFSFD-----VF--AGDFARS------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 ygpLACGGTQVVfegVP--TWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIkaaeadDKVHPKSYDLSSLRIIgTVGEPIN 345
Cdd:cd17650 157 ---LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVM------AYVYRNGLDLSAMRLL-IVGSDGC 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 346 PEAW-MWYHKHVGQeRCPIVDTWWQTET--------GGhmITPLPGATPTVPGSctlPLPGIMAAVVDETGQDVPNGQGG 416
Cdd:cd17650 224 KAQDfKTLAARFGQ-GMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERLQPQPVGVAG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 417 ILVVKRPWPAmiRTIWGDPERFRKSYYPEEL--GGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALV 494
Cdd:cd17650 298 ELYIGGAGVA--RGYLNRPELTAERFVENPFapGERMYRTGD-LARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLA 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 495 SHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAALAKTLRDW-VGKQIGPIakpkdirfgDNLPKTRSGKIMRR 573
Cdd:cd17650 375 RHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYmIPSYYVQL---------DALPLTPNGKVDRR 445
|
..
gi 1860891105 574 LL 575
Cdd:cd17650 446 AL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-575 |
8.70e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.88 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:PRK12467 1589 EAVALVFGEQ-----ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERL 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTADE-QARggktLPLKsiadeavamggcEAVKSVIVYRRTggkiDWHAGRDLWMHELAdaesdtcap 200
Cdd:PRK12467 1664 AYMIEDSGIELLLTQSHlQAR----LPLP------------DGLRSLVLDQED----DWLEGYSDSNPAVN--------- 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 ewVGAEHPLFILYTSGSTGKPKGVQHSTGGYLlwaaQTMKWTFDWkpddvFWCTADIGWVTGHTYI-------TYGPLaC 273
Cdd:PRK12467 1715 --LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEA-----YQLSAADVVLQFTSFAfdvsvweLFWPL-I 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 274 GGTQVVFEGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkVHPksydlSSLRIIGTVGEPINPEA---WM 350
Cdd:PRK12467 1783 NGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV--EHP-----LSLRRVVCGGEALEVEAlrpWL 1855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 351 wyhkhvgqERCP---IVDTWWQTETGGHMIT-PLPGATPTVPGSCTL--PLPGIMAAVVDETGQDVPNGQGGILVV---- 420
Cdd:PRK12467 1856 --------ERLPdtgLFNLYGPTETAVDVTHwTCRRKDLEGRDSVPIgqPIANLSTYILDASLNPVPIGVAGELYLggvg 1927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 421 -KRPW---PAMirtiwgDPERFRKSYYpEELGGRLYLAGDGTvRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSH 496
Cdd:PRK12467 1928 lARGYlnrPAL------TAERFVADPF-GTVGSRLYRTGDLA-RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQ 1999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 497 ELVAEAAVVGRpDDTTGEAVVAFVV-LKRSRPEGEEA-AALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRL 574
Cdd:PRK12467 2000 GGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKA 2078
|
.
gi 1860891105 575 L 575
Cdd:PRK12467 2079 L 2079
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
192-577 |
9.25e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 116.63 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDTCAPEwVGAEHPLFILYTSGSTGKPKGVQ---HSTGGYLLWAAQTMKWTfdwkPDDVFWCTADIGWVTGHTYITY 268
Cdd:PRK07787 115 HARSWHRYPE-PDPDAPALIVYTSGTTGPPKGVVlsrRAIAADLDALAEAWQWT----ADDVLVHGLPLFHVHGLVLGVL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 269 GPLACGGTqVVFEGVPTwPDAgrfWKMIGDHKVTVFYTAPTaIRSLIkaaeADDKVHPKSydLSSLRII--GTVGEPInp 346
Cdd:PRK07787 190 GPLRIGNR-FVHTGRPT-PEA---YAQALSEGGTLYFGVPT-VWSRI----AADPEAARA--LRGARLLvsGSAALPV-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 347 eawmwyhkHVGQERC-----PIVDTWWQTETgghMITPLPGAT-PTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGI--L 418
Cdd:PRK07787 256 --------PVFDRLAaltghRPVERYGMTET---LITLSTRADgERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVgeL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 419 VVKRPW--------PAMIRTIWGDPERFRksyypeelggrlylAGDGTVRDKDtGYFTIMGRID-DVLNVSGHRLGTMEI 489
Cdd:PRK07787 325 QVRGPTlfdgylnrPDATAAAFTADGWFR--------------TGDVAVVDPD-GMHRIVGREStDLIKSGGYRIGAGEI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 490 ESALVSHELVAEAAVVGRPDDTTGEAVVAFVVlkrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGK 569
Cdd:PRK07787 390 ETALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVA--ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGK 461
|
....*...
gi 1860891105 570 IMRRLLRS 577
Cdd:PRK07787 462 VLKKQLLS 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
41-583 |
1.12e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 117.36 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPmsieGIVAMqacarIGATHSVVFGGFSAKS 120
Cdd:PRK08162 32 PDRPAVIHGD-----RRRTWAETYARCRRLASALARRGIGRGDTVAVLLP----NIPAM-----VEAHFGVPMAGAVLNT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LNERLvDVGAVALVTADEQARGGKTLP-LKSIADEAVAMGGCEAVKSVIV----YR--RTGGKIDWHAgrdlWMHElADA 193
Cdd:PRK08162 98 LNTRL-DAASIAFMLRHGEAKVLIVDTeFAEVAREALALLPGPKPLVIDVddpeYPggRFIGALDYEA----FLAS-GDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 194 ESDTCAP--EWvgaeHPLFILYTSGSTGKPKGV-QHSTGGYLLWAAQTMKWtfDWKPDDV-------FWCTadiGWVTGH 263
Cdd:PRK08162 172 DFAWTLPadEW----DAIALNYTSGTTGNPKGVvYHHRGAYLNALSNILAW--GMPKHPVylwtlpmFHCN---GWCFPW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 264 TyITygplACGGTQVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKV--HPksydlsslrIIGTVG 341
Cdd:PRK08162 243 T-VA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGidHP---------VHAMVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 342 EPINPEAWMWYHKHVGQErcpIVDTWWQTETGGHMitplpgatpTV----PGSCTLPLP---------GIM------AAV 402
Cdd:PRK08162 305 GAAPPAAVIAKMEEIGFD---LTHVYGLTETYGPA---------TVcawqPEWDALPLDeraqlkarqGVRyplqegVTV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 403 VD-ETGQDVPN-GQ--GGILvvkrpwpamirtiwgdperFR-----KSYYP------EELGGRLYLAGDGTVRDKDtGYF 467
Cdd:PRK08162 373 LDpDTMQPVPAdGEtiGEIM-------------------FRgnivmKGYLKnpkateEAFAGGWFHTGDLAVLHPD-GYI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 468 TIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpegEEAAALAKTLRDWVGKQI 547
Cdd:PRK08162 433 KIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK------DGASATEEEIIAHCREHL 506
|
570 580 590
....*....|....*....|....*....|....*.
gi 1860891105 548 GPIAKPKDIRFGDnLPKTRSGKIMRRLLRSLAKGEA 583
Cdd:PRK08162 507 AGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSLK 541
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
58-578 |
2.48e-27 |
|
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: 116.09 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAK----SLNERLVDVGAVAL 133
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNEReldhSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 134 VTADEQARGGKTLPLKS---IADEAVAMGGCEAVKSVIVYRRTGGKidwhagrdlwmheladAESDTCAPEWVGAEHPLF 210
Cdd:cd17642 125 KGLQKVLNVQKKLKIIKtiiILDSKEDYKGYQCLYTFITQNLPPGF----------------NEYDFKPPSFDRDEQVAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFegVPTWpDAG 290
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVL--MYKF-EEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 291 RFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIV-DTWWQ 369
Cdd:cd17642 266 LFLRSLQDYKVQSALLVPTLFAFFAKSTLVD------KYDLSNLHEIASGGAPLSKEVGEAVAKRFK---LPGIrQGYGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 370 TE-TGGHMITPlpgATPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPwpaMIRtiwgdperfrKSYYPEEL 447
Cdd:cd17642 337 TEtTSAILITP---EGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP---MIM----------KGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 448 GGRLYLAGDGTVRDKDTGY------FTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVV 521
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYydedghFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 522 LKRSRPEGEeaaalaKTLRDWVGKQIGPIAKPK-DIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:cd17642 481 LEAGKTMTE------KEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
43-579 |
1.91e-26 |
|
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: 113.02 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVifEADDGtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGathsvvfGGFsaksln 122
Cdd:cd05918 15 APAV--CAWDG---SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-------GAF------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 erlvdvgaVALVTADEQARggktlpLKSIadeavamggCEAVKSVIVyrrtggkidwhagrdlwmheLADAESDtcapew 202
Cdd:cd05918 77 --------VPLDPSHPLQR------LQEI---------LQDTGAKVV--------------------LTSSPSD------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 vgaehPLFILYTSGSTGKPKGV--QH---STG----GYLLWAAQTMKW------TFDwkpddVfwCTADIgwvtghtyit 267
Cdd:cd05918 108 -----AAYVIFTSGSTGKPKGVviEHralSTSalahGRALGLTSESRVlqfasyTFD-----V--SILEI---------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 YGPLACGGTqVVfegVPtwPDAGR---FWKMIGDHKVT-VFYTaPTAIRSLikaaeaddkvHPKsyDLSSLRIIGTVGEP 343
Cdd:cd05918 166 FTTLAAGGC-LC---IP--SEEDRlndLAGFINRLRVTwAFLT-PSVARLL----------DPE--DVPSLRTLVLGGEA 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 344 INPEawmwyhkhvgqercpIVDTWWQ----------TETGGHMIT--PLPGATPTVPGsctLPLPGImAAVVDETGQD-- 409
Cdd:cd05918 227 LTQS---------------DVDTWADrvrlinaygpAECTIAATVspVVPSTDPRNIG---RPLGAT-CWVVDPDNHDrl 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 410 VPNGQGGILVVKRPwpAMIRTIWGDPERFRKSYYP---------EELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVS 480
Cdd:cd05918 288 VPIGAVGELLIEGP--ILARGYLNDPEKTAAAFIEdpawlkqegSGRGRRLYRTGD-LVRYNPDGSLEYVGRKDTQVKIR 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 481 GHR--LGtmEIESALVSH---ELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEG-----------EEAAALAKTLRDWVG 544
Cdd:cd05918 365 GQRveLG--EIEHHLRQSlpgAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsDEFRALVAELRSKLR 442
|
570 580 590
....*....|....*....|....*....|....*
gi 1860891105 545 KQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd05918 443 QRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
42-576 |
2.38e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 112.79 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFeADDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:PRK13390 12 DRPAVIV-AETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTadeqarggkTLPLKSIADEAvamGGCEAVKSVIvyrrtGGKIDwhagrdlwmhELADAESDTCAPE 201
Cdd:PRK13390 89 DYIVGDSGARVLVA---------SAALDGLAAKV---GADLPLRLSF-----GGEID----------GFGSFEAALAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAEHPL--FILYTSGSTGKPKGVQ--------HSTGGYLLWAAQTMkwtFDWKPDDVFWCTADIGwvtgHTyityGPL 271
Cdd:PRK13390 142 PRLTEQPCgaVMLYSSGTTGFPKGIQpdlpgrdvDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 272 -------ACGGTQVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAaeaDDKVHPKsYDLSSLRIIGTVGEPI 344
Cdd:PRK13390 211 rwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKL---DADVRTR-YDVSSLRAVIHAAAPC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 345 NPEAWMWYHKHVGqercPIVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAaVVDETGQDVPNGQGGILVVKRPw 424
Cdd:PRK13390 283 PVDVKHAMIDWLG----PIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGDLH-ICDDDGNELPAGRIGTVYFERD- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 pAMIRTIWGDPERFRKSYYPEElgGRLYLAGD-GTVRDKdtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAA 503
Cdd:PRK13390 357 -RLPFRYLNDPEKTAAAQHPAH--PFWTTVGDlGSVDED--GYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVA 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860891105 504 VVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK13390 432 VIGVPDPEMGEQVKAVIQLVEGIRGSDE---LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
209-569 |
3.60e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 110.16 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 209 LFILYTSGSTGKPKGV---QHSTGGYLLWAAQTMK--WTFDWKPDDVFWCTADIGWVT------GHTYITYGPLACGGTQ 277
Cdd:cd05924 6 LYILYTGGTTGMPKGVmwrQEDIFRMLMGGADFGTgeFTPSEDAHKAAAAAAGTVMFPapplmhGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 278 VVFEGVPTWPDAgrFWKMIGDHKVTVFYTAPTAI-RSLIKAAEAddkvhPKSYDLSSLRIIGTVGEPINPEawmwyHKHV 356
Cdd:cd05924 86 VVLPDDRFDPEE--VWRTIEKHKVTSMTIVGDAMaRPLIDALRD-----AGPYDLSSLFAISSGGALLSPE-----VKQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 GQERCP---IVDTWWQTETGGHMITPlpgATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwPAMIRTIWG 433
Cdd:cd05924 154 LLELVPnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARR-GHIPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 434 DPERFRKSYyPEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:cd05924 230 DEAKTAETF-PEVDGVRYAVPGDRATVEAD-GTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 514 EAVVAFVVLKR-SRPEGEEaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGK 569
Cdd:cd05924 308 QEVVAVVQLREgAGVDLEE-------LREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
32-522 |
6.35e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 112.50 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAgNGQRVAvIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:COG1022 17 LRRRAAR-FPDRVA-LREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTAD-EQARggktlPLKSIADEavamggCEAVKSVIVYRRTGGK-----IDWHA---- 181
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDqEQLD-----KLLEVRDE------LPSLRHIVVLDPRGLRddprlLSLDEllal 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 182 GRDLWMHELADAESDTcapewVGAEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVF-----WCtad 256
Cdd:COG1022 164 GREVADPAELEARRAA-----VKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 257 igWVTGHTyITYGPLACGGTQVVFEGV-----------PTW----PdagRFWKMI-----------GDHKVTVFYTA-PT 309
Cdd:COG1022 235 --HVFERT-VSYYALAAGATVAFAESPdtlaedlrevkPTFmlavP---RVWEKVyagiqakaeeaGGLKRKLFRWAlAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 310 AIRslIKAAEADDKVHPKSYDL------------------SSLRIIGTVGEPINPEAWMWYHKhVGqerCPIVDTWWQTE 371
Cdd:COG1022 309 GRR--YARARLAGKSPSLLLRLkhaladklvfsklrealgGRLRFAVSGGAALGPELARFFRA-LG---IPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGhMIT-PLPGAtpTVPGSCTLPLPGIMAAVVDEtgqdvpngqgGILVVKRPwpamirTI----WGDPERFRKSYYPEE 446
Cdd:COG1022 383 TSP-VITvNRPGD--NRIGTVGPPLPGVEVKIAED----------GEILVRGP------NVmkgyYKNPEATAEAFDADG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 447 lggrlYLA-GD-GTVrDKDtGYFTIMGRIDDVLNVSGhrlGTM----EIESALVSHELVAEAAVVG--RPddttgeAVVA 518
Cdd:COG1022 444 -----WLHtGDiGEL-DED-GFLRITGRKKDLIVTSG---GKNvapqPIENALKASPLIEQAVVVGdgRP------FLAA 507
|
....
gi 1860891105 519 FVVL 522
Cdd:COG1022 508 LIVP 511
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
32-582 |
7.07e-26 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 111.64 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVEAGNGQRVAVIFEADDGTvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSV 111
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDGT-SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 112 VFGGFSAKSLNERLVDVGAVALVTADEQARGGKTLPLKSIADEAVAMGgceaVKSVIVYRRTGGKIDWHAGRdlwmhela 191
Cdd:PRK05857 96 ADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVD----IAAVTRESEHSLDAASLAGN-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 daesdtcaPEWvGAEHPLFILYTSGSTGKPKGVqhstggyLLwaaqtmkwtfdwkPDDVFWCTADI---------GWVTG 262
Cdd:PRK05857 164 --------ADQ-GSEDPLAMIFTSGTTGEPKAV-------LL-------------ANRTFFAVPDIlqkeglnwvTWVVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 263 HTyiTYGPLAC---GGTQVVFEG-------VPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydls 332
Cdd:PRK05857 215 ET--TYSPLPAthiGGLWWILTClmhgglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVP------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 333 SLRIIGTVGEPInPEAWMWYHKHVGQERCPIvdtWWQTETGGHMITpLPGATPTVP----GSCTLPLPGIMAAVVDETGQ 408
Cdd:PRK05857 287 SLRLVGYGGSRA-IAADVRFIEATGVRTAQV---YGLSETGCTALC-LPTDDGSIVkieaGAVGRPYPGVDVYLAATDGI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 409 DvPNGQG-------GILVVKRpwPAMIRTIWGDPERFRksyypEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSG 481
Cdd:PRK05857 362 G-PTAPGagpsasfGTLWIKS--PANMLGYWNNPERTA-----EVLIDGWVNTGDLLERRED-GFFYIKGRSSEMIICGG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 482 HRLGTMEIESALVSHELVAEAAVVGRPDDTTGeAVVAFVVLKRSRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDN 561
Cdd:PRK05857 433 VNIAPDEVDRIAEGVSGVREAACYEIPDEEFG-ALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTD 511
|
570 580
....*....|....*....|.
gi 1860891105 562 LPKTRSGKIMRRLLRSLAKGE 582
Cdd:PRK05857 512 IPRTQSGKVMRASLAAAATAD 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
58-575 |
1.42e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.95 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALvtad 137
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLL---- 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarggktlplksIADEAV--AMGGCEAvksvivyrrtgGKIDWHAGRDLwmhELADAESDTCAPEWVGAEHPLFILYTS 215
Cdd:PRK05691 2290 -------------LSDRALfeALGELPA-----------GVARWCLEDDA---AALAAYSDAPLPFLSLPQHQAYLIYTS 2342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 216 GSTGKPKGVQHSTGGYLLWAAQTMKwTFDWKPDDvfwCTAdigwvtgHTY-ITYG--------PLACGGtQVVFEGVPTW 286
Cdd:PRK05691 2343 GSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL-------HFYsINFDaaserllvPLLCGA-RVVLRAQGQW 2410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 287 pDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydlssLRIIGTVGEPINPEAWmwyhKHVGQERCP--IV 364
Cdd:PRK05691 2411 -GAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP-------VRMCITGGEALTGEHL----QRIRQAFAPqlFF 2478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 365 DTWWQTETgghMITPLPGATP-TVP-GSCTLPLPGIM----AAVVDETGQDVPNGQGGILVV----------KRpwPAMi 428
Cdd:PRK05691 2479 NAYGPTET---VVMPLACLAPeQLEeGAASVPIGRVVgarvAYILDADLALVPQGATGELYVggaglaqgyhDR--PGL- 2552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 429 rtiwgDPERFRKSYYPEElGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRp 508
Cdd:PRK05691 2553 -----TAERFVADPFAAD-GGRLYRTGD-LVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL- 2624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 509 DDTTGEAVVAFVVLKRSRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK05691 2625 DTPSGKQLAGYLVSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
58-576 |
1.43e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 110.84 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIE-GIVAMQACARIGathsvVFGGFSAKSLNERLVD----VGAVA 132
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEyGIVALGIMAAGG-----VFSGANPTALESEIKKqaeaAGAKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 133 LVTADEQARGGKTLPLKSIadeavamggceavksVIVYRRTGGKIDWhagRDLWmhELADAESDTCAPEWVGAEHPLFIL 212
Cdd:PLN02330 131 IVTNDTNYGKVKGLGLPVI---------------VLGEEKIEGAVNW---KELL--EAADRAGDTSDNEEILQTDLCALP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 213 YTSGSTGKPKGVQHSTGGYLLWAAQTMkwtFDWKPDDVFWCTAdIGWVT-----GHTYITYGPLACGGTQVVFEGVptwp 287
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANLCSSL---FSVGPEMIGQVVT-LGLIPffhiyGITGICCATLRNKGKVVVMSRF---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRI--IGTVGEPINPEAWMWYHKHVG----QERC 361
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEE------FDLSKLKLqaIMTAAAPLAPELLTAFEAKFPgvqvQEAY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 362 PIVDTWWQTETGGhmiTPLPGATPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVkRPWPAMIrtiwgdperfrk 440
Cdd:PLN02330 337 GLTEHSCITLTHG---DPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCV-RSQCVMQ------------ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 SYYPEELGGRLYLAGDGTVRDKDTGYFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGE 514
Cdd:PLN02330 401 GYYNNKEETDRTIDEDGWLHTGDIGYIDddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 515 AVVAFVVLKRSRPEGEEaaalakTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PLN02330 481 IPAACVVINPKAKESEE------DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
208-572 |
1.58e-25 |
|
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: 107.74 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 PLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKwTFDWKPDDVFWCTADIGWVTGhTYITYGPLACGGTQVVFEGVptwp 287
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIH-AMGLTEADVYLNMLPLFHIAG-LNLALATFHAGGANVVMEKF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkvhpkSYDLSSLRIIGTVGEPINPEAWmwyhkhvgQERCPivDTW 367
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKS------GVDLSSLRHVLGLDAPETIQRF--------EETTG--ATF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 368 W----QTETGGhMITPLPGATPtvPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpaMI-RTIWGDPE----RF 438
Cdd:cd17637 140 WslygQTETSG-LVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGP---LVfQGYWNLPEltayTF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 439 RKSYYPeelggrlylAGDGTVRDKDtGYFTIMGRI--DDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAV 516
Cdd:cd17637 214 RNGWHH---------TGDLGRFDED-GYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 517 VAFVVLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:cd17637 284 KAVCVLK------PGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-575 |
2.89e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.97 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTA 136
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEqarggktLPLKSIADEAVAMggceavksvivyrrtggkidwhagrdlwMHELADAESDTCAPEWVGAEHPLFILYTSG 216
Cdd:PRK12316 3162 SH-------LRLPLAQGVQVLD----------------------------LDRGDENYAEANPAIRTMPENLAYVIYTSG 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWvTGHTYITYGPLACGGTqVVFEGVPTWPDAGRFWKMI 296
Cdd:PRK12316 3207 STGKPKGVGIRHSA-LSNHLCWMQQAYGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGAR-VVLAGPEDWRDPALLVELI 3283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 297 GDHKVTVfytaPTAIRSLIKAAEADDKVHpksyDLSSLRIIGTVGEPINPEAwmwYHKHVGQErcPIVDTWWQTET---G 373
Cdd:PRK12316 3284 NSEGVDV----LHAYPSMLQAFLEEEDAH----RCTSLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEAtitV 3350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 374 GHMITPLPGATPTVPGSctlPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAmiRTIWGDP----ERFRKSYYPEelGG 449
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGR---PIANRACYILDGSLEPVPVGALGELYLGGEGLA--RGYHNRPgltaERFVPDPFVP--GE 3423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 450 RLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVgrpdDTTGEAVVAFVVLKRSRPEG 529
Cdd:PRK12316 3424 RLYRTGD-LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDL 3498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1860891105 530 EEA--AALAKTLRDWVgkqigpiaKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK12316 3499 REAlkAHLKASLPEYM--------VPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
59-576 |
7.27e-25 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 108.99 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EQARggktlPLKSIADEAvamggceAVKSVIVyRRTGGKIDWHAG-----------RDLWMHELADAESDTCA------- 199
Cdd:PRK08974 130 NFAH-----TLEKVVFKT-------PVKHVIL-TRMGDQLSTAKGtlvnfvvkyikRLVPKYHLPDAISFRSAlhkgrrm 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 200 ----PEWVGaEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTmKWTfdwkpddvfwctadigwvtghtyitYGPLACGG 275
Cdd:PRK08974 197 qyvkPELVP-EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQA-KAA-------------------------YGPLLHPG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 276 TQVVFEGVP------------------------TWP-DAGRFWKMIGDHKvtvfYTAPTAIRSLIKAAEADDKVHpkSYD 330
Cdd:PRK08974 250 KELVVTALPlyhifaltvncllfielggqnlliTNPrDIPGFVKELKKYP----FTAITGVNTLFNALLNNEEFQ--ELD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 331 LSSLRIigTVGepinpeAWMWYHKHVGQErcpivdtwWQTETGGHMI--------TPLPGATP----TVPGSCTLPLPGI 398
Cdd:PRK08974 324 FSSLKL--SVG------GGMAVQQAVAER--------WVKLTGQYLLegygltecSPLVSVNPydldYYSGSIGLPVPST 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 399 MAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERfrksyyPEELGGRLYLA-GDGTVRDKDtGYFTIMGRIDDVL 477
Cdd:PRK08974 388 EIKLVDDDGNEVPPGEPGELWVKGP--QVMLGYWQRPEA------TDEVIKDGWLAtGDIAVMDEE-GFLRIVDRKKDMI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 478 NVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaaLAKTLRDWV-GKQIgpiakPKDI 556
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEE---LITHCRRHLtGYKV-----PKLV 530
|
570 580
....*....|....*....|
gi 1860891105 557 RFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK08974 531 EFRDELPKSNVGKILRRELR 550
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
58-579 |
2.48e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 107.22 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALV-- 134
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 135 -------------TADE---QARGGKTLP------LKSIADEAVAMGGCEAVKSVIVYRRTggkidWHAGRDLWMHelad 192
Cdd:PRK12492 130 nmfgklvqevlpdTGIEyliEAKMGDLLPaakgwlVNTVVDKVKKMVPAYHLPQAVPFKQA-----LRQGRGLSLK---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 193 aesdtcaPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQtmkwtfdwkpddVFWCTADIGwVTGHtyitygPLA 272
Cdd:PRK12492 201 -------PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQ------------VRACLSQLG-PDGQ------PLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 273 CGGTQVVFEGVPTWP----DAGRFWKMI-GDHKVTVfyTAPTAIRSLIK-----------------AAEADdkvHP--KS 328
Cdd:PRK12492 255 KEGQEVMIAPLPLYHiyafTANCMCMMVsGNHNVLI--TNPRDIPGFIKelgkwrfsallglntlfVALMD---HPgfKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 329 YDLSSLRIIGTVGEPI---NPEAWmwyHKHVGqerCPIVDTWWQTETgghmiTPLPGATP----TVPGSCTLPLPGIMAA 401
Cdd:PRK12492 330 LDFSALKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTET-----SPVASTNPygelARLGTVGIPVPGTALK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 402 VVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERfrksyYPEELGGRLYL-AGDGTVRDKDtGYFTIMGRIDDVLNVS 480
Cdd:PRK12492 399 VIDDDGNELPLGERGELCIKGP--QVMKGYWQQPEA-----TAEALDAEGWFkTGDIAVIDPD-GFVRIVDRKKDLIIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 481 GHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAALAKTlrDWVGKQIgpiakPKDIRFGD 560
Cdd:PRK12492 471 GFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKE--NFTGYKV-----PKHIVLRD 543
|
570
....*....|....*....
gi 1860891105 561 NLPKTRSGKIMRRLLRSLA 579
Cdd:PRK12492 544 SLPMTPVGKILRRELRDIA 562
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
205-579 |
2.93e-24 |
|
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: 106.26 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGtQVVFEGVP 284
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPNP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 TwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEaddkvhpkSYDLSSLRIIGTVGEPINPEAWMWYHKHVGqerCPIV 364
Cdd:cd05909 224 L--DYKKIPELIYDKKATILLGTPTFLRGYARAAH--------PEDFSSLRLVVAGAEKLKDTLRQEFQEKFG---IRIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 365 DTWWQTETGGHMITPLPgATPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRpwPAMIRTIWGDPERfrksyY 443
Cdd:cd05909 291 EGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRG--PNVMLGYLNEPEL-----T 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 444 PEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALvsHELVA---EAAVVGRPDDTTGEAVVAFV 520
Cdd:cd05909 363 SFAFGDGWYDTGD-IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDIL--SEILPednEVAVVSVPDGRKGEKIVLLT 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 521 VlkRSRPEGEEAAALAKTlrdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd05909 440 T--TTDTDPSSLNDILKN------AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
186-577 |
3.83e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 106.30 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 186 WMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADI-------- 257
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPLfhsnavma 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 258 GWVTGhtyitygpLACGGTQVV---FEGVPTWPDAGRFwkmigdhKVTVFYTAPTAIRSLIKAAEA-DDKVHPksydlss 333
Cdd:PRK07867 211 GWAVA--------LAAGASIALrrkFSASGFLPDVRRY-------GATYANYVGKPLSYVLATPERpDDADNP------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 334 LRII-GTVGEPINPEAWmwyhkhvgQER--CPIVDTWWQTEtGGHMITPLPGaTPtvPGSCTLPLPGImaAVVD-ETGQD 409
Cdd:PRK07867 269 LRIVyGNEGAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGV--AIVDpDTGTE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 410 VPNG---QGGIL--------VVKRPWPAMIRTIWGDPERFRksyypEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLN 478
Cdd:PRK07867 335 CPPAedaDGRLLnadeaigeLVNTAGPGGFEGYYNDPEADA-----ERMRGGVYWSGDLAYRDAD-GYAYFAGRLGDWMR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 479 VSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPegEEAAALAKTLRDwvGKQIGPIAKPKDIRF 558
Cdd:PRK07867 409 VDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAK--FDPDAFAEFLAA--QPDLGPKQWPSYVRV 484
|
410
....*....|....*....
gi 1860891105 559 GDNLPKTRSGKIMRRLLRS 577
Cdd:PRK07867 485 CAELPRTATFKVLKRQLSA 503
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
40-541 |
4.12e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 106.88 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 40 NGQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGAT-----HSVVfG 114
Cdd:PRK08279 50 HPDRPALLFED-----QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvallnTQQR-G 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 115 GFSAKSLNErlvdVGAVALVTADEQArggktlplksiadeavamggcEAVKSVIVYRRTGGKIdWHAGRDLWMHELAD-- 192
Cdd:PRK08279 124 AVLAHSLNL----VDAKHLIVGEELV---------------------EAFEEARADLARPPRL-WVAGGDTLDDPEGYed 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 193 -----AESDTCAPEW---VGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQtMKWTFDWKPDDVFWCTADIGWVTGHT 264
Cdd:PRK08279 178 laaaaAGAPTTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG-FGGLLRLTPDDVLYCCLPLYHNTGGT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 265 YITYGPLACGGTQVV---FEgvptwpdAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE-ADDKVHpksydlsSLRIIgtV 340
Cdd:PRK08279 257 VAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRATAFQYIGELCRYLLNQPPkPTDRDH-------RLRLM--I 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 341 GEPINPEAWMWYHKHVGQERcpIVDTWWQTETGGHMITPL--PGATPTVPGSCTLPlpgimAAVVD---ETGQDVPNGQG 415
Cdd:PRK08279 321 GNGLRPDIWDEFQQRFGIPR--ILEFYAASEGNVGFINVFnfDGTVGRVPLWLAHP-----YAIVKydvDTGEPVRDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 416 GILVVKRPWP----AMI---RTIWG--DPER---------FRKsyypeelGGRLYLAGDgTVRDKDTGYFTIMGRIDDVL 477
Cdd:PRK08279 394 RCIKVKPGEVglliGRItdrGPFDGytDPEAsekkilrdvFKK-------GDAWFNTGD-LMRDDGFGHAQFVDRLGDTF 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 478 -----NVSghrlgTMEIESALVSHELVAEAAVVGRP-DDTTGEAVVAFVVLKrsrpEGEE--AAALAKTLRD 541
Cdd:PRK08279 466 rwkgeNVA-----TTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLA----DGAEfdLAALAAHLYE 528
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
58-600 |
5.00e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 107.04 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQAC-ARigathsvvfggfsakslnerlvdvGAVALVTA 136
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLAClAR------------------------GVMAFLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEQARGGKTLPLKSIADEAVAMGG--CEAVKSVIVYRRTggkidwhagrDLwMHELADAESDTCAPewVGAEHPLFILYT 214
Cdd:PRK06060 87 PELHRDDHALAARNTEPALVVTSDalRDRFQPSRVAEAA----------EL-MSEAARVAPGGYEP--MGGDALAYATYT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 215 SGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVfEGVPTWPDAG---- 290
Cdd:PRK06060 154 SGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAails 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 291 -RFwkmigdhKVTVFYTAPTAIRSLIKAAEADDkvhpksydLSSLRIIGTVGEPINPEAWMWYHKHVGQerCPIVDTWWQ 369
Cdd:PRK06060 233 aRF-------GPSVLYGVPNFFARVIDSCSPDS--------FRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 370 TETGGHMITPlpgatpTV----PGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFrksyype 445
Cdd:PRK06060 296 TEVGQTFVSN------RVdewrLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGP--AIAKGYWNRPDSP------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 446 eLGGRLYLAGDGTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVlkRS 525
Cdd:PRK06060 361 -VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--AT 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 526 RPEGEEAAALAKTLRDWVgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGEAITQDTSTLENPAILDQL 600
Cdd:PRK06060 438 SGATIDGSVMRDLHRGLL-NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQR 511
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
51-578 |
5.06e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 106.08 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 51 DDGTVTRVTYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVG 129
Cdd:PLN02574 60 DSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 130 AVALVTADEQArgGKTLPLKsiadeavamggceaVKSVIVyrRTGGKIDWHAGRDLWMHELADAESDTCAPEWVGAEHPL 209
Cdd:PLN02574 140 VGLAFTSPENV--EKLSPLG--------------VPVIGV--PENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDDVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 210 FILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDW----KPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVpt 285
Cdd:PLN02574 202 AIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeypGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF-- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 286 wpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEAddkvhPKSYDLSSLRIIGTVGEPINP---EAWMWYHKHVGqercp 362
Cdd:PLN02574 280 --DASDMVKVIDRFKVTHFPVVPPILMALTKKAKG-----VCGEVLKSLKQVSCGAAPLSGkfiQDFVQTLPHVD----- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 363 IVDTWWQTETGGHMITPLPGATPTVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKS 441
Cdd:PLN02574 348 FIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGP--GVMKGYLNNPKATQST 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 442 YYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVV 521
Cdd:PLN02574 426 IDKD---GWLR-TGDIAYFDED-GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 522 LKRSRPEGEEAaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:PLN02574 501 RRQGSTLSQEA------VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
58-580 |
8.09e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 105.73 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFAN-ALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTA 136
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 D------EQARGGKtlPLKSIADEAVA--MGGCEAVKSVIVYRRTGGKI-DWHAGRDLWMHE-LADAESDTCAPEWVGAE 206
Cdd:PRK08751 131 DnfgttvQQVIADT--PVKQVITTGLGdmLGFPKAALVNFVVKYVKKLVpEYRINGAIRFREaLALGRKHSMPTLQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 207 HPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTfdwkpddvfwcTADIGWVTGH-TYITYGPL----ACGGTQVVFE 281
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWL-----------AGTGKLEEGCeVVITALPLyhifALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 282 GVP------TWP-DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksYDLSSLRIIGTVGEPINPEAWMWYHK 354
Cdd:PRK08751 278 KIGgcnhliSNPrDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ------IDFSSLKMTLGGGMAVQRSVAERWKQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 355 HVGqerCPIVDTWWQTETG-GHMITPLpgATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWG 433
Cdd:PRK08751 352 VTG---LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 434 DPERFRKSYYPEelgGRLYlAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:PRK08751 425 RPEETAKVMDAD---GWLH-TGD-IARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSG 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860891105 514 EAVVAFVVLKRSRPEGEEAAALAKTlrdwvgkQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAK 580
Cdd:PRK08751 500 EIVKVVIVKKDPALTAEDVKAHARA-------NLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
208-579 |
1.82e-23 |
|
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: 101.64 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 PLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWtFDWKPDDVFWCTADIGWVTGhTYITYGPLACGGTQVVFEgvPTWP 287
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSR-LGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLE--RNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAgrfwKMIGDHKVTVFYTAPTAIRSLIKAAEADDkvhpksyDLSSLRIIGTVGEPINPEAwmwyHKHVGQERCPIVDTW 367
Cdd:cd17630 78 LA----EDLAPPGVTHVSLVPTQLQRLLDSGQGPA-------ALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 368 WQTETGGHMITPLPGATPTvpGSCTLPLPGIMAAVVDetgqdvpngqGGILVVKRPWPAMIRTIWGDPERFRKsyypeel 447
Cdd:cd17630 143 GMTETASQVATKRPDGFGR--GGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPEFNE------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 448 ggrlylagDGTVRDKDTGYF------TIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVV 521
Cdd:cd17630 204 --------DGWFTTKDLGELhadgrlTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 522 LKRSRPEGEeaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd17630 276 GRGPADPAE--------LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-572 |
2.48e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 101.57 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 206 EHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGpLACGGTQVVFEGVPT 285
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 286 WPDagrFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPKsydlssLRIIGTVGE-PINPE-AWMWYHKHVGqercpI 363
Cdd:cd17635 80 YKS---LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPS------LRLIGYGGSrAIAADvRFIEATGLTN-----T 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 364 VDTWWQTETGGHMITPLPGATPTVpGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWpaMIRTIWGDPERFRKSYy 443
Cdd:cd17635 146 AQVYGLSETGTALCLPTDDDSIEI-NAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 444 peeLGGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLk 523
Cdd:cd17635 222 ---IDGWVN-TGDLGERRED-GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1860891105 524 rsrpEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:cd17635 296 ----SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
361-576 |
3.98e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 103.69 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 CPIVDTWWQTETgghmiTPLPGATP---TVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDPER 437
Cdd:PRK05677 352 CAICEGYGMTET-----SPVVSVNPsqaIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPEA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 438 FRKSYYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVV 517
Cdd:PRK05677 425 TDEILDSD---GWLK-TGDIALIQED-GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIK 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 518 AFVVLKRSrpegeeAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK05677 500 VFVVVKPG------ETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
45-573 |
1.14e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 101.89 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 45 AVIFEADDgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNER 124
Cdd:PRK05852 34 ALVVTADR---IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 125 LVDVGAVAlVTADEQARGGKTLPLKSIADEAVAMGGceavksviVYRRTGGKIDWHAGrdlwmhELADAESDTCAPEWVG 204
Cdd:PRK05852 111 SQAAGARV-VLIDADGPHDRAEPTTRWWPLTVNVGG--------DSGPSGGTLSVHLD------AATEPTPATSTPEGLR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLfILYTSGSTGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDDVfwCTADIGWVTGHTYIT--YGPLACGGTQVVfeg 282
Cdd:PRK05852 176 PDDAM-IMFTGGTTGLPKMVPW-THANIASSVRAIITGYRLSPRDA--TVAVMPLYHGHGLIAalLATLASGGAVLL--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 283 vptwPDAGRF-----WKMIGDHKVTVFYTAPTAIRSLIKAA--EADDKVHPKsydlssLRIIGTVGEPINPEAWMWYHKH 355
Cdd:PRK05852 249 ----PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAatEPSGRKPAA------LRFIRSCSAPLTAETAQALQTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 356 VGqerCPIVDTWWQTET---------GGHMITPLPGATPTVPGSCTlplpGIMAAVVDETGQDVPNGQGGILVVKRPwpA 426
Cdd:PRK05852 319 FA---APVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAVGEVWLRGT--T 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 427 MIRTIWGDPERFRKSYypeelggrlylaGDGTVRDKD------TGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVA 500
Cdd:PRK05852 390 VVRGYLGDPTITAANF------------TDGWLRTGDlgslsaAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVM 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 501 EAAVVGRPDDTTGEAVVAFVVLKRS-RPEGEEAAALAKTlrdwvgkQIGPIAKPKDIRFGDNLPKTRSGKIMRR 573
Cdd:PRK05852 458 EAAVFGVPDQLYGEAVAAVIVPRESaPPTAEELVQFCRE-------RLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
211-572 |
2.94e-22 |
|
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: 97.96 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGV----QHSTGGYLLWAAQTmkwtfDWKPDDVFWCTADIGwvtgHTY-ITYGPLAC---GGT---QVV 279
Cdd:cd17638 5 IMFTSGTTGRSKGVmcahRQTLRAAAAWADCA-----DLTEDDRYLIINPFF----HTFgYKAGIVAClltGATvvpVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 280 FegvptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddkvHP--KSYDLSSLRIIGTVGEPINPEAWMWYHKHVG 357
Cdd:cd17638 76 F-------DVDAILEAIERERITVLPGPPTLFQSLLD--------HPgrKKFDLSSLRAAVTGAATVPVELVRRMRSELG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 358 QERcpIVDTWWQTETG-GHMITPLPGATpTVPGSCTLPLPGIMAAVVDetgqdvpngQGGILVvkRPWPAMIRTIwGDPE 436
Cdd:cd17638 141 FET--VLTAYGLTEAGvATMCRPGDDAE-TVATTCGRACPGFEVRIAD---------DGEVLV--RGYNVMQGYL-DDPE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 437 RFRKSYypeELGGRLYLAGDGTVRDKdtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAV 516
Cdd:cd17638 206 ATAEAI---DADGWLHTGDVGELDER--GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 517 VAFVVLKRSRPEGEEAaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:cd17638 281 KAFVVARPGVTLTEED------VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
208-576 |
4.24e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 99.81 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 PLFILYTSGSTGKPKGVQHS-TGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYItYGPLACGGTQVVFEGVPtw 286
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRL-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 287 pDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPKSYDLSSlriigtvGEPINPEAwMWYHKHVGQERCPIVDT 366
Cdd:cd05915 232 -DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVV-------GGSAAPRS-LIARFERMGVEVRQGYG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 367 WWQTETGGHMITPLPgATPTVPGSCTLPLPGI--------MAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPERF 438
Cdd:cd05915 303 LTETSPVVVQNFVKS-HLESLSEEEKLTLKAKtglpiplvRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEAT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 439 RKSYYPeelgGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVA 518
Cdd:cd05915 382 RSALTP----DGFFRTGDIAVWDEE-GYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 519 FVVLKRSRPEGEEAAALAKtlrdwvgKQIGPIAK-PKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05915 457 VVVPRGEKPTPEELNEHLL-------KAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
206-575 |
4.78e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 99.43 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 206 EHPLFILYTSGSTGKPKGV--QHSTGGYLLWAAQtmKWTFDWKPDDVFWcTADIGWVTGHTYITygPLACGGTQVVFEGV 283
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVmiEHQSLVNLSHGLI--KEYGITSSDRVLQ-FASIAFDVAAEEIY--VTLLSGATLVLRPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 284 PTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIkaaeaDDKVHPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQeRCPI 363
Cdd:cd17644 181 EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLV-----LELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGN-FIQL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 364 VDTWWQTE----TGGHMITPLPGATPTVPgSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAMIRTIWGDP---- 435
Cdd:cd17644 255 INVYGPTEatiaATVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHIGGV--GLARGYLNRPelta 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 436 ERFRKSYYPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEA 515
Cdd:cd17644 332 EKFISHPFNSSESERLYKTGD-LARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 516 VVAFVVlkrsrPEGEEAAALAKtLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17644 411 LVAYIV-----PHYEESPSTVE-LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
40-581 |
7.67e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 100.38 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 40 NGQRVAVIfeadDGTVTRVTYAELLARVSRFANALKkRGIAKGDRVVIYMPMSIEGIVAMQACARIGAThSVvfggfsak 119
Cdd:PRK08633 628 NWSRLAVA----DSTGGELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGKV-PV-------- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 120 SLNerlvdvgavalVTADEQArggktlpLKSiadeAVAMGGceaVKSVIVYR----RTGGKIDWHA----GRDLWMHELA 191
Cdd:PRK08633 694 NLN-----------YTASEAA-------LKS----AIEQAQ---IKTVITSRkfleKLKNKGFDLElpenVKVIYLEDLK 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 192 DAESDT---CA-------PEW---------VGAEHPLFILYTSGSTGKPKGVQHStGGYLLWAAQTMKWTFDWKPDDVFW 252
Cdd:PRK08633 749 AKISKVdklTAllaarllPARllkrlygptFKPDDTATIIFSSGSEGEPKGVMLS-HHNILSNIEQISDVFNLRNDDVIL 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 253 CTADIGWVTGHTYITYGPLaCGGTQVVFEGVPTwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaDDKVHPKsyDLS 332
Cdd:PRK08633 828 SSLPFFHSFGLTVTLWLPL-LEGIKVVYHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR----NKKLHPL--MFA 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 333 SLRIIGTVGEPINPEAWMWYHKHVGQErcpIVDTWWQTETgghmiTPLpgATPTVP---------------GSCTLPLPG 397
Cdd:PRK08633 899 SLRLVVAGAEKLKPEVADAFEEKFGIR---ILEGYGATET-----SPV--ASVNLPdvlaadfkrqtgskeGSVGMPLPG 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 398 IMAAVVD-ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERfRKSYYPEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDV 476
Cdd:PRK08633 969 VAVRIVDpETFEELPPGEDGLILIGGP--QVMKGYLGDPEK-TAEVIKDIDGIGWYVTGDKGHLDED-GFLTITDRYSRF 1044
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 477 LNVSGHR--LGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVvlkrsRPEGEEAAALAKTLRDwvgKQIGPIAKPK 554
Cdd:PRK08633 1045 AKIGGEMvpLGAVEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLH-----TCGAEDVEELKRAIKE---SGLPNLWKPS 1116
|
570 580
....*....|....*....|....*..
gi 1860891105 555 DIRFGDNLPKTRSGKIMRRLLRSLAKG 581
Cdd:PRK08633 1117 RYFKVEALPLLGSGKLDLKGLKELALA 1143
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
50-575 |
7.67e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 100.50 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 50 ADDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVG 129
Cdd:PRK10252 478 ADARY--QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDAR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 130 AVALVTADEQARGGKTLPLKSIADEAVamggceavksvivyrrtggkidwhagrdlwmhELADAESdtcAPEWVGA-EHP 208
Cdd:PRK10252 556 PSLLITTADQLPRFADVPDLTSLCYNA--------------------------------PLAPQGA---APLQLSQpHHT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 209 LFILYTSGSTGKPKGV---QHSTGGYLLWaaqtMKWTFDWKPDDVFW----CTADIG-----WvtghtyitygPLACGGT 276
Cdd:PRK10252 601 AYIIFTSGSTGRPKGVmvgQTAIVNRLLW----MQNHYPLTADDVVLqktpCSFDVSvweffW----------PFIAGAK 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVFEgvptwPDAGR----FWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydLSSLRIIGTVGEPINPEAWMWY 352
Cdd:PRK10252 667 LVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQS----CASLRQVFCSGEALPADLCREW 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 353 HKHVGQERCPI-------VD-TWWqtETGGHMITPLPGAtpTVPgsCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPW 424
Cdd:PRK10252 738 QQLTGAPLHNLygpteaaVDvSWY--PAFGEELAAVRGS--SVP--IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 PAmiRTIWGDP----ERFRKSyyPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVA 500
Cdd:PRK10252 812 LA--QGYLGRPdltaSRFIAD--PFAPGERMYRTGD-VARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 501 EAAVVGR----PDDTTGEA--VVAFVVlkrsrpEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRL 574
Cdd:PRK10252 887 QAVTHACvinqAAATGGDArqLVGYLV------SQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA 960
|
.
gi 1860891105 575 L 575
Cdd:PRK10252 961 L 961
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
57-577 |
8.63e-22 |
|
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: 98.15 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHsvvfggfsakslnerlvdvgavalvta 136
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAY--------------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 deqarggktLPLksiaDEAVAmggceAVKSVIVYRRTGGKIDWHAGRDlwmHELAdaesdtcapewvgaehplFILYTSG 216
Cdd:cd17653 75 ---------VPL----DAKLP-----SARIQAILRTSGATLLLTTDSP---DDLA------------------YIIFTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQ--HSTggyLLWAAQTMKWTFDWKPDD--------VFW-CTADIgwvtghtyitYGPLACGGTQVVFEGVPT 285
Cdd:cd17653 116 STGIPKGVMvpHRG---VLNYVSQPPARLDVGPGSrvaqvlsiAFDaCIGEI----------FSTLCNGGTLVLADPSDP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 286 WPDAGRfwkmigdhKVTVFYTAPTAIRSLikaaeaddkvHPKSYDlsSLRIIGTVGEPINPeawmwyhkhvgqercPIVD 365
Cdd:cd17653 183 FAHVAR--------TVDALMSTPSILSTL----------SPQDFP--NLKTIFLGGEAVPP---------------SLLD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 366 TWWQ----------TETGghMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGG-ILVVKrpwPAMIRTIWGD 434
Cdd:cd17653 228 RWSPgrrlynaygpTECT--ISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGeICISG---VQVARGYLGN 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 PERFRKSYYPEEL--GGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIES-ALVSHELVAEAAVVgrpddT 511
Cdd:cd17653 303 PALTASKFVPDPFwpGSRMYRTGDYGRWTED-GGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-----V 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860891105 512 TGEAVVAFVVlkrsrPEGEEAAALAKTLRdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:cd17653 377 VNGRLVAFVT-----PETVDVDGLRSELA----KHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
207-572 |
1.01e-21 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 96.32 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 207 HPLFILYTSGSTGKPKGV---QHStggyllWAAqtmkwTFDWKPDDVFWCTADIGWVTG---HTYITYG---PLACGGTQ 277
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYyrsERS------WIE-----SFVCNEDLFNISGEDAILAPGplsHSLFLYGaisALYLGGTF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 278 VVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVhpksydlsslRIIGTVGEPINPEAwmwyhKHVG 357
Cdd:cd17633 70 IGQRKF----NPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKI----------KSIFSSGQKLFEST-----KKKL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 358 QERCP---IVDTWWQTETGghMITPLPGATPTVPGSCTLPLPGIMAAVVDETGqdvpnGQGGILVVKRPwpaMIrtiwgd 434
Cdd:cd17633 131 KNIFPkanLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE---MV------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 435 perfrksYYPEELGGRLYLAGDGTVRD----KDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDD 510
Cdd:cd17633 195 -------FSGYVRGGFSNPDGWMSVGDigyvDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDA 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 511 TTGEAVVAFVvlkrsrpEGEEAAalAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:cd17633 268 RFGEIAVALY-------SGDKLT--YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
208-568 |
8.10e-21 |
|
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: 93.91 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 208 PLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVtGHTYITYGPLACGGTQVVFEGVptwp 287
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQA-LLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAGRFWKMIGDHKVTVFYTAPTAIRSlIKAAEADDKvhpksYDLSSLRIIGTVGE---PINPEAWMWYHKHVGQErcpiv 364
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQ-IVELNADGL-----YDLSSLRSSPAAPEwndMATVDTSPWGRKPGGYG----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 365 dtwwQTETGGhMITpLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVkRPWPAMiRTIWGDPE----RFRk 440
Cdd:cd17636 145 ----QTEVMG-LAT-FAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-RGPTVM-AGYWNRPEvnarRTR- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 syypeelgGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFV 520
Cdd:cd17636 216 --------GGWHHTNDLGRREPD-GSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1860891105 521 VLKrsrpegEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSG 568
Cdd:cd17636 287 VLK------PGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
57-580 |
1.76e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 94.85 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGiAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLvdvgavalvta 136
Cdd:PRK07638 26 VLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 deqarggktlplkSIADEAVamggceavksVIVYRRTGGKIDWHAGR----DLWMhELADAESDTCAPEWVGAEHPLFIL 212
Cdd:PRK07638 94 -------------AISNADM----------IVTERYKLNDLPDEEGRvieiDEWK-RMIEKYLPTYAPIENVQNAPFYMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 213 YTSGSTGKPKG---VQHStggyllW--AAQTMKWTFDWKPDDvfwcTADIGWVTGHTYITYGP---LACGGTQVVfegVP 284
Cdd:PRK07638 150 FTSGSTGKPKAflrAQQS------WlhSFDCNVHDFHMKRED----SVLIAGTLVHSLFLYGAistLYVGQTVHL---MR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 TWPDAGRFWKMIGDhKVTVFYTAPTAIRSLIKAAEADDkvhpksydlSSLRIIGTVGEpinpeaWMWYHKHVGQERCPIV 364
Cdd:PRK07638 217 KFIPNQVLDKLETE-NISVMYTVPTMLESLYKENRVIE---------NKMKIISSGAK------WEAEAKEKIKNIFPYA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 365 ---DTWWQTETGghMITPL-PGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPWPAMIRTIWGDPerfrk 440
Cdd:PRK07638 281 klyEFYGASELS--FVTALvDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL----- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 syyPEELGGRLYLagdgTVRD----KDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAV 516
Cdd:PRK07638 354 ---ARELNADGWM----TVRDvgyeDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860891105 517 VAFVvlkrsrpegeEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAK 580
Cdd:PRK07638 427 VAII----------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
206-587 |
4.00e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 94.32 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 206 EH-PLFILYTSGSTGKPKGVQHS-TGGYLLWAAQTMKWTFDWKPddVFWCTADIGWVTGHTYiTYGPLACGGTQVVFEGV 283
Cdd:PLN03102 185 EHdPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 284 pTWPDagrFWKMIGDHKVTVFYTAPTAIRSLIKAAEADdkVHPKSYDLSSLriigTVGEPinPEAWMWyhKHVGQERCPI 363
Cdd:PLN03102 262 -TAPE---IYKNIEMHNVTHMCCVPTVFNILLKGNSLD--LSPRSGPVHVL----TGGSP--PPAALV--KKVQRLGFQV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 364 VDTWWQTE-TGGHMITPLPGATPTVPGSCTLPLPG------IMAAVVD----ETGQDVP-NGQG-GILVVKRPwpAMIRT 430
Cdd:PLN03102 328 MHAYGLTEaTGPVLFCEWQDEWNRLPENQQMELKArqgvsiLGLADVDvknkETQESVPrDGKTmGEIVIKGS--SIMKG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 431 IWGDPERFRKSYYPEELGgrlylAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDD 510
Cdd:PLN03102 406 YLKNPKATSEAFKHGWLN-----TGDVGVIHPD-GHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 511 TTGEAVVAFVVLKRSRPEGEEAAALAKT----LRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLAKGEAITQ 586
Cdd:PLN03102 480 TWGETPCAFVVLEKGETTKEDRVDKLVTrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVED 559
|
.
gi 1860891105 587 D 587
Cdd:PLN03102 560 E 560
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
43-575 |
4.88e-20 |
|
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: 93.31 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:cd17656 4 AVAVVFENQ-----KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTADEQArggktlplKSIADEavamggceavKSVIVyrrtggkIDWhagrDLWMHElaDAESDTCApew 202
Cdd:cd17656 79 YIMLDSGVRVVLTQRHLK--------SKLSFN----------KSTIL-------LED----PSISQE--DTSNIDYI--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 VGAEHPLFILYTSGSTGKPKGVQ--HSTGGYLLwaAQTMKWTFDWKPDDVFW---CTADI-------GWVTGHT-YIT-- 267
Cdd:cd17656 125 NNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVcyqeifsTLLSGGTlYIIre 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 ---------YGPLACGGTQVVFegVPTwpdagRFWKMIGDHKvTVFYTAPTAIRSLIKAAEaddkvhpksydlsSLRIIG 338
Cdd:cd17656 203 etkrdveqlFDLVKRHNIEVVF--LPV-----AFLKFIFSER-EFINRFPTCVKHIITAGE-------------QLVITN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 339 TVGEPINpEAWMWYHKHVGQERCPIVDTWwqteTGGHMItPLPGATPT-VPGSCTLPLpgimaaVVDETGQDVPNGQGGI 417
Cdd:cd17656 262 EFKEMLH-EHNVHLHNHYGPSETHVVTTY----TINPEA-EIPELPPIgKPISNTWIY------ILDQEQQLQPQGIVGE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 418 LVVKRPwpAMIRTIWGDPERFRKSYYPEELGG--RLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVS 495
Cdd:cd17656 330 LYISGA--SVARGYLNRQELTAEKFFPDPFDPneRMYRTGDLARYLPD-GNIEFLGRADHQVKIRGYRIELGEIEAQLLN 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 496 HELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEeaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ--------LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
186-577 |
5.14e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.55 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 186 WMHELADAESDTCAPEwVGAEHPLFILYTSGSTGKPKGVQHSTGgYLLWAAQTMKWTFDWKPDDVFWCTADI-------- 257
Cdd:PRK13388 131 YAELVAAAGALTPHRE-VDAMDPFMLIFTSGTTGAPKAVRCSHG-RLAFAGRALTERFGLTRDDVCYVSMPLfhsnavma 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 258 GWvtghtyityGPLACGGTQVVFegVPTWpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAE-ADDKVHPksydlssLRI 336
Cdd:PRK13388 209 GW---------APAVASGAAVAL--PAKF-SASGFLDDVRRYGATYFNYVGKPLAYILATPErPDDADNP-------LRV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 337 -IGTVGEPINPEAWmwyhkhvgQER--CPIVDTWWQTETGGhMITPLPGaTPtvPGSCTLPLPGImaAVVD-ETGQDVPN 412
Cdd:PRK13388 270 aFGNEASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGV--AIYNpETLTECAV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 413 ---GQGGIL---------VVKRPWPAMIRTIWGDP----ERFRksyypeelGGRlYLAGDGTVRDKDtGYFTIMGRIDDV 476
Cdd:PRK13388 336 arfDAHGALlnadeaigeLVNTAGAGFFEGYYNNPeataERMR--------HGM-YWSGDLAYRDAD-GWIYFAGRTADW 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 477 LNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLkrSRPEGEEAAALAKTLRDwvGKQIGPIAKPKDI 556
Cdd:PRK13388 406 MRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVL--RDGATFDPDAFAAFLAA--QPDLGTKAWPRYV 481
|
410 420
....*....|....*....|.
gi 1860891105 557 RFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK13388 482 RIAADLPSTATNKVLKRELIA 502
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
41-580 |
3.36e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 91.44 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVAVIFEAddgtvTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMP-----------MSIEGIVAMQACARIGATH 109
Cdd:PLN02479 34 PTRKSVVHGS-----VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPnipamyeahfgVPMAGAVVNCVNIRLNAPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 110 SVVFGGFSAKS---LNERLVDVGAVALVTADEQARGGKTLP-LKSIADEAVAMGGCEAV--KSVIVYRR---TGG-KIDW 179
Cdd:PLN02479 109 IAFLLEHSKSEvvmVDQEFFTLAEEALKILAEKKKSSFKPPlLIVIGDPTCDPKSLQYAlgKGAIEYEKfleTGDpEFAW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 180 HAGRDLWmheladaesdtcapewvgaeHPLFILYTSGSTGKPKGV-QHSTGGYLLWAAQTMKWTFD------WK-PddVF 251
Cdd:PLN02479 189 KPPADEW--------------------QSIALGYTSGTTASPKGVvLHHRGAYLMALSNALIWGMNegavylWTlP--MF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 252 WCTadiGWVtghtyITYGPLACGGTQVVFEGVptwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADD------KVH 325
Cdd:PLN02479 247 HCN---GWC-----FTWTLAALCGTNICLRQV----TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilplprVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 326 -------PKSYDLSSL-----RIIGTVG--EPINPE---AWM--WYH---------------KHVGQERCPIVDTwwQTe 371
Cdd:PLN02479 315 vmtagaaPPPSVLFAMsekgfRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT--KT- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 tgghmITPLPGATPTVpgsctlplpgimaavvdetGQDVPNGQGgilVVKrpwpAMIRTIWGDPERFRKSYYPeelggrl 451
Cdd:PLN02479 392 -----MKPVPADGKTM-------------------GEIVMRGNM---VMK----GYLKNPKANEEAFANGWFH------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 ylAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrSRPEGEE 531
Cdd:PLN02479 434 --SGDLGVKHPD-GYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLK-PGVDKSD 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1860891105 532 AAALAKTLRDWVGKQIGPIAKPKDIRFGDnLPKTRSGKIMRRLLRSLAK 580
Cdd:PLN02479 510 EAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
42-575 |
1.44e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFEADDgtvtrVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:PRK05691 1146 ERIALVWDGGS-----LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERL 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 NERLVDVGAVALVTadeqarggktlplksiadEAVAMGGCEAVKSVIVyrrtggkidwhagrdLWMHELADAESDTCAPE 201
Cdd:PRK05691 1221 AYMLADSGVELLLT------------------QSHLLERLPQAEGVSA---------------IALDSLHLDSWPSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 W-VGAEHPLFILYTSGSTGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGhTYITYGPLACgGTQVVF 280
Cdd:PRK05691 1268 LhLHGDNLAYVIYTSGSTGQPKGVG-NTHAALAERLQWMQATYALDDSDVLMQKAPISFDVS-VWECFWPLIT-GCRLVL 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 EGVPTWPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddkvHPKSYDLSSLRIIGTVGEPINPE---------AWMW 351
Cdd:PRK05691 1345 AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID--------EPLAAACTSLRRLFSGGEALPAElrnrvlqrlPQVQ 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 352 YHKHVGQERCPIVDTWWQTETGGHMITPLpgatptvpgscTLPLPGIMAAVVDETGQDVPNGQGGILVVKRpwPAMIRTI 431
Cdd:PRK05691 1417 LHNRYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIGG--AGLARGY 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 WGDP----ERFRKSYYPEElGGRLYLAGDGtVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGR 507
Cdd:PRK05691 1484 LGRPaltaERFVPDPLGED-GARLYRTGDR-ARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR 1561
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 508 pDDTTGEAVVAFVVLKRSRPEGEEA--AALAKTLRDW-VGKQIGPIakpkdirfgDNLPKTRSGKIMRRLL 575
Cdd:PRK05691 1562 -EGAAGAQLVGYYTGEAGQEAEAERlkAALAAELPEYmVPAQLIRL---------DQMPLGPSGKLDRRAL 1622
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
402-585 |
2.22e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 88.51 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 402 VVDETGQDVPNGQGGILVVKRPWpaMIRTIWGDPERFRKSYYPEELggrlYLAGDGTVRDKDtGYFTIMGRIDDVLNVSG 481
Cdd:PRK10946 367 VADADGNPLPQGEVGRLMTRGPY--TFRGYYKSPQHNASAFDANGF----YCSGDLVSIDPD-GYITVVGREKDQINRGG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 482 HRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEAAALAKTLRDwvgKQIGPIAKPKDIRFGDN 561
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK----EPLKAVQLRRFLRE---QGIAEFKLPDRVECVDS 512
|
170 180
....*....|....*....|....
gi 1860891105 562 LPKTRSGKIMRRLLRSLAKGEAIT 585
Cdd:PRK10946 513 LPLTAVGKVDKKQLRQWLASRASA 536
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
52-506 |
2.18e-17 |
|
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: 85.21 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 52 DGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAV 131
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 132 ALVTAdeqarggktlplKSIADEAVAMGGCEAVKSVIVYRRTGGKIDWHAGRDLWMHELADAESDTcapewvGAEHPLFI 211
Cdd:cd05932 81 ALFVG------------KLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTR------FPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 212 LYTSGSTGKPKGVQHSTGGYlLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLAcGGTQVVF-EGVPTWP-DA 289
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLY-GGVLVAFaESLDTFVeDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 290 GRfwkmigdHKVTVFYTAP-------------------------TAIRSLIKaaeadDKVHpKSYDLSSLRIIGTVGEPI 344
Cdd:cd05932 221 QR-------ARPTLFFSVPrlwtkfqqgvqdkipqqklnlllkiPVVNSLVK-----RKVL-KGLGLDQCRLAGCGSAPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 345 NPEAWMWYHKhVGqerCPIVDTWWQTETGGHMITPLPGATPTvpGSCTLPLPGIMAAVVDetgqdvpngQGGILVVKrpw 424
Cdd:cd05932 288 PPALLEWYRS-LG---LNILEAYGMTENFAYSHLNYPGRDKI--GTVGNAGPGVEVRISE---------DGEILVRS--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 425 PAMIRTIWGDPERFRKSYYPEelgGRLYlAGDGTVRDKDtGYFTIMGRIDDVLNVS-GHRLGTMEIESALVSHELVAEAA 503
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTAD---GFLR-TGDKGELDAD-GNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVC 424
|
...
gi 1860891105 504 VVG 506
Cdd:cd05932 425 VIG 427
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
57-579 |
1.18e-16 |
|
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: 82.79 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTa 136
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 deqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesDTCapewvgaehplFILYTSG 216
Cdd:cd05940 82 -----------------------------------------------------------DAA-----------LYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 217 STGKPKGVQHSTGGYLLWAAQTMKWTFDwKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVptwpDAGRFWKMI 296
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGSGGA-LPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 297 GDHKVTVFYTAPTAIRSLIKA-AEADDKVHpksydlsSLRIIgtVGEPINPEAWMWYHKHVGQERcpIVDTWWQTEtGGH 375
Cdd:cd05940 167 RKYQATIFQYIGELCRYLLNQpPKPTERKH-------KVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAATE-GNS 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 376 MITPLPGATPTVPGSCTLPLPGIMAAVVD---ETGQ----------DVPNGQGGILV--VKRPWPAmirTIWGDPERFRK 440
Cdd:cd05940 235 GFINFFGKPGAIGRNPSLLRKVAPLALVKydlESGEpirdaegrciKVPRGEPGLLIsrINPLEPF---DGYTDPAATEK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 SYYPEEL--GGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRP-DDTTGEAVV 517
Cdd:cd05940 312 KILRDVFkkGDAWFNTGD-LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGM 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 518 AFVVLKrsRPEGEEAAALAKTLRdwvgKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:cd05940 391 AAIVLQ--PNEEFDLSALAAHLE----KNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
42-574 |
1.67e-16 |
|
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: 82.06 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 42 QRVAVIFeaddGTVtRVTYAELLARVSRFANALKKRGIAKGD-RVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAks 120
Cdd:cd17648 2 DRVAVVY----GDK-RLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 lnERlvdvgaVALVTADEQARGgktlplksiadeavamggceavksVIvyrrTGGKidwhagrdlwmhELAdaesdtcap 200
Cdd:cd17648 75 --ER------IQFILEDTGARV------------------------VI----TNST------------DLA--------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 ewvgaehplFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDD---------VF------WCTADIGwvtGHTY 265
Cdd:cd17648 98 ---------YAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDeavlffsnyVFdffveqMTLALLN---GQKL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 266 ItygplacggtqVVFEGVPTWPDagRFWKMIGDHKVTVFYTAPTAIrslikaaeaddkvhpKSYDLS---SLRIIGTVGE 342
Cdd:cd17648 166 V-----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVL---------------QQYDLArlpHLKRVDAAGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 343 PINPEAwmwYHKHVGQERCPIVDTWWQTETG-GHMITPLPGATPTvPGSCTLPLPGIMAAVVDETGQDVPNGQGGILV-- 419
Cdd:cd17648 218 EFTAPV---FEKLRSRFAGLIINAYGPTETTvTNHKRFFPGDQRF-DKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYlg 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 420 ---VKRPW---PAMIRtiwgdpERFRKSYYPEE----LG--GRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTM 487
Cdd:cd17648 294 gdgVARGYlnrPELTA------ERFLPNPFQTEqeraRGrnARLYKTGD-LVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 488 EIESALVSHELVAEAAVVGRPDDTTGEAV-----VAFVVlkrSRPEGEEAAAlaktLRDWVGKQIGPIAKPKDIRFGDNL 562
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYYL---PEPGHVPESD----LLSFLRAKLPRYMVPARLVRLEGI 439
|
570
....*....|...
gi 1860891105 563 PKTRSGKI-MRRL 574
Cdd:cd17648 440 PVTINGKLdVRAL 452
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
35-576 |
3.53e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 81.72 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 35 HVEAGNGQRvAVIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVviympmsieGIVAMQACARIGATHSVVFG 114
Cdd:PRK06018 18 HAARIHGNR-EVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRV---------ATIAWNTWRHLEAWYGIMGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 115 GFSAKSLNERLV--DVGAVALVTADEQARGGKT-LP-LKSIADEavamggCEAVKSVIVYrrTGGKI------------- 177
Cdd:PRK06018 88 GAICHTVNPRLFpeQIAWIINHAEDRVVITDLTfVPiLEKIADK------LPSVERYVVL--TDAAHmpqttlknavaye 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 178 DWHAGRD---LWmhelADAESDTCAPewvgaehplfILYTSGSTGKPKGVQHSTGGYLLWAAQTMKwtfdwkPDDVFWCT 254
Cdd:PRK06018 160 EWIAEADgdfAW----KTFDENTAAG----------MCYTSGTTGDPKGVLYSHRSNVLHALMANN------GDALGTSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 255 ADI-----------GWVTGHTyityGPLAcgGTQVVFEGVPTwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDK 323
Cdd:PRK06018 220 ADTmlpvvplfhanSWGIAFS----APSM--GTKLVMPGAKL--DGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 324 VHPksyDLSSLRIIGTVgepiNPEAWMWYHKHVGQErcpIVDTWWQTETG--GHMITpLPGATPTVPGSCTL-------- 393
Cdd:PRK06018 292 KLP---HLKMVVCGGSA----MPRSMIKAFEDMGVE---VRHAWGMTEMSplGTLAA-LKPPFSKLPGDARLdvlqkqgy 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 394 PLPGIMAAVVDETGQDVP-NGQG-GILVVKRPWPAmirtiwgdperfrKSYYpeELGGRL------YLAGDGTVRDKDtG 465
Cdd:PRK06018 361 PPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVA-------------AAYY--RVDGEIldddgfFDTGDVATIDAY-G 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 466 YFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKrsrpEGEEAaalakTLRDWVGK 545
Cdd:PRK06018 425 YMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLK----PGETA-----TREEILKY 495
|
570 580 590
....*....|....*....|....*....|....
gi 1860891105 546 QIGPIAK---PKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:PRK06018 496 MDGKIAKwwmPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
57-506 |
2.55e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 79.17 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVta 136
Cdd:PRK09274 41 ELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 deqarggkTLPLKSIAdEAVAMGGCEAVKSVIVyrrTGgkidwhaGRDLW-MHELADAESDTCA----PEWVGAEHPLFI 211
Cdd:PRK09274 119 --------GIPKAHLA-RRLFGWGKPSVRRLVT---VG-------GRLLWgGTTLATLLRDGAAapfpMADLAPDDMAAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 212 LYTSGSTGKPKGVQHSTGgylLWAAQ--TMKWTFDWKPDDVfwctaDIgwvtgHTYitygPL------ACGGTQVVFEGV 283
Cdd:PRK09274 180 LFTSGSTGTPKGVVYTHG---MFEAQieALREDYGIEPGEI-----DL-----PTF----PLfalfgpALGMTSVIPDMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 284 PTWP---DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVhpksydLSSLRIIGTVGEPINPEAWMWYHKHVGQ-- 358
Cdd:PRK09274 243 PTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIK------LPSLRRVISAGAPVPIAVIERFRAMLPPda 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 359 ---------ERCPIV---------DTWWQTETGGhmitplpgatptvpGSCT-LPLPGIMAAVVD------ETGQDV--- 410
Cdd:PRK09274 317 eiltpygatEALPISsiesreilfATRAATDNGA--------------GICVgRPVDGVEVRIIAisdapiPEWDDAlrl 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 411 PNGQGGILVVKRPwpaMI-RTIWGDPERFRKSYYPEELGGRLYLAGDGTVRDkDTGYFTIMGRIDDVLNVSGHRLGTMEI 489
Cdd:PRK09274 383 ATGEIGEIVVAGP---MVtRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLD-AQGRLWFCGRKAHRVETAGGTLYTIPC 458
|
490
....*....|....*..
gi 1860891105 490 ESALVSHELVAEAAVVG 506
Cdd:PRK09274 459 ERIFNTHPGVKRSALVG 475
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
444-575 |
2.63e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.15 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 444 PEELggrLYLAGDGTVRDKDTGYFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVV 517
Cdd:PRK08308 281 PEEI---VVKMGDKEIFTKDLGYKSergtlhFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 518 AFVVlkrsrpeGEEAAALAKtLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:PRK08308 358 AKVI-------SHEEIDPVQ-LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
1-31 |
3.84e-15 |
|
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: 69.81 E-value: 3.84e-15
10 20 30
....*....|....*....|....*....|.
gi 1860891105 1 WHTPFTKVLDESDAPFYKWFDDGELNASYNC 31
Cdd:pfam16177 25 WFKPFDKVLDGSNGPFAKWFVGGKLNVCYNC 55
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
43-575 |
4.13e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 77.98 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEADdgtvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN 122
Cdd:cd17645 14 HVAVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTadeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheladaesdtcapew 202
Cdd:cd17645 89 YMLADSSAKILLT------------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 203 vGAEHPLFILYTSGSTGKPKGV---QHSTGGYLLW------------AAQTMKWTFDWKPDDVFwctadigwvtghTYIT 267
Cdd:cd17645 102 -NPDDLAYVIYTSGSTGLPKGVmieHHNLVNLCEWhrpyfgvtpadkSLVYASFSFDASAWEIF------------PHLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 268 YGplacGGTQVVFEGVPTwpDAGRFWKMIGDHKVTVFYTaPTairsliKAAEaddkvHPKSYDLSSLRIIGTVGEPINPE 347
Cdd:cd17645 169 AG----AALHVVPSERRL--DLDALNDYFNQEGITISFL-PT------GAAE-----QFMQLDNQSLRVLLTGGDKLKKI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 348 AWMWYHkhvgqercpIVDTWWQTETGgHMITPLPGATPTVPGSCTLPLPGIMAAVVDETGQDVPNGQGGILVVKRPwpAM 427
Cdd:cd17645 231 ERKGYK---------LVNNYGPTENT-VVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 428 IRTIWGDPERFRKSY--YPEELGGRLYLAGDgTVRDKDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVV 505
Cdd:cd17645 299 ARGYLNRPELTAEKFivHPFVPGERMYRTGD-LAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVL 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 506 GRPDDTTGEAVVAFVVLKRSRPEGEeaaalaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLL 575
Cdd:cd17645 378 AKEDADGRKYLVAYVTAPEEIPHEE--------LREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
58-521 |
5.20e-15 |
|
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: 78.03 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTad 137
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmhelaDAESDTCApewvgaehplFILYTSGS 217
Cdd:cd17639 84 ------------------------------------------------------DGKPDDLA----------CIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGYLLWAAQTMKWTFDW-KPDDvfwctadigwvtghTYITYGPLA------------------------ 272
Cdd:cd17639 100 TGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDD--------------RYLAYLPLAhifelaaenvclyrggtigygspr 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 273 ---------CGGTQVVFE-----GVPtwpdagRFWKMI-----------GDHKVTVFYTA----PTAIRSLIKAAEADDK 323
Cdd:cd17639 166 tltdkskrgCKGDLTEFKptlmvGVP------AIWDTIrkgvlaklnpmGGLKRTLFWTAyqskLKALKEGPGTPLLDEL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 324 VHPKSYDL--SSLRIIGTVGEPINPEAwmwyHKHVGQERCPIVDTWWQTETGGHMITPLPGATPTvpGSCTLPLPGIMAA 401
Cdd:cd17639 240 VFKKVRAAlgGRLRYMLSGGAPLSADT----QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLET--GRVGPPLPCCEIK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 402 VVD--ETGQ--DVPNGQGGILVvkrpwpamirtiwGDPERFrKSYYPEELGGRLYLAGDGTVRDKDTGYFT------IMG 471
Cdd:cd17639 314 LVDweEGGYstDKPPPRGEILI-------------RGPNVF-KGYYKNPEKTKEAFDGDGWFHTGDIGEFHpdgtlkIID 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 472 RIDD-VLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTgeaVVAFVV 521
Cdd:cd17639 380 RKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVV 427
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
463-578 |
5.52e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 76.62 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 463 DTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVlkrsrPEGEEAAALAKtLRDW 542
Cdd:PRK07824 245 DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPAPTLEA-LRAH 318
|
90 100 110
....*....|....*....|....*....|....*.
gi 1860891105 543 VGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:PRK07824 319 VARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
211-577 |
1.67e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.19 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGVQHS---TGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITygpLACGGTQVVFEGVptwp 287
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApqlRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLT---IALGGTVLTHRHF---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 288 DAGRFWKMIGDHKVTVFYTAPTAIRSLIkaaEADDKVHPKSyDLSSLRIIGTVGEPINPEAWMWYHKHVGQercPIVDTW 367
Cdd:PRK13383 252 DAEAALAQASLHRADAFTAVPVVLARIL---ELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 368 WQTETG-GHMITPlpGATPTVPGSCTLPLPGIMAAVVDETGQDV-PNGQGGILVvkrpwpamirtiwgdperfrksyyPE 445
Cdd:PRK13383 325 GSTEVGiGALATP--ADLRDAPETVGKPVAGCPVRILDRNNRPVgPRVTGRIFV------------------------GG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 446 ELGGRLYLAG------DGTVRDKDTGYFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTG 513
Cdd:PRK13383 379 ELAGTRYTDGggkavvDGMTSTGDMGYLDnagrlfIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFG 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 514 EAVVAFVVLkrsRP-EGEEAAAlaktLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRS 577
Cdd:PRK13383 459 HRLAAFVVL---HPgSGVDAAQ----LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
51-582 |
1.80e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.36 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 51 DDGTVTRVTYAELLARVSRFANALKKR-GIAKGDRVVIYMPMSIEGIVAMQACARIGAthsvVFggfsaKSLNERLVDVG 129
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA----VF-----NPLNKQLMNDQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 130 AVALVTADEQarggKTLplksIADEAVA------MGGCEAVKSVIVyrrTGGK-IDWHAGRDLWMHELADAES----DTC 198
Cdd:PRK05620 103 IVHIINHAED----EVI----VADPRLAeqlgeiLKECPCVRAVVF---IGPSdADSAAAHMPEGIKVYSYEAlldgRST 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 199 APEW-VGAEH-PLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKW-TFDWKPDDVFWCTADIGWVtghtyITYG-PLAC- 273
Cdd:PRK05620 172 VYDWpELDETtAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdSLAVTHGESFLCCVPIYHV-----LSWGvPLAAf 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 274 -GGTQVVFEGVPTwpDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEaddKVHPKSYDLSSLRIIGTVGEPINPEAWmwy 352
Cdd:PRK05620 247 mSGTPLVFPGPDL--SAPTLAKIIATAMPRVAHGVPTLWIQLMVHYL---KNPPERMSLQEIYVGGSAVPPILIKAW--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 353 hkhvgQER--CPIVDTWWQTETG--GHMITPLPGatptVPGSCTLP-------LPGIMAAVVDETGQDVP--NGQGGILV 419
Cdd:PRK05620 319 -----EERygVDVVHVWGMTETSpvGTVARPPSG----VSGEARWAyrvsqgrFPASLEYRIVNDGQVMEstDRNEGEIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 420 VKRPWPAM------IRTIWGDPERFRKSYYPEelgGRLYLAGDGTVRDKDT------GYFTIMGRIDDVLNVSGHRLGTM 487
Cdd:PRK05620 390 VRGNWVTAsyyhspTEEGGGAASTFRGEDVED---ANDRFTADGWLRTGDVgsvtrdGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 488 EIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAA-LAKTLRDwvgkQIGPIAKPKDIRFGDNLPKTR 566
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAErLRDQLRD----RLPNWMLPEYWTFVDEIDKTS 542
|
570
....*....|....*..
gi 1860891105 567 SGKIMRRLLRS-LAKGE 582
Cdd:PRK05620 543 VGKFDKKDLRQhLADGD 559
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
49-457 |
7.22e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 74.70 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 49 EADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN----ER 124
Cdd:PRK12582 72 EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDhaklKH 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 125 LVDVGAVALVTADEQARGGKTLplksiadEAVAMGGCEavksVIVYRRTGGKIDWHAGRDLWMHELAD---AESDTCAPE 201
Cdd:PRK12582 152 LFDLVKPRVVFAQSGAPFARAL-------AALDLLDVT----VVHVTGPGEGIASIAFADLAATPPTAavaAAIAAITPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 202 WVGAehplfILYTSGSTGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDD-----VFWctadIGW--VTGHTYITYGPLACG 274
Cdd:PRK12582 221 TVAK-----YLFTSGSTGMPKAVIN-TQRMMCANIAMQEQLRPREPDPpppvsLDW----MPWnhTMGGNANFNGLLWGG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVFEGVPTwpdAGRFWKMIGD-HKV--TVFYTAPTAIRSLIKAAEADDKVHPKSYdlSSLRIIGTVGEPINPEAW-- 349
Cdd:PRK12582 291 GTLYIDDGKPL---PGMFEETIRNlREIspTVYGNVPAGYAMLAEAMEKDDALRRSFF--KNLRLMAYGGATLSDDLYer 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 350 MWYH--KHVGqERCPIVDTWWQTETGGhmiTPLPGATPT-VPGSCTLPLPGIMAAVvdetgqdVPNGQGGILVVKRpwPA 426
Cdd:PRK12582 366 MQALavRTTG-HRIPFYTGYGATETAP---TTTGTHWDTeRVGLIGLPLPGVELKL-------APVGDKYEVRVKG--PN 432
|
410 420 430
....*....|....*....|....*....|.
gi 1860891105 427 MIRTIWGDPERFRKSYypEELGgrLYLAGDG 457
Cdd:PRK12582 433 VTPGYHKDPELTAAAF--DEEG--FYRLGDA 459
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
56-557 |
1.13e-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: 73.55 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVt 135
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 adeqarggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwmheLADAESDTCApewvgaehplfILYTS 215
Cdd:cd17640 83 ------------------------------------------------------VENDSDDLAT-----------IIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 216 GSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIgWvtgHTY---ITYGPLACGGTQVvFEGVPTWPDAgrf 292
Cdd:cd17640 98 GTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-YTSIRTLKDD--- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 293 wkmIGDHKVTVFYTAP---TAIRSLIkaaeaDDKVHPKSYD----LSSLRIIGTVGEPINPEAWMWYH-----KHVGqer 360
Cdd:cd17640 169 ---LKRVKPHYIVSVPrlwESLYSGI-----QKQVSKSSPIkqflFLFFLSGGIFKFGISGGGALPPHvdtffEAIG--- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 361 CPIVDTWWQTETGGHMITPLPGATptVPGSCTLPLPGIMAAVVD-ETGQDVPNGQGGILVVKRPwPAMirtiwgdperfr 439
Cdd:cd17640 238 IEVLNGYGLTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGP-QVM------------ 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 440 KSYYPEELGGRLYLAGDGTVRDKDTGYFT------IMGRIDD--VLNvSGHRLGTMEIESALVSHELVAEAAVVGRPDDT 511
Cdd:cd17640 303 KGYYKNPEATSKVLDSDGWFNTGDLGWLTcggelvLTGRAKDtiVLS-NGENVEPQPIEEALMRSPFIEQIMVVGQDQKR 381
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1860891105 512 TGEAVVafvvlkrsrPEGEEAAALAKTLRDWVGKQIGPIAKPKDIR 557
Cdd:cd17640 382 LGALIV---------PNFEELEKWAKESGVKLANDRSQLLASKKVL 418
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
56-575 |
1.69e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.01 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIG------ATHSVVfggfsakslnERLVDVG 129
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSSPA----------ERIEMII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 130 AVAlvtadeqarggKTLPLKSIADEAVAMGGCEAVKSVivyrrtggkidwhagrdlwmhELADAESDTCAPE---WVGAE 206
Cdd:PRK04813 96 EVA-----------KPSLIIATEELPLEILGIPVITLD---------------------ELKDIFATGNPYDfdhAVKGD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 207 HPLFILYTSGSTGKPKGVQ----------------HSTGGYLLWAAQTmKWTFDWKPDDVFWCtadigwvtghtyitygp 270
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQishdnlvsftnwmledFALPEGPQFLNQA-PYSFDLSVMDLYPT----------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 271 LACGGTQVVFEGVPTwPDAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHPksydlsSLRIIGTVGEPI-NPEAW 349
Cdd:PRK04813 206 LASGGTLVALPKDMT-ANFKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLP------NLTHFLFCGEELpHKTAK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 350 MWYhkhvgqERCP---IVDTWWQTETGGHM----IT--------PLP-GATPtvPGSCTLplpgimaaVVDETGQDVPNG 413
Cdd:PRK04813 279 KLL------ERFPsatIYNTYGPTEATVAVtsieITdemldqykRLPiGYAK--PDSPLL--------IIDEEGTKLPDG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 414 QGGILVVKRPwpAMIRTIWGDPERFRKSYYPEElGGRLYLAGD-GTVRDkdtGYFTIMGRIDDVLNVSGHRLGTMEIESA 492
Cdd:PRK04813 343 EQGEIVISGP--SVSKGYLNNPEKTAEAFFTFD-GQPAYHTGDaGYLED---GLLFYQGRIDFQIKLNGYRIELEEIEQN 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 493 LVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEeaAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMR 572
Cdd:PRK04813 417 LRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFERE--FELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
...
gi 1860891105 573 RLL 575
Cdd:PRK04813 495 KAL 497
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
49-507 |
4.00e-13 |
|
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: 72.07 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 49 EADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIY---MPMSIEGIVAMQACARIgathSVvfgGFSAKSLNER- 124
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILgdnRPEWVWAELAAQAIGAL----SL---GIYQDSMAEEv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 125 --LVDVGAVALVTADEQARGGKTLPlksIADEAvamggcEAVKSVIVYRRTGGKiDWHAGRDLWMHEL------ADAESD 196
Cdd:cd17641 76 ayLLNYTGARVVIAEDEEQVDKLLE---IADRI------PSVRYVIYCDPRGMR-KYDDPRLISFEDVvalgraLDRRDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 197 TCAPEWVGAEHP---LFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKwtFDWK-PDDVFWCTADIGWVTGHTYITYGPLA 272
Cdd:cd17641 146 GLYEREVAAGKGedvAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPLgPGDEYVSVLPLPWIGEQMYSVGQALV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 273 CGGT-------------------QVVFEGVPTWP-----------DAGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADD 322
Cdd:cd17641 224 CGFIvnfpeepetmmedlreigpTFVLLPPRVWEgiaadvrarmmDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 323 KVHPKSYDL-----------SSLRIIGTVGEPINPEAWMWYHKhVGqerCPIVDTWWQTETGGHMITPLPGATPtvPGSC 391
Cdd:cd17641 304 LASWLADALlfrplrdrlgfSRLRSAATGGAALGPDTFRFFHA-IG---VPLKQLYGQTELAGAYTVHRDGDVD--PDTV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 392 TLPLPGimAAV-VDETGQdvpngqggiLVVKRpwPAMIRTIWGDPERFRKSyypeelggrlyLAGDGTVRDKDTGYFT-- 468
Cdd:cd17641 378 GVPFPG--TEVrIDEVGE---------ILVRS--PGVFVGYYKNPEATAED-----------FDEDGWLHTGDAGYFKen 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1860891105 469 ----IMGRIDDVLNVS-GHRLGTMEIESALVSHELVAEAAVVGR 507
Cdd:cd17641 434 ghlvVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
205-582 |
1.04e-12 |
|
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: 70.59 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLFILYTSGSTGKPKGVQHsTGGYLLWAAQTMKWTFDWKPDDVF--W--CTADIGWVTGHtyitYGPLACGGTQVVf 280
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVML-THENLVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIAGMNQYL- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 281 egVPTWPDAGR--FW-KMIGDHKVTVFYTAPTAIRSLIKAAEaDDKVHpkSYDLSSLRIIGTVGEPINPEAWMWYHKHV- 356
Cdd:cd05908 179 --MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKTLK-PEKAN--DWDLSSIRMILNGAEPIDYELCHEFLDHMs 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 --GQERCPIVDTWWQTET---------GGHMIT------------PLPGATPTVPGSCTL-----PLPGIMAAVVDETGQ 408
Cdd:cd05908 254 kyGLKRNAILPVYGLAEAsvgaslpkaQSPFKTitlgrrhvthgePEPEVDKKDSECLTFvevgkPIDETDIRICDEDNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 409 DVPNGQGGILVVKrpwpamirtiwgdPERFRKSYYPEELGGRLYLAGDGTVRDKDTGY-----FTIMGRIDDVLNVSGHR 483
Cdd:cd05908 334 ILPDGYIGHIQIR-------------GKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFirngrLVITGREKDIIFVNGQN 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 484 LGTMEIESALVSHE--LVAEAAVVGRPD-DTTGEAVVAFVVLKRSRpegEEAAALAKTLRD-------WVGKQIGPIAKp 553
Cdd:cd05908 401 VYPHDIERIAEELEgvELGRVVACGVNNsNTRNEEIFCFIEHRKSE---DDFYPLGKKIKKhlnkrggWQINEVLPIRR- 476
|
410 420 430
....*....|....*....|....*....|
gi 1860891105 554 kdirfgdnLPKTRSGKIMR-RLLRSLAKGE 582
Cdd:cd05908 477 --------IPKTTSGKVKRyELAQRYQSGE 498
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
57-576 |
3.03e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.44 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTa 136
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVT- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEQARggktlplkSIADEaVAMGGCEAVKSVIVYRRTGGKI-----DWHAGRDLWMHELADAESDTC-APEWVgaehpLF 210
Cdd:PLN02860 111 DETCS--------SWYEE-LQNDRLPSLMWQVFLESPSSSVfiflnSFLTTEMLKQRALGTTELDYAwAPDDA-----VL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGVQHStggYLLWAAQTM-KWTF-DWKPDDVFWCTA---DIGWVTGHTYItygpLACGGTQVVfegVPT 285
Cdd:PLN02860 177 ICFTSGTTGRPKGVTIS---HSALIVQSLaKIAIvGYGEDDVYLHTAplcHIGGLSSALAM----LMVGACHVL---LPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 286 WpDAGRFWKMIGDHKVTVFYTAPTAIRSLIK--AAEADDKVHPK-------SYDLSSLRIIGTVGEPINPEAWMWYHKhv 356
Cdd:PLN02860 247 F-DAKAALQAIKQHNVTSMITVPAMMADLISltRKSMTWKVFPSvrkilngGGSLSSRLLPDAKKLFPNAKLFSAYGM-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 gQERC----------PIVDTWWQTETGGHMITPLPGATPTvpGSCT-LPLPGIMAAVvdetGQDVPNGQGGILVvkRPWP 425
Cdd:PLN02860 324 -TEACssltfmtlhdPTLESPKQTLQTVNQTKSSSVHQPQ--GVCVgKPAPHVELKI----GLDESSRVGRILT--RGPH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 426 AMIRtIWGDPerfrkSYYPEELGGRLYLA-GDGTVRDkDTGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAV 504
Cdd:PLN02860 395 VMLG-YWGQN-----SETASVLSNDGWLDtGDIGWID-KAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 505 VGRPDDTTGEAVVAFVVLK--------RSRPEGEEAAALAKTLRDWVGKQ-IGPIAKPKDI-RFGDNLPKTRSGKIMRRL 574
Cdd:PLN02860 468 VGVPDSRLTEMVVACVRLRdgwiwsdnEKENAKKNLTLSSETLRHHCREKnLSRFKIPKLFvQWRKPFPLTTTGKIRRDE 547
|
..
gi 1860891105 575 LR 576
Cdd:PLN02860 548 VR 549
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
38-578 |
4.95e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.48 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 38 AGNGQRVAVIFEADDGTvtRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGA--------TH 109
Cdd:PRK07768 12 ARTSPRGMVTGEPDAPV--RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAsltmlhqpTP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 110 SVVFGGFSAKSLNeRLVDVGAVALVTADeqarggktlPLKSIADEAVAMGgceavksVIVYRRTggkidwhagrDLWMHE 189
Cdd:PRK07768 90 RTDLAVWAEDTLR-VIGMIGAKAVVVGE---------PFLAAAPVLEEKG-------IRVLTVA----------DLLAAD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 190 LADaesdtcaPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGylLWA-AQTMKWTFDWKPDD---VFW--CTADIGWVTGH 263
Cdd:PRK07768 143 PID-------PVETGEDDLALMQLTSGSTGSPKAVQITHGN--LYAnAEAMFVAAEFDVETdvmVSWlpLFHDMGMVGFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 264 TYitygPLACGGTQVV-----FEGVP-TWPdagrfwKMIGDHKVTV-----FYTAPTAiRSLIKAAEaddkvhPKSYDLS 332
Cdd:PRK07768 214 TV----PMYFGAELVKvtpmdFLRDPlLWA------ELISKYRGTMtaapnFAYALLA-RRLRRQAK------PGAFDLS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 333 SLRIIGTVGEPINP---EAWMWYHKHVGQERCPIVDTWWQTET---------GGHMITPLPG---------ATPTVPG-- 389
Cdd:PRK07768 277 SLRFALNGAEPIDPadvEDLLDAGARFGLRPEAILPAYGMAEAtlavsfspcGAGLVVDEVDadllaalrrAVPATKGnt 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 390 ----SCTLPLPGIMAAVVDETGQDVPNGQGGILVVKrpwpamirtiwGDPerfRKSYYPEELGGRLYLAGDGTVRDKDTG 465
Cdd:PRK07768 357 rrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR-----------GES---VTPGYLTMDGFIPAQDADGWLDTGDLG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 466 YFT------IMGRIDDVLNVSGHRLGTMEIESALVSHELV--AEAAVVGRPDDTTGEAvVAFVVLKRSRPEGEEAAALAK 537
Cdd:PRK07768 423 YLTeegevvVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrpGNAVAVRLDAGHSREG-FAVAVESNAFEDPAEVRRIRH 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1860891105 538 TLRDWVGKQIGpiAKPKDIRF---GdNLPKTRSGKIMRRLLRSL 578
Cdd:PRK07768 502 QVAHEVVAEVG--VRPRNVVVlgpG-SIPKTPSGKLRRANAAEL 542
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
56-456 |
5.04e-12 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 68.61 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN----ERLVDVGAV 131
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDlaklKHLFELLKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 132 ALVTADEQARGGKTLplksiaDEAVAMGgceavKSVIVYRRTGgkidwhAGRD-LWMHELADAESDTCAPEWVGAEHPLF 210
Cdd:cd05921 104 GLVFAQDAAPFARAL------AAIFPLG-----TPLVVSRNAV------AGRGaISFAELAATPPTAAVDAAFAAVGPDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 I---LYTSGSTGKPKGVQHSTGgyLLWAAQTMK---WTF---------DWKP-DDVFWCTADIGWVtghtyitygpLACG 274
Cdd:cd05921 167 VakfLFTSGSTGLPKAVINTQR--MLCANQAMLeqtYPFfgeeppvlvDWLPwNHTFGGNHNFNLV----------LYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVFEGVPTwpdAGRFWKMIGDHK---VTVFYTAPTAIRSLIKAAEADDKVHPKSYDlsSLRIIGTVGEPINPEAWMW 351
Cdd:cd05921 235 GTLYIDDGKPM---PGGFEETLRNLReisPTVYFNVPAGWEMLVAALEKDEALRRRFFK--RLKLMFYAGAGLSQDVWDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 352 YH----KHVGqERCPIVDTWWQTETGghmitplPGATPTV-----PGSCTLPLPGIMAAVvdetgqdVPNgqGGILVVKR 422
Cdd:cd05921 310 LQalavATVG-ERIPMMAGLGATETA-------PTATFTHwpterSGLIGLPAPGTELKL-------VPS--GGKYEVRV 372
|
410 420 430
....*....|....*....|....*....|....
gi 1860891105 423 PWPAMIRTIWGDPERFRKSYypEELGgrLYLAGD 456
Cdd:cd05921 373 KGPNVTPGYWRQPELTAQAF--DEEG--FYCLGD 402
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
34-581 |
7.09e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 68.19 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 34 RHveAGNGQRVAVIFEADdgtVTRVTYAELLARVSRFANALKKRGIAKGDRVviympmsieGIVAMQACARIGATHSVVF 113
Cdd:PRK07008 21 RH--AGDTEIVSRRVEGD---IHRYTYRDCERRAKQLAQALAALGVEPGDRV---------GTLAWNGYRHLEAYYGVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 114 GGFSAKSLNERLV-DVGAVALVTADEQARGGKT--LPLKsiadEAVAmGGCEAVKSVIVYrrtggkidwhAGRDlwmHEL 190
Cdd:PRK07008 87 SGAVCHTINPRLFpEQIAYIVNHAEDRYVLFDLtfLPLV----DALA-PQCPNVKGWVAM----------TDAA---HLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 191 ADAESDTCAPEWVGAEH-----PLF-------ILYTSGSTGKPKGVQHSTGGYLLWA-AQTMKWTFDWKPDDV------- 250
Cdd:PRK07008 149 AGSTPLLCYETLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMGLSARDAvlpvvpm 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 251 FWCTAdigWVTGHTyityGPLAcgGTQVVFEGvptwP--DAGRFWKMIGDHKVTVFYTAPTAIRSLIKaaeaddKVHPKS 328
Cdd:PRK07008 229 FHVNA---WGLPYS----APLT--GAKLVLPG----PdlDGKSLYELIEAERVTFSAGVPTVWLGLLN------HMREAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 329 YDLSSLR--IIGtvGEPINPEAWMWYHKHVGQErcpIVDTWWQTEtgghmITPLpGATptvpgsCTL------------- 393
Cdd:PRK07008 290 LRFSTLRrtVIG--GSACPPAMIRTFEDEYGVE---VIHAWGMTE-----MSPL-GTL------CKLkwkhsqlpldeqr 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 394 --------PLPGIMAAVVDETGQDVP-NGQG-GILVVKRPWpaMIRtiwgdpERFRKSYYPeeLGGRLYLAGDGTVRDKD 463
Cdd:PRK07008 353 kllekqgrVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPW--VID------RYFRGDASP--LVDGWFPTGDVATIDAD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 464 tGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVaFVVLKRSRPEGEEAAALA----KTL 539
Cdd:PRK07008 423 -GFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPL-LVVVKRPGAEVTREELLAfyegKVA 500
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1860891105 540 RDWVgkqigpiakPKDIRFGDNLPKTRSGKIMRRLLRSLAKG 581
Cdd:PRK07008 501 KWWI---------PDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
204-587 |
1.10e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.27 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 204 GAEHPLFILYTSGSTGKPKGV----------QHSTGGYLLWA-----AQTMKWTFD---WKpddvfwctadigwvtghty 265
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVmveqrgmlnnQLSKVPYLALSeadviAQTASQSFDisvWQ------------------- 3927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 266 ITYGPLACGGTQVVFEGVPTWPDAgrFWKMIGDHKVTVFYTAPtairSLIKAAEADDKVhpksyDLSSLRIIGTVGEPIN 345
Cdd:PRK05691 3928 FLAAPLFGARVEIVPNAIAHDPQG--LLAHVQAQGITVLESVP----SLIQGMLAEDRQ-----ALDGLRWMLPTGEAMP 3996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 346 PE-AWMWYHKH--------VGQERCPIVDTWWQTETGGHMITPLPGATPTVPGSCTLplpgimaavVDETGQDVPNGQGG 416
Cdd:PRK05691 3997 PElARQWLQRYpqiglvnaYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYL---------LDEALELVPLGAVG 4067
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 417 ILVVKRPwpAMIRTIWGDPERFRKSYYPEELGG---RLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESAL 493
Cdd:PRK05691 4068 ELCVAGT--GVGRGYVGDPLRTALAFVPHPFGApgeRLYRTGDLARRRSD-GVLEYVGRIDHQVKIRGYRIELGEIEARL 4144
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 494 VSHELVAEAAvVGRPDDTTGEAVVAFVVlkrSRPEGEEAAALAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRR 573
Cdd:PRK05691 4145 HEQAEVREAA-VAVQEGVNGKHLVGYLV---PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRK 4220
|
410
....*....|....
gi 1860891105 574 LLRSLAKGEAITQD 587
Cdd:PRK05691 4221 ALPALDIGQLQSQA 4234
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
51-398 |
2.59e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 66.44 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 51 DDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLN-ERLVDVG 129
Cdd:PRK08180 63 ADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVSQDfGKLRHVL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 130 AV---ALVTADEQARGGKTLplksiadEAVAMGGCEavksVIVYRRTGGKIDWHAGRDLwmheLADAESDTCAP--EWVG 204
Cdd:PRK08180 143 ELltpGLVFADDGAAFARAL-------AAVVPADVE----VVAVRGAVPGRAATPFAAL----LATPPTAAVDAahAAVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLFILYTSGSTGKPKGVQHSTGgyLLWAAQTMK---WTF---------DWKPddvfWctadigwvtGHTY------- 265
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHR--MLCANQQMLaqtFPFlaeeppvlvDWLP----W---------NHTFggnhnlg 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 266 ITygpLACGGTQVVFEGVPTwpdAGRFWKMIGDHKV---TVFYTAPTAIRSLIKAAEADDKVHPKSYdlSSLRIIGTVGE 342
Cdd:PRK08180 273 IV---LYNGGTLYIDDGKPT---PGGFDETLRNLREispTVYFNVPKGWEMLVPALERDAALRRRFF--SRLKLLFYAGA 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 343 PINPEAWMWYH----KHVGqERCPIVDTWWQTETGghmitplPGAT----PTV-PGSCTLPLPGI 398
Cdd:PRK08180 345 ALSQDVWDRLDrvaeATCG-ERIRMMTGLGMTETA-------PSATfttgPLSrAGNIGLPAPGC 401
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
382-579 |
3.50e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.40 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 382 GATPTVPGSCTLpLPGIMAAVVDETGQDVPNGQGGIlvvkRPWPAMIRTIWGdpERFRKSYYPEELGGRLYL-AGDGTVR 460
Cdd:PRK07445 262 GMTETASQIATL-KPDDFLAGNNSSGQVLPHAQITI----PANQTGNITIQA--QSLALGYYPQILDSQGIFeTDDLGYL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 461 DKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEaaalaktLR 540
Cdd:PRK07445 335 DAQ-GYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEE-------LK 406
|
170 180 190
....*....|....*....|....*....|....*....
gi 1860891105 541 DWVGKQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:PRK07445 407 TAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
58-575 |
6.74e-11 |
|
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: 64.77 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTAD 137
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 EqarggktlplksiadEAVAMggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewvgaehplfILYTSGS 217
Cdd:cd05914 88 E---------------DDVAL----------------------------------------------------INYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQhSTGGYLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTqVVFEGVPTWP--DAGRFWK- 294
Cdd:cd05914 101 TGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAH-VVFLDKIPSAkiIALAFAQv 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 295 --MIGDHKV-TVFYTAPTAIRSLIKAAEADDKVHPKSYDLS---------------SLRIIGTVGEPINPEAWMWYHKhV 356
Cdd:cd05914 179 tpTLGVPVPlVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKirklafkkvheafggNIKEFVIGGAKINPDVEEFLRT-I 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 357 GqerCPIVDTWWQTETGghmitPLPGATP---TVPGSCTLPLPGIMAAVVDEtgqDVPNGQGGILVVKrpwPAMIRTIWG 433
Cdd:cd05914 258 G---FPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRIDSP---DPATGEGEIIVRG---PNVMKGYYK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 434 DPERFRKSYYPEelgGRLYlAGD-GTVrdKDTGYFTIMGRIDDV-LNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDT 511
Cdd:cd05914 324 NPEATAEAFDKD---GWFH-TGDlGKI--DAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 512 TGEAVVAFVVLKRS---RPEGEEAaaLAKTLRDWVGKQIGPIAKPKDIR-FGDNLPKTRSGKIMRRLL 575
Cdd:cd05914 398 VALAYIDPDFLDVKalkQRNIIDA--IKWEVRDKVNQKVPNYKKISKVKiVKEEFEKTPKGKIKRFLY 463
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
59-272 |
2.91e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 63.21 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTADE 138
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 139 QarggktlpLKSIADEAvamGGCEAVKSVIVYRRTGGKIDwhagrdlwmHELADAESDTCAP----EWVGAEHPL----- 209
Cdd:PLN02387 188 Q--------LKKLIDIS---SQLETVKRVIYMDDEGVDSD---------SSLSGSSNWTVSSfsevEKLGKENPVdpdlp 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 210 ------FILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVfwctadigwvtghtYITYGPLA 272
Cdd:PLN02387 248 spndiaVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLA 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
43-582 |
4.37e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 43 RVAVIFEADDGTVTRV-TYAELLARVSRFANALKKRGiAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSL 121
Cdd:PRK05691 25 RLALRFLADDPGEGVVlSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 122 N-ERLVDVgavalvTADEQARggktlPLKSIADEAVAMGGCEAVKSvivyrrtggkidwhAGRDLWMheLADAESDTCAP 200
Cdd:PRK05691 104 HqERLLSI------IADAEPR-----LLLTVADLRDSLLQMEELAA--------------ANAPELL--CVDTLDPALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 201 EWVG----AEHPLFILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTF--DWKPDDVFwctadIGWVTghTYITYGpLACG 274
Cdd:PRK05691 157 AWQEpalqPDDIAFLQYTSGSTALPKGVQVSHGN-LVANEQLIRHGFgiDLNPDDVI-----VSWLP--LYHDMG-LIGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 275 GTQVVFEGVPT--------------WPDAgrfwkmIGDHKVTVFYTAPTAIRsLIKAAEADDKVhpKSYDLSSLRIIGTV 340
Cdd:PRK05691 228 LLQPIFSGVPCvlmspayflerplrWLEA------ISEYGGTISGGPDFAYR-LCSERVSESAL--ERLDLSRWRVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 341 GEPI-----------------NPEAWMWYHkhvGQERCPIVDTWWQTetgGHMITPL-------------PGATPTVPgS 390
Cdd:PRK05691 299 SEPIrqdslerfaekfaacgfDPDSFFASY---GLAEATLFVSGGRR---GQGIPALeldaealarnraePGTGSVLM-S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 391 CTLPLPGIMAAVVD-ETGQDVPNGQGGILvvkrpW---PAMIRTIWGDPERFRKSYYpeELGGRLYL-AGD-GTVRDkdt 464
Cdd:PRK05691 372 CGRSQPGHAVLIVDpQSLEVLGDNRVGEI-----WasgPSIAHGYWRNPEASAKTFV--EHDGRTWLrTGDlGFLRD--- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 465 GYFTIMGRIDDVLNVSGHRLGTMEIESALVShelvaEAAVV--GRpddttgeaVVAFVVlkrsRPEGEEAAALAKTLRDW 542
Cdd:PRK05691 442 GELFVTGRLKDMLIVRGHNLYPQDIEKTVER-----EVEVVrkGR--------VAAFAV----NHQGEEGIGIAAEISRS 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 543 VGKQIGPIAKPKDIRFG-----------------DNLPKTRSGKIMRRLLRS-LAKGE 582
Cdd:PRK05691 505 VQKILPPQALIKSIRQAvaeacqeapsvvlllnpGALPKTSSGKLQRSACRLrLADGS 562
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-541 |
1.83e-09 |
|
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: 60.17 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 57 RVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQAcarigathsvvfggfsakslnerLVDVGAVALVTa 136
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFA-----------------------LFKAGAVPVLI- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 dEQARGGKTLplksiadeavamGGCeavksvivyrrtggkidwhagrdlwmheLADAESDTcapeWVG---AEHPLFILY 213
Cdd:cd05910 58 -DPGMGRKNL------------KQC----------------------------LQEAEPDA----FIGipkADEPAAILF 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 214 TSGSTGKPKGVQHSTGGYllwAAQ--TMKWTFDWKPDDVFWCTADIgwvtghtYITYGPlACGGTQVVFEGVPTWP---D 288
Cdd:cd05910 93 TSGSTGTPKGVVYRHGTF---AAQidALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDPTRParaD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 289 AGRFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDKvhpksyDLSSLRIIGTVGEPINPEAWMWYHKHVGQErCPIVDTWW 368
Cdd:cd05910 162 PQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGI------TLPSLRRVLSAGAPVPIALAARLRKMLSDE-AEILTPYG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 369 QTET------GGH-MITPLPGATPTVPGSCT-LPLPGIMAAVVDETGQD---------VPNGQGGILVVKRpwPAMIRTI 431
Cdd:cd05910 235 ATEAlpvssiGSReLLATTTAATSGGAGTCVgRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTG--PTVTPTY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 WGDPERFRKSYYPEELGGRLYLAGD-GTVRDKDTGYFtiMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRpdd 510
Cdd:cd05910 313 VNRPVATALAKIDDNSEGFWHRMGDlGYLDDEGRLWF--CGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--- 387
|
490 500 510
....*....|....*....|....*....|.
gi 1860891105 511 TTGEAVVAFVVLKRSRPEGEEAAALAKTLRD 541
Cdd:cd05910 388 GKPGCQLPVLCVEPLPGTITPRARLEQELRA 418
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
56-579 |
2.67e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 59.75 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 56 TRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVT 135
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 ADEQArggktlplksiadeavamggceavksvivyrrtggkidwhagrdlwMHELADAESDTCAPewVGAEHPLFILYTS 215
Cdd:cd05939 82 NLLDP----------------------------------------------LLTQSSTEPPSQDD--VNFRDKLFYIYTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 216 GSTGKPKG--VQHSTggyLLWAAQTMKWTFDWKPDDVFWCTADIgWVTGHTYITYGPLACGGTQVV----FEgvptwpdA 289
Cdd:cd05939 114 GTTGLPKAavIVHSR---YYRIAAGAYYAFGMRPEDVVYDCLPL-YHSAGGIMGVGQALLHGSTVVirkkFS-------A 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 290 GRFWKMIGDHKVTVFYTAPTAIRSLIKAaeaddkvhPKSYDLSSLRIIGTVGEPINPEAWMWYHKHVGQERcpIVDTWWQ 369
Cdd:cd05939 183 SNFWDDCVKYNCTIVQYIGEICRYLLAQ--------PPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQ--IGEFYGA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 370 TETGGHM--ITPLPGATPTVP--GSCTLPL------PGIMAAVVDETGQDVP--NGQGGILVVKrpwpamirTIWGDPER 437
Cdd:cd05939 253 TEGNSSLvnIDNHVGACGFNSriLPSVYPIrlikvdEDTGELIRDSDGLCIPcqPGEPGLLVGK--------IIQNDPLR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 438 FRKSYYPE------------ELGGRLYLAGDGTVRDkDTGYFTIMGRIDDVLNVSGHRLGTMEIEsALVSHEL-VAEAAV 504
Cdd:cd05939 325 RFDGYVNEgatnkkiardvfKKGDSAFLSGDVLVMD-ELGYLYFKDRTGDTFRWKGENVSTTEVE-GILSNVLgLEDVVV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 505 VG-RPDDTTGEAVVAFVVlkrsRPEGEE-----AAALAKTLRdwvgkqigPIAKPKDIRFGDNLPKTRSGKIMRRLLRSL 578
Cdd:cd05939 403 YGvEVPGVEGRAGMAAIV----DPERKVdldrfSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
.
gi 1860891105 579 A 579
Cdd:cd05939 471 G 471
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
205-583 |
1.06e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.44 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 AEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTfDWKPDDVFWCTADIGWVTGHTyitygplacGGTQV-VFEGV 283
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDKVFNALPVFHSFGLT---------GGLVLpLLSGV 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 284 PTW-----------PDagrfwkMIGDHKVTVFYTAPTAIRSLIKAAeaddkvHPksYDLSSLRIIGTVGEPINPEAWMWY 352
Cdd:PRK06814 862 KVFlypsplhyriiPE------LIYDTNATILFGTDTFLNGYARYA------HP--YDFRSLRYVFAGAEKVKEETRQTW 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 353 hkhvgqercpivdtwwqTETGGHMITPLPGATPTVPG-SCTLP-----------LPGIMAAVVDETGQDvpngQGGILVV 420
Cdd:PRK06814 928 -----------------MEKFGIRILEGYGVTETAPViALNTPmhnkagtvgrlLPGIEYRLEPVPGID----EGGRLFV 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 421 KRPwPAMIRTIwgdpeRFRKSYYPEELGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGhrlgtmEIESALVSHELVA 500
Cdd:PRK06814 987 RGP-NVMLGYL-----RAENPGVLEPPADGWYDTGDIVTIDEE-GFITIKGRAKRFAKIAG------EMISLAAVEELAA 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 501 EA------AVVGRPDDTTGEAVVAFVvlkrSRPEGEEAAALAKTLRdwvgKQIGPIAKPKDIRFGDNLPKTRSGKI---- 570
Cdd:PRK06814 1054 ELwpdalhAAVSIPDARKGERIILLT----TASDATRAAFLAHAKA----AGASELMVPAEIITIDEIPLLGTGKIdyva 1125
|
410
....*....|...
gi 1860891105 571 MRRLLRSLAKGEA 583
Cdd:PRK06814 1126 VTKLAEEAAAKPE 1138
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
211-579 |
1.20e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.72 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 211 ILYTSGSTGKPKGVQHSTGGyLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEG------VP 284
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyriVP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 285 twpdagrfwKMIGDHKVTVFYTAPTAIRSLIKAAeaddkvHPksYDLSSLRIIGTVGEPINPEAwmwyhKHVGQER--CP 362
Cdd:PRK08043 449 ---------ELVYDRNCTVLFGTSTFLGNYARFA------NP--YDFARLRYVVAGAEKLQEST-----KQLWQDKfgLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 363 IVDTWWQTETGGHMITPLPGATPtvPGSCTLPLPGIMAAVVDETGQDvpngQGGILVVKRPwpamirtiwgdpeRFRKSY 442
Cdd:PRK08043 507 ILEGYGVTECAPVVSINVPMAAK--PGTVGRILPGMDARLLSVPGIE----QGGRLQLKGP-------------NIMNGY 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 443 YPEELGGRL----------------YLAGDgTVRDKDTGYFTIMGRIDDVLNVSGH--RLGTMEIESALVSHElvAEAAV 504
Cdd:PRK08043 568 LRVEKPGVLevptaenargemergwYDTGD-IVRFDEQGFVQIQGRAKRFAKIAGEmvSLEMVEQLALGVSPD--KQHAT 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 505 VGRPDDTTGEAVVAFVV---LKRsrpegEEAAALAKTLrdwvgkQIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSLA 579
Cdd:PRK08043 645 AIKSDASKGEALVLFTTdseLTR-----EKLQQYAREH------GVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
214-561 |
2.51e-07 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 53.40 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 214 TSGSTGKPKGVQHSTGG--YLLWAAQTMKWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTqvVFEGVPTWPDagR 291
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDldVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGAL--VIPAGGGNTE--R 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 292 FWKMIGDHKVTVFYTAPTAIRSLIKAAEaDDKVHPKSydlSSLRIIGTVGEPINPEAWMWYHKHVGQERCpivDTWWQTE 371
Cdd:cd05913 162 QLQLIKDFGPTVLCCTPSYALYLAEEAE-EEGIDPRE---LSLKVGIFGAEPWTEEMRKRIERRLGIKAY---DIYGLTE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 372 TGGhmitplpgatPTVPGSCTLPL------PGIMAAVVD-ETGQDVPNGQGGILVV----KRPWPaMIRTIWGDPERFRk 440
Cdd:cd05913 235 IIG----------PGVAFECEEKDglhiweDHFIPEIIDpETGEPVPPGEVGELVFttltKEAMP-LIRYRTRDITRLL- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 441 syYPEELGGRLYLAGDGtvrdkdtgyftIMGRIDDVLNVSGHRLGTMEIESALVSH-ELVAEAAVVGRPDDTTGEAVVAf 519
Cdd:cd05913 303 --PGPCPCGRTHRRIDR-----------ITGRSDDMLIIRGVNVFPSQIEDVLLKIpGLGPHYQLILTRQEHLDELTIK- 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1860891105 520 VVLKRSRPEGEEAAALAKTLRD-------------WVGKQIGPIAKPKDIRFGDN 561
Cdd:cd05913 369 VEVRPEADDDEKLEALKQRLERhiksvlgvtveveLVEPGSLPRSEGKAKRVIDK 423
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
58-224 |
1.38e-06 |
|
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: 51.30 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALK-KRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVAL-VT 135
Cdd:cd17632 68 ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 136 ADeqarggkTLPLksiADEAVAMGGceAVKSVIV--YRRtggKIDWHA-------------GRDLWMHELADAESDTCAP 200
Cdd:cd17632 148 AE-------HLDL---AVEAVLEGG--TPPRLVVfdHRP---EVDAHRaalesarerlaavGIPVTTLTLIAVRGRDLPP 212
|
170 180
....*....|....*....|....*....
gi 1860891105 201 -----EWVGAEHPLFILYTSGSTGKPKGV 224
Cdd:cd17632 213 aplfrPEPDDDPLALLIYTSGSTGTPKGA 241
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-590 |
6.66e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 49.23 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 53 GTVTRV-TYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHS-----VVFGGFSA--KSLNER 124
Cdd:PRK09192 44 GQLEEAlPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 125 LVDVGAVALVTADEqarggktlpLKSIADEAVamGGCEAVKSVivyrrtggkidwhAGRDLWMHELADAESDTCAPEwvg 204
Cdd:PRK09192 124 LASAQPAAIITPDE---------LLPWVNEAT--HGNPLLHVL-------------SHAWFKALPEADVALPRPTPD--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 205 aeHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDD--VFWCT--ADIGWVtghtyityG----PLACggt 276
Cdd:PRK09192 177 --DIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDrcVSWLPfyHDMGLV--------GflltPVAT--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 277 QVVFEGVPTWPDAGR--FW-KMIGDHKVTVFYTAPTAIRSLIKAAEADDKVHpksYDLSSLRIIGTVGEPINPEAWMWYH 353
Cdd:PRK09192 244 QLSVDYLPTRDFARRplQWlDLISRNRGTISYSPPFGYELCARRVNSKDLAE---LDLSCWRVAGIGADMIRPDVLHQFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 354 KHVGQ----ERC----------------PIVDTWWQTET-------GGHMITPLPGATPTVPG--SCTLPLPGIMAAVVD 404
Cdd:PRK09192 321 EAFAPagfdDKAfmpsyglaeatlavsfSPLGSGIVVEEvdrdrleYQGKAVAPGAETRRVRTfvNCGKALPGHEIEIRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 405 ETGQDVPNGQGGILVVKRPwpAMIRTIWGDPERFRKsyypeelggrlyLAGDGTVRDKDTGYFT-----IMGRIDDVLNV 479
Cdd:PRK09192 401 EAGMPLPERVVGHICVRGP--SLMSGYFRDEESQDV------------LAADGWLDTGDLGYLLdgylyITGRAKDLIII 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 480 SGHRLGTMEIESALVSH-ELVA-EAAVVGRPDDTtGEAVVAFVVLKRSRPEgeEAAALAKTLRDWVGKQIGPIAK----- 552
Cdd:PRK09192 467 NGRNIWPQDIEWIAEQEpELRSgDAAAFSIAQEN-GEKIVLLVQCRISDEE--RRGQLIHALAALVRSEFGVEAAvelvp 543
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1860891105 553 PKdirfgdNLPKTRSGKimrrLLRSLAK-----GEAITQDTST 590
Cdd:PRK09192 544 PH------SLPRTSSGK----LSRAKAKkrylsGAFASLDVAA 576
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
58-272 |
1.21e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.43 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 58 VTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLVDVGAVALVTad 137
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarGGKTLP-LKSIADEaVAMGGCeavksVIVYRRT-GGKIDWHAGRDL-WMHELADAESdtcapewVGAEHPL----- 209
Cdd:PTZ00216 200 ----NGKNVPnLLRLMKS-GGMPNT-----TIIYLDSlPASVDTEGCRLVaWTDVVAKGHS-------AGSHHPLnipen 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860891105 210 -----FILYTSGSTGKPKGVQHsTGGYLLWAAQTMkwtfDWKPDDVFWCTADigwvtGHTYITYGPLA 272
Cdd:PTZ00216 263 nddlaLIMYTSGTTGDPKGVMH-THGSLTAGILAL----EDRLNDLIGPPEE-----DETYCSYLPLA 320
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
59-576 |
1.49e-05 |
|
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: 47.81 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKK-RGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVvfggfsaksLNERLvdvgavalvtad 137
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAF---------INYNL------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 138 eqarGGKTLPlksiadEAVAMGGCEAVksvivyrrtggkidwhagrdlwmheLADAESdtcapewvgaehPLFILYTSGS 217
Cdd:cd05937 66 ----SGDPLI------HCLKLSGSRFV-------------------------IVDPDD------------PAILIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 218 TGKPKGVQHSTGGYLLWAAQTMKWTFDWKPDDVFWCTAdIGWVTGHTYITYGPLACGGTQVV---FEgvptwpdAGRFWK 294
Cdd:cd05937 99 TGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMP-LYHGTAAFLGACNCLMSGGTLALsrkFS-------ASQFWK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 295 MIGDHKVTVFYTAPTAIRSLIKA-AEADDKVHpksydlsslRIIGTVGEPINPEAWMWYHKHVGqerCPIVDTWWQTETG 373
Cdd:cd05937 171 DVRDSGATIIQYVGELCRYLLSTpPSPYDRDH---------KVRVAWGNGLRPDIWERFRERFN---VPEIGEFYAATEG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 374 GHMITPLpGATPTVPGSC-------TLPLPGIMAAV-VD-ETGQDVPNGQGGILV---VKRPWPAMIRtIWGDPERFRKS 441
Cdd:cd05937 239 VFALTNH-NVGDFGAGAIghhglirRWKFENQVVLVkMDpETDDPIRDPKTGFCVrapVGEPGEMLGR-VPFKNREAFQG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 442 YYPEE-------------LGGRLYLAGDGTVRDKDtGYFTIMGRIDDVLNVSGHRLGTMEIESALVSHELVAEAAVVG-R 507
Cdd:cd05937 317 YLHNEdatesklvrdvfrKGDIYFRTGDLLRQDAD-GRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvK 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860891105 508 PDDTTGEAVVAFVVLKRS--RPEGEEAAALAKTLRDWVGKqigpIAKPKDIRFGDNLPKTRSGKIMRRLLR 576
Cdd:cd05937 396 VPGHDGRAGCAAITLEESsaVPTEFTKSLLASLARKNLPS----YAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
41-224 |
4.56e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.37 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 41 GQRVavIFEADDGTVTRVTYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKS 120
Cdd:PLN02861 63 GRRQ--VTDSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 121 LnERLVDVGAVALVTADEQArggktlpLKSIadeAVAMGGCEA-VKSVIVYrrtgGKIDWHagrdlwMHELADAESDTCA 199
Cdd:PLN02861 141 V-EFIINHAEVSIAFVQESK-------ISSI---LSCLPKCSSnLKTIVSF----GDVSSE------QKEEAEELGVSCF 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1860891105 200 pEW--------VGAEHP-------LFILYTSGSTGKPKGV 224
Cdd:PLN02861 200 -SWeefslmgsLDCELPpkqktdiCTIMYTSGTTGEPKGV 238
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
48-224 |
1.46e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.55 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 48 FEAD-DGTVTRVTYAELLARVSRFANALKKRGiAKGDRVVIYMPMSIEGIVA----MQAcARIGATHSVVFGGFSAKSLN 122
Cdd:PRK05850 25 YEQDpAGVAETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAflgaLQA-GLIAVPLSVPQGGAHDERVS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 123 ERLVDVGAVALVTAdeqarggktlplKSIAD---EAVAMGGCEAVKSVIvyrrtggKIDwhagrdlwmheLADAES-DTC 198
Cdd:PRK05850 103 AVLRDTSPSVVLTT------------SAVVDdvtEYVAPQPGQSAPPVI-------EVD-----------LLDLDSpRGS 152
|
170 180
....*....|....*....|....*.
gi 1860891105 199 APEWVGAEHPLFILYTSGSTGKPKGV 224
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGV 178
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
214-349 |
4.06e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 43.21 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 214 TSGSTGKPKGVQHSTGGYLLWA---AQTMkWTFDWKPDDVFWCTADIGWVTGHTYITYGPLACGGTQVVFEGVPTwpdaG 290
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAelfARSL-RAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNT----E 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860891105 291 RFWKMIGDHKVTVFYTAPTAIRSLIKAAEADDkVHPKSYDLSSLrIIGtvGEPInPEAW 349
Cdd:COG1541 166 RQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEG-IDPRDLSLKKG-IFG--GEPW-SEEM 219
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
54-102 |
4.30e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 43.11 E-value: 4.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1860891105 54 TVTRVTYAELLARVSRFANALKKRGIAK-GDRVVIYMPMSIEGIVAMQAC 102
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKKVGLKpGDRVALMYPDPLDFVAAFYGC 60
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
59-570 |
4.38e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 43.28 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGIAKGDRVVIYMPMSIEGIVAMQACARIGATHSVVFGGFSAKSLNERLvdvgAVAlvtade 138
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYL----GVA------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 139 QARGgktlpLKSIADEAVAmggceavksvivyrrtggkidwhagrdlwmheladaesdtcapewVGAEHPLFILYTSGST 218
Cdd:cd17647 92 KPRG-----LIVIRAAGVV---------------------------------------------VGPDSNPTLSFTSGSE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 219 GKPKGV--QH-STGGYLLWAAQTmkwtFDWKPDDVFWCTADIGwvtgHTYIT---YGPLACGGTQVVfegvPTWPDA--- 289
Cdd:cd17647 122 GIPKGVlgRHfSLAYYFPWMAKR----FNLSENDKFTMLSGIA----HDPIQrdmFTPLFLGAQLLV----PTQDDIgtp 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 290 GRFWKMIGDHKVTVFYTAPtAIRSLIkAAEADDKVhPKSY------------DLSSLRIIGtvgepinpeawmwyhkhvg 357
Cdd:cd17647 190 GRLAEWMAKYGATVTHLTP-AMGQLL-TAQATTPF-PKLHhaffvgdiltkrDCLRLQTLA------------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 358 qERCPIVDTWWQTETG---GHMITPLPGATPTVPGSctlpLPGIMAAvvdetGQDVPNGQggILVVKRPWPAMIRTI--- 431
Cdd:cd17647 248 -ENVRIVNMYGTTETQravSYFEVPSRSSDPTFLKN----LKDVMPA-----GRGMLNVQ--LLVVNRNDRTQICGIgev 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 --------------WGDPE----RFRKSYY--PEELGG------------------RLYLAGDgTVRDKDTGYFTIMGRI 473
Cdd:cd17647 316 geiyvragglaegyRGLPElnkeKFVNNWFvePDHWNYldkdnnepwrqfwlgprdRLYRTGD-LGRYLPNGDCECCGRA 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 474 DDVLNVSGHRLGTMEIESALVSHELVAEAAVVGRPDDTTGEAVVAFVVLKRSRPEGEEAAA------------------- 534
Cdd:cd17647 395 DDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQedvpkevstdpivkgligy 474
|
570 580 590
....*....|....*....|....*....|....*...
gi 1860891105 535 --LAKTLRDWVGKQIGPIAKPKDIRFGDNLPKTRSGKI 570
Cdd:cd17647 475 rkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
32-576 |
1.39e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 32 LDRHVeAGNGQRVA---VIFEAD-DGTVTRVTYAELLARVSRFANALKkRGIAKGDRVVIYMPMSIEGIVAMQACARIGA 107
Cdd:PRK12476 40 IERNI-ANVGDTVAyryLDHSHSaAGCAVELTWTQLGVRLRAVGARLQ-QVAGPGDRVAILAPQGIDYVAGFFAAIKAGT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 108 THSVVFggfsAKSL---NERLvdvgavALVTADEQarggktlPLKSIADEAVAmggcEAVKSVIVYRRTGgkidwHAGRD 184
Cdd:PRK12476 118 IAVPLF----APELpghAERL------DTALRDAE-------PTVVLTTTAAA----EAVEGFLRNLPRL-----RRPRV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 185 LWMHELADAESDTCAPEWVGAEHPLFILYTSGSTGKPKGVQ---HSTGGYLLWAAQTMkwtfdwkpDDVFWCTADIGWV- 260
Cdd:PRK12476 172 IAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEithRAVGTNLVQMILSI--------DLLDRNTHGVSWLp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 261 ----TGHTYITYgPLACGGTQVVFEGVPTWPDAGRFWKMIGD--HKVTVFYTAP------TAIRSLIKAAEaddkvhpkS 328
Cdd:PRK12476 244 lyhdMGLSMIGF-PAVYGGHSTLMSPTAFVRRPQRWIKALSEgsRTGRVVTAAPnfayewAAQRGLPAEGD--------D 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 329 YDLSSL-RIIGTvgEPINPEAWMWYHK--------------------------HVGQERCPIVDTWWQTETGGHMITPLP 381
Cdd:PRK12476 315 IDLSNVvLIIGS--EPVSIDAVTTFNKafapyglprtafkpsygiaeatlfvaTIAPDAEPSVVYLDREQLGAGRAVRVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 382 GATP--TVPGSCTLPLPGIMAAVVDE-TGQDVPNGQGGILvvkrpW---PAMIRTIWGDPERFRKSYYpEELGGRL---- 451
Cdd:PRK12476 393 ADAPnaVAHVSCGQVARSQWAVIVDPdTGAELPDGEVGEI-----WlhgDNIGRGYWGRPEETERTFG-AKLQSRLaegs 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 452 YLAG---DGT-VRDKDTGYFT-----IMGRIDDVLNVSGHRLGTMEIE------SALVSHELVAEAAVvgrPDDTTGEAV 516
Cdd:PRK12476 467 HADGaadDGTwLRTGDLGVYLdgelyITGRIADLIVIDGRNHYPQDIEatvaeaSPMVRRGYVTAFTV---PAEDNERLV 543
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860891105 517 VafVVLKRSRPEGEEAAALAKTLRDWVGKQIGpiAKPKDIRF--GDNLPKTRSGKIMRRLLR 576
Cdd:PRK12476 544 I--VAERAAGTSRADPAPAIDAIRAAVSRRHG--LAVADVRLvpAGAIPRTTSGKLARRACR 601
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
59-227 |
1.92e-03 |
|
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: 41.05 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 59 TYAELLARVSRFANALKKRGI--AKGDRVVIYMPMSIEGIVAMQACARIGAThsVVfggfsakSLNERLvdvGAVALVTA 136
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLV--TV-------PLYDTL---GPEAIEYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 137 DEQARGG-----KTLPLKSIaDEAVAMgGCEAVKSvivyrrtggkidwhagrdlwmHELADAEsDTCApewvgaehplfI 211
Cdd:cd05927 75 LNHAEISivfcdAGVKVYSL-EEFEKL-GKKNKVP---------------------PPPPKPE-DLAT-----------I 119
|
170
....*....|....*.
gi 1860891105 212 LYTSGSTGKPKGVQHS 227
Cdd:cd05927 120 CYTSGTTGNPKGVMLT 135
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
432-573 |
2.95e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 40.70 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 432 WGDPERFRKSYypeelGGRLYLAGDGT-----VRDKDTGYFT-----IMGRIDDVLNVSGHRLGTMEIESAL--VSHELV 499
Cdd:PRK05850 412 WQKPEETERTF-----GATLVDPSPGTpegpwLRTGDLGFISegelfIVGRIKDLLIVDGRNHYPDDIEATIqeITGGRV 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860891105 500 AEAAVvgrPDDTTgEAVVAFVVLKRSRPEGEEAAALAKTLRDWVgkqIGPIAKPKDIRFGD-------NLPKTRSGKIMR 572
Cdd:PRK05850 487 AAISV---PDDGT-EKLVAIIELKKRGDSDEEAMDRLRTVKREV---TSAISKSHGLSVADlvlvapgSIPITTSGKIRR 559
|
.
gi 1860891105 573 R 573
Cdd:PRK05850 560 A 560
|
|
| |
