|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
63-679 |
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: 1090.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 63 ESYvKEWAKTVGPNSDEWWAAKAREtLDWYDDFKTVRAGGFEHGDVQWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEADE 142
Cdd:cd05966 1 EQY-KELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 143 PSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECK 222
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 223 VLITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDKWWDEECAKMPAYCPCERMASEDPLFILY 302
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 303 TSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTPSRYW 382
Cdd:cd05966 239 TSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 383 DFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNQCAIVDTYWMTETGSISI 462
Cdd:cd05966 319 DIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 463 APLPGAISTKPGSATFPFFGMDVDIIDPQTGQVleGNDVEGVLVARRPWPSIARTVYRDHKRYLETYMKPYPGYFFFGDG 542
Cdd:cd05966 399 TPLPGATPLKPGSATRPFFGIEPAILDEEGNEV--EGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 543 AARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlKATKEADLSK 622
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKD----GEEPSDELRK 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 623 ELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEgDQLGDLSSIAD 679
Cdd:cd05966 553 ELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE-EELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
61-689 |
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: 1043.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 61 NYESYVKEWAKTVGpNSDEWWAAKARETLDWYDDFKTVRAGGFEhGDVQWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEA 140
Cdd:TIGR02188 3 NLEQYKELYEESIE-DPDKFWAKLARELLDWFKPFTKVLDWSFP-PFYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 141 DEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCE 220
Cdd:TIGR02188 81 DEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 221 CKVLITTDEGRRGGKTIATKQIVDAALQQCPL-VENVLVLRRTGNKV-PMTEGRDKWWDEECAKMPAYCPCERMASEDPL 298
Cdd:TIGR02188 161 AKLVITADEGLRGGKVIPLKAIVDEALEKCPVsVEHVLVVRRTGNPVvPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTP 378
Cdd:TIGR02188 241 FILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 379 SRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNQCAIVDTYWMTETG 458
Cdd:TIGR02188 321 GRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 459 SISIAPLPGAISTKPGSATFPFFGMDVDIIDPqTGQVLEGNDVEGVLVARRPWPSIARTVYRDHKRYLETYMKPYPGYFF 538
Cdd:TIGR02188 401 GIMITPLPGATPTKPGSATLPFFGIEPAVVDE-EGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 539 FGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFdlkaTKEA 618
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGY----EPDD 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 619 DLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEGDQLGDLSSIADPQIVEEVKQK 689
Cdd:TIGR02188 556 ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIEA 626
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
40-690 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 976.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 40 LFAPPPRMqgkegRPKPHIGPnyESYVKEWAKTVGpNSDEWWAAKAREtLDWYDDFKTVraggFEHGDV--QWFPEGTLN 117
Cdd:PRK00174 1 VFPPPAEF-----AANALIDM--EQYKALYQESVE-DPEGFWAEQAKR-LDWFKPFDTV----LDWNAPfiKWFEDGELN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 118 AAYNCLDRHYYKNPKKTAIIYEADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIG 197
Cdd:PRK00174 68 VSYNCLDRHLKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 198 AIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDKWWD 277
Cdd:PRK00174 148 AVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEGRDLWWH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 278 EECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIY 357
Cdd:PRK00174 228 ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GPLANGITTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWY 437
Cdd:PRK00174 308 GPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 438 NDFAGKNQCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPqTGQVLEGNdVEGVLVARRPWPSIART 517
Cdd:PRK00174 388 YKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDE-EGNPLEGG-EGGNLVIKDPWPGMMRT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 518 VYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTG 597
Cdd:PRK00174 466 IYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 598 QAVYAFVTMKPEfdlkATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEgDQLGDLSSI 677
Cdd:PRK00174 546 QGIYAFVTLKGG----EEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGE-EILGDTSTL 620
|
650
....*....|...
9C8S_C 678 ADPQIVEEVKQKV 690
Cdd:PRK00174 621 ADPSVVEKLIEAR 633
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
109-688 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 813.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 109 QWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEaDEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAA 188
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 189 AFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPM 268
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 269 TEgrDKWWDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGW 348
Cdd:COG0365 160 EG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 349 ITGHSYIIYGPLANGITTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEP 428
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 429 INPEAWHWYNDFAGknqCAIVDTYWMTETGSISIAPLPGaISTKPGSATFPFFGMDVDIIDPQtGQVLEGNdVEGVLVAR 508
Cdd:COG0365 318 LNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDED-GNPVPPG-EEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 509 RPWPSIARTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAV 588
Cdd:COG0365 392 GPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 589 VGCADDLTGQAVYAFVTMKPEFDLkatkEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEg 668
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVLKPGVEP----SDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR- 546
|
570 580
....*....|....*....|
9C8S_C 669 dQLGDLSSIADPQIVEEVKQ 688
Cdd:COG0365 547 -PLGDTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
108-686 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 673.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 108 VQWFPEGTLNAAYNCLDRHYYK-NPKKTAIIYEADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQA 186
Cdd:PLN02654 79 IEWFKGGKTNICYNCLDRNVEAgNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 187 AAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQ----------CPLVENV 256
Cdd:PLN02654 159 PIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDEsakngvsvgiCLTYENQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 257 LVLRRTGNKvpMTEGRDKWWDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHP 336
Cdd:PLN02654 239 LAMKREDTK--WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 337 DDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDL 416
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSR 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 417 SSLRVLGSVGEPINPEAWHWYNDFAGKNQCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDpQTGQVL 496
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVD-EKGKEI 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 497 EGnDVEGVLVARRPWPSIARTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESA 576
Cdd:PLN02654 476 EG-ECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 577 LILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIM 656
Cdd:PLN02654 555 LVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVE----GVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIM 630
|
570 580 590
....*....|....*....|....*....|
9C8S_C 657 RRVLRKIVAGEGDQLGDLSSIADPQIVEEV 686
Cdd:PLN02654 631 RRILRKIASRQLDELGDTSTLADPGVVDQL 660
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
76-656 |
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: 629.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 76 NSDEWWAAKARETLDWYDDFKTVRAGGFEHGDV--QWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEADEPSESREVSYEE 153
Cdd:cd17634 10 NDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPsiKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTSQSRTISYRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 154 LMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRG 233
Cdd:cd17634 90 LHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 234 GKTIATKQIVDAALQ-QCPLVENVLVLRRTGNKVPMTEGRDKWWDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKG 312
Cdd:cd17634 170 GRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 313 VVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTPSRYWDFVDKWKATQ 392
Cdd:cd17634 250 VLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 393 LYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNQCAIVDTYWMTETGSISIAPLPGAISTK 472
Cdd:cd17634 330 LYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 473 PGSATFPFFGMDVDIIDPQtGQVLEGNdVEGVLVARRPWPSIARTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMW 552
Cdd:cd17634 410 AGSATRPVFGVQPAVVDNE-GHPQPGG-TEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYW 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 553 IKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlKATKEADLSKELAIQVRKVI 632
Cdd:cd17634 488 ITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNH----GVEPSPELYAELRNWVRKEI 563
|
570 580
....*....|....*....|....
9C8S_C 633 GPFAAPKKIYLVSDLPKTRSGKIM 656
Cdd:cd17634 564 GPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
76-686 |
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: 561.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 76 NSDEWWAAKAREtLDWYDDFKTVRAGGfEHGDVQWFPEGTLNAAYNCLDRHYYK-NPKKTAIIYEADEPSESREVSYEEL 154
Cdd:cd05967 11 EPEAFWAEQARL-IDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAgRGDQIALIYDSPVTGTERTYTYAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 155 MQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGG 234
Cdd:cd05967 89 LDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGIEPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 235 KTIATKQIVDAALQQCPL-VENVLVLRRtGNK--VPMTEGRDKWWDeECAKMPAYCPCERMASEDPLFILYTSGSTGKPK 311
Cdd:cd05967 169 KVVPYKPLLDKALELSGHkPHHVLVLNR-PQVpaDLTKPGRDLDWS-ELLAKAEPVDCVPVAATDPLYILYTSGTTGKPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 312 GVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPV-YPTPSRYWDFVDKWKA 390
Cdd:cd05967 247 GVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 391 TQLYTAPTAIRLLRRM--GEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETGSISIAPLPG- 467
Cdd:cd05967 327 NALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGl 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 468 -AISTKPGSATFPFFGMDVDIIDpQTGQVLEGNDvEGVLVARRPW-PSIARTVYRDHKRYLETYMKPYPGYFFFGDGAAR 545
Cdd:cd05967 404 ePLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNE-LGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 546 DYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefDLKATkEADLSKELA 625
Cdd:cd05967 482 DEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKE--GVKIT-AEELEKELV 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 626 IQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVagEGDQLGDLSSIADPQIVEEV 686
Cdd:cd05967 559 ALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
78-692 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 541.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 78 DEWWAAKAREtLDWYDDFKTVraggFEHGD---VQWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEADEPSESREVSYEEL 154
Cdd:PRK10524 16 EAFWAEQARR-IDWQTPFTQV----LDYSNppfARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDEERTYTFRQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 155 MQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGG 234
Cdd:PRK10524 91 HDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGSRGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 235 KTIATKQIVDAALQQC---PlvENVLVLRRTGNKVPMTEGRDKWWDEECAK-MPAYCPCERMASEDPLFILYTSGSTGKP 310
Cdd:PRK10524 171 KVVPYKPLLDEAIALAqhkP--RHVLLVDRGLAPMARVAGRDVDYATLRAQhLGARVPVEWLESNEPSYILYTSGTTGKP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 311 KGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTPSRYWDFVDKWKA 390
Cdd:PRK10524 249 KGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 391 TQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETG--SISIAPLPGA 468
Cdd:PRK10524 329 NRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGwpILAIARGVED 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 469 ISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDvEGVLVARRPW-PSIARTVYRDHKRYLETYMKPYPG--YFFFgDGAAR 545
Cdd:PRK10524 406 RPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNE-KGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFGRqvYSTF-DWGIR 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 546 DYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMK-PEFDLKATKEADLSKEL 624
Cdd:PRK10524 484 DADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKdSDSLADREARLALEKEI 563
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 625 AIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVagEGDQLGDLSSIADPQIVEEVKQKVTG 692
Cdd:PRK10524 564 MALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA--EGRDPGDLTTIEDPAALQQIRQALEE 629
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
61-680 |
4.28e-169 |
|
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: 498.17 E-value: 4.28e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 61 NYESYVKEWAKTVGPNSDEWWAAKARETLDWYDDFKTVR--AGGFEHGdvQWFPEGTLNAAYNCLDRHYYKNPKKTAIIY 138
Cdd:cd05968 5 GIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLdlSGGKPWA--AWFVGGRMNIVEQLLDKWLADTRTRPALRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 139 EAdEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVND 218
Cdd:cd05968 83 EG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 219 CECKVLITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDKWWDEECAKMPAYcpCERMASEDPL 298
Cdd:cd05968 162 AEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDG--AERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGhSYIIYGPLANGITTAVFESTPVYPTP 378
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 379 SRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNQCAIVDTYWMTET- 457
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEIs 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 458 ----GSISIAPLpgaistKPGSATFPFFGMDVDIIDPQTGQVlegNDVEGVLVARRPWPSIARTVYRDHKRYLETYMKPY 533
Cdd:cd05968 399 ggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPA---RPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 534 PGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFdlk 613
Cdd:cd05968 470 DNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--- 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 614 aTKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEgdQLGDLSSIADP 680
Cdd:cd05968 547 -TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
84-679 |
4.85e-151 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 450.12 E-value: 4.85e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 84 KARETLDWyddfKTVRAggfehgDVQWFPEGTLNAAYNCLDRHYYKNPK-KTAIIYEADEPSESreVSYEELMQETCRVA 162
Cdd:PRK04319 20 ETYATFSW----EEVEK------EFSWLETGKVNIAYEAIDRHADGGRKdKVALRYLDASRKEK--YTYKELKELSNKFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 163 NVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgrrggktIATKQI 242
Cdd:PRK04319 88 NVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA-------LLERKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 243 VDaalqQCPLVENVLVLRRTGNKVPMTEGrdkwWDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHsTAGYLL 322
Cdd:PRK04319 161 AD----DLPSLKHVLLVGEDVEEGPGTLD----FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH-VHNAML 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 323 GTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPvypTPSRYWDFVDKWKATQLYTAPTAIRL 402
Cdd:PRK04319 232 QHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 403 LRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETGSISIAPLPgAISTKPGSATFPFFG 482
Cdd:PRK04319 309 LMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 483 MDVDIIDPQtGQVLEGNdVEGVLVARRPWPSIARTVYRDHKRYLETYMkpyPGYFFFGDGAARDYDGYMWIKGRVDDVIN 562
Cdd:PRK04319 385 IEAAIVDDQ-GNELPPN-RMGNLAIKKGWPSMMRGIWNNPEKYESYFA---GDWYVSGDSAYMDEDGYFWFQGRVDDVIK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 563 VSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkATKEadLSKELAIQVRKVIGPFAAPKKIY 642
Cdd:PRK04319 460 TSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEE--LKEEIRGFVKKGLGAHAAPREIE 535
|
570 580 590
....*....|....*....|....*....|....*...
9C8S_C 643 LVSDLPKTRSGKIMRRVLRkivAGE-GDQLGDLSSIAD 679
Cdd:PRK04319 536 FKDKLPKTRSGKIMRRVLK---AWElGLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
150-663 |
2.75e-123 |
|
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: 374.15 E-value: 2.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDE 229
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 230 GRrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcERMASEDPLFILYTSGSTGK 309
Cdd:cd05969 82 LY----------------------------------------------------------ERTDPEDPTLLHYTSGTTGT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 310 PKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPvypTPSRYWDFVDKWK 389
Cdd:cd05969 104 PKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 390 ATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETGSISIAPLPGaI 469
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC-M 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 470 STKPGSATFPFFGMDVDIIDpQTGQVLEGNDVeGVLVARRPWPSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDG 549
Cdd:cd05969 256 PIKPGSMGKPLPGVKAAVVD-ENGNELPPGTK-GILALKPGWPSMFRGIWNDEERYKNSFID---GWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 550 YMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFdlKATKEadLSKELAIQVR 629
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDE--LKEEIINFVR 406
|
490 500 510
....*....|....*....|....*....|....
9C8S_C 630 KVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:cd05969 407 QKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
149-662 |
3.94e-106 |
|
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: 329.30 E-value: 3.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 149 VSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTd 228
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 egrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaSEDPLFILYTSGSTG 308
Cdd:cd05972 80 -----------------------------------------------------------------AEDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 309 KPKGVVHsTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVypTPSRYWDFVDKW 388
Cdd:cd05972 95 LPKGVLH-THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 389 KATQLYTAPTAIRLLRRMGEDHvknHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcaIVDTYWMTETGsISIAPLPGa 468
Cdd:cd05972 172 GVTSFCGPPTAYRMLIKQDLSS---YKFSHLRLVVSAGEPLNPEVIEWWRAATGLP---IRDGYGQTETG-LTVGNFPD- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 469 ISTKPGSATFPFFGMDVDIIDpQTGQVLEGNDvEGVLVARRPWPSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYD 548
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIID-DDGRELPPGE-EGDIAIKLPPPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDED 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 549 GYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFdlKATKEadLSKELAIQV 628
Cdd:cd05972 319 GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGY--EPSEE--LAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|....
9C8S_C 629 RKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
123-564 |
2.59e-96 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 303.46 E-value: 2.59e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIiyeadEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDEgrrggktiATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDKWWDEECAK 282
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 MPaycpcERMASEDPLFILYTSGSTGKPKGVVHSTaGYLLGTALTLKYV----FDAHPDDRFACMADIGWITGHSYIIYG 358
Cdd:pfam00501 148 PP-----PPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 PLANGITTAVFESTPVyPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAWHWYN 438
Cdd:pfam00501 222 PLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRLVLSGGAPLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFAGknqCAIVDTYWMTETGSISIAPLPGAIS-TKPGSATFPFFGMDVDIIDPQTGQVLeGNDVEGVLVARRPWpsIART 517
Cdd:pfam00501 299 ELFG---GALVNGYGLTETTGVVTTPLPLDEDlRSLGSVGRPLPGTEVKIVDDETGEPV-PPGEPGELCVRGPG--VMKG 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
9C8S_C 518 VYRDHKRYLETYMKpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVS 564
Cdd:pfam00501 373 YLNDPELTAEAFDE--DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
123-665 |
3.76e-88 |
|
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: 283.24 E-value: 3.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITtdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecak 282
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mpaycpcermasedpLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLAN 362
Cdd:COG0318 103 ---------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 363 GITTAVFEStpvyPTPSRYWDFVDKWKATQLYTAPT-AIRLLRRMGEDhvkNHDLSSLRVLGSVGEPINPEAWHWYNDFA 441
Cdd:COG0318 167 GATLVLLPR----FDPERVLELIERERVTVLFGVPTmLARLLRHPEFA---RYDLSSLRLVVSGGAPLPPELLERFEERF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 442 GknqCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGndVEGVLVARRPWpsIARTVYRD 521
Cdd:COG0318 240 G---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPG--EVGEIVVRGPN--VMKGYWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 522 HKRYLETYMkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVY 601
Cdd:COG0318 313 PEATAEAFR---DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 602 AFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:COG0318 390 AFVVLRPGAELDA-------EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
78-684 |
8.34e-82 |
|
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: 271.84 E-value: 8.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 78 DEWWAAkareTLDWYDdfkTVRAGGFEHGDV--------QWFPEGTLNAAYNCLdRHyyKNPKKTAIIYeADEPSESREV 149
Cdd:cd05943 31 GAFWAA----VWDFSG---VRGSKPYDVVVVsgrimpgaRWFPGARLNYAENLL-RH--ADADDPAAIY-AAEDGERTEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDE 229
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 230 GRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPM---TEGRDKWWDEECAKMPAyCPC--ERMASEDPLFILYTS 304
Cdd:cd05943 180 YTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPdlsKIAKALTLEDFLATGAA-GELefEPLPFDHPLYILYSS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 305 GSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIiyGPLANGITTAVFESTPVYPTPSRYWDF 384
Cdd:cd05943 259 GTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSPFYPDTNALWDL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 385 VDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcaivdtYWMtetGSIS--- 461
Cdd:cd05943 337 ADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKPD-------VLL---ASISggt 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 462 --IAPLPGAISTKP---GSATFPFFGMDVDIIDPQTGQVLegnDVEGVLVARRPWPSIArtVY----RDHKRYLETYMKP 532
Cdd:cd05943 407 diISCFVGGNPLLPvyrGEIQCRGLGMAVEAFDEEGKPVW---GEKGELVCTKPFPSMP--VGfwndPDGSRYRAAYFAK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 533 YPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDL 612
Cdd:cd05943 482 YPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEL 561
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9C8S_C 613 katkEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEgdQLGDLSSIADPQIVE 684
Cdd:cd05943 562 ----DDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGR--PVKNAGALANPESLD 627
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
112-661 |
8.64e-81 |
|
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: 266.67 E-value: 8.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 112 PEgTLNAAYNCLDRHYYKNPKKTAIIYeADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFL 191
Cdd:cd05970 13 PE-NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 192 ACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGrrggktiATKQIVDAALQQCPlveNVLVLRRTGNKVPmteg 271
Cdd:cd05970 91 ALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-------NIPEEIEKAAPECP---SKPKLVWVGDPVP---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 272 rDKW--WDEECAKMPAYCP----CERMASEDPLFILYTSGSTGKPKGVVHSTAgYLLGTALTLKYVFDAHPDDRFACMAD 345
Cdd:cd05970 157 -EGWidFRKLIKNASPDFErptaNSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 346 IGWITGHSYIIYGPLANGitTAVFestpVYP----TPSRYWDFVDKWKATQLYTAPTAIRLLRRmgEDhVKNHDLSSLRV 421
Cdd:cd05970 235 TGWGKAVWGKIYGQWIAG--AAVF----VYDydkfDPKALLEKLSKYGVTTFCAPPTIYRFLIR--ED-LSRYDLSSLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 422 LGSVGEPINPEAWHWYNDFAGknqCAIVDTYWMTETgSISIAPLPGaISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDV 501
Cdd:cd05970 306 CTTAGEALNPEVFNTFKEKTG---IKLMEGFGQTET-TLTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 502 EGVLVARRPWP-SIARTVYRDHKRYLETYmkpYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILH 580
Cdd:cd05970 381 EIVIRTSKGKPvGLFGGYYKDAEKTAEVW---HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQH 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 581 KGVAETAVVGCADDLTGQAVYAFVTMKPefDLKATKEadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05970 458 PAVLECAVTGVPDPIRGQVVKATIVLAK--GYEPSEE--LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
.
9C8S_C 661 R 661
Cdd:cd05970 534 R 534
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
296-656 |
9.35e-81 |
|
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: 259.91 E-value: 9.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYvFDAHPDDRFACMADIGWItGHSYIIYGPLANGITTAVFEStpvy 375
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 376 PTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDhvKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGknqCAIVDTYWMT 455
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 456 ETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGndVEGVLVARRPWPsIARTVYRDHKRYLETYmkpyPG 535
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPG--EIGELVVRGPSV-MKGYWNNPEATAAVDE----DG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 536 YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkat 615
Cdd:cd04433 223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADL--- 299
|
330 340 350 360
....*....|....*....|....*....|....*....|.
9C8S_C 616 keadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIM 656
Cdd:cd04433 300 ----DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
107-685 |
2.77e-76 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 257.80 E-value: 2.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 107 DVQWFPEGTLNAAYNCLdRHyyKNPKKTAIIYeADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQA 186
Cdd:PRK03584 77 GARWFPGARLNYAENLL-RH--RRDDRPAIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 187 AAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKv 266
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPA- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 267 PMTEGRDKW--WDEECAKMPAYCP-CERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRF--- 340
Cdd:PRK03584 232 AAAAALPGAllWEDFLAPAEAAELeFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFfwy 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 341 -ACmadiGWI------TGhsyiiygpLANGITTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKN 413
Cdd:PRK03584 312 tTC----GWMmwnwlvSG--------LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGET 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 414 HDLSSLRVLGSVGEPINPEAWHW-YNDFAGknqcaivDTYWmtetGSIS--------------IAPL-PGAISTkpgsat 477
Cdd:PRK03584 380 HDLSALRTIGSTGSPLPPEGFDWvYEHVKA-------DVWL----ASISggtdicscfvggnpLLPVyRGEIQC------ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 478 fPFFGMDVDIIDPQtGQVLEGndVEGVLVARRPWPSIArtVY----RDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWI 553
Cdd:PRK03584 443 -RGLGMAVEAWDED-GRPVVG--EVGELVCTKPFPSMP--LGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVI 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 554 KGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkatkEADLSKELAIQVRKVIG 633
Cdd:PRK03584 517 YGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTL----DDALRARIRTTIRTNLS 592
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
9C8S_C 634 PFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEG-DQLGDLSSIADPQIVEE 685
Cdd:PRK03584 593 PRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPvKKAVNRDALANPEALDW 645
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
150-662 |
1.76e-68 |
|
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: 230.87 E-value: 1.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITtde 229
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 230 grrggktiatkqivDAAlqqcplvenvlvlrrtgnkvpmteGRDKwwdeecakmpaycpcermASEDPLFILYTSGSTGK 309
Cdd:cd05973 79 --------------DAA------------------------NRHK------------------LDSDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 310 PKGVVHSTAgYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPvypTPSRYWDFVDKWK 389
Cdd:cd05973 103 PKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGF---SVESTWRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 390 ATQLYTAPTAIRLLRRMGEDhVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGknqCAIVDTYWMTETGSISIAPLPGAI 469
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHALEH 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 470 STKPGSATFPFFGMDVDIIDPQTGQVLEGndVEGVL-VARRPWPSIARTVYrdhkrYLETYMKPYPGYFFFGDGAARDYD 548
Cdd:cd05973 255 PVHAGSAGRAMPGWRVAVLDDDGDELGPG--EPGRLaIDIANSPLMWFRGY-----QLPDTPAIDGGYYLTGDTVEFDPD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 549 GYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkatKEADLSKELAIQV 628
Cdd:cd05973 328 GSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE----GTPALADELQLHV 403
|
490 500 510
....*....|....*....|....*....|....
9C8S_C 629 RKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05973 404 KKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
120-661 |
7.01e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 231.61 E-value: 7.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 120 YNCLDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAI 199
Cdd:PRK06187 9 GRILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 200 HSAVFAGFSAESLRDRVNDCECKVLITTDEGRrggktiatkQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDkwWDEE 279
Cdd:PRK06187 83 LHPINIRLKPEEIAYILNDAEDRVVLVDSEFV---------PLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGE--YEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 280 CAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTaLTLKYVFDAHPDDR-------FACMAdIGWItgh 352
Cdd:PRK06187 152 LAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHS-LAVCAWLKLSRDDVylvivpmFHVHA-WGLP--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 353 syiiYGPLANGITTavfestpVYP---TPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPI 429
Cdd:PRK06187 227 ----YLALMAGAKQ-------VIPrrfDPENLLDLIETERVTFFFAVPTIWQML--LKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 430 NPEAwhwYNDFAGKNQCAIVDTYWMTETGS-ISIAPLP---GAISTKPGSATFPFFGMDVDIIDPQtGQVLEGNDVE-GV 504
Cdd:PRK06187 294 PPAL---LREFKEKFGIDLVQGYGMTETSPvVSVLPPEdqlPGQWTKRRSAGRPLPGVEARIVDDD-GDELPPDGGEvGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 505 LVARRPWpsIARTVYRDHKRYLETYmkpYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVA 584
Cdd:PRK06187 370 IIVRGPW--LMQGYWNRPEATAETI---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 585 ETAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK06187 445 EVAVIGVPDEKWGERPVAVVVLKPGATLDA-------KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
76-688 |
1.54e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 228.47 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 76 NSDEWWAAKARETLDWYDDFKTVRAGGFEHGDvqWFPEGTLNAAYNCLDRHYyKNPKK---TAIIYEADEPSESREVSYE 152
Cdd:PTZ00237 20 NPESFWDEVAKKYVHWDKMYDKVYSGDEIYPD--WFKGGELNTCYNVLDIHV-KNPLKrdqDALIYECPYLKKTIKLTYY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 153 ELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRR 232
Cdd:PTZ00237 97 QLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 233 GGKTIA-TKQIVDAALQQCPLVENVLVLRR-------------TGNKVPMTEGrdkwWDEECAKMP--------AYCPCE 290
Cdd:PTZ00237 177 NDEIITfTPNLKEAIELSTFKPSNVITLFRnditsesdlkkieTIPTIPNTLS----WYDEIKKIKennqspfyEYVPVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rmaSEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIiYGPLANGITTAVFE 370
Cdd:PTZ00237 253 ---SSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 371 STPVYPT--PSRYWDFVDKWKATQLYTAPTAIRLLRRM---GEDHVKNHDLSSLRVLGSVGEPIN---PEawhwYNDFAG 442
Cdd:PTZ00237 329 GGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEesiPE----YIENKL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 443 KNQCAIVdtYWMTETGSISIapLPGAISTKPGSAT-FPFFGMDVDIIDPQtGQVLEGNDVeGVLVARRPWP-SIARTVYR 520
Cdd:PTZ00237 405 KIKSSRG--YGQTEIGITYL--YCYGHINIPYNATgVPSIFIKPSILSED-GKELNVNEI-GEVAFKLPMPpSFATTFYK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 521 DHKRYLETYMKpYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAV 600
Cdd:PTZ00237 479 NDEKFKQLFSK-FPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 601 YAFVTMKPEFDLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEGDQLGDlsSIADP 680
Cdd:PTZ00237 558 IGLLVLKQDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPD--NVNDS 635
|
....*...
9C8S_C 681 QIVEEVKQ 688
Cdd:PTZ00237 636 EIFYKIKE 643
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
146-661 |
5.50e-65 |
|
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: 221.54 E-value: 5.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 146 SREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLI 225
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 226 TtdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwDEecakmpaycpcermaSEDPLFILYTSG 305
Cdd:cd05971 84 T--------------------------------------------------DG---------------SDDPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 306 STGKPKGVVHSTAgYLLGTALTLKYVFDAHP--DDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVypTPSRYWD 383
Cdd:cd05971 99 TTGPPKGALHAHR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF--DPKAALD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 384 FVDKWKATQLYTAPTAIRLLRRMGEDhvKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGknqCAIVDTYWMTETGSIsIA 463
Cdd:cd05971 176 LMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFG---VEVNEFYGQTECNLV-IG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 464 PLPGAISTKPGSATFPFFGMDVDIIDpQTGQVLEgNDVEGVLVARRPWPSIARTVYRDHKrylETYMKPYPGYFFFGDGA 543
Cdd:cd05971 250 NCSALFPIKPGSMGKPIPGHRVAIVD-DNGTPLP-PGEVGEIAVELPDPVAFLGYWNNPS---ATEKKMAGDWLLTGDLG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 544 ARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFdlkaTKEADLSKE 623
Cdd:cd05971 325 RKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE----TPSDALARE 400
|
490 500 510
....*....|....*....|....*....|....*...
9C8S_C 624 LAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05971 401 IQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
150-662 |
6.70e-65 |
|
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: 223.88 E-value: 6.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVL-KSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTD 228
Cdd:cd05928 43 SFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 EgrrggktiaTKQIVDAALQQCPLVENVLVLRrtgnkvpmTEGRDKWWD--EECAKMPAYCPCERMASEDPLFILYTSGS 306
Cdd:cd05928 123 E---------LAPEVDSVASECPSLKTKLLVS--------EKSRDGWLNfkELLNEASTEHHCVETGSQEPMAIYFTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAV-----FESTPVYPTPSRY 381
Cdd:cd05928 186 TGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhhlprFDPLVILKTLSSY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 382 wdfvdkwKATQLYTAPTAIRLLRrmgEDHVKNHDLSSLRVLGSVGEPINP---EAWhwyndfagKNQCA--IVDTYWMTE 456
Cdd:cd05928 266 -------PITTFCGAPTVYRMLV---QQDLSSYKFPSLQHCVTGGEPLNPevlEKW--------KAQTGldIYEGYGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 457 TGSIsiAPLPGAISTKPGSATFPFFGMDVDIIDpQTGQVL----EGNdvegvlVARRPWPSIARTVYRDHKRYLETYMKP 532
Cdd:cd05928 328 TGLI--CANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLppgtEGD------IGIRVKPIRPFGLFSGYVDNPEKTAAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 533 YPGYFFF-GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFd 611
Cdd:cd05928 399 IRGDFYLtGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQF- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
9C8S_C 612 lKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05928 478 -LSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
123-661 |
7.60e-57 |
|
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: 201.44 E-value: 7.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNP-KKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHS 201
Cdd:cd05959 9 VDLNLNEGRgDKTAFIDDA------GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 202 AVFAGFSAESLRDRVNDCECKVLITTDEgrrggktiATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDKWWDEECA 281
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGE--------LAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 282 KMPAycpceRMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLA 361
Cdd:cd05959 155 LKPA-----ATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 362 NGITTAVFestPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRmgEDHVKNHDLSSLRVLGSVGEPINPEAWH-WYNDF 440
Cdd:cd05959 230 VGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGErWKARF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 441 AgknqCAIVDTYWMTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQVleGNDVEGVLVARRPwpSIArTVY- 519
Cdd:cd05959 305 G----LDILDGIGSTEMLHIFLSNRPGRV--RYGTTGKPVPGYEVELRDEDGGDV--ADGEPGELYVRGP--SSA-TMYw 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 520 --RDHKRylETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTG 597
Cdd:cd05959 374 nnRDKTR--DTFQG---EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 598 QAVYAFVTMKPEFDLKATKEADLsKELaiqVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05959 449 TKPKAFVVLRPGYEDSEALEEEL-KEF---VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
123-657 |
8.57e-57 |
|
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: 199.37 E-value: 8.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLIttdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecak 282
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mpaycpcermasEDPLFILYTSGSTGKPKGVVHSTaGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLAN 362
Cdd:cd17631 98 ------------DDLALLMYTSGTTGRPKGAMLTH-RNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 363 GITTAVFEStpvyPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAg 442
Cdd:cd17631 165 GGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPMPERLLRALQARG- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 443 knqCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPqtgqvlEGNDVE----GVLVARRP------W- 511
Cdd:cd17631 238 ---VKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDP------DGREVPpgevGEIVVRGPhvmagyWn 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 -PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:cd17631 309 rPEATAAAFRD-------------GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 591 CADDLTGQAVYAFVTMKPEFDLKATkeadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMR 657
Cdd:cd17631 376 VPDEKWGEAVVAVVVPRPGAELDED-------ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
123-666 |
1.00e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 198.62 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:PRK08316 17 LRRSARRYPDKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDegrrggktiATKQIVDAALQQCPLVENVLVLRRTGNKVPmteGRDKWWDEECAK 282
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDP---------ALAPTAEAALALLPVDTLILSLVLGGREAP---GGWLDFADWAEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 MPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTagyllgTALTLKYVfdahpddrfACMADIGW----ITGHSYIIY- 357
Cdd:PRK08316 159 GSVAEPDVELADDDLAQILYTSGTESLPKGAMLTH------RALIAEYV---------SCIVAGDMsaddIPLHALPLYh 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 --------GP-LANGITTAVFEStpvyPTPSRYWDFVDKWKATQLYTAPTA-IRLLRRMGEDhvkNHDLSSLR------- 420
Cdd:PRK08316 224 caqldvflGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD---TRDLSSLRkgyygas 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 421 -----VLGSVGEPInPEAWHWyndfagknQCaivdtYWMTEtgsisIAPL-----PGAISTKPGSATFPFFGMDVDIIDP 490
Cdd:PRK08316 297 impveVLKELRERL-PGLRFY--------NC-----YGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 491 qtgqvlEGNDVE----GVLVARRP------WPSIART--VYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVD 558
Cdd:PRK08316 358 ------DGNDVApgevGEIVHRSPqlmlgyWDDPEKTaeAFRG-------------GWFHSGDLGVMDEEGYITVVDRKK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 559 DVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAP 638
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE-------DELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|....*...
9C8S_C 639 KKIYLVSDLPKTRSGKIMRRVLRKIVAG 666
Cdd:PRK08316 492 KRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
133-661 |
4.05e-54 |
|
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: 191.91 E-value: 4.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 133 KTAIiYEADepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESL 212
Cdd:cd05919 1 KTAF-YAAD-----RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 213 RDRVNDCECKVLITTDEgrrggktiatkqivDAAlqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcerm 292
Cdd:cd05919 75 AYIARDCEARLVVTSAD--------------DIA---------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 293 asedplFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADI--GWITGHSyiIYGPLANGITTAVFe 370
Cdd:cd05919 95 ------YLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 371 stPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGknqCAIVD 450
Cdd:cd05919 166 --PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILD 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 451 TYWMTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQVleGNDVEGVLVARRPwpSIARTVYRDHKRYLETYM 530
Cdd:cd05919 239 GIGATEVGHIFLSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTI--PPGEEGDLLVRGP--SAAVGYWNNPEKSRATFN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 531 KpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEF 610
Cdd:cd05919 313 G---GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPA 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
9C8S_C 611 DLKATkeadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05919 390 APQES----LARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
144-656 |
2.63e-53 |
|
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: 190.89 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKV 223
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LITTdegrrgGKTIATkqiVDAALQQCPLVENVLVLRRTGNKVPmteGRDKWWDEEC-AKMPAYCPCERMASEDPLFILY 302
Cdd:cd05911 86 IFTD------PDGLEK---VKEAAKELGPKDKIIVLDDKPDGVL---SIEDLLSPTLgEEDEDLPPPLKDGKDDTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 303 TSGSTGKPKGVVHSTAGYLLGTALTLKYVFD-AHPDDRFACMADIGWITGHSYIIYGPLaNGITTAV---FEstpvyptP 378
Cdd:cd05911 154 SSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIImpkFD-------S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 379 SRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAwhwYNDFAGK-NQCAIVDTYWMTET 457
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKEL---QELLAKRfPNATIKQGYGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 458 GSISIAPLPGaiSTKPGSATFPFFGMDVDIIDPQTGQVLeGNDVEGVLVARRpwPSIARTVYRDHKRYLETYMKpyPGYF 537
Cdd:cd05911 301 GGILTVNPDG--DDKPGSVGRLLPNVEAKIVDDDGKDSL-GPNEPGEICVRG--PQVMKGYYNNPEATKETFDE--DGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 538 FFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkatKE 617
Cdd:cd05911 374 HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKL---TE 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
9C8S_C 618 ADLSKELAIQVrkvigpfAAPKK----IYLVSDLPKTRSGKIM 656
Cdd:cd05911 451 KEVKDYVAKKV-------ASYKQlrggVVFVDEIPKSASGKIL 486
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
285-661 |
2.05e-51 |
|
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: 184.60 E-value: 2.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 285 AYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGI 364
Cdd:cd05958 87 ALCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 365 TTAVFESTpvypTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGkn 444
Cdd:cd05958 167 SGVLLEEA----TPDLLLSAIARYKPTVLFTAPTAYRAM--LAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 445 qCAIVDTYWMTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDPqtgqvlEGNDVE----GVLVARRPwpsiarTVYR 520
Cdd:cd05958 239 -IPIIDGIGSTEMFHIFISARPGDA--RPGATGKPVPGYEAKVVDD------EGNPVPdgtiGRLAVRGP------TGCR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 521 --DHKRYlETYMKPypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQ 598
Cdd:cd05958 304 ylADKRQ-RTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGV 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 599 AVYAFVTMKPEfdlkATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05958 381 VVKAFVVLRPG----VIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
143-662 |
2.48e-49 |
|
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: 180.20 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 143 PSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECK 222
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 223 VLITTDEGR----RGGKT--IATKQI-VDAALQQCPLVENVLVLRRTGNKVPMTEGRdkwwdeecakmpaycpcerMASE 295
Cdd:cd05926 89 LVLTPKGELgpasRAASKlgLAILELaLDVGVLIRAPSAESLSNLLADKKNAKSEGV-------------------PLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVvHSTAGYLLGTALTLKYVFDAHPDDRFACMADIgwitghsYIIYGPLANGITTAVFESTPVY 375
Cdd:cd05926 150 DLALILHTSGTTGRPKGV-PLTHRNLAASATNITNTYKLTPDDRTLVVMPL-------FHVHGLVASLLSTLAAGGSVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 376 P---TPSRYWDFVDKWKATqLYTA-PTAIR-LLRRMGEDHVKNHdlSSLRVLGSVGEPINPEAWHwynDFAGKNQCAIVD 450
Cdd:cd05926 222 PprfSASTFWPDVRDYNAT-WYTAvPTIHQiLLNRPEPNPESPP--PKLRFIRSCSASLPPAVLE---ALEATFGAPVLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 451 TYWMTETGS-ISIAPLPgAISTKPGSATFPFfGMDVDIIDPqTGQVLEgNDVEGVLVARRPwpSIARTVYRDHKRYLETY 529
Cdd:cd05926 296 AYGMTEAAHqMTSNPLP-PGPRKPGSVGKPV-GVEVRILDE-DGEILP-PGVVGEICLRGP--NVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 530 MKPypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPe 609
Cdd:cd05926 370 FKD--GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE- 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
9C8S_C 610 fDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05926 447 -GASVTEE-----ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
123-661 |
7.22e-49 |
|
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: 178.14 E-value: 7.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:cd05936 5 LEEAARRFPDKTALIFM------GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDegrrggktiatkqivdaalqqcPLVENVLVLRRTGNKVPMTEgrdkwwdeecak 282
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAV----------------------SFTDLLAAGAPLGERVALTP------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mpaycpcermasEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTLK-YVFDAH-PDDRFACMADIgwitghsYIIYG-- 358
Cdd:cd05936 125 ------------EDVAVLQYTSGTTGVPKGAML-THRNLVANALQIKaWLEDLLeGDDVVLAALPL-------FHVFGlt 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 -----PLANGITtAVFESTPVyptPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINPEA 433
Cdd:cd05936 185 valllPLALGAT-IVLIPRFR---PIGVLKEIRKHRVTIFPGVPTMYIAL--LNAPEFKKRDFSSLRLCISGGAPLPVEV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 434 whwYNDFAGKNQCAIVDTYWMTETGS-ISIAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQVLEGNdvEGVLVARRP-- 510
Cdd:cd05936 259 ---AERFEELTGVPIVEGYGLTETSPvVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGE--VGELWVRGPqv 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 ----W--PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVA 584
Cdd:cd05936 332 mkgyWnrPEETAEAFVD-------------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVA 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 585 ETAVVGCADDLTGQAVYAFVTMKPefDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05936 399 EAAVVGVPDPYSGEAVKAFVVLKE--GASLTEE-----EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
147-661 |
3.86e-45 |
|
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: 166.70 E-value: 3.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 tdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaseDPLFILYTSGS 306
Cdd:cd05934 82 ---------------------------------------------------------------------DPASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAgYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTpvypTPSRYWDFVD 386
Cdd:cd05934 93 TGPPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF----SASRFWSDVR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 387 KWKATQLYTAPTAIRLLRRMGEDHVKNHDLssLRVLGsvGEPINPEAWHwynDFAGKNQCAIVDTYWMTETGSISIAPLP 466
Cdd:cd05934 168 RYGATVTNYLGAMLSYLLAQPPSPDDRAHR--LRAAY--GAPNPPELHE---EFEERFGVRLLEGYGMTETIVGVIGPRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 467 GAisTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARRPWpSIARTVYRDHKRYLETYMKpypGYFFFGDGAARD 546
Cdd:cd05934 241 EP--RRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGW-GFFKGYYNMPEATAEAMRN---GWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 547 YDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlkatKEADLSKELAI 626
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRP-------GETLDPEELFA 387
|
490 500 510
....*....|....*....|....*....|....*
9C8S_C 627 QVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
131-660 |
8.39e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 168.60 E-value: 8.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKS-YGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSA 209
Cdd:PRK08314 24 PDKTAIVFYG------RAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 210 ESLRDRVNDCECKVLITTDE---------GRRGGKTIATKQIVDAALQQCPLVENVLvLRRTGNKVPMTEGRDKWWDEEC 280
Cdd:PRK08314 98 EELAHYVTDSGARVAIVGSElapkvapavGNLRLRHVIVAQYSDYLPAEPEIAVPAW-LRAEPPLQALAPGGVVAWKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 281 AKmpAYCPCERMASEDPLFIL-YTSGSTGKPKGVVHsTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGP 359
Cdd:PRK08314 177 AA--GLAPPPHTAGPDDLAVLpYTSGTTGVPKGCMH-THRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 360 LANGITTAVFestpvyptpSRyWD------FVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPInPEA 433
Cdd:PRK08314 254 IYAGATVVLM---------PR-WDreaaarLIERYRVTHWTNIPTMVVDF--LASPGLAERDLSSLRYIGGGGAAM-PEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 434 whwyndFAGK--NQCAI--VDTYWMTETGSISIAPLPGAisTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVA-- 507
Cdd:PRK08314 321 ------VAERlkELTGLdyVEGYGLTETMAQTHSNPPDR--PKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHgp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 508 -------RRPWPSIARTVYRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILH 580
Cdd:PRK08314 393 qvfkgywNRPEATAEAFIEIDGKRFFRT-----------GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKH 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 581 KGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK08314 462 PAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-----EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
99-667 |
4.85e-44 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 166.38 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 99 RAGGFEHGDvqwfpegTLNaayNCLDRHYYKNPKKTAIIYEADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSI 178
Cdd:PRK13295 16 IAAGHWHDR-------TIN---DDLDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 179 YLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgRRGGKTIATKQIVDAALqqcPLVENVLV 258
Cdd:PRK13295 86 QLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKT-FRGFDHAAMARRLRPEL---PALRHVVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 259 LRrtgnkvpmTEGRDKW--------WDEEcAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTLKY 330
Cdd:PRK13295 162 VG--------GDGADSFeallitpaWEQE-PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMH-TANTLMANIVPYAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 331 VFDAHPDDrFACMAD-IGWITGHSYIIYGPLANGiTTAVFEstpvyptpsrywdfvDKWKATQlytaptAIRLLRRMG-- 407
Cdd:PRK13295 232 RLGLGADD-VILMASpMAHQTGFMYGLMMPVMLG-ATAVLQ---------------DIWDPAR------AAELIRTEGvt 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 408 ------------EDHVK--NHDLSSLRVLGSVGEPINP----EAWHwynDFAGKnqcaIVDTYWMTETGSISIAPLPGAI 469
Cdd:PRK13295 289 ftmastpfltdlTRAVKesGRPVSSLRTFLCAGAPIPGalveRARA---ALGAK----IVSAWGMTENGAVTLTKLDDPD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 470 STKPGSATFPFFGMDVDIIDPQTGQVLEGNdvEGVLVARRPwpsiarTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDG 549
Cdd:PRK13295 362 ERASTTDGCPLPGVEVRVVDADGAPLPAGQ--IGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 550 YMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKP--EFDLKATKEADLSKELAIQ 627
Cdd:PRK13295 434 YIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgqSLDFEEMVEFLKAQKVAKQ 513
|
570 580 590 600
....*....|....*....|....*....|....*....|
9C8S_C 628 VrkvigpfaAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGE 667
Cdd:PRK13295 514 Y--------IPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
131-660 |
2.28e-43 |
|
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: 163.56 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIyeadEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEGrrggktiaTKQIVDAALQqcplvenvLVLRRTGNKVPMTEGRDKWWDEEcakmpAYCPCE 290
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAEL--------AEKLASLALP--------VVLLDSAEFDSLSFSDLLFEADE-----AEPPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RMASEDPLFILYTSGSTGKPKGVV--H-----STAGYLLGTALTLkyvfdaHPDDRFACMADIGWITGHSYIIYGPLANG 363
Cdd:cd05904 154 VIKQDDVAALLYSSGTTGRSKGVMltHrnliaMVAQFVAGEGSNS------DSEDVFLCVLPMFHIYGLSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 364 ITTAV---FESTPVYptpsrywDFVDKWKATQLYTAPTAIRLLRRmgEDHVKNHDLSSLRVLGSVGEPINPEAWHwynDF 440
Cdd:cd05904 228 ATVVVmprFDLEELL-------AAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIE---AF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 441 AGK-NQCAIVDTYWMTETGSISIA-PLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDvEGVLVARRpwPSI---- 514
Cdd:cd05904 296 RAKfPNVDLGQGYGMTESTGVVAMcFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQ-TGELWIRG--PSImkgy 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 515 -------ARTVyrDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETA 587
Cdd:cd05904 373 lnnpeatAATI--DKEGWLHT-----------GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAA 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 588 VVGCADDLTGQAVYAFVTMKPEFDLkatKEADLSKELAIQV---RKVigpfaapKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05904 440 VIPYPDEEAGEVPMAFVVRKPGSSL---TEDEIMDFVAKQVapyKKV-------RKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
94-679 |
9.38e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 161.28 E-value: 9.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 94 DFKTVRAGGFEHGDVqwfPEGTlnaaYNCLDRHYYKNPKKTAIIY--EADEPSESREVSYEELMQETCRVANVLKSYGVK 171
Cdd:PRK07529 9 DIEAIEAVPLAARDL---PAST----YELLSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 172 KGDAVSIYLPMTWQaaaaflacarigaIHSAVFAG------------FSAESLRDRVNDCECKVLITTdeGRRGGKTIAT 239
Cdd:PRK07529 82 PGDVVAFLLPNLPE-------------THFALWGGeaagianpinplLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 240 KqiVDAALQQCPLVENVLVL----RRTGNK---VPMTEG----RDKWWDEECAKMPAYCP-CERMASEDPLFILY-TSGS 306
Cdd:PRK07529 147 K--VAEVLAALPELRTVVEVdlarYLPGPKrlaVPLIRRkahaRILDFDAELARQPGDRLfSGRPIGPDDVAAYFhTGGT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTA-----GYLLGTALTLKyvfdahPDDR----------FACMAdigwitghsyIIYGPLANGITTavfes 371
Cdd:PRK07529 225 TGMPKLAQHTHGnevanAWLGALLLGLG------PGDTvfcglplfhvNALLV----------TGLAPLARGAHV----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 372 tpVYPTPS---------RYWDFVDKWKATQLYTAPTAIRLLRRMgedHVKNHDLSSLRVLGSVGEPINPEAwhwYNDFAG 442
Cdd:PRK07529 284 --VLATPQgyrgpgviaNFWKIVERYRINFLSGVPTVYAALLQV---PVDGHDISSLRYALCGAAPLPVEV---FRRFEA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 443 KNQCAIVDTYWMTE-TGSISIAPLPGAIstKPGSA--TFPFFGMDVDIIDPQTGQVLE-GNDVEGVLVARRPwpsiarTV 518
Cdd:PRK07529 356 ATGVRIVEGYGLTEaTCVSSVNPPDGER--RIGSVglRLPYQRVRVVILDDAGRYLRDcAVDEVGVLCIAGP------NV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 519 Y-------RDHKRYLEtymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:PRK07529 428 FsgyleaaHNKGLWLE------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGR 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 592 ADDLTGQAVYAFVTMKPefDLKATKEadlskELAIQVRKVIGPFAA-PKKIYLVSDLPKTRSGKI---------MRRVLR 661
Cdd:PRK07529 502 PDAHAGELPVAYVQLKP--GASATEA-----ELLAFARDHIAERAAvPKHVRILDALPKTAVGKIfkpalrrdaIRRVLR 574
|
650
....*....|....*...
9C8S_C 662 KIVAGEGDQLGDLSSIAD 679
Cdd:PRK07529 575 AALRDAGVEAEVVDVVED 592
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
129-662 |
1.75e-41 |
|
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: 158.41 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFS 208
Cdd:TIGR03098 12 RLPDATALVHH------DRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 209 AESLRDRVNDCECKVLITTDEGRRggktiatkqIVDAALQQCPLVENVLvlrRTGNKVPMTEGRDKW----WDEECAKMP 284
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLD---------LLHPALPGCHDLRTLI---IVGDPAHASEGHPGEepasWPKLLALGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 285 AYcPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVfDAHPDDRFACMADIGWITGHsyiiygplaNGI 364
Cdd:TIGR03098 154 AD-PPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYL-ENRPDDRLLAVLPLSFDYGF---------NQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 365 TTAVFESTPV----YPTPSRYWDFVDKWKATQLYTAPTairLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDF 440
Cdd:TIGR03098 223 TTAFYVGATVvlhdYLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 441 AGKNQcaIVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNdvEGVLVARRPWpsIARTVYR 520
Cdd:TIGR03098 300 LPNAR--LFLMYGLTEAFRSTYLP-PEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGE--EGELVHRGAL--VAMGYWN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 521 DHKRYLETYmKPYPGY----------FFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:TIGR03098 373 DPEKTAERF-RPLPPFpgelhlpelaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFG 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 591 CADDLTGQAVYAFVT--MKPEFDLKAtkeadLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:TIGR03098 452 VPDPTLGQAIVLVVTppGGEELDRAA-----LLAEC----RARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
148-660 |
9.97e-41 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 154.56 E-value: 9.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 148 EVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITT 227
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 228 DEgrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaSEDPLFILYTSGST 307
Cdd:cd05935 81 SE----------------------------------------------------------------LDDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 308 GKPKGVVHsTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFestpvyptpSRyWD---- 383
Cdd:cd05935 97 GLPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM---------AR-WDreta 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 384 --FVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcaIVDTYWMTETGSIS 461
Cdd:cd05935 166 leLIEKYKVTFWTNIPTMLVDL--LATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLR---FVEGYGLTETMSQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 462 IAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQVLEGNdVEGVLVARRPwpSIARTVYRDHKRYLETYMKpYPGYFFF-- 539
Cdd:cd05935 241 HTNPPLRP--KLQCLGIP*FGVDARVIDIETGRELPPN-EVGEIVVRGP--QIFKGYWNRPEETEESFIE-IKGRRFFrt 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 540 GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEad 619
Cdd:cd05935 315 GDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE-- 392
|
490 500 510 520
....*....|....*....|....*....|....*....|.
9C8S_C 620 lskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05935 393 ---DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
149-662 |
1.24e-38 |
|
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: 148.48 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 149 VSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNdceckvlittd 228
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 egrRGGKTIAtkqIVDaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcERMASEDPLFILYTSGSTG 308
Cdd:cd05974 70 ---RGGAVYA---AVD---------------------------------------------ENTHADDPMLLYFTSGTTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 309 KPKGVVHSTAGYLLGTALTLkYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTpsRYWDFVDKW 388
Cdd:cd05974 99 KPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAK--RVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 389 KATQLYTAPTAIRLLRRmgedhvknHDLSSLRV----LGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETgSISIAP 464
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQ--------QDLASFDVklreVVGAGEPLNPEVIEQVRRAWGL---TIRDGYGQTET-TALVGN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 465 LPGAIsTKPGSATFPFFGMDVDIIDPQTGQVLEGnDVEGVLVARRPWPSIARtvYRDHKRYLETYMKPypGYFFFGDGAA 544
Cdd:cd05974 244 SPGQP-VKAGSMGRPLPGYRVALLDPDGAPATEG-EVALDLGDTRPVGLMKG--YAGDPDKTAHAMRG--GYYRTGDIAM 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 545 RDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlKATKEADLSKEL 624
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRA----GYEPSPETALEI 393
|
490 500 510
....*....|....*....|....*....|....*...
9C8S_C 625 AIQVRKVIGPFAAPKKIYLVsDLPKTRSGKIMRRVLRK 662
Cdd:cd05974 394 FRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
131-660 |
1.36e-38 |
|
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: 148.83 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd05930 1 PDAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEGrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmPAYcpce 290
Cdd:cd05930 75 RLAYILEDSGAKLVLTDPDD-----------------------------------------------------LAY---- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rmasedplfILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWItGHSYIIYGPLANGITTAVFE 370
Cdd:cd05930 98 ---------VIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 371 STPVYpTPSRYWDFVDKWKATQLYTAPTAIRLLrrmgEDHVKNHDLSSLRVLGSVGEPINPEAWH-WyndFAGKNQCAIV 449
Cdd:cd05930 167 EEVRK-DPEALADLLAEEGITVLHLTPSLLRLL----LQELELAALPSLRLVLVGGEALPPDLVRrW---RELLPGARLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 450 DTYWMTETGSIS----IAPLPGAISTKP-GSatfPFFGMDVDIIDPQTGQVLEGND----VEGVLVAR----RPWPSIAR 516
Cdd:cd05930 239 NLYGPTEATVDAtyyrVPPDDEEDGRVPiGR---PIPNTRVYVLDENLRPVPPGVPgelyIGGAGLARgylnRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 517 TV---YRDHKRYLETymkpypgyfffGDGAARDYDG---YMwikGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:cd05930 316 FVpnpFGPGERMYRT-----------GDLVRWLPDGnleFL---GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVA 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 591 CADDLTGQAVYAFVTMKPEFDLkatKEADLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05930 382 REDGDGEKRLVAYVVPDEGGEL---DEEELRAHL----AERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
109-662 |
2.75e-38 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 151.77 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 109 QWFPEGTLNAAYNCLDRHYYKNPKKTAIIY--EADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQA 186
Cdd:PLN03052 167 QWLPGAVLNVAECCLTPKPSKTDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 187 AAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIAT-KQIVDAalqQCPLVEnVLVLRRTGNK 265
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLySRVVEA---KAPKAI-VLPADGKSVR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 266 VPMTEGrDKWWDEECAKM-PAYCPCERMASEDPL----FILYTSGSTGKPKGV--VHSTAgyllgtaltLKYVFD--AHP 336
Cdd:PLN03052 323 VKLREG-DMSWDDFLARAnGLRRPDEYKAVEQPVeaftNILFSSGTTGEPKAIpwTQLTP---------LRAAADawAHL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 337 D----DRFACMADIGWITGHsYIIYGPLANGITTAVFESTPVYPTPSRywdFVDKWKATQLYTAPTAIRLLRRMGedHVK 412
Cdd:PLN03052 393 DirkgDIVCWPTNLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAK---FVQDAKVTMLGTVPSIVKTWKNTN--CMA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 413 NHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcAIVDTYWMTETGSISIAplpGAISTKPGSATF--PFFGMDVDIID- 489
Cdd:PLN03052 467 GLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTELGGGFVT---GSLLQPQAFAAFstPAMGCKLFILDd 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 490 ---------PQTGQVLEGNDVEGvlvarrpwpSIARTVYRDHKrylETYMKPYPGY-----FFFGDGAARDYDGYMWIKG 555
Cdd:PLN03052 542 sgnpypddaPCTGELALFPLMFG---------ASSTLLNADHY---KVYFKGMPVFngkilRRHGDIFERTSGGYYRAHG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 556 RVDDVINVSGHRLSTAEVE----SAlilHKGVAETAVVGCADDLTG--QAVYAFVTMKPEFDLKATKEADLSKELAIQvr 629
Cdd:PLN03052 610 RADDTMNLGGIKVSSVEIErvcnAA---DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQ-- 684
|
570 580 590
....*....|....*....|....*....|...
9C8S_C 630 KVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:PLN03052 685 KKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
296-662 |
4.36e-38 |
|
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: 147.05 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGittAVFESTPvY 375
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHAN-LAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAG---ASVEFLP-K 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 376 PTPSRYWDFVDKWKATQLYTAPTA-IRLL---RRMGEDHVKNHD--LSSLR--VLGSVGEPInpeawHWYNDFAGKNQCA 447
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyyEAHFTDPQFARAaaAERLRlmVSGSAALPV-----PTLEEWEAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 448 IVDTYWMTETGSISIAPLPGaiSTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARrpwPSIARTVYRDHKRYLE 527
Cdd:cd05941 240 LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRG---PSVFKEYWNKPEATKE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 528 TYMKPypGYFFFGDGAARDYDGYMWIKGRV-DDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTM 606
Cdd:cd05941 315 EFTDD--GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 607 KPEfdlKATKEADlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05941 393 RAG---AAALSLE---ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
158-661 |
5.37e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 147.20 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 158 TCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVF----AGFSAESLRDRVNDCECKVLITTdegrrg 233
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLAD------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 234 gKTIATKqiVDAALQQCPLVENVLvlrrtgnkvpmteGRDKWWDEEcAKMPAYcpceRMASEDPLFILYTSGSTGKPKGV 313
Cdd:cd05922 77 -AGAADR--LRDALPASPDPGTVL-------------DADGIRAAR-ASAPAH----EVSHEDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 314 VHSTAGYLLGTALTLKYVfDAHPDDRFACMADIGWITGHSyIIYGPLANGITTAVfesTPVYPTPSRYWDFVDKWKATQL 393
Cdd:cd05922 136 RLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL---TNDGVLDDAFWEDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 394 YTAPTAIRLLRRMGEDHVKnhdLSSLRVLGSVGEPINPEAWHWYNDFAGKNQcaIVDTYWMTE-TGSISIAPlPGAISTK 472
Cdd:cd05922 211 AGVPSTYAMLTRLGFDPAK---LPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEaTRRMTYLP-PERILEK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 473 PGSATFPFFGMDVDIIDPQtGQVLEGNDVeGVLVARRPwpsiarTVYRDHKRYLETYMKP--YPGYFFFGDGAARDYDGY 550
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDD-GTPTPPGEP-GEIVHRGP------NVMKGYWNDPPYRRKEgrGGGVLHTGDLARRDEDGF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 551 MWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGcADDLTGQAVYAFVTMKPEFDLKatkeaDLSKELAiqvrK 630
Cdd:cd05922 357 LFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVG-LPDPLGEKLALFVTAPDKIDPK-----DVLRSLA----E 426
|
490 500 510
....*....|....*....|....*....|.
9C8S_C 631 VIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05922 427 RLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
131-662 |
8.99e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 147.74 E-value: 8.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:PRK07656 19 GDKEAYVFG------DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEgrrggkTIATKQIVDAALqqcPLVENVLVLRrTGNKVPMTEGRDKWWDEECAKMPAYCPCE 290
Cdd:PRK07656 93 EAAYILARGDAKALFVLGL------FLGVDYSATTRL---PALEHVVICE-TEEDDPHTEKMKTFTDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rMASEDPLFILYTSGSTGKPKGVV----------HSTAGYLlgtaltlkyvfDAHPDDRFACMADIGWITGHSYIIYGPL 360
Cdd:PRK07656 163 -VDPDDVADILFTSGTTGRPKGAMlthrqllsnaADWAEYL-----------GLTEGDRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 361 ANGITT---AVFEstpvyptPSRYWDFVDKWKATQLYTAPTAIRLLRrmgeDHVK--NHDLSSLRVLGSVGEPINPEAWH 435
Cdd:PRK07656 231 MRGATIlplPVFD-------PDEVFRLIETERITVLPGPPTMYNSLL----QHPDrsAEDLSSLRLAVTGAASMPVALLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 436 wynDFAGKNQCAIVDT-YWMTE-TGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQtGQVLEGNDVeGVLVARRPwps 513
Cdd:PRK07656 300 ---RFESELGVDIVLTgYGLSEaSGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNEL-GEEVPVGEV-GELLVRGP--- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 514 iartvyrdhkryleTYMKPY---P----------GYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILH 580
Cdd:PRK07656 372 --------------NVMKGYyddPeataaaidadGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 581 KGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK07656 438 PAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE-------EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
..
9C8S_C 661 RK 662
Cdd:PRK07656 511 RE 512
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-667 |
3.04e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 145.49 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 121 NCLDRHYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIh 200
Cdd:PRK03640 6 NWLKQRAFLTPDRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 201 sAVFAG--FSAESLRDRVNDCECKVLITTDEgrrggktiatkqivdaaLQQcplvENVLVLRRTGNKVPMTEGRDKWWDE 278
Cdd:PRK03640 79 -AVLLNtrLSREELLWQLDDAEVKCLITDDD-----------------FEA----KLIPGISVKFAELMNGPKEEAEIQE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 279 ECakmpaycPCERMASedplfILYTSGSTGKPKGVVHSTAGYL---LGTALTLKYvfdaHPDDRFACMADIGWITGHSY- 354
Cdd:PRK03640 137 EF-------DLDEVAT-----IMYTSGTTGKPKGVIQTYGNHWwsaVGSALNLGL----TEDDCWLAAVPIFHISGLSIl 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 355 ---IIYGplangittavfesTPVYPTPSRYWDFVDKW----KATQLYTAPTAI-RLLRRMGEDHVKnhdlSSLR--VLGs 424
Cdd:PRK03640 201 mrsVIYG-------------MRVVLVEKFDAEKINKLlqtgGVTIISVVSTMLqRLLERLGEGTYP----SSFRcmLLG- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 425 vGEPINPeawhwyndfAGKNQCA-----IVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDpqTGQVLEGN 499
Cdd:PRK03640 263 -GGPAPK---------PLLEQCKekgipVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEK--DGVVVPPF 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 500 DVEGVLVARrpwPSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALIL 579
Cdd:PRK03640 331 EEGEIVVKG---PNVTKGYLNREDATRETFQD---GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 580 HKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkatkeadlSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRV 659
Cdd:PRK03640 405 HPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT---------EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHE 475
|
....*...
9C8S_C 660 LRKIVAGE 667
Cdd:PRK03640 476 LKQLVEEM 483
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
180-676 |
2.94e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 143.03 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 180 LPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIAT-KQIVDAALQQCplvenvLV 258
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLySKVVEAAPAKA------IV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 259 LRRTGNK--VPMTEGRDKWWDEECAKMPAYCPCER------MASEDPLFILYTSGSTGKPKGV--VHSTAgylLGTALTL 328
Cdd:PLN03051 75 LPAAGEPvaVPLREQDLSWCDFLGVAAAQGSVGGNeyspvyAPVESVTNILFSSGTTGEPKAIpwTHLSP---LRCASDG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 329 KYVFDAHPDDRFACMADIGWITGhSYIIYGPLANGITTAVFESTPVYPTpsrYWDFVDKWKATQLYTAPTAIRLLRRMGE 408
Cdd:PLN03051 152 WAHMDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 409 DHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNQcAIVDTYWMTETGS--ISIAPL-PGAistkPGSATFPFFGMDV 485
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASgyISSTLLqPQA----PGAFSTASLGTRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 486 DIIDpqTGQVLEGNDVEGV-LVARRPwPSIA---RTVYRDHKrylETYMKPYPGYFF-------FGDGAARDYDGYMWIK 554
Cdd:PLN03051 303 VLLN--DNGVPYPDDQPCVgEVALAP-PMLGasdRLLNADHD---KVYYKGMPMYGSkgmplrrHGDIMKRTPGGYFCVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 555 GRVDDVINVSGHRLSTAEVESALI-LHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDL--KATKEADLSKELAIQVRKV 631
Cdd:PLN03051 377 GRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKgfDQARPEALQKKFQEAIQTN 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
9C8S_C 632 IGPFAAPKKIYLVSDLPKTRSGKIMRRVLRkivagegDQLGDLSS 676
Cdd:PLN03051 457 LNPLFKVSRVKIVPELPRNASNKLLRRVLR-------DQLKKELS 494
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
125-655 |
8.22e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 142.87 E-value: 8.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 125 RHYYK-NPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAV 203
Cdd:PRK06178 40 RAWAReRPQRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 204 FAGFSAESLRDRVNDCECKVLITTDegrrggktiATKQIVDAALQQCPLvENVLVLRRTG-----NKVPMTEGRDK---- 274
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALD---------QLAPVVEQVRAETSL-RHVIVTSLADvlpaePTLPLPDSLRAprla 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 275 ---WWD--EECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTlkYVFDAHP---DDRFACMADI 346
Cdd:PRK06178 184 aagAIDllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEH-TQRDMVYTAAA--AYAVAVVggeDSVFLSFLPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 347 GWITGHSYIIYGPLANGITTAVFestpvyptpSRyWDFVDKWKATQLYTAPTAIRLLRRMGE--DH--VKNHDLSSLRVL 422
Cdd:PRK06178 261 FWIAGENFGLLFPLFSGATLVLL---------AR-WDAVAFMAAVERYRVTRTVMLVDNAVElmDHprFAEYDLSSLRQV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 423 GSVG--EPINPEAWHWYNDFAGknqCAIVDTYW-MTET---GSISIAPLPGA--ISTKPGSATFPFFGMDVDIIDPQTGQ 494
Cdd:PRK06178 331 RVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcDTFTAGFQDDDfdLLSQPVFVGLPVPGTEFKICDFETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 495 VLE-GndVEGVLVARRP------W--PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSG 565
Cdd:PRK06178 408 LLPlG--AEGEIVVRTPsllkgyWnkPEATAEALRD-------------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 566 HRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPkKIYLVS 645
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA-------AALQAWCRENMAVYKVP-EIRIVD 544
|
570
....*....|
9C8S_C 646 DLPKTRSGKI 655
Cdd:PRK06178 545 ALPMTATGKV 554
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
149-662 |
1.51e-35 |
|
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: 139.82 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 149 VSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTD 228
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 EGRrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmteGRDKwwdeecAKMPAycpcermaseDPLFILYTSGSTG 308
Cdd:cd05903 82 RFR---------------------------------------QFDP------AAMPD----------AVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 309 KPKGVVHSTAGYLLGT-ALTLKYVFDahPDDRFACMADIGWITGHSYIIYGPLANGiTTAVFESTPvypTPSRYWDFVDK 387
Cdd:cd05903 107 EPKGVMHSHNTLSASIrQYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLG-APVVLQDIW---DPDKALALMRE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 388 WKATQLYTAPTAIRLLRRMGEDhvKNHDLSSLRVLGSVGEPINP----EAWHWYNDFagknqcaIVDTYWMTETGSI--S 461
Cdd:cd05903 181 HGVTFMMGATPFLTDLLNAVEE--AGEPLSRLRTFVCGGATVPRslarRAAELLGAK-------VCSAYGSTECPGAvtS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 462 IAP-LPGAISTKPGSatfPFFGMDVDIIDpQTGQVLEGNdVEGVLVARRPwpsiaRTVYRDHKRYLETYMKPYPGYFFFG 540
Cdd:cd05903 252 ITPaPEDRRLYTDGR---PLPGVEIKVVD-DTGATLAPG-VEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 541 DGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTmkpefdLKATKEADL 620
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVV------TKSGALLTF 395
|
490 500 510 520
....*....|....*....|....*....|....*....|..
9C8S_C 621 SKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05903 396 DELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
136-662 |
1.69e-33 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 135.07 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 136 IIYeADEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDR 215
Cdd:cd12119 14 IVS-RTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 216 VNDCECKVLITTDEgrrggktiaTKQIVDAALQQCPLVENVLVLRrTGNKVPMTEGrDKWWDEEcakmpaycpcERMASE 295
Cdd:cd12119 93 INHAEDRVVFVDRD---------FLPLLEAIAPRLPTVEHVVVMT-DDAAMPEPAG-VGVLAYE----------ELLAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLF------------ILYTSGSTGKPKGVVHSTAGYLLGT-ALTLKYVFDAHPDDRFACMADI----GW-------ITG 351
Cdd:cd12119 152 SPEYdwpdfdentaaaICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMfhvnAWglpyaaaMVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 352 HSYIIYGPlangittavfestpvYPTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINP 431
Cdd:cd12119 232 AKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGL--LDHLEANGRDLSSLRRVVIGGSAVPR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 432 EAWHWYNDfagknqcAIVDTY--W-MTETGSI-SIAPLPGAISTKPGSATF--------PFFGMDVDIIDPQTGQVLEGN 499
Cdd:cd12119 295 SLIEAFEE-------RGVRVIhaWgMTETSPLgTVARPPSEHSNLSEDEQLalrakqgrPVPGVELRIVDDDGRELPWDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 500 DVEGVLVARRPWpsIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALIL 579
Cdd:cd12119 368 KAVGELQVRGPW--VTKSYYKNDEESEALTED---GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 580 HKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRV 659
Cdd:cd12119 443 HPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA-------EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
...
9C8S_C 660 LRK 662
Cdd:cd12119 516 LRE 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
123-661 |
2.30e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 132.03 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHyyknPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYL---PMTWQaaaaflacarigAI 199
Cdd:PRK06188 22 LKRY----PDRPALVLG------DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSlnrPEVLM------------AI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 200 HSAVFAGFSAESL---------RDRVNDCECKVLITtDEGR---RGGktiatkqivdAALQQCPLVENVLVLRrtgnkvP 267
Cdd:PRK06188 80 GAAQLAGLRRTALhplgslddhAYVLEDAGISTLIV-DPAPfveRAL----------ALLARVPSLKHVLTLG------P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 268 MTEGRDKWwdEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTAltlkyvfdahpddrfACMADIG 347
Cdd:PRK06188 143 VPDGVDLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 348 WITGHSYIIYGPLANGittavfESTPVYPT--------------PSRYWDFVDKWKATQLYTAPTAI-RLLrrmgeDH-- 410
Cdd:PRK06188 206 WPADPRFLMCTPLSHA------GGAFFLPTllrggtvivlakfdPAEVLRAIEEQRITATFLVPTMIyALL-----DHpd 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 411 VKNHDLSSLRVLGSVGEPINPeawhwyndfaGKNQCAI-------VDTYWMTETGS-ISIAPLPGAISTKP---GSATFP 479
Cdd:PRK06188 275 LRTRDLSSLETVYYGASPMSP----------VRLAEAIerfgpifAQYYGQTEAPMvITYLRKRDHDPDDPkrlTSCGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 480 FFGMDVDIIDPQTGQVLEGND----VEGVLVARRPW--PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWI 553
Cdd:PRK06188 345 TPGLRVALLDEDGREVAQGEVgeicVRGPLVMDGYWnrPEETAEAFRD-------------GWLHTGDVAREDEDGFYYI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 554 KGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATkeadlskELAIQVRKVIG 633
Cdd:PRK06188 412 VDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA-------ELQAHVKERKG 484
|
570 580
....*....|....*....|....*...
9C8S_C 634 PFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
115-661 |
3.20e-32 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 131.34 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 115 TLNAAYNCLDRHYyknPKKTAIIYEaDEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYL---P---MTWqaaa 188
Cdd:PRK08008 8 HLRQMWDDLADVY---GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLdncPefiFCW---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 189 afLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgrrggktiaTKQIVDAALQQCP-LVENVLVLRRTGnkvP 267
Cdd:PRK08008 80 --FGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ---------FYPMYRQIQQEDAtPLRHICLTRVAL---P 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 268 MTEGRDKwWDEECAKMPAYCpCER--MASEDPLFILYTSGSTGKPKGVV--HST---AGYLLG--TALTLKYVF-----D 333
Cdd:PRK08008 146 ADDGVSS-FTQLKAQQPATL-CYAppLSTDDTAEILFTSGTTSRPKGVVitHYNlrfAGYYSAwqCALRDDDVYltvmpA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 334 AHPDdrFACMADIGWITGhsyiiygplanGITTAVFEStpvYpTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKN 413
Cdd:PRK08008 224 FHID--CQCTAAMAAFSA-----------GATFVLLEK---Y-SARAFWGQVCKYRATITECIPMMIRTL--MVQPPSAN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 414 HDLSSLRvlgsvgepinpEAWHWYN-------DFAGKNQCAIVDTYWMTETgsisiapLPGAISTKPG------SATFPF 480
Cdd:PRK08008 285 DRQHCLR-----------EVMFYLNlsdqekdAFEERFGVRLLTSYGMTET-------IVGIIGDRPGdkrrwpSIGRPG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 481 FGMDVDIIDPQtGQVLEGNDVEGVLVARRPWPSIARTVYRDHKRYLETyMKPyPGYFFFGDGAARDYDGYMWIKGRVDDV 560
Cdd:PRK08008 347 FCYEAEIRDDH-NRPLPAGEIGEICIKGVPGKTIFKEYYLDPKATAKV-LEA-DGWLHTGDTGYVDEEGFFYFVDRRCNM 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 561 INVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlkatkEADLSKELAIQ-VRKVIGPFAAPK 639
Cdd:PRK08008 424 IKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE--------GETLSEEEFFAfCEQNMAKFKVPS 495
|
570 580
....*....|....*....|..
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK08008 496 YLEIRKDLPRNCSGKIIKKNLK 517
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
143-660 |
3.45e-32 |
|
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: 131.09 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 143 PSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCE-C 221
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 222 KVLITTDEGrrggktiATKQIVDAALqqCPLVENVLVlrrtGNKVPMTEGrdkwwdeecaKMPAYCPCErmaSEDPLFIL 301
Cdd:cd05923 103 AAVIAVDAQ-------VMDAIFQSGV--RVLALSDLV----GLGEPESAG----------PLIEDPPRE---PEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 302 YTSGSTGKPKGVV---HSTAGYLLGTALTLKYVFDAHpdDRFACMADIGWITGHSYIIYGPLANGITTAVfestPVYPTP 378
Cdd:cd05923 157 YTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 379 SRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAgknQCAIVDTYWMTETG 458
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDAL--AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL---PGEKVNIYGTTEAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 459 SISIAPLPgaistKPGSATFPFFGMDVDIIDPQTG-QVLEGNDVEGVLVARRPwpsiARTVYRDHKRYLE-TYMKPYPGY 536
Cdd:cd05923 306 NSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSpDEALANGEEGELIVAAA----ADAAFTGYLNQPEaTAKKLQDGW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 537 FFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlkATK 616
Cdd:cd05923 377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-----GTL 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
9C8S_C 617 EAD------LSKELAiqvrkvigPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05923 452 SADeldqfcRASELA--------DFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
150-588 |
2.00e-31 |
|
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: 127.00 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSY-GVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTD 228
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 EGR-----RGGKTIATKQIVDAALQQCPLVENvlvlrrtgnkvpmtegrdkwwdeecakmpaycPCERMASEDPLFILYT 303
Cdd:TIGR01733 81 ALAsrlagLVLPVILLDPLELAALDDAPAPPP--------------------------------PDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 304 SGSTGKPKGVV--HSTAGYLLGtALTLKYVFDahPDDRFACMADIGWitGHSYI-IYGPLANGITTAVFESTPVYPTPSR 380
Cdd:TIGR01733 129 SGSTGRPKGVVvtHRSLVNLLA-WLARRYGLD--PDDRVLQFASLSF--DASVEeIFGALLAGATLVVPPEDEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 381 YWDFVDKWKATQLYTAPTAIRLLRRMGEDhvknhDLSSLRVLGSVGEPINPEA---WHWyndfAGKNqCAIVDTYWMTE- 456
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEALTPALvdrWRA----RGPG-ARLINLYGPTEt 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 457 TGSISIAPLPGAISTKPGSATF--PFFGMDVDIIDPQTGQVLEGND----VEGVLVAR----RP------------WPSI 514
Cdd:TIGR01733 274 TVWSTATLVDPDDAPRESPVPIgrPLANTRLYVLDDDLRPVPVGVVgelyIGGPGVARgylnRPeltaerfvpdpfAGGD 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 515 ARTVYRdhkryleTymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAV 588
Cdd:TIGR01733 354 GARLYR-------T-----------GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
124-661 |
4.28e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 127.89 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 124 DRHYYKNPKKTAIIYeadePSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAV 203
Cdd:PRK13391 4 GIHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 204 FAGFSAESLRDRVNDCECKVLITtdegrrggkTIATKQIVDAALQQCPLVENVLVLRRTGNkvpmtegRDKWWD-EECAk 282
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALIT---------SAAKLDVARALLKQCPGVRHRLVLDGDGE-------LEGFVGyAEAV- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mpAYCPCERMASE---DPLfiLYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDA----HPDDRFACMADIgwitGHSyi 355
Cdd:PRK13391 143 --AGLPATPIADEslgTDM--LYSSGTTGRPKGIKRPLPEQPPDTPLPLTAFLQRlwgfRSDMVYLSPAPL----YHS-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 356 iyGPLA-NGITTAVFESTPVYPT--PSRYWDFVDKWKATQLYTAPTA-IRLLrRMGEDHVKNHDLSSLRVLGSVGEPINP 431
Cdd:PRK13391 213 --APQRaVMLVIRLGGTVIVMEHfdAEQYLALIEEYGVTHTQLVPTMfSRML-KLPEEVRDKYDLSSLEVAIHAAAPCPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 432 EAWHWYNDFAGknqcAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGmDVDIIDPQtGQVLEgndvegvlvarrpw 511
Cdd:PRK13391 290 QVKEQMIDWWG----PIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDD-GAELP-------------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 PSIARTVYRDHKRYLEtYMK----------PYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHK 581
Cdd:PRK13391 350 PGEPGTIWFEGGRPFE-YLNdpaktaearhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHP 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 582 GVAETAVVGCADDLTGQAVYAFVTMKPEFDlkatKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK13391 429 KVADAAVFGVPNEDLGEEVKAVVQPVDGVD----PGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
289-662 |
5.45e-31 |
|
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: 125.92 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 289 CERMASedplfILYTSGSTGKPKGVVHSTAGYL---LGTALTLkyvfDAHPDDRFACMADIGWITGHSYIIYGplangit 365
Cdd:cd05912 76 LDDIAT-----IMYTSGTTGKPKGVQQTFGNHWwsaIGSALNL----GLTEDDNWLCALPLFHISGLSILMRS------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 366 taVFESTPVYptpsrywdFVDKWKATQLYTA------------PTAI-RLLRRMGEdhvknHDLSSLR--VLGsvGEPIN 430
Cdd:cd05912 140 --VIYGMTVY--------LVDKFDAEQVLHLinsgkvtiisvvPTMLqRLLEILGE-----GYPNNLRciLLG--GGPAP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 431 PEAWHwyndfagknQCA-----IVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDP-----QTGQV-LEGN 499
Cdd:cd05912 203 KPLLE---------QCKekgipVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDgqppyEVGEIlLKGP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 500 DVEGVLVARRPwpsIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALIL 579
Cdd:cd05912 274 NVTKGYLNRPD---ATEESFEN-------------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 580 HKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkatkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRV 659
Cdd:cd05912 338 HPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE---------EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
...
9C8S_C 660 LRK 662
Cdd:cd05912 409 LKQ 411
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
302-662 |
6.55e-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: 124.52 E-value: 6.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 302 YTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGittavfeSTPVYPTPSRY 381
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG-------AHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 382 ---------WDFVDKWKATQLYTAPTAIR-LLRRMGedhvkNHDLSSLRVLGSVGEPINPEAwhwYNDFAGKNQCAIVDT 451
Cdd:cd05944 81 rnpglfdnfWKLVERYRITSLSTVPTVYAaLLQVPV-----NADISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 452 YWMTETGSI-SIAPLPGAIstKPGSA--TFPFFGMDVDIIDPQTGQVLE--GNDVEGVLVARRPwpsiartvyrDHKRYL 526
Cdd:cd05944 153 YGLTEATCLvAVNPPDGPK--RPGSVglRLPYARVRIKVLDGVGRLLRDcaPDEVGEICVAGPG----------VFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 527 ETYMK----PYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYA 602
Cdd:cd05944 221 YTEGNknafVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 603 FVTMKPefDLKATKEadlskELAIQVRKVIGPFAA-PKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05944 301 YVQLKP--GAVVEEE-----ELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
128-660 |
3.21e-30 |
|
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: 124.28 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 128 YKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTwqaaaaflaCARIGAIHSAVFAGF 207
Cdd:cd05945 2 AANPDRPAVVEG------GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKS---------PDAIAAFLAALKAGH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 208 S-----AESLRDRVNdceckvlittdegrrggktiatkQIVDAAlqQCPLVenvlvlrrtgnkvpMTEGRDkwwdeecak 282
Cdd:cd05945 67 AyvpldASSPAERIR-----------------------EILDAA--KPALL--------------IADGDD--------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mPAYcpcermasedplfILYTSGSTGKPKGVVHSTAGYLLGTALTLKYvFDAHPDDRFACMADIgwitghS-----YIIY 357
Cdd:cd05945 99 -NAY-------------IIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAPF------SfdlsvMDLY 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GPLANGITTAVFESTpVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNhdLSSLRVLGSVGEPI-NPEAWHW 436
Cdd:cd05945 158 PALASGATLVPVPRD-ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPES--LPSLRHFLFCGEVLpHKTARAL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 YNDFAGknqCAIVDTYWMTE-TGSISIAPLPGAISTKPGSAT--FPFFGMDVDIIDPQTGQVLEGndVEGVLVARRPwpS 513
Cdd:cd05945 235 QQRFPD---ARIYNTYGPTEaTVAVTYIEVTPEVLDGYDRLPigYAKPGAKLVILDEDGRPVPPG--EKGELVISGP--S 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 514 IArtvyrdhKRYLETYMKPypGYFFF----------GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGV 583
Cdd:cd05945 308 VS-------KGYLNNPEKT--AAAFFpdegqrayrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 584 AETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEadLSKELAiqvrKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05945 379 KEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKA--IKAELA----ERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
144-661 |
3.62e-30 |
|
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: 124.76 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCeckv 223
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 littdegrrGGKTIATKQIVDAALqqcpLVENVLVLrrtgnkvpmtegrdkWWDEECAKMPAYCPCE-RMASEDPLFILY 302
Cdd:cd17651 92 ---------GPVLVLTHPALAGEL----AVELVAVT---------------LLDQPGAAAGADAEPDpALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 303 TSGSTGKPKGVV--HSTAGYLLGTaltLKYVFDAHPDDRFACMADIGW-ITGHSyiIYGPLANGiTTAVFESTPVYPTPS 379
Cdd:cd17651 144 TSGSTGRPKGVVmpHRSLANLVAW---QARASSLGPGARTLQFAGLGFdVSVQE--IFSTLCAG-ATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 380 RYWDFVDKWKATQLYtAPTAirLLRRMGEdHVKNHD--LSSLRVLGSVGEP--INPEAWHWyndFAGKNQCAIVDTYWMT 455
Cdd:cd17651 218 ALAAWLDEQRISRVF-LPTV--ALRALAE-HGRPLGvrLAALRYLLTGGEQlvLTEDLREF---CAGLPGLRLHNHYGPT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 456 ETGSISIAPLPGAISTKPGSATF--PFFGMDVDIIDP--------QTGQVLEGndveGVLVAR----RPWPSIARTV--- 518
Cdd:cd17651 291 ETHVVTALSLPGDPAAWPAPPPIgrPIDNTRVYVLDAalrpvppgVPGELYIG----GAGLARgylnRPELTAERFVpdp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 519 YRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQ 598
Cdd:cd17651 367 FVPGARMYRT-----------GDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 599 AVYAFVTMKPEFDLKATkeadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd17651 436 RLVAYVVGDPEAPVDAA-------ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
296-664 |
2.77e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.97 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMAdIGWITGHSYIIYGPLANGITTAvfestpvy 375
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRSLLAGAELVL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 376 ptPSRYWDFvdkwKATQLYTAPTAIRL----LRRMGEDHVKNHDLSSLRVLGSVGEPINPEAwhwyNDFAGKNQCAIVDT 451
Cdd:cd17630 72 --LERNQAL----AEDLAPPGVTHVSLvptqLQRLLDSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 452 YWMTETGSisiaplpgAISTKPGSATfpffgmdvdiIDPQTGQVLEGNDVeGVLVARRPWPSiARTVYRDHKRYLETYMK 531
Cdd:cd17630 142 YGMTETAS--------QVATKRPDGF----------GRGGVGVLLPGREL-RIVEDGEIWVG-GASLAMGYLRGQLVPEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 532 PYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFD 611
Cdd:cd17630 202 NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
9C8S_C 612 lkatkeadlSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIV 664
Cdd:cd17630 282 ---------PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
144-661 |
3.78e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 122.11 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKV 223
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LIttdegrrgGKTIATKQIVDAALQQCPLVE-----NVLVLRRTGNKVPMTEGRDKWWDEECAKMPAYcpcERMASEDPL 298
Cdd:PRK12406 87 LI--------AHADLLHGLASALPAGVTVLSvptppEIAAAYRISPALLTPPAGAIDWEGWLAQQEPY---DGPPVPQPQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVVHS--TAGYLLGTALTLKYVFDAHPDDRFACmadigwiTG---HSyiiyGPLANGITTAVFESTP 373
Cdd:PRK12406 156 SMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALL-------TGplyHS----APNAYGLRAGRLGGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 374 VYPT---PSRYWDFVDKWKATQLYTAPTA-IRLLRrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIV 449
Cdd:PRK12406 225 VLQPrfdPEELLQLIERHRITHMHMVPTMfIRLLK-LPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP---VIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 450 DTYWMTETGSISIAPLPGAIStKPGSATFPFFGMDVDIIDpQTGQVLEGNDVeGVLVARRPwpSIARTVYRDH---KRYL 526
Cdd:PRK12406 301 EYYGSTESGAVTFATSEDALS-HPGTVGKAAPGAELRFVD-EDGRPLPQGEI-GEIYSRIA--GNPDFTYHNKpekRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 527 ETymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTM 606
Cdd:PRK12406 376 DR-----GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEP 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 607 KPEFDLkatKEADLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK12406 451 QPGATL---DEADIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
147-665 |
8.32e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 121.65 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAI---HSAVFagfSAESLRDRVNDCECKV 223
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLY---TAHELEHPFEDHGARV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LITTD------EGRRGG---KTIATKQIVDA--ALQQCPLVENVLVLRRTGNK----VPMTEGRDKWWDEECAKMPAYCP 288
Cdd:PRK05605 133 AIVWDkvaptvERLRRTtplETIVSVNMIAAmpLLQRLALRLPIPALRKARAAltgpAPGTVPWETLVDAAIGGDGSDVS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 289 CERMASEDPLFILYTSGSTGKPKGVVhstagyllgtaLTlkyvfdaHPDDRFACMADIGWITG---------------Hs 353
Cdd:PRK05605 213 HPRPTPDDVALILYTSGTTGKPKGAQ-----------LT-------HRNLFANAAQGKAWVPGlgdgpervlaalpmfH- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 354 yiIYGpLANGITTAVF-ESTPV-YPTPS--RYWDFVDKWKATQLYTAPTAIRLLRRMGEDHvkNHDLSSLRVLGSVGEPI 429
Cdd:PRK05605 274 --AYG-LTLCLTLAVSiGGELVlLPAPDidLILDAMKKHPPTWLPGVPPLYEKIAEAAEER--GVDLSGVRNAFSGAMAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 430 NPEAWHWYNDFAGKNqcaIVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARR 509
Cdd:PRK05605 349 PVSTVELWEKLTGGL---LVEGYGLTETSPIIVGN-PMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEGELLVRG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 510 PwpsiarTVYRD-HKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAV 588
Cdd:PRK05605 425 P------QVFKGyWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 589 VGCADDLTGQAVYAFVTMKPefdlKATKEADLSKELAiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:PRK05605 499 VGLPREDGSEEVVAAVVLEP----GAALDPEGLRAYC---REHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELL 568
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
147-667 |
1.62e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 119.91 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TDEGRRGGktiatkqivdaalqqcPLVENVLVLRRTGnkvpmtegrdkwwDEECAKMPAYCPCERmasedPLFILYTSGS 306
Cdd:PRK09088 101 DDAVAAGR----------------TDVEDLAAFIASA-------------DALEPADTPSIPPER-----VSLILFTSGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAV---FEstpvyPTPSRYWD 383
Cdd:PRK09088 147 SGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVsngFE-----PKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 384 FVDKWKATQLYTAPTAIRLLRRMgedhvKNHDLSSLRVLGSV---GEPINPEAWHWYNDfagkNQCAIVDTYWMTETGSI 460
Cdd:PRK09088 221 GDPALGITHYFCVPQMAQAFRAQ-----PGFDAAALRHLTALftgGAPHAAEDILGWLD----DGIPMVDGFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 461 SIAPL-PGAISTKPGSATFPFFGMDVDIIDPQtgqvleGNDVE----GVLVARRPwpSIARTVYRDHKRYLETYMKPypG 535
Cdd:PRK09088 292 FGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQ------GNDCPagvpGELLLRGP--NLSPGYWRRPQATARAFTGD--G 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 536 YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKAt 615
Cdd:PRK09088 362 WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDL- 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
9C8S_C 616 keADLSKELAIQVRKvigpFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGE 667
Cdd:PRK09088 441 --ERIRSHLSTRLAK----YKVPKHLRLVDALPRTASGKLQKARLRDALAAG 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
131-662 |
3.70e-28 |
|
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: 118.56 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd12118 18 PDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLIttdegrrggktiatkqiVDAALQQCPLVEnvlvlrrTGNKVPMTEgrdkWWDEECakmpaycpce 290
Cdd:cd12118 92 EIAFILRHSEAKVLF-----------------VDREFEYEDLLA-------EGDPDFEWI----PPADEW---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rmaseDPLFILYTSGSTGKPKGVVHSTAG-YLlgTALTLKYVFDAHPDDRFACMADI----GWItghsyIIYGPLANGIT 365
Cdd:cd12118 134 -----DPIALNYTSGTTGRPKGVVYHHRGaYL--NALANILEWEMKQHPVYLWTLPMfhcnGWC-----FPWTVAAVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 366 TAVFESTpvypTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDhvknhDLSSL--RVLGSVGEPINPEAWhwyndFAGK 443
Cdd:cd12118 202 NVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPS-----DARPLphRVHVMTAGAPPPAAV-----LAKM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 444 NQCA--IVDTYWMTET-GSISIAP-------LPG----AISTKPGSATFPFFGMDVdiIDPQTGQVLEGNDVE-GVLVAR 508
Cdd:cd12118 268 EELGfdVTHVYGLTETyGPATVCAwkpewdeLPTeeraRLKARQGVRYVGLEEVDV--LDPETMKPVPRDGKTiGEIVFR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 509 RPwpSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAV 588
Cdd:cd12118 346 GN--IVMKGYLKNPEATAEAFRG---GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 589 VGCADDLTGQAVYAFVTMKPEFdlKATKEadlskELAIQVRKVIGPFAAPKKIYlVSDLPKTRSGKIMRRVLRK 662
Cdd:cd12118 421 VARPDEKWGEVPCAFVELKEGA--KVTEE-----EIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVLRD 486
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
144-661 |
4.21e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 118.85 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKV 223
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LITTDEGRrggktiatkqivDAALQQCPLVENVLVLRRTgnkvpMTEGRDKW--WDEECAKMPAYCPCERMASEDplfIL 301
Cdd:PRK08276 87 LIVSAALA------------DTAAELAAELPAGVPLLLV-----VAGPVPGFrsYEEALAAQPDTPIADETAGAD---ML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 302 YTSGSTGKPKGV------VHSTAGYLLGTALTLkYVFDAHPDDRFACMADI------GWITGhsyiiygPLANGITTAVF 369
Cdd:PRK08276 147 YSSGTTGRPKGIkrplpgLDPDEAPGMMLALLG-FGMYGGPDSVYLSPAPLyhtaplRFGMS-------ALALGGTVVVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 370 ESTpvypTPSRYWDFVDKWKATQLYTAPTA-IRLLRRmgEDHVKN-HDLSSLRVLGSVGEPINPEA----WHWYNDfagk 443
Cdd:PRK08276 219 EKF----DAEEALALIERYRVTHSQLVPTMfVRMLKL--PEEVRArYDVSSLRVAIHAAAPCPVEVkramIDWWGP---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 444 nqcAIVDTYWMTETGSISIAPLPGAIsTKPGSATFPFFGmDVDIIDPQtgqvleGNDV----EGVLVARRPWPSIA---- 515
Cdd:PRK08276 289 ---IIHEYYASSEGGGVTVITSEDWL-AHPGSVGKAVLG-EVRILDED------GNELppgeIGTVYFEMDGYPFEyhnd 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 516 ----RTVYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:PRK08276 358 pektAAARNPH------------GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 592 ADDLTGQAVYAFVTMKPefdlKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK08276 426 PDEEMGERVKAVVQPAD----GADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
131-654 |
4.47e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 118.83 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:PRK07798 17 PDRVALVCGD------RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLIttdEGRRGGKTIAtkqivdAALQQCPLVENVLVLRRTGNKVPMTEGRDkWWDEECAKMPAYCPCE 290
Cdd:PRK07798 91 ELRYLLDDSDAVALV---YEREFAPRVA------EVLPRLPKLRTLVVVEDGSGNDLLPGAVD-YEDALAAGSPERDFGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RmaSEDPLFILYTSGSTGKPKGVV--HSTAGYLLGTALTLKYVFDAHPDDRFACMADIGwiTGHSYIIYGPLANGIT--- 365
Cdd:PRK07798 161 R--SPDDLYLLYTGGTTGMPKGVMwrQEDIFRVLLGGRDFATGEPIEDEEELAKRAAAG--PGMRRFPAPPLMHGAGqwa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 366 ---------TAVFESTPVYpTPSRYWDFVDKWKATQL------YTAPTaIRLLRRMGEdhvknHDLSSLRVLGSVGEPIN 430
Cdd:PRK07798 237 afaalfsgqTVVLLPDVRF-DADEVWRTIEREKVNVItivgdaMARPL-LDALEARGP-----YDLSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 431 P---EAWHwyndfAGKNQCAIVDTYWMTETGSISIA-PLPGAISTkpGSATFPFfGMDVDIIDPQTGQVLEGNDVEGVLv 506
Cdd:PRK07798 310 PsvkEALL-----ELLPNVVLTDSIGSSETGFGGSGtVAKGAVHT--GGPRFTI-GPRTVVLDEDGNPVEPGSGEIGWI- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 507 ARRPwpSIARTVYRDHKRYLETYmKPYPG--YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVA 584
Cdd:PRK07798 381 ARRG--HIPLGYYKDPEKTAETF-PTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 585 ETAVVGCADDLTGQAVYAFVTmkpefdLKATKEADLSkELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGK 654
Cdd:PRK07798 458 DALVVGVPDERWGQEVVAVVQ------LREGARPDLA-ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-663 |
7.77e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.72 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEadePSESReVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:PRK12583 24 FDATVARFPDREALVVR---HQALR-YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDeGRRGGKTIATKQ--IVDAALQQC--------PLVENVLVLrrtgnKVPMTEGR 272
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICAD-AFKTSDYHAMLQelLPGLAEGQPgalacerlPELRGVVSL-----APAPPPGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 273 DKWwdEECAKMPAYCPCERMAS-------EDPLFILYTSGSTGKPKGVV--HSTA---GYLLGTALTLKyvfdahPDDR- 339
Cdd:PRK12583 174 LAW--HELQARGETVSREALAErqasldrDDPINIQYTSGTTGFPKGATlsHHNIlnnGYFVAESLGLT------EHDRl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 340 ---------FAC-MADIGWITGHSYIIYgplangittavfestpvyptPSRYWD------FVDKWKATQLYTAPTAirLL 403
Cdd:PRK12583 246 cvpvplyhcFGMvLANLGCMTVGACLVY--------------------PNEAFDplatlqAVEEERCTALYGVPTM--FI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 404 RRMGEDHVKNHDLSSLRVLGSVGEPINPEAwhwYNDFAGKNQCA-IVDTYWMTETGSISIA-----PLPGAISTKpgSAT 477
Cdd:PRK12583 304 AELDHPQRGNFDLSSLRTGIMAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSPVSLQttaadDLERRVETV--GRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 478 FPFfgMDVDIIDPQTGQVLEGNDVEgvlVARRPWpSIARTVYRDHKRYLETYMKPypGYFFFGDGAARDYDGYMWIKGRV 557
Cdd:PRK12583 379 QPH--LEVKVVDPDGATVPRGEIGE---LCTRGY-SVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 558 DDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefDLKATKEadlskELAIQVRKVIGPFAA 637
Cdd:PRK12583 451 KDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP--GHAASEE-----ELREFCKARIAHFKV 523
|
570 580
....*....|....*....|....*.
9C8S_C 638 PKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK12583 524 PRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
147-660 |
1.02e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.21 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TDE--GRRGGKTIATKQ---IVDAALQQCPLVENVL---VLRRTGN---KVPMTEGRDKWWDEECAKMPAY-CPCErmAS 294
Cdd:PRK06710 128 LDLvfPRVTNVQSATKIehvIVTRIADFLPFPKNLLypfVQKKQSNlvvKVSESETIHLWNSVEKEVNTGVeVPCD--PE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFAcmadIGWITghSYIIYGPLANgITTAVFESTPV 374
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVV----LGVLP--FFHVYGMTAV-MNLSIMQGYKM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 375 YPTPS----RYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcaIVD 450
Cdd:PRK06710 279 VLIPKfdmkMVFEAIKKHKVTLFPGAPTIYIAL--LNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK---LVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 451 TYWMTETGSISIAPLPGAISTkPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARrpwPSIARTVYRDHKrylETYM 530
Cdd:PRK06710 354 GYGLTESSPVTHSNFLWEKRV-PGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKG---PQIMKGYWNKPE---ETAA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 531 KPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPef 610
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE-- 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
9C8S_C 611 DLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK06710 505 GTECSEE-----ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
300-661 |
9.61e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 114.86 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 300 ILYTSGSTGKPKGVVHSTAGyllgTALTLKYVFDAHPddrfacmadigWITGHSYIIYGPL------ANGITTAVFESTP 373
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPG----GIGTLKAILDRTP-----------WRAEEPTVIVAPMfhawgfSQLVLAASLACTI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 374 VYP---TPSRYWDFVDKWKATQLYTAPTairLLRRMGE--DHVKN-HDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcA 447
Cdd:PRK13382 266 VTRrrfDPEATLDLIDRHRATGLAVVPV---MFDRIMDlpAEVRNrYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---V 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 448 IVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGnDVEGVLVARRpwpsiarTVYRDH----- 522
Cdd:PRK13382 340 IYNNYNATEAGMIATAT-PADLRAAPDTAGRPAEGTEIRILDQDFREVPTG-EVGTIFVRND-------TQFDGYtsgst 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 523 KRYLETYMKPypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYA 602
Cdd:PRK13382 411 KDFHDGFMAS-------GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
9C8S_C 603 FVTMKPefDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK13382 484 FVVLKP--GASATPE-----TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
293-654 |
1.56e-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: 111.71 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 293 ASEDPLFILYTSGSTGKPKGVV---HSTAGYLLGTALTLKYVF--DAHPDDRFACMADIGWITGhSYIIYGPLANGITTA 367
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGADFGTGEFtpSEDAHKAAAAAAGTVMFPA-PPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 368 VFESTPVYPTPSRY-----WDFVDKWKATQL------YTAPTaIRLLRRMGedhvkNHDLSSLRVLGSVGEPINPEawHW 436
Cdd:cd05924 80 LLGGQTVVLPDDRFdpeevWRTIEKHKVTSMtivgdaMARPL-IDALRDAG-----PYDLSSLFAISSGGALLSPE--VK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 YNDFAGKNQCAIVDTYWMTETGSISIAPLPGAIstkPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVlVARRPwpSIAR 516
Cdd:cd05924 152 QGLLELVPNITLVDAFGSSETGFTGSGHSAGSG---PETGPFTRANPDTVVLDDDGRVVPPGSGGVGW-IARRG--HIPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 517 TVYRDHKRYLETYmKPYPG--YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADD 594
Cdd:cd05924 226 GYYGDEAKTAETF-PEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 595 LTGQAVYAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGK 654
Cdd:cd05924 305 RWGQEVVAVVQLREGAGVDL-------EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
131-660 |
1.59e-26 |
|
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: 113.17 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd17643 1 PEAVAVVDED------RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEGrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmPAYcpce 290
Cdd:cd17643 75 RIAFILADSGPSLLLTDPDD-----------------------------------------------------LAY---- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rmasedplfILYTSGSTGKPKGVV--HSTAGYLLGTAltlKYVFDAHPDDRfacmadigWITGHSYI-------IYGPLA 361
Cdd:cd17643 98 ---------VIYTSGSTGRPKGVVvsHANVLALFAAT---QRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 362 NGITTAVFESTpVYPTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLR--VLGsvGEPINPEAWH-WYN 438
Cdd:cd17643 158 HGGRLVVVPYE-VARSPEDFARLLRDEGVTVLNQTPSAFYQL--VEAADRDGRDPLALRyvIFG--GEALEAAMLRpWAG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFaGKNQCAIVDTYWMTETG------SISIAPLPGAISTKPGSatfPFFGMDVDIID----PQ----TGQVLegndVEGV 504
Cdd:cd17643 233 RF-GLDRPQLVNMYGITETTvhvtfrPLDAADLPAAAASPIGR---PLPGLRVYVLDadgrPVppgvVGELY----VSGA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 505 LVAR----RPWPSIARTVyrdhkryLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILH 580
Cdd:cd17643 305 GVARgylgRPELTAERFV-------ANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 581 KGVAETAVVGCADDLTGQAVYAFVtmkpefDLKATKEADLSkELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd17643 378 PSVRDAAVIVREDEPGDTRLVAYV------VADDGAAADIA-ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
147-660 |
3.36e-26 |
|
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: 112.30 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TDegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaSEDPLFILYTSGS 306
Cdd:cd05907 84 ED-----------------------------------------------------------------PDDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTPSRywdfvd 386
Cdd:cd05907 99 TGRPKGVMLSHRN-ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLS------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 387 KWKATQLYTAPT-------AIR------LLRRMGEDHVknhdLSSLRVLGSVGEPINPEAWHWYNDfAGknqCAIVDTYW 453
Cdd:cd05907 172 EVRPTVFLAVPRvwekvyaAIKvkavpgLKRKLFDLAV----GGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 454 MTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDpqTGQVLegndVEGVLVARRPW---PSIARTVYRDhkryletym 530
Cdd:cd05907 244 LTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIAD--DGEIL----VRGPNVMLGYYknpEATAEALDAD--------- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 531 kpypGYFFFGDGAARDYDGYMWIKGRVDDVI-NVSGHRLSTAEVESALILHKGVAETAVVGcaDDLtgQAVYAFVTMKPE 609
Cdd:cd05907 307 ----GWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG--DGR--PFLVALIVPDPE 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 610 F--------------DLKATKEADLSKELAIQVRKV---IGPFAAPKKIYLvsdLPK---------TRSGKIMRRVL 660
Cdd:cd05907 379 AleawaeehgiaytdVAELAANPAVRAEIEAAVEAAnarLSRYEQIKKFLL---LPEpftiengelTPTLKLKRPVI 452
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
123-665 |
7.08e-26 |
|
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: 112.16 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIyeadepSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIhsA 202
Cdd:COG1021 31 LRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFS---AEsLRDRVNDCECKVLITTDegRRGGktIATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEgrdkwWDEE 279
Cdd:COG1021 103 VFALPAhrrAE-ISHFAEQSEAVAYIIPD--RHRG--FDYRALARELQAEVPSLRHVLVVGDAGEFTSLDA-----LLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 280 cakmPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLlgtaltlkYVFDA-------HPDDRFACMADIGwitgH 352
Cdd:COG1021 173 ----PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--------YSVRAsaeicglDADTVYLAALPAA----H 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 353 SYI-----IYGPLANGiTTAVFESTPvypTPSRYWDFVDKWKATqlYTA---PTAIRLLRRMGEDHvknHDLSSLRVLGS 424
Cdd:COG1021 237 NFPlsspgVLGVLYAG-GTVVLAPDP---SPDTAFPLIERERVT--VTAlvpPLALLWLDAAERSR---YDLSSLRVLQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 425 VGEPINPEAwhwyndfA-------GknqCAIVDTYWMTEtGSISIAPL---PGAIST---KPGSAtfpffGMDVDIIDPq 491
Cdd:COG1021 308 GGAKLSPEL-------ArrvrpalG---CTLQQVFGMAE-GLVNYTRLddpEEVILTtqgRPISP-----DDEVRIVDE- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 492 tgqvlEGNDV----EGVLVARRPWpsIARTVYRDhkryletymkpyP----------GYFFFGDGAARDYDGYMWIKGRV 557
Cdd:COG1021 371 -----DGNPVppgeVGELLTRGPY--TIRGYYRA------------PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 558 DDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMK-PEFDLKATKEADLSKELAIqvrkvigpFA 636
Cdd:COG1021 432 KDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRgEPLTLAELRRFLRERGLAA--------FK 503
|
570 580
....*....|....*....|....*....
9C8S_C 637 APKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:COG1021 504 LPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
572-654 |
1.19e-25 |
|
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: 100.70 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 572 EVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkatkeaDLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTR 651
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE-------LLEEELVAHVREELGPYAVPKEVVFVDELPKTR 73
|
...
9C8S_C 652 SGK 654
Cdd:pfam13193 74 SGK 76
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
244-673 |
2.21e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 110.54 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 244 DAALQQCPLV----ENVLVLRRTGNKVPMTEGRDKWWDEECAKMPAYCPCERMASEDPLFILY-TSGSTGKPKGVVhSTA 318
Cdd:PRK07867 96 DIAHADCQLVltesAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRVADPDDLFMLIfTSGTSGDPKAVR-CTH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 319 GYLLGTALTLKYVFDAHPDD-------RF---ACMAdiGWITGhsyiiygpLANGITTAV---FESTPVYPTPSR----Y 381
Cdd:PRK07867 175 RKVASAGVMLAQRFGLGPDDvcyvsmpLFhsnAVMA--GWAVA--------LAAGASIALrrkFSASGFLPDVRRygatY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 382 WDFVDKWKATQLYTAPTAirllrrmgeDHVKNhdlsSLRVL-GSVGEPINPEAwhwyndFAGKNQCAIVDTYWMTETGsI 460
Cdd:PRK07867 245 ANYVGKPLSYVLATPERP---------DDADN----PLRIVyGNEGAPGDIAR------FARRFGCVVVDGFGSTEGG-V 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 461 SIAPLPGaisTKPGSATfPFFGmDVDIIDPQTGQ-----------VLEGNDVEGVLVARRPwPSIARTVYRDHKRYLEty 529
Cdd:PRK07867 305 AITRTPD---TPPGALG-PLPP-GVAIVDPDTGTecppaedadgrLLNADEAIGELVNTAG-PGGFEGYYNDPEADAE-- 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 530 mKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPE 609
Cdd:PRK07867 377 -RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPG 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 610 FDLKATKEADLskeLAIQVRkvIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKivagEGDQLGD 673
Cdd:PRK07867 456 AKFDPDAFAEF---LAAQPD--LGPKQWPSYVRVCAELPRTATFKVLKRQLSA----EGVDCAD 510
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
128-661 |
3.31e-25 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 109.97 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 128 YKNPKKTAIiyeadEPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGF 207
Cdd:PRK07514 13 FADRDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 208 SAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVdaalqqcPLVEnVLVLRRTGnkvPMTEGrdkwwdeeCAKMPAYC 287
Cdd:PRK07514 88 TLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGA-------PHVE-TLDADGTG---SLLEA--------AAAAPDDF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 288 PCERMASEDPLFILYTSGSTGKPKGVVhSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANG---I 364
Cdd:PRK07514 149 ETVPRGADDLAAILYTSGTTGRSKGAM-LSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGasmI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 365 TTAVFEStpvyptpsrywDFVDKW--KATQLYTAPT-AIRLL--RRMGEDHVKNhdlssLRVLGSVGEPINPEAwhwYND 439
Cdd:PRK07514 228 FLPKFDP-----------DAVLALmpRATVMMGVPTfYTRLLqePRLTREAAAH-----MRLFISGSAPLLAET---HRE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 440 FAGKNQCAIVDTYWMTETGSISIAPLPGAisTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVeGVLVARRP------W-- 511
Cdd:PRK07514 289 FQERTGHAILERYGMTETNMNTSNPYDGE--RRAGTVGFPLPGVSLRVTDPETGAELPPGEI-GMIEVKGPnvfkgyWrm 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 PSIARTVYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:PRK07514 366 PEKTAEEFRAD------------GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 592 ADDLTGQAVYAFVTMKPEFDLkatKEADLSKELAIQVRKvigpFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK07514 434 PHPDFGEGVTAVVVPKPGAAL---DEAAILAALKGRLAR----FKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
129-660 |
3.38e-25 |
|
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: 109.60 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFS 208
Cdd:cd12117 9 RTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 209 AESLRDRVNDCECKVLITtDEGRRGGktiatkqivdAALQQCPLVenvlvlrrtgnkvpmtegRDKWWDEECAKMPAYCP 288
Cdd:cd12117 83 AERLAFMLADAGAKVLLT-DRSLAGR----------AGGLEVAVV------------------IDEALDAGPAGNPAVPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 289 CermaSEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVfDAHPDDRFACMADIGWiTGHSYIIYGPLANGITTAV 368
Cdd:cd12117 134 S----PDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 369 FESTPVYpTPSRYWDFVDKWKATQLY-TAPtairLLRRMGEDHVKNhdLSSLRVLGSVGEPINPEAWHwyndfAGKNQCA 447
Cdd:cd12117 207 APKGTLL-DPDALGALIAEEGVTVLWlTAA----LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVR-----RVLAACP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 448 ---IVDTYWMTE----TGSISIAPLPGAISTKP-GSatfPFFGMDVDIIDPQtGQVLEgNDVEGVL------VAR----R 509
Cdd:cd12117 275 glrLVNGYGPTEnttfTTSHVVTELDEVAGSIPiGR---PIANTRVYVLDED-GRPVP-PGVPGELyvggdgLALgylnR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 510 PwpsiARTVyrdhKRYLETymkPYPG---YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:cd12117 350 P----ALTA----ERFVAD---PFGPgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREA 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 587 AVVGCADDLTGQAVYAFVTMKPEFDLKATKEAdlskelaiqVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd12117 419 VVVVREDAGGDKRLVAYVVAEGALDAAELRAF---------LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
295-657 |
7.03e-25 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 106.58 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTaVFESTPV 374
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCV-TGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 375 YPTpsrYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKnhDLSSLRVLGSVGE-PINPEAwhwyNDFAGKNQCAIVDTYW 453
Cdd:cd17635 80 YKS---LFKILTTNAVTTTCLVPTLLSKLVSELKSANA--TVPSLRLIGYGGSrAIAADV----RFIEATGLTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 454 MTETGSISIAPLpGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNdvEGVLVARRPWpsIARTVYRDHKRYLETYMKpy 533
Cdd:cd17635 151 LSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSAS--FGTIWIKSPA--NMLGYWNNPERTAEVLID-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 534 pGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLK 613
Cdd:cd17635 224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDEN 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
9C8S_C 614 ATkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMR 657
Cdd:cd17635 303 AI------RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
129-605 |
7.82e-25 |
|
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: 110.72 E-value: 7.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPmtwqaaaaflacaR----IGAIHSAVF 204
Cdd:COG1020 488 RTPDAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLE-------------RslemVVALLAVLK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 205 AG---------FSAESLRDRVNDCECKVLITTDEgrrggktiatkqiVDAALQQCPLveNVLVLrrtgnkvpmtegrDkw 275
Cdd:COG1020 549 AGaayvpldpaYPAERLAYMLEDAGARLVLTQSA-------------LAARLPELGV--PVLAL-------------D-- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 276 wDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMA----DIgwitg 351
Cdd:COG1020 599 -ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDRVLQFAslsfDA----- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 352 hSYI-IYGPLANGITTAVFESTPVyPTPSRYWDFVDKWKATQLYTAPTAIRLLrrmgeDHVKNHDLSSLRVLGSVGEPIN 430
Cdd:COG1020 672 -SVWeIFGALLSGATLVLAPPEAR-RDPAALAELLARHRVTVLNLTPSLLRAL-----LDAAPEALPSLRLVLVGGEALP 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 431 PEAW-HWYNDFAGknqCAIVDTYWMTETgSI--SIAPLPGAISTkPGSATF--PFFGMDVDIIDPQtgqvleGNDV---- 501
Cdd:COG1020 745 PELVrRWRARLPG---ARLVNLYGPTET-TVdsTYYEVTPPDAD-GGSVPIgrPIANTRVYVLDAH------LQPVpvgv 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 502 --E----GVLVAR----RPwpsiARTVyrdhKRYLetymkPYPgyffFGDGAARDY----------DG---YMwikGRVD 558
Cdd:COG1020 814 pgElyigGAGLARgylnRP----ELTA----ERFV-----ADP----FGFPGARLYrtgdlarwlpDGnleFL---GRAD 873
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
9C8S_C 559 DVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVT 605
Cdd:COG1020 874 DQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVV 920
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
123-662 |
1.20e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 109.03 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEADEpsESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLP------------MTwqaaaaf 190
Cdd:COG1022 17 LRRRAARFPDRVALREKEDG--IWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDnrpewviadlaiLA------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 191 lacarIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgrrggktiATKQIVDAALQQCPLVENVLVLRRTGNKVP--- 267
Cdd:COG1022 88 -----AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQ--------EQLDKLLEVRDELPSLRHIVVLDPRGLRDDprl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 268 ------MTEGRDKWWDEECAKMPAycpceRMASEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTLKYVFDAHPDDRFA 341
Cdd:COG1022 155 lsldelLALGREVADPAELEARRA-----AVKPDDLATIIYTSGTTGRPKGVML-THRNLLSNARALLERLPLGPGDRTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 342 C---MAdigWITGHSyIIYGPLANGITTAVFESTP------------VYPTPSRYWdfvDKWKA---TQLYTAPT----- 398
Cdd:COG1022 229 SflpLA---HVFERT-VSYYALAAGATVAFAESPDtlaedlrevkptFMLAVPRVW---EKVYAgiqAKAEEAGGlkrkl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 399 ---AIRLLRRMGEDHVKNHDLSS------------------------LRVLGSVGEPINPEAWHWYNDfAGKNqcaIVDT 451
Cdd:COG1022 302 frwALAVGRRYARARLAGKSPSLllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIP---VLEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 452 YWMTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDpqTGQVLegndVEGVLVARRPW--P-SIARTVYRDhkrylet 528
Cdd:COG1022 378 YGLTETSPVITVNRPGDN--RIGTVGPPLPGVEVKIAE--DGEIL----VRGPNVMKGYYknPeATAEAFDAD------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 529 ymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVS-GHRLSTAEVESALILHKGVAETAVVGcaDD---LTgqavyAFV 604
Cdd:COG1022 443 ------GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG--DGrpfLA-----ALI 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 605 TMKPEF--------DLKATKEADLSKELAIQ--VRKVI-------GPFAAPKKIYLvsdLPK---------TRSGKIMRR 658
Cdd:COG1022 510 VPDFEAlgewaeenGLPYTSYAELAQDPEVRalIQEEVdranaglSRAEQIKRFRL---LPKeftiengelTPTLKLKRK 586
|
....
9C8S_C 659 VLRK 662
Cdd:COG1022 587 VILE 590
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
131-662 |
1.52e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 108.30 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIyeaDEPSESreVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPmTW-QAAAAFLACARIGAIHSAVFAGFSA 209
Cdd:PRK06087 37 PDKIAVV---DNHGAS--YTYSALDHAASRLANWLLAKGIEPGDRVAFQLP-GWcEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 210 ESLRDRVNDCECKVLITTDEGRrggKTIATKQIVdAALQQCPLVENVLVLRRTGNKVPmtegrDKWWDEECAKMP--AYC 287
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAPTLFK---QTRPVDLIL-PLQNQLPQLQQIVGVDKLAPATS-----SLSLSQIIADYEplTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 288 PCerMASEDPLFILYTSGSTGKPKGVV--H-----STAGYLLGTALTlkyvfdahPDDRFACMADIGWITGHSYIIYGPL 360
Cdd:PRK06087 182 IT--THGDELAAVLFTSGTEGLPKGVMltHnnilaSERAYCARLNLT--------WQDVFMMPAPLGHATGFLHGVTAPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 361 ANGITTAVFESTpvypTPSRYWDFVDKWKATQLYTA-PTAIRLLRRMGEDHVknhDLSSLRVLGSVGEPInP-----EAW 434
Cdd:PRK06087 252 LIGARSVLLDIF----TPDACLALLEQQRCTCMLGAtPFIYDLLNLLEKQPA---DLSALRFFLCGGTTI-PkkvarECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 435 HwyndfAGKNQCAIvdtYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGndVEGVLVARRPWPSI 514
Cdd:PRK06087 324 Q-----RGIKLLSV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPG--CEGEEASRGPNVFM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 515 ArtvYRDHK----RYLETymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:PRK06087 394 G---YLDEPeltaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
9C8S_C 591 CADDLTGQAVYAFVTMKPEfdlkaTKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:PRK06087 466 MPDERLGERSCAYVVLKAP-----HHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
131-660 |
2.30e-24 |
|
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: 106.99 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd12116 1 PDATAVRDD------DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEGRrggktiatkqivDAALQQCPLVENVLVLRRTGNKVPMTEgrdkwwdeecakmpaycpce 290
Cdd:cd12116 75 RLRYILEDAEPALVLTDDALP------------DRLPAGLPVLLLALAAAAAAPAAPRTP-------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rMASEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGW-ITGHSyiIYGPLANGITTAVF 369
Cdd:cd12116 123 -VSPDDLAYVIYTSGSTGRPKGVVVSHRN-LVNFLHSMRERLGLGPGDRLLAVTTYAFdISLLE--LLLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 370 ESTPVYpTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDhvknhDLSSLRVL-GsvGEPINPeawhwynDFAGKNQ--- 445
Cdd:cd12116 199 PRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ-----GRAGLTALcG--GEALPP-------DLAARLLsrv 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 446 CAIVDTYWMTETgSI--SIAPLPGAISTKPgsATFPFFGMDVDIIDPQTGQVLEGndVEGVL------VARRPW--PSIA 515
Cdd:cd12116 264 GSLWNLYGPTET-TIwsTAARVTAAAGPIP--IGRPLANTQVYVLDAALRPVPPG--VPGELyiggdgVAQGYLgrPALT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 516 RTVYRDHkryletymkPYPG----YFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:cd12116 339 AERFVPD---------PFAGpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 592 ADDLTGQAVyAFVTMKpefDLKATKEADLSKELAIQVrkvigP-FAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd12116 410 EDGGDRRLV-AYVVLK---AGAAPDAAALRAHLRATL-----PaYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-664 |
2.69e-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: 107.03 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 142 EPSESREVSYEELMQETCRVANVLKSYgVKKGDAVSIYLPMTwqaaaaflacarIG---AIHSAVFAG-------FSA-- 209
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKM-TKEGENVGVMLPPS------------AGgalANFALALSGkvpvmlnYTAgl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 210 ESLRDRVNDCECKVLITTdegRRGGKTIATKQIVDAAlQQCPLV--ENVLvlrrtgNKVpmtegrdKWWDEECAKMPAYC 287
Cdd:cd05909 68 RELRACIKLAGIKTVLTS---KQFIEKLKLHHLFDVE-YDARIVylEDLR------AKI-------SKADKCKAFLAGKF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 288 PCERMA---------SEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYG 358
Cdd:cd05909 131 PPKWLLrifgvapvqPDDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 PLANGIttAVFestpVYPTPSRYW---DFVDKWKATQLYTAPTAIR-LLRRmgedhVKNHDLSSLRVLGSVGEPINPEAw 434
Cdd:cd05909 210 PLLSGI--KVV----FHPNPLDYKkipELIYDKKATILLGTPTFLRgYARA-----AHPEDFSSLRLVVAGAEKLKDTL- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 435 hwYNDFAGKNQCAIVDTYWMTETG---SISIAPLPgaisTKPGSATFPFFGMDVDIIDPQTGQVLEGNdVEGVLVARRpw 511
Cdd:cd05909 278 --RQEFQEKFGIRILEGYGTTECSpviSVNTPQSP----NKEGTVGRPLPGMEVKIVSVETHEEVPIG-EGGLLLVRG-- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 PSIARTVYRDHKRyleTYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGV-AETAVVG 590
Cdd:cd05909 349 PNVMLGYLNEPEL---TSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVS 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 591 CADDLTGQAVYAFVTmkpefdlkaTKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIV 664
Cdd:cd05909 426 VPDGRKGEKIVLLTT---------TTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
131-661 |
2.93e-24 |
|
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: 106.30 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd17649 1 PDAVALVFG------DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITtdegrRGGKTIAtkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpce 290
Cdd:cd17649 75 RLRYMLEDSGAGLLLT-----HHPRQLA---------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rmasedplFILYTSGSTGKPKGVVHStAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIiYGPLANGiTTAVFE 370
Cdd:cd17649 98 --------YVIYTSGSTGTPKGVAVS-HGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICG-ACVVLR 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 371 STPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNhDLSSLRVLGSVGEPINPE-AWHWyndfaGKNQCAIV 449
Cdd:cd17649 167 PDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPElLRRW-----LKAPVRLF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 450 DTYWMTETgsiSIAPL--PGAISTKPGSATFP----FFGMDVDIIDPQTGQVLEGNDVE----GVLVAR----RPwpsiA 515
Cdd:cd17649 241 NAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVGVTGElyigGEGLARgylgRP----E 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 516 RTvyrdHKRYLET-YMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADD 594
Cdd:cd17649 314 LT----AERFVPDpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 595 LTGQAVyAFVTMKpefdlKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd17649 390 GGKQLV-AYVVLR-----AAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-668 |
9.91e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 105.63 E-value: 9.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 121 NCLDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIH 200
Cdd:PRK07786 21 NQLARHALMQPDAPALRFLG------NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 201 SAVFAGFSAESLRDRVNDCECKVLITtdEGRRGGKTIATKQIVdaalqqcPLVENVLVLRRTGNKVPMteGRDKWWDEEC 280
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVSDCGAHVVVT--EAALAPVATAVRDIV-------PLLSTVVVAGGSSDDSVL--GYEDLLAEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 281 akmPAYCPCErMASEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDrfacmaDIGWITGHSYII--YG 358
Cdd:PRK07786 164 ---PAHAPVD-IPNDSPALIMYTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGADINS------DVGFVGVPLFHIagIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 PLANGITTAVfeSTPVYPT----PSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLsSLRVLGSVGEPINPEAW 434
Cdd:PRK07786 233 SMLPGLLLGA--PTVIYPLgafdPGQLLDVLEAEKVTGIFLVPAQWQAV--CAEQQARPRDL-ALRVLSWGAAPASDTLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 435 H-WYNDFAGknqCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPqtgqvlEGNDVegvlvarrPWPS 513
Cdd:PRK07786 308 RqMAATFPE---AQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDE------NMNDV--------PVGE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 514 IARTVYRDHKRYLETYMKPYP-------GYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:PRK07786 371 VGEIVYRAPTLMSGYWNNPEAtaeafagGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEV 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 587 AVVGCADDLTGQAVYAFVTMKPEFDLKATKEAD--LSKELAiqvrkvigPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIV 664
Cdd:PRK07786 451 AVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAefLTDRLA--------RYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
....
9C8S_C 665 AGEG 668
Cdd:PRK07786 523 GACV 526
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
131-662 |
1.01e-23 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 105.78 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEADEPSESREVSYEELMQETCRVANVLKSYGvKKGDAVSIYLPM----------TWQAaaaflacariGAIh 200
Cdd:cd05931 7 PDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPgldfvaaflgCLYA----------GAI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 201 sAV-----FAGFSAESLRDRVNDCECKVLITTDEGRRGgktiatkqiVDAALQQCPLVENVLVLRRTgnkVPMTEGRDKW 275
Cdd:cd05931 75 -AVplpppTPGRHAERLAAILADAGPRVVLTTAAALAA---------VRAFAASRPAAGTPRLLVVD---LLPDTSAADW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 276 wdeecakmpaycPCERMASEDPLFILYTSGSTGKPKGVVhSTAGYLLGTALTLKYVFDAHPDDRFA----CMADIGWITG 351
Cdd:cd05931 142 ------------PPPSPDPDDIAYLQYTSGSTGTPKGVV-VTHRNLLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 352 hsyiIYGPLANGItTAVFEStpvyPT-----PSRYWDFVDKWKATqlYT-APT-AIRL-LRRMGEDHVKNHDLSSLRVLG 423
Cdd:cd05931 209 ----LLTPLYSGG-PSVLMS----PAaflrrPLRWLRLISRYRAT--ISaAPNfAYDLcVRRVRDEDLEGLDLSSWRVAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 424 SVGEPINPEAWHWYND-FA--GKNQCAIVDTYWMTE-TGSISIAPL----------------PGAISTKPGSATFPFF-- 481
Cdd:cd05931 278 NGAEPVRPATLRRFAEaFApfGFRPEAFRPSYGLAEaTLFVSGGPPgtgpvvlrvdrdalagRAVAVAADDPAARELVsc 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 482 -----GMDVDIIDPQTGQVLEGNDVeGVLVARRpwPSIARtvyrdhkryletymkpypGYF--------FFGDGAARD-- 546
Cdd:cd05931 358 grplpDQEVRIVDPETGRELPDGEV-GEIWVRG--PSVAS------------------GYWgrpeataeTFGALAATDeg 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 547 -----------YDGYMWIKGRVDDVINVSGHRLSTAEVESAL-----ILHKGVAetAVVGCADDLTGQ--AVYAFVTMKP 608
Cdd:cd05931 417 gwlrtgdlgflHDGELYITGRLKDLIIVRGRNHYPQDIEATAeeahpALRPGCV--AAFSVPDDGEERlvVVAEVERGAD 494
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 609 EFDLKATKE---ADLSKELAIQVRKVIgpFAAPKKIylvsdlPKTRSGKIMRRVLRK 662
Cdd:cd05931 495 PADLAAIAAairAAVAREHGVAPADVV--LVRPGSI------PRTSSGKIQRRACRA 543
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
147-666 |
1.27e-23 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 105.45 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TdegrrggktiatKQIVD--AALQQCPLVENVLVLRRTGNKVPMTEGRDKwwDEEcakmpaYCPCERMASEDPLFILYTS 304
Cdd:PLN02246 129 Q------------SCYVDklKGLAEDDGVTVVTIDDPPEGCLHFSELTQA--DEN------ELPEVEISPDDVVALPYSS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 305 GSTGKPKGV-------VHSTAGYLLGTALTLKYvfdaHPDDRFACMADIGWITGHSYIIYGPLANGITTAV---FESTPV 374
Cdd:PLN02246 189 GTTGLPKGVmlthkglVTSVAQQVDGENPNLYF----HSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpkFEIGAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 375 YptpsrywDFVDKWKATqlyTAPTAIRLLRRMGE-DHVKNHDLSSLRVLGSVGEPINPEAwhwYNDFAGKNQCAIV-DTY 452
Cdd:PLN02246 265 L-------ELIQRHKVT---IAPFVPPIVLAIAKsPVVEKYDLSSIRMVLSGAAPLGKEL---EDAFRAKLPNAVLgQGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 453 WMTETG---SISIA----PLPgaisTKPGSATFPFFGMDVDIIDPQTG----------------QVLEG--NDVEgvlva 507
Cdd:PLN02246 332 GMTEAGpvlAMCLAfakePFP----VKSGSCGTVVRNAELKIVDPETGaslprnqpgeicirgpQIMKGylNDPE----- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 508 rrpwpSIARTVyrDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETA 587
Cdd:PLN02246 403 -----ATANTI--DKDGWLHT-----------GDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 588 VVGCADDLTGQAVYAFVTMKPEFDLkatKEADLSKELAIQV--RKVIgpfaapKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:PLN02246 465 VVPMKDEVAGEVPVAFVVRSNGSEI---TEDEIKQFVAKQVvfYKRI------HKVFFVDSIPKAPSGKILRKDLRAKLA 535
|
.
9C8S_C 666 G 666
Cdd:PLN02246 536 A 536
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
142-662 |
1.68e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.06 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 142 EPSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCEC 221
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 222 KVLITTDEGRRGGKTIATKqivdaalqqcplvenVLVLRRTGNKVPMTegrdkwWDE------ECAKMPAYcpcERMASE 295
Cdd:PLN02330 129 KLIVTNDTNYGKVKGLGLP---------------VIVLGEEKIEGAVN------WKElleaadRAGDTSDN---EEILQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLkyvFDAHPDdrfacmaDIGWITGHSYI----IYGplANGITTAVFES 371
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSL---FSVGPE-------MIGQVVTLGLIpffhIYG--ITGICCATLRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 372 TPVYPTPSRY--WDFVDKWKATQLYTAPTAIRLLRRMGEDH-VKNHDLS--SLRVLGSVGEPINPEAWHWY-NDFAGknq 445
Cdd:PLN02330 253 KGKVVVMSRFelRTFLNALITQEVSFAPIVPPIILNLVKNPiVEEFDLSklKLQAIMTAAAPLAPELLTAFeAKFPG--- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 446 CAIVDTYWMTETGSISIA---PLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNdVEGVLVARRpwPSIARTVYRDH 522
Cdd:PLN02330 330 VQVQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKN-TPGELCVRS--QCVMQGYYNNK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 523 KRYLETYMKpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYA 602
Cdd:PLN02330 407 EETDRTIDE--DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAA 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 603 FVTMKPEfdlKATKEADLSKELAIQV---RKVigpfaapKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:PLN02330 485 CVVINPK---AKESEEDILNFVAANVahyKKV-------RVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
126-661 |
2.39e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 104.20 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 126 HYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFA 205
Cdd:PRK06145 11 HARRTPDRAALVYR------DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 206 GFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQcplveNVLVLRRTGnkvpmtegrdkwwdEECAKMPA 285
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQA-----DSRRLAQGG--------------LEIPPQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 286 YCPcermasEDPLFILYTSGSTGKPKGVVHS-------TAGYLLGTALTlkyvfdahPDDRFACMADIGWITGHSYIIYG 358
Cdd:PRK06145 146 VAP------TDLVRLMYTSGTTDRPKGVMHSygnlhwkSIDHVIALGLT--------ASERLLVVGPLYHVGAFDLPGIA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 PLANGITTAV---FESTPVYPTPSRYwDFVDKWKA----TQLYTAPTAIRllrrmgedhvknHDLSSLRVLGSVGEPiNP 431
Cdd:PRK06145 212 VLWVGGTLRIhreFDPEAVLAAIERH-RLTCAWMApvmlSRVLTVPDRDR------------FDLDSLAWCIGGGEK-TP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 432 EAWhwYNDFAGKNQCA-IVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDpQTGQVLEGNdVEGVLVARRP 510
Cdd:PRK06145 278 ESR--IRDFTRVFTRArYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPN-MKGEICMRGP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 wpSIARTVYRDHKRYLETYmkpYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:PRK06145 354 --KVTKGYWKDPEKTAEAF---YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 591 CADDLTGQAVYAFVTMKPefdlKATKEADlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK06145 429 VHDDRWGERITAVVVLNP----GATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
108-663 |
2.45e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 104.62 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 108 VQWFPEGTLNAAyncldrHYYKNPKKTAIIyeadepSESREVSYEELMQETCRVANVLKSYGVKKGDAVSI--------Y 179
Cdd:PRK07788 46 RRYGPFAGLVAH------AARRAPDRAALI------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVlarnhrgfV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 180 LPMTwqaaaaflACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgrrggktiatkqIVDAALQQCPLVENVLVL 259
Cdd:PRK07788 114 LALY--------AAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE------------FTDLLSALPPDLGRLRAW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 260 RRTGNKVPMTEGRDKWWDEECAKM---PAYCPcERMASedplFILYTSGSTGKPKGVVHSTAGYLLGTALTLkyvfdahp 336
Cdd:PRK07788 174 GGNPDDDEPSGSTDETLDDLIAGSstaPLPKP-PKPGG----IVILTSGTTGTPKGAPRPEPSPLAPLAGLL-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 337 dDRfacmadIGWITGHSYIIYGPL------ANGITTAVFESTPVYP---TPSRYWDFVDKWKATQLYTAPTairLLRRM- 406
Cdd:PRK07788 241 -SR------VPFRAGETTLLPAPMfhatgwAHLTLAMALGSTVVLRrrfDPEATLEDIAKHKATALVVVPV---MLSRIl 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 407 --GEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMD 484
Cdd:PRK07788 311 dlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGP---VLYNLYGSTEVAFATIAT-PEDLAEAPGTVGRPPKGVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 485 VDIIDPQtGQVLEGNDVeGVLVARRPWPSIARTVYRDHKR---YLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVI 561
Cdd:PRK07788 387 VKILDEN-GNEVPRGVV-GRIFVGNGFPFEGYTDGRDKQIidgLLSS-----------GDVGYFDEDGLLFVDGRDDDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 562 NVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefdlkatkEADLSKElAIQ--VRKVIGPFAAPK 639
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP--------GAALDED-AIKdyVRDNLARYKVPR 524
|
570 580
....*....|....*....|....
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK07788 525 DVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
131-660 |
2.51e-23 |
|
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: 103.89 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd12114 1 PDATAVICGD------GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEgrrggktiatkqivdaALQQCPLVENVLVlrrtgnkvpmtegrdkwWDEECAKMPAYCPCE 290
Cdd:cd12114 75 RREAILADAGARLVLTDGP----------------DAQLDVAVFDVLI-----------------LDLDALAAPAPPPPV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RMASEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMA----DIGwitghSYIIYGPLANGitt 366
Cdd:cd12114 122 DVAPDDLAYVIFTSGSTGTPKGVMISHRA-ALNTILDINRRFAVGPDDRVLALSslsfDLS-----VYDIFGALSAG--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 367 avfeSTPVYPTPSR-----YW-DFVDKWKATQLYTAPTAIRLLRRMGEDhvKNHDLSSLR-VLGSvGEPINPEAWHWYND 439
Cdd:cd12114 193 ----ATLVLPDEARrrdpaHWaELIERHGVTLWNSVPALLEMLLDVLEA--AQALLPSLRlVLLS-GDWIPLDLPARLRA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 440 FAGknQCAIVDTYWMTETG--SI--SIAPLPGAISTKP-GsatFPFFGMDVDIIDPQtgqvleGNDV----------EGV 504
Cdd:cd12114 266 LAP--DARLISLGGATEASiwSIyhPIDEVPPDWRSIPyG---RPLANQRYRVLDPR------GRDCpdwvpgelwiGGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 505 LVARRPWPSIARTVYR-----DHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALIL 579
Cdd:cd12114 335 GVALGYLGDPELTAARfvthpDGERLYRT-----------GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 580 HKGVAETAVVGcADDLTGQAVYAFVTMKPEFDlkatkeADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRV 659
Cdd:cd12114 404 HPGVARAVVVV-LGDPGGKRLAAFVVPDNDGT------PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAA 476
|
.
9C8S_C 660 L 660
Cdd:cd12114 477 L 477
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
123-663 |
3.72e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 103.40 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIyeadepSESREVSYEELMQETCRVANVLK-SYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHS 201
Cdd:PRK06839 8 IEKRAYLHPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 202 AVFAGFSAESLRDRVNDCECKVLITTDEGRRGGKTIATKQIVDAALQQCPLVEnvLVLRRTGNKVPMTEgrdkwwdeeca 281
Cdd:PRK06839 82 PLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKE--IEDRKIDNFVEKNE----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 282 kmpaycpcermasEDPLFILYTSGSTGKPKGVVhSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLA 361
Cdd:PRK06839 149 -------------SASFIICYTSGTTGKPKGAV-LTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 362 NGITTAVfestPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAWHWYNDFA 441
Cdd:PRK06839 215 AGGVIIV----PRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEELMREFIDRG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 442 ---GKNqcaivdtYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNdvEGVLVARRPwpSIARTV 518
Cdd:PRK06839 289 flfGQG-------FGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGE--VGELLIRGP--NVMKEY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 519 YRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQ 598
Cdd:PRK06839 358 WNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 599 AVYAFVTMKPEFDLkatkeadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK06839 435 IPIAFIVKKSSSVL-------IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
150-663 |
5.99e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 103.30 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIttde 229
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 230 grrggktiatkqiVDAALqqCPLVENVLVLRRTGNKVPMTEGRDKW-WDEECAKMP-----AYCPCERMASEDPLFILYT 303
Cdd:PRK06155 124 -------------VEAAL--LAALEAADPGDLPLPAVWLLDAPASVsVPAGWSTAPlppldAPAPAAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 304 SGSTGKPKGVVHSTA-----GYLLGTALTLKyvfdahPDD-RFACMADIGwiTGHSYIIYGPLANGITTAVfesTPVYpT 377
Cdd:PRK06155 189 SGTTGPSKGVCCPHAqfywwGRNSAEDLEIG------ADDvLYTTLPLFH--TNALNAFFQALLAGATYVL---EPRF-S 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 378 PSRYWDFVDKWKATQLYT--APTAIrLLRRMGEDHVKNHdlsSLRVLGSVGEPInpeawHWYNDFAGKNQCAIVDTYWMT 455
Cdd:PRK06155 257 ASGFWPAVRRHGATVTYLlgAMVSI-LLSQPARESDRAH---RVRVALGPGVPA-----ALHAAFRERFGVDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 456 ETGSISIAPLPgaiSTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARRPWpSIARTVYRDHKRYLETYMKPYpg 535
Cdd:PRK06155 328 ETNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPF-AFATGYFGMPEKTVEAWRNLW-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 536 yFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKP----EF- 610
Cdd:PRK06155 402 -FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgtalEPv 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
9C8S_C 611 DLKATKEADLSKelaiqvrkvigpFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK06155 481 ALVRHCEPRLAY------------FAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
300-661 |
6.27e-23 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 102.46 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 300 ILYTSGSTGKPKGVVHSTAGYLLGTALtlkyvfdahpddRFACMADIGWITGHSYIIYGPL-------------ANGITT 366
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDT------------LMAAALGFGPGADSVYLSPAPLyhaapfrwsmtalFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 367 AVFESTpvypTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEPINP---EAW-HW------ 436
Cdd:cd05929 198 VLMEKF----DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWiDWggpiiw 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 --YNDFAGKNQCAIVDTYWMTETGSISiaplpgaistKPGSATFPFFGMDVDIIDP-QTGQV-LEGNDveGVLVARRP-W 511
Cdd:cd05929 274 eyYGGTEGQGLTIINGEEWLTHPGSVG----------RAVLGKVHILDEDGNEVPPgEIGEVyFANGP--GFEYTNDPeK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 PSIArtvYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:cd05929 342 TAAA---RNEG------------GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGV 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 592 ADDLTGQAVYAFV-TMKPEFDLKAtkeadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05929 407 PDEELGQRVHAVVqPAPGADAGTA-----LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
129-660 |
1.17e-22 |
|
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: 101.63 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIyeadepSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFS 208
Cdd:cd12115 11 RTPDAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 209 AESLRDRVNDCECKVLITTdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycp 288
Cdd:cd12115 85 PERLRFILEDAQARLVLTD------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 289 cermaSEDPLFILYTSGSTGKPKGVV--HSTAGYLLGTALTlkyVFDAhpDDRFACMA------DIGwitghSYIIYGPL 360
Cdd:cd12115 104 -----PDDLAYVIYTSGSTGRPKGVAieHRNAAAFLQWAAA---AFSA--EELAGVLAstsicfDLS-----VFELFGPL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 361 ANGITTAVFESTPVYPtpsrywDFVDKWKATQLYTAPTAIRLLRRMGedhvknhDL-SSLRVLGSVGEPINPEAwhwYND 439
Cdd:cd12115 169 ATGGKVVLADNVLALP------DLPAAAEVTLINTVPSAAAELLRHD-------ALpASVRVVNLAGEPLPRDL---VQR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 440 FAGKNQCA-IVDTYWMTETGSIS-IAPLPGAISTKPgSATFPFFGMDVDIID------PQ--TGQVLEGndveGVLVAR- 508
Cdd:cd12115 233 LYARLQVErVVNLYGPSEDTTYStVAPVPPGASGEV-SIGRPLANTQAYVLDralqpvPLgvPGELYIG----GAGVARg 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 509 ---RPWPSIARTV---YRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKG 582
Cdd:cd12115 308 ylgRPGLTAERFLpdpFGPGARLYRT-----------GDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 583 VAETAVVGCADDLTGQAVYAFVTMKPEfdlkatkEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd12115 377 VREAVVVAIGDAAGERRLVAYIVAEPG-------AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
295-661 |
1.25e-22 |
|
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: 100.04 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVV---HSTA--GYLLGTALTLKyvfdahPDDRFACMADIgwitghsYIIYGPLANGITTAVF 369
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATlthHNIVnnGYFIGERLGLT------EQDRLCIPVPL-------FHCFGSVLGVLACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 370 ESTPVYPTPSrywdF--------VDKWKATQLYTAPTA-IRLLrrmGEDHVKNHDLSSLR--VLGsvGEPINPEAWH-WY 437
Cdd:cd05917 69 GATMVFPSPS----FdplavleaIEKEKCTALHGVPTMfIAEL---EHPDFDKFDLSSLRtgIMA--GAPCPPELMKrVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 438 NDFagkNQCAIVDTYWMTETGSISIAPLPGA-ISTKPGSATFPFFGMDVDIIDPQTGQVLEGNdVEGVLVARRPwpSIAR 516
Cdd:cd05917 140 EVM---NMKDVTIAYGMTETSPVSTQTRTDDsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVG-VPGELCIRGY--SVMK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 517 TVYRDHKRYLETYMKPypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLT 596
Cdd:cd05917 214 GYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 597 GQAVYAFVTMKPEfdlKATKEADLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:cd05917 292 GEEVCAWIRLKEG---AELTEEDIKAYC----KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
295-661 |
1.58e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 101.22 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVVHS-----------------TAGYLLGTALTLkyvFDAHpddrfacmadiGWITGhsyiIY 357
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSrraiaadldalaeawqwTADDVLVHGLPL---FHVH-----------GLVLG----VL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GPLANGITtavFESTpVYPTPSRYWDFVDKwKATQLYTAPTairLLRRMGEDHVKNHDLSSLRVL--GSVGEPInpeawH 435
Cdd:PRK07787 190 GPLRIGNR---FVHT-GRPTPEAYAQALSE-GGTLYFGVPT---VWSRIAADPEAARALRGARLLvsGSAALPV-----P 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 436 WYNDFAGKNQCAIVDTYWMTETgSISIAPLPGAiSTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARRPW---- 511
Cdd:PRK07787 257 VFDRLAALTGHRPVERYGMTET-LITLSTRADG-ERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQVRGPTlfdg 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 ----PSIARTVYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVD-DVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:PRK07787 335 ylnrPDATAAAFTAD------------GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREA 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 587 AVVGCADDLTGQAVYAFVTMKPEFDlkatkeadlSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK07787 403 AVVGVPDDDLGQRIVAYVVGADDVA---------ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
296-657 |
2.21e-22 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 98.63 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGYLlgtaltlkyvfdahpdDRFACMADIGWITGHSYI-IYGPLA-----NGITTAVF 369
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI----------------ESFVCNEDLFNISGEDAIlAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 370 ESTPVY----PTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHvknhdlSSLRVLGSVGEPINPEAWHwyNDFAGKNQ 445
Cdd:cd17633 65 LGGTFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE------SKIKSIFSSGQKLFESTKK--KLKNIFPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 446 CAIVDTYWMTETGSISiAPLPGAiSTKPGSATFPFFGMDVDIIDpqtgqvlEGNDVEGVLVARRPwpsIARTVYRDHKRY 525
Cdd:cd17633 137 ANLIEFYGTSELSFIT-YNFNQE-SRPPNSVGRPFPNVEIEIRN-------ADGGEIGKIFVKSE---MVFSGYVRGGFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 526 LETymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVT 605
Cdd:cd17633 205 NPD------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
9C8S_C 606 MKpefdlKATKeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMR 657
Cdd:cd17633 279 GD-----KLTY-----KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
276-661 |
7.78e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 99.72 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 276 WDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYL-LGTALTLKYvfDAHPDDRFAC----------MA 344
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYVsmplfhsnavMA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 345 diGWitghsyiiyGP-LANGITTAVfestPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdHVKNHDlSSLRVlg 423
Cdd:PRK13388 209 --GW---------APaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPE-RPDDAD-NPLRV-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 424 SVGEPINPEAwhwYNDFAGKNQCAIVDTYWMTEtGSISIAPLPGaisTKPGSATFPFFGmdVDIIDPQT----------- 492
Cdd:PRK13388 270 AFGNEASPRD---IAEFSRRFGCQVEDGYGSSE-GAVIVVREPG---TPPGSIGRGAPG--VAIYNPETltecavarfda 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 493 -GQVLEGNDVEGVLVARRPwPSIARTVYRDHKRYLEtymKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTA 571
Cdd:PRK13388 341 hGALLNADEAIGELVNTAG-AGFFEGYYNNPEATAE---RMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 572 EVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkatKEADLSKELAIQvrKVIGPFAAPKKIYLVSDLPKTR 651
Cdd:PRK13388 417 PIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF---DPDAFAAFLAAQ--PDLGTKAWPRYVRIAADLPSTA 491
|
410
....*....|
9C8S_C 652 SGKIMRRVLR 661
Cdd:PRK13388 492 TNKVLKRELI 501
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
126-661 |
1.12e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 98.93 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 126 HYYKNPKKTAIIyeADEPSEsrEVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFA 205
Cdd:PRK13390 6 HAQIAPDRPAVI--VAETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 206 GFSAESLRDRVNDCECKVLITTdegrrggktiatkqivdAALQQcplvenvlVLRRTGNKVPMT---EGR-DKWWDEECA 281
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVAS-----------------AALDG--------LAAKVGADLPLRlsfGGEiDGFGSFEAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 282 KMPAYCPCermaSEDPL--FILYTSGSTGKPKGVVHSTAGYLLgtaltlkyvfDAHPDDRFAcmadigwITGHSYiiygp 359
Cdd:PRK13390 137 LAGAGPRL----TEQPCgaVMLYSSGTTGFPKGIQPDLPGRDV----------DAPGDPIVA-------IARAFY----- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 360 lanGITTA--VFESTPVYPTPSRYW-----------------------DFVDKWKATQLYTAPTAIRLLRRMGEDHVKNH 414
Cdd:PRK13390 191 ---DISESdiYYSSAPIYHAAPLRWcsmvhalggtvvlakrfdaqatlGHVERYRITVTQMVPTMFVRLLKLDADVRTRY 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 415 DLSSLRVLGSVGEPINPEAWHWYNDFAGKnqcAIVDTYWMTETGSISIAPLPGAIStKPGSATFPFFGmDVDIIDpQTGQ 494
Cdd:PRK13390 268 DVSSLRAVIHAAAPCPVDVKHAMIDWLGP---IVYEYYSSTEAHGMTFIDSPDWLA-HPGSVGRSVLG-DLHICD-DDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 495 VLEGNDVEGVLVARRPWPsiartvYRDHKRYLETYMKPYPGYFFF---GDGAARDYDGYMWIKGRVDDVINVSGHRLSTA 571
Cdd:PRK13390 342 ELPAGRIGTVYFERDRLP------FRYLNDPEKTAAAQHPAHPFWttvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 572 EVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkatKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTR 651
Cdd:PRK13390 416 ETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIR----GSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTP 491
|
570
....*....|
9C8S_C 652 SGKIMRRVLR 661
Cdd:PRK13390 492 TGKLVKGLLR 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
294-665 |
1.76e-21 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 98.38 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 294 SEDPLFILYTSGSTGKPKGVV--HSTagyLLGTALTLKYVFDAHPDDRF---------ACMADigwitghsyiIYGPLAN 362
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSESRVlqfasytfdVSILE----------IFTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 363 GITTAVfestpvyptPSRY------WDFVDKWKATQLYTAPTAIRLLRRmgedhvknHDLSSLRVLGSVGEPINPEAW-H 435
Cdd:cd05918 172 GGCLCI---------PSEEdrlndlAGFINRLRVTWAFLTPSVARLLDP--------EDVPSLRTLVLGGEALTQSDVdT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 436 WyndfagKNQCAIVDTYWMTETGSISIAPLPGAiSTKPGSATFPfFGMDVDIIDPQT----------GQVLegndVEGVL 505
Cdd:cd05918 235 W------ADRVRLINAYGPAECTIAATVSPVVP-STDPRNIGRP-LGATCWVVDPDNhdrlvpigavGELL----IEGPI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 506 VAR----RPwpsiART--VYRDHKRYLETYMKPYPGYFFF-GDGAARDYDG---YMwikGRVDDVINVSGHRLSTAEVES 575
Cdd:cd05918 303 LARgylnDP----EKTaaAFIEDPAWLKQEGSGRGRRLYRtGDLVRYNPDGsleYV---GRKDTQVKIRGQRVELGEIEH 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 576 ALILHKGVAETAVVGC---ADDLTGQAVYAFVTMKPEFDLKA---TKEADLSKELAIQVRKVIG-------PFAAPKKIY 642
Cdd:cd05918 376 HLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdgdSLFLEPSDEFRALVAELRSklrqrlpSYMVPSVFL 455
|
410 420
....*....|....*....|...
9C8S_C 643 LVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:cd05918 456 PLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
295-669 |
3.59e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 97.80 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVV--HSTAGYLLGTALTlkyvfDAHPDdrfacmadigwITGHS-YIIYGPL----------- 360
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVltHGQMAFVITNHLA-----DLMPG-----------TTEQDaSLVVAPLshgagihqlcq 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 361 -ANGITTAVFESTPVypTPSRYWDFVDKWKATQLYTAPTAIRLlrrMGED-HVKNHDLSSLRVLGSVGEPINPEAWHWYN 438
Cdd:PRK07470 227 vARGAATVLLPSERF--DPAEVWALVERHRVTNLFTVPTILKM---LVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRAL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFAGKnqcAIVDTYWMTE-TGSISIapLPGAI-------STKPGSATFPFFGMDVDIIDPQtGQVLEGNDVeGVLVARRP 510
Cdd:PRK07470 302 AKLGK---VLVQYFGLGEvTGNITV--LPPALhdaedgpDARIGTCGFERTGMEVQIQDDE-GRELPPGET-GEICVIGP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 wpsiarTVYRDHKRYLETYMKPY-PGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVV 589
Cdd:PRK07470 375 ------AVFAGYYNNPEANAKAFrDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 590 GCADDLTGQAVYAFVTMKPEFDLkatKEADLSKELAIQVRKvigpFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEGD 669
Cdd:PRK07470 449 GVPDPVWGEVGVAVCVARDGAPV---DEAELLAWLDGKVAR----YKLPKRFFFWDALPKSGYGKITKKMVREELEERGL 521
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
131-660 |
4.08e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 97.37 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIyeadepSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:PRK13383 49 PGRTAII------DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEgrrggktiATKQIVDAAlqqcplvENVLVLRrtgnkvPMTEGRdkwwdEECAKMPAYCPCE 290
Cdd:PRK13383 123 ALAAALRAHHISTVVADNE--------FAERIAGAD-------DAVAVID------PATAGA-----EESGGRPAVAAPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RMasedplfILYTSGSTGKPKGVVHS-TAGYLLGTALTLKyvfdahpdDRFACMadigwiTGHSYIIYGPLANGITTAVF 369
Cdd:PRK13383 177 RI-------VLLTSGTTGKPKGVPRApQLRSAVGVWVTIL--------DRTRLR------TGSRISVAMPMFHGLGLGML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 370 ESTPVYP---TPSRYWDFVDKWKATQLYTAP--TAIR-LLRRMGE--DHVKNHD-LSSLRVLGSVGEPINPEAWHWYNDF 440
Cdd:PRK13383 236 MLTIALGgtvLTHRHFDAEAALAQASLHRADafTAVPvVLARILElpPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 441 AGKnqcAIVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMDVDIID-------PQ-TGQVLEGNDVEGvlvarrpwp 512
Cdd:PRK13383 316 YGD---ILYNGYGSTEVGIGALAT-PADLRDAPETVGKPVAGCPVRILDrnnrpvgPRvTGRIFVGGELAG--------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 513 siartvyrdhKRYLETYMKPY-PGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC 591
Cdd:PRK13383 383 ----------TRYTDGGGKAVvDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C8S_C 592 ADDLTGQAVYAFVTMKPEFDLKATKEADLSKELaiqvrkvIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK13383 453 PDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR-------VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
123-679 |
7.95e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 96.55 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:PRK08162 24 LERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDEgrrggktiaTKQIVDAALQQCPlvenvlvlrrtGNKVPMTEGRDkwwdeecak 282
Cdd:PRK08162 98 LNTRLDAASIAFMLRHGEAKVLIVDTE---------FAEVAREALALLP-----------GPKPLVIDVDD--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 283 mPAYCPCER---------MASEDPLF-------------ILYTSGSTGKPKGVV-HSTAGYLLGTALTLKYVFDAHPD-- 337
Cdd:PRK08162 149 -PEYPGGRFigaldyeafLASGDPDFawtlpadewdaiaLNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGMPKHPVyl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 338 ---DRFACMadiGWitGHSYIIYGPLANGITTAVFEstpvyptPSRYWDFVDKWKATQLYTAPTAIRLL------RRMGE 408
Cdd:PRK08162 228 wtlPMFHCN---GW--CFPWTVAARAGTNVCLRKVD-------PKLIFDLIREHGVTHYCGAPIVLSALinapaeWRAGI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 409 DHvknhdlsslRVLGSVGEPINPEAWhwyndFAGKNQCAIVDT--YWMTET-GSISI-------APLPGA----ISTKPG 474
Cdd:PRK08162 296 DH---------PVHAMVAGAAPPAAV-----IAKMEEIGFDLThvYGLTETyGPATVcawqpewDALPLDeraqLKARQG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 475 SATFPFFGMDVdiIDPQTGQvlegndvegvlvarrPWPSIART----VYRDHkryleTYMKPY------------PGYFF 538
Cdd:PRK08162 362 VRYPLQEGVTV--LDPDTMQ---------------PVPADGETigeiMFRGN-----IVMKGYlknpkateeafaGGWFH 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 539 FGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPefDLKATKEa 618
Cdd:PRK08162 420 TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD--GASATEE- 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 619 dlskELAIQVRKVIGPFAAPKKIYLvSDLPKTRSGKIMRRVLRkivagegDQLGDLSSIAD 679
Cdd:PRK08162 497 ----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLR-------EQAKSLKAIDL 545
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
104-668 |
6.85e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.80 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 104 EHGDVQWFPEGTLNAAYNCLDRHYYKNPKKTAIIYEADEPSesreVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMT 183
Cdd:PRK05852 3 FMGGAAPMASDFGPRIADLVEVAATRLPEAPALVVTADRIA----ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 184 WQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEGrrggktiaTKQIVDAALQQCPLVENVLVLRRTG 263
Cdd:PRK05852 79 AEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADG--------PHDRAEPTTRWWPLTVNVGGDSGPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 264 NKVPMTEgrdkwWDEECAKMPAYCPCERMASEDPLfILYTSGSTGKPKGV----------VHS-TAGYLLGtaltlkyvf 332
Cdd:PRK05852 151 GGTLSVH-----LDAATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVpwthaniassVRAiITGYRLS--------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 333 dahpdDRFACMADIGWITGHsyiiyGPLANGITTAVFESTPVYPTPSRY-----WDFVDKWKATQLYTAPTAIRLLRRMG 407
Cdd:PRK05852 216 -----PRDATVAVMPLYHGH-----GLIAALLATLASGGAVLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 408 EDHVKNHDLSSLRVLGSVGEPINPE-AWHWYNDFAGKNQCAivdtYWMTE-TGSISIAPLPGAISTK-PGSATFPFF--- 481
Cdd:PRK05852 286 ATEPSGRKPAALRFIRSCSAPLTAEtAQALQTEFAAPVVCA----FGMTEaTHQVTTTQIEGIGQTEnPVVSTGLVGrst 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 482 GMDVDIIDPQtGQVLEGNDVEGVLVARrpwPSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVI 561
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRG---TTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 562 NVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTmkPEFDLKATKEadlskELAIQVRKVIGPFAAPKKI 641
Cdd:PRK05852 435 NRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE-----ELVQFCRERLAAFEIPASF 507
|
570 580
....*....|....*....|....*..
9C8S_C 642 YLVSDLPKTRSGKIMRRVLRKIVAGEG 668
Cdd:PRK05852 508 QEASGLPHTAKGSLDRRAVAEQFGHSV 534
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
125-664 |
9.14e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 92.92 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 125 RHYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGvKKGDAVSIYLPmtwqaaaAFLACARIGAihSAVF 204
Cdd:PRK07638 9 KHASLQPNKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLE-------NRIEFLQLFA--GAAM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 205 AGFSAESLRDRVNDCECKVLITtdegrrggktiatkqIVDAALqqcplvenVLVLRRTGNKVPMTEGR----DKWWDEEC 280
Cdd:PRK07638 73 AGWTCVPLDIKWKQDELKERLA---------------ISNADM--------IVTERYKLNDLPDEEGRvieiDEWKRMIE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 281 AKMPAYCPCERmASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTlKYVFDAHPDDRFAcmadigwITG---HSYIIY 357
Cdd:PRK07638 130 KYLPTYAPIEN-VQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCN-VHDFHMKREDSVL-------IAGtlvHSLFLY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GplanGITTAVFESTpVYP----TPSRYWDFVDKWKATQLYTAPTAIRLLRRmgEDHVKNHdlsSLRVLGSVGE------ 427
Cdd:PRK07638 201 G----AISTLYVGQT-VHLmrkfIPNQVLDKLETENISVMYTVPTMLESLYK--ENRVIEN---KMKIISSGAKweaeak 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 428 ----PINPEAWHWynDFAGKNQCAIVdTYWMTETGSisiaplpgaisTKPGSATFPFFGMDVDIIDPqTGQVLEGNDvEG 503
Cdd:PRK07638 271 ekikNIFPYAKLY--EFYGASELSFV-TALVDEESE-----------RRPNSVGRPFHNVQVRICNE-AGEEVQKGE-IG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 504 VLVARRPWPSIArtvYRDHKRYLETymKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGV 583
Cdd:PRK07638 335 TVYVKSPQFFMG---YIIGGVLARE--LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAV 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 584 AETAVVGCADDLTGQAVYAFVtmkpefDLKATKeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK07638 410 DEIVVIGVPDSYWGEKPVAII------KGSATK-----QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
.
9C8S_C 664 V 664
Cdd:PRK07638 479 I 479
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
123-661 |
1.59e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 92.50 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIyeaDEPsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:PRK06164 16 LDAHARARPDAVALI---DED---RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDegrrGGKTIATKQIVDAALQQC-PLVENVLVLRRTGNKVPmTEGRDKWWDEECA 281
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPDAlPPLRAIAVVDDAADATP-APAPGARVQLFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 282 KMPAYCP--CERMASEDPLFILY-TSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIyG 358
Cdd:PRK06164 165 PDPAPPAaaGERAADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL-G 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 359 PLANGITTAVFestPVYPTPsRYWDFVDKWKATQLYTAPTAI-RLLRRMGEDhvknHDLSSLRVLGsvgepinpeawhwY 437
Cdd:PRK06164 243 ALAGGAPLVCE---PVFDAA-RTARALRRHRVTHTFGNDEMLrRILDTAGER----ADFPSARLFG-------------F 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 438 NDFAGK--NQCAIVDTYWMTETG-----------SISIAPLPGAISTKPGSA-TFPffGMDVDIIDPQTGQVLEgNDVEG 503
Cdd:PRK06164 302 ASFAPAlgELAALARARGVPLTGlygssevqalvALQPATDPVSVRIEGGGRpASP--EARVRARDPQDGALLP-DGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 504 VLVARRPW--------PSIARTVYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVES 575
Cdd:PRK06164 379 EIEIRAPSlmrgyldnPDATARALTDD------------GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 576 ALILHKGVAETAVVGCadDLTGQAV-YAFVTmkpefdLKATKEADlSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSG- 653
Cdd:PRK06164 447 ALEALPGVAAAQVVGA--TRDGKTVpVAFVI------PTDGASPD-EAGLMAACREALAGFKVPARVQVVEAFPVTESAn 517
|
570
....*....|
9C8S_C 654 --KIMRRVLR 661
Cdd:PRK06164 518 gaKIQKHRLR 527
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
131-660 |
1.85e-19 |
|
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: 91.95 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITT-DEGRRGGKTIATKQIVDAALqqcplvenvlvlrrtgnkvpmtegrdkwwdeecAKMPAYCPC 289
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------------AAPPATPPL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 290 ERMASEDPLFILYTSGSTGKPKGVV---HSTAGYLLGtaltLKYVFDAHPDDRFACMADIGWITGhSYIIYGPLANGitt 366
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMvthAGIVNRLLW----MQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAG--- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 367 avfeSTPVYPTPSRYWD------FVDKWKATQLYTAPTAIRLLRRMGEDHvknhDLSSLRVLGSVGEPINPEAwhwYNDF 440
Cdd:cd17646 205 ----ARLVVARPGGHRDpaylaaLIREHGVTTCHFVPSMLRVFLAEPAAG----SCASLRRVFCSGEALPPEL---AARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 441 AGKNQCAIVDTYWMTETgSISIA--PLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVE----GVLVAR----RP 510
Cdd:cd17646 274 LALPGAELHNLYGPTEA-AIDVThwPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGElylgGVQLARgylgRP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 WPSIARTV---YRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETA 587
Cdd:cd17646 353 ALTAERFVpdpFGPGSRMYRT-----------GDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 588 VVGCADDLTGQAVYAFVTmkpefdLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd17646 422 VVARAAPAGAARLVGYVV------PAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
415-661 |
3.29e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.65 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 415 DLSSLRVLGSVGEPIN---PEAWHwynDFAGKNqcaIVDTYWMTETgSISIAPLPGAISTKPGSATFPFFGMDVDIIDPq 491
Cdd:PRK08974 323 DFSSLKLSVGGGMAVQqavAERWV---KLTGQY---LLEGYGLTEC-SPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDD- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 492 tgqvlEGNDVE----GVLVARRP------W--PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDD 559
Cdd:PRK08974 395 -----DGNEVPpgepGELWVKGPqvmlgyWqrPEATDEVIKD-------------GWLATGDIAVMDEEGFLRIVDRKKD 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 560 VINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKpefDLKATKEadlskELAIQVRKVIGPFAAPK 639
Cdd:PRK08974 457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK---DPSLTEE-----ELITHCRRHLTGYKVPK 528
|
250 260
....*....|....*....|..
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK08974 529 LVEFRDELPKSNVGKILRRELR 550
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
148-590 |
3.97e-19 |
|
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: 90.99 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 148 EVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITt 227
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 228 degrrgGKT---IATKQIVDAALQQCPLVenvlvlrrtgnkvPMTEGRDKW-WDEECAKMPAYCPCERMASEDPLFILYT 303
Cdd:cd05932 85 ------GKLddwKAMAPGVPEGLISISLP-------------PPSAANCQYqWDDLIAQHPPLEERPTRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 304 SGSTGKPKGVVHSTAGYLLgTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPT------ 377
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAW-AAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEdvqrar 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 378 PS------RYW--------DFVDKWKATQLYTAPTAIRLLRR-----MGEDHVknhdlsslRVLGSVGEPINPEAWHWYN 438
Cdd:cd05932 225 PTlffsvpRLWtkfqqgvqDKIPQQKLNLLLKIPVVNSLVKRkvlkgLGLDQC--------RLAGCGSAPVPPALLEWYR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFaGKNqcaIVDTYWMTETGSISIAPLPGaiSTKPGSATFPFFGMDVDIIDpqTGQVLEGNdvegvlvarrpwPSIARTV 518
Cdd:cd05932 297 SL-GLN---ILEAYGMTENFAYSHLNYPG--RDKIGTVGNAGPGVEVRISE--DGEILVRS------------PALMMGY 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 519 YRDHKRYLETYMKpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVS-GHRLSTAEVESALILHKGVAETAVVG 590
Cdd:cd05932 357 YKDPEATAEAFTA--DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
129-660 |
7.77e-19 |
|
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: 90.08 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFS 208
Cdd:cd17655 9 KTPDHTAVVFE------DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 209 AESLRDRVNDCECKVLITT---DEGRRGGKTIAtkQIVDAALQQCPlVENvlvLRRTGNkvpmtegrdkwwdeecakmpa 285
Cdd:cd17655 83 EERIQYILEDSGADILLTQshlQPPIAFIGLID--LLDEDTIYHEE-SEN---LEPVSK--------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 286 ycpcermaSEDPLFILYTSGSTGKPKGVVHSTAGYL-LGTALTLKYVFDAHpdDRFACMADIGWiTGHSYIIYGPLANGI 364
Cdd:cd17655 136 --------SDDLAYVIYTSGSTGKPKGVMIEHRGVVnLVEWANKVIYQGEH--LRVALFASISF-DASVTEIFASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 365 TTAVFESTPVYPTPSrYWDFVDKWKATQLYTAPTAIRLLrrmgeDHVKNHDLSSLRVLGSVGEPINPE-AWHWYNDFagK 443
Cdd:cd17655 205 TLYIVRKETVLDGQA-LTQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALSTElAKKIIELF--G 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 444 NQCAIVDTYWMTETgsisiaplpgaistkpgsatfpffgmdvdIIDPQTGQVLEGNDvegvlvaRRPWPSIARTVYRDHK 523
Cdd:cd17655 277 TNPTITNAYGPTET-----------------------------TVDASIYQYEPETD-------QQVSVPIGKPLGNTRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 524 RYLETYMKPYP----GYFFF-GDGAARDY---------------------------------DGYMWIKGRVDDVINVSG 565
Cdd:cd17655 321 YILDQYGRPQPvgvaGELYIgGEGVARGYlnrpeltaekfvddpfvpgermyrtgdlarwlpDGNIEFLGRIDHQVKIRG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 566 HRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEaDLSKELaiqvrkvigP-FAAPKKIYLV 644
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLRE-FLAREL---------PdYMIPSYFIKL 470
|
570
....*....|....*.
9C8S_C 645 SDLPKTRSGKIMRRVL 660
Cdd:cd17655 471 DEIPLTPNGKVDRKAL 486
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
300-657 |
7.88e-19 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 88.33 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 300 ILYTSGSTGKPKGVVhSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITT---AVFESTPVYP 376
Cdd:cd17638 5 IMFTSGTTGRSKGVM-CAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVvpvAVFDVDAILE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 377 TpsrywdfVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLR--VLGSVGEPIN-PEAWHWYNDFAgknqcAIVDTYW 453
Cdd:cd17638 84 A-------IERERITVLPGPPTLFQSL--LDHPGRKKFDLSSLRaaVTGAATVPVElVRRMRSELGFE-----TVLTAYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 454 MTETGSISIAPlPG----AISTKPGSAtfpFFGMDVDIIDPqtGQVLegndVEGvlvarrpwPSIARTVYRDHKRYLETY 529
Cdd:cd17638 150 LTEAGVATMCR-PGddaeTVATTCGRA---CPGFEVRIADD--GEVL----VRG--------YNVMQGYLDDPEATAEAI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 530 mkPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPE 609
Cdd:cd17638 212 --DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
9C8S_C 610 FDLkaTKEAdlskeLAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMR 657
Cdd:cd17638 290 VTL--TEED-----VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
144-662 |
1.02e-18 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 89.29 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKV 223
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LITTDegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermASEDPLFILYT 303
Cdd:cd17653 98 LLTTD----------------------------------------------------------------SPDDLAYIIFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 304 SGSTGKPKGVV--HS-TAGYLLGTALTLkyvfDAHPDDRFACMADIGW--ITGhsyIIYGPLANGittavfeSTPVYPTP 378
Cdd:cd17653 114 SGSTGIPKGVMvpHRgVLNYVSQPPARL----DVGPGSRVAQVLSIAFdaCIG---EIFSTLCNG-------GTLVLADP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 379 SRYWDFVDKwKATQLYTAPTAIRLLRRmgedhvknHDLSSLRVLGSVGEPINP---EAWhwyndfaGKNQCaIVDTYWMT 455
Cdd:cd17653 180 SDPFAHVAR-TVDALMSTPSILSTLSP--------QDFPNLKTIFLGGEAVPPsllDRW-------SPGRR-LYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 456 ETgSISIAPLpgaiSTKPGSAT---FPFFGMDVDIIDPQTGQVLEGNDVE----GVLVARRPWPSIARTVYrdhkRYLET 528
Cdd:cd17653 243 EC-TISSTMT----ELLPGQPVtigKPIPNSTCYILDADLQPVPEGVVGEicisGVQVARGYLGNPALTAS----KFVPD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 529 ymKPYPGYFFF--GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVgcadDLTGQAVYAFVTm 606
Cdd:cd17653 314 --PFWPGSRMYrtGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAA----IVVNGRLVAFVT- 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 607 kPEfdlkATKEADLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd17653 387 -PE----TVDVDGLRSEL----AKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
295-663 |
1.08e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 90.27 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVVhSTAGYLLGTALTLkyvfdahpddrFACMADIGwITGHS---------------YIIYGP 359
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAM-LTHGNLVANMLQV-----------RACLSQLG-PDGQPlmkegqevmiaplplYHIYAF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 360 LANGITTAVFESTPVYPT-PSRYWDFVD---KWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGEP-INPEAW 434
Cdd:PRK12492 274 TANCMCMMVSGNHNVLITnPRDIPGFIKelgKWRFSALLGLNTLFVAL--MDHPGFKDLDFSALKLTNSGGTAlVKATAE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 435 HWyndfAGKNQCAIVDTYWMTETGSISIAPLPGAIStKPGSATFPFFGMDVDIIDPQTGQVLEGND----VEGVLVARRP 510
Cdd:PRK12492 352 RW----EQLTGCTIVEGYGLTETSPVASTNPYGELA-RLGTVGIPVPGTALKVIDDDGNELPLGERgelcIKGPQVMKGY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 WPSIARTVyrdhkRYLETymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVG 590
Cdd:PRK12492 427 WQQPEATA-----EALDA-----EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIG 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 591 CADDLTGQAVYAFVTmkpefdlkaTKEADLS-KELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK12492 497 VPDERSGEAVKLFVV---------ARDPGLSvEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
148-662 |
1.14e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 89.80 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 148 EVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITT 227
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 228 DEgrrggktiatkqIVDAALQQCPLVENVlvlrrTGNKVPMTEgRDKWWDEECAKMPAYCPCERMASEDPLFILYTSGST 307
Cdd:cd05915 104 PN------------LLPLVEAIRGELKTV-----QHFVVMDEK-APEGYLAYEEALGEEADPVRVPERAACGMAYTTGTT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 308 GKPKGVVHSTAG-YLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFEstpvYPTPSRYWDFVD 386
Cdd:cd05915 166 GLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP----RLDPASLVELFD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 387 KWKATQLYTAPTAIRLLRRmGEDHVKNHDLSSLRVLGSVGEPinPEAW---HWYNDFAGKNQCAIVDTY-------WMTE 456
Cdd:cd05915 242 GEGVTFTAGVPTVWLALAD-YLESTGHRLKTLRRLVVGGSAA--PRSLiarFERMGVEVRQGYGLTETSpvvvqnfVKSH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 457 TGSIsiaPLPGAISTKPGSAtFPFFGMDVDIIDPQTGQVLEGNDVEGVLVARRPwpSIARTVYRDHKRYLETYMKPypGY 536
Cdd:cd05915 319 LESL---SEEEKLTLKAKTG-LPIPLVRLRVADEEGRPVPKDGKALGEVQLKGP--WITGGYYGNEEATRSALTPD--GF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 537 FFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMkpefdlkatK 616
Cdd:cd05915 391 FRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP---------R 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
9C8S_C 617 EADLSKELAIQV--RKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05915 462 GEKPTPEELNEHllKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
148-663 |
1.86e-18 |
|
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: 89.12 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 148 EVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITT 227
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 228 degRRGGKTIATKQivdaalQQCPLVENVLVLRRT---GNKVPM----TEGRDKWWDEECAKMPAYCPCERMAsedplFI 300
Cdd:cd17642 124 ---KKGLQKVLNVQ------KKLKIIKTIIILDSKedyKGYQCLytfiTQNLPPGFNEYDFKPPSFDRDEQVA-----LI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 301 LYTSGSTGKPKGV--VHSTAGYLLGTALTLKYVFDAHPDDR----------FACMADIGWITGHSYIIYGPlangittaV 368
Cdd:cd17642 190 MNSSGSTGLPKGVqlTHKNIVARFSHARDPIFGNQIIPDTAiltvipfhhgFGMFTTLGYLICGFRVVLMY--------K 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 369 FESTPVYPTpsrywdfVDKWKATQLYTAPTAIRLLRRmgEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNDFAGKNqcAI 448
Cdd:cd17642 262 FEEELFLRS-------LQDYKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLP--GI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 449 VDTYWMTETGS-ISIAPlpgAISTKPGSA--TFPFFgmDVDIIDPQTGQVLEGNDvEGVLVARRPwpSIARTVYRDHKRY 525
Cdd:cd17642 331 RQGYGLTETTSaILITP---EGDDKPGAVgkVVPFF--YAKVVDLDTGKTLGPNE-RGELCVKGP--MIMKGYVNNPEAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 526 LETYMKPypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVT 605
Cdd:cd17642 403 KALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
9C8S_C 606 MKPEfdlKATKEADLSKELAIQVrkvigpfAAPKK----IYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:cd17642 481 LEAG---KTMTEKEVMDYVASQV-------STAKRlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
296-657 |
2.77e-18 |
|
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: 86.55 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWITGHsyiiygplanGITTAVFE---ST 372
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGL----------NLALATFHaggAN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 373 PVYP--TPSRYWDFVDKWKATQLYT-APTAIRLLRRMGEDHVknhDLSSLRVLGSVGEPINPEAWHwyndfaGKNQCAIV 449
Cdd:cd17637 70 VVMEkfDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRFE------ETTGATFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 450 DTYWMTET-GSISIAPlpgaISTKPGSATFPFFGMDVDIIDPQTGQVLEGND----VEGVLVARRPW--PSIARTVYRDh 522
Cdd:cd17637 141 SLYGQTETsGLVTLSP----YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETgeivVRGPLVFQGYWnlPELTAYTFRN- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 523 kryletymkpypGYFFFGDGAARDYDGYMWIKGRV--DDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAV 600
Cdd:cd17637 216 ------------GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
9C8S_C 601 YAFVTMKPEFDLKAtkeadlsKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMR 657
Cdd:cd17637 284 KAVCVLKPGATLTA-------DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
105-663 |
7.58e-18 |
|
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: 87.34 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 105 HGDVQWFPEGTLNAAYNCLDRHyyknpkktaIIYEADEPSESReVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTW 184
Cdd:cd05906 6 EGAPRTLLELLLRAAERGPTKG---------ITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 185 QAaaaflacarIGAIHSAVFAGFSAeslrdrvndCECKVLITTDEGRRggktiATKQIVDAaLQqcpLVENVLVLRRTGN 264
Cdd:cd05906 76 DF---------IPAFWACVLAGFVP---------APLTVPPTYDEPNA-----RLRKLRHI-WQ---LLGSPVVLTDAEL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 265 KVPMtEGRDKWWDEE------------CAKMPAYCPCErmaSEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKyVF 332
Cdd:cd05906 129 VAEF-AGLETLSGLPgirvlsieelldTAADHDLPQSR---PDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 333 DAHPDDRFacmadIGWItghsyiiygPLANgITTAVFEST-PVY--------PT------PSRYWDFVDKWKATQLYtAP 397
Cdd:cd05906 204 GLTPQDVF-----LNWV---------PLDH-VGGLVELHLrAVYlgcqqvhvPTeeiladPLRWLDLIDRYRVTITW-AP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 398 T-AIRLLRR-MGEDHVKNHDLSSLRVLGSVGEPINPEAwhwYNDFA------GKNQCAIVDTYWMTETGSISIAPLPGAI 469
Cdd:cd05906 268 NfAFALLNDlLEEIEDGTWDLSSLRYLVNAGEAVVAKT---IRRLLrllepyGLPPDAIRPAFGMTETCSGVIYSRSFPT 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 470 STKPGSATF-----PFFGMDVDIIDPQTGQVLEGndVEGVLVARRPwpSIARTVYRDHKRYLETYMKPypGYFFFGDGAA 544
Cdd:cd05906 345 YDHSQALEFvslgrPIPGVSMRIVDDEGQLLPEG--EVGRLQVRGP--VVTKGYYNNPEANAEAFTED--GWFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 545 RDyDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCA----DDLTGQAVYAFVtmkPEFDLkATKEADL 620
Cdd:cd05906 419 LD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAvrdpGAETEELAIFFV---PEYDL-QDALSET 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
9C8S_C 621 SKELAIQVRKVIGpfAAPKkiYLV----SDLPKTRSGKIMRRVLRKI 663
Cdd:cd05906 494 LRAIRSVVSREVG--VSPA--YLIplpkEEIPKTSLGKIQRSKLKAA 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
144-665 |
7.69e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKV 223
Cdd:PRK12467 533 FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 224 LITTDEGRRggktiatkqivdaalqQCPLVENVLVLrrtgnkvPMTEGRDKWwdeecAKMPAYCPCERMASEDPLFILYT 303
Cdd:PRK12467 613 LLTQSHLLA----------------QLPVPAGLRSL-------CLDEPADLL-----CGYSGHNPEVALDPDNLAYVIYT 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 304 SGSTGKPKGVV--HST-AGYLLGTALTLKYVfdahPDDRFACMADIGWITGHsYIIYGPLANGiTTAVFESTPVYPTPSR 380
Cdd:PRK12467 665 SGSTGQPKGVAisHGAlANYVCVIAERLQLA----ADDSMLMVSTFAFDLGV-TELFGALASG-ATLHLLPPDCARDAEA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 381 YWDFVDKWKATQLYTAPTAIRLLRRMGedhvKNHDLSSLRVLGSVGEPINPEA---WhwyndFAGKNQCAIVDTYWMTET 457
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQAS----RVALPRPQRALVCGGEALQVDLlarV-----RALGPGARLINHYGPTET 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 458 GSisiaplpgaistkpGSATFPFFGMDVDIIDPQTGQVLEGndvegvlvarrpwpsiaRTVYRdhkryLETYMKPYPG-- 535
Cdd:PRK12467 810 TV--------------GVSTYELSDEERDFGNVPIGQPLAN-----------------LGLYI-----LDHYLNPVPVgv 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 536 ---YFFFGDGAARDY----------------------------------DGYMWIKGRVDDVINVSGHRLSTAEVESALI 578
Cdd:PRK12467 854 vgeLYIGGAGLARGYhrrpaltaerfvpdpfgadggrlyrtgdlaryraDGVIEYLGRMDHQVKIRGFRIELGEIEARLL 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 579 LHKGVAETAVVGCADDLTGQAVyAFVTmkPEFDLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRR 658
Cdd:PRK12467 934 AQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
....*..
9C8S_C 659 VLRKIVA 665
Cdd:PRK12467 1011 ALPKPDA 1017
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
415-661 |
7.98e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 87.38 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 415 DLSSLRV-LG---SVGEPInpeAWHWYNdfagKNQCAIVDTYWMTETGSISIAPlPGAISTKPGSATFPFFGMDVDIIDP 490
Cdd:PRK07059 325 DFSKLIVaNGggmAVQRPV---AERWLE----MTGCPITEGYGLSETSPVATCN-PVDATEFSGTIGLPLPSTEVSIRDD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 491 qtgqvlEGNDVE----GVLVARRP------WpsiartvyrdhKRYLETYMKPYP-GYFFFGDGAARDYDGYMWIKGRVDD 559
Cdd:PRK07059 397 ------DGNDLPlgepGEICIRGPqvmagyW-----------NRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 560 VINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKpefDLKATkEADLSKELAIQVRKvigpFAAPK 639
Cdd:PRK07059 460 MILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK---DPALT-EEDVKAFCKERLTN----YKRPK 531
|
250 260
....*....|....*....|..
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK07059 532 FVEFRTELPKTNVGKILRRELR 553
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
303-667 |
9.62e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.48 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 303 TSGSTGKPKGVV----------HSTAGYLLGTALTLKyvfdAHPDDRFACMAdigwITGHSYII-YGPLANGITTAvFEs 371
Cdd:PRK07824 43 TSGTTGTPKGAMltaaaltasaDATHDRLGGPGQWLL----ALPAHHIAGLQ----VLVRSVIAgSEPVELDVSAG-FD- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 372 tpvyptPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVknhdLSSLRVLGSV---GEPINPEAWhwynDFAGKNQCAI 448
Cdd:PRK07824 113 ------PTALPRAVAELGGGRRYTSLVPMQLAKALDDPAA----TAALAELDAVlvgGGPAPAPVL----DAAAAAGINV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 449 VDTYWMTETGSISI---APLPGAistkpgsatfpffgmDVDIIDpqtGQVLEGNdvegvlvarrpwPSIARTvYR---DH 522
Cdd:PRK07824 179 VRTYGMSETSGGCVydgVPLDGV---------------RVRVED---GRIALGG------------PTLAKG-YRnpvDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 523 KRYLEtymkpyPGYFFFGDGAARDyDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYA 602
Cdd:PRK07824 228 DPFAE------PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 603 FVtmkpefdLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGE 667
Cdd:PRK07824 301 AV-------VGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
150-662 |
9.87e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.11 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 150 SYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTde 229
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 230 grrggktIATKQIVDAALQQCPLVENVLVLRRTG----NKVPMTEGRDKWWDEECAKMPAYCPCERMASEdplfILYTSG 305
Cdd:PRK06018 119 -------LTFVPILEKIADKLPSVERYVVLTDAAhmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAG----MCYTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 306 STGKPKGVVHSTAGYLLGTALTLkyvfdaHPDDRFACMADIgwitghsYIIYGPL--ANGITTAVfeSTP------VYPT 377
Cdd:PRK06018 188 TTGDPKGVLYSHRSNVLHALMAN------NGDALGTSAADT-------MLPVVPLfhANSWGIAF--SAPsmgtklVMPG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 378 P----SRYWDFVDKWKATQLYTAPTA-IRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNdfagknqCAIVDTY 452
Cdd:PRK06018 253 AkldgASVYELLDTEKVTFTAGVPTVwLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMG-------VEVRHAW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 453 WMTETGSI-SIAPLPGAISTKPGSAT--------FPFFGMDVDIIDPqtgqvlEGNDVE------GVLVARRPwpSIART 517
Cdd:PRK06018 326 GMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGVEMKITDD------AGKELPwdgktfGRLKVRGP--AVAAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 518 VYRDHKRYLETymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTG 597
Cdd:PRK06018 398 YYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWD 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 598 QAVYAFVTMKPefDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:PRK06018 473 ERPLLIVQLKP--GETATRE-----EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-666 |
1.19e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 130 NPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSA 209
Cdd:PRK12316 4564 TPDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPR 4637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 210 ESLRDRVNDCECKVLITTDEgrrggktiatkqivdaALQQCPLVENV--LVLRRTGNkvpmtegrdkwWDEecakMPAYC 287
Cdd:PRK12316 4638 ERLAYMMEDSGAALLLTQSH----------------LLQRLPIPDGLasLALDRDED-----------WEG----FPAHD 4686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 288 PCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYvFDAHPDDR---FACMADIGWITGhsyiIYGPLANGi 364
Cdd:PRK12316 4687 PAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER-YELTPDDRvlqFMSFSFDGSHEG----LYHPLING- 4760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 365 tTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLrrmGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYndFAGKN 444
Cdd:PRK12316 4761 -ASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQL---AEHAERDGEPPSLRVYCFGGEAVAQASYDLA--WRALK 4834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 445 QCAIVDTYWMTETgSISIAPLPGAISTKPGSATFP----FFGMDVDIIDPQTGQVLEGNDVE----GVLVARRPWPSIAR 516
Cdd:PRK12316 4835 PVYLFNGYGPTET-TVTVLLWKARDGDACGAAYMPigtpLGNRSGYVLDGQLNPLPVGVAGElylgGEGVARGYLERPAL 4913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 517 TVYRdhkryletyMKPYPgyffFGDGAARDY----------DGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:PRK12316 4914 TAER---------FVPDP----FGAPGGRLYrtgdlaryraDGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 587 AVVGCADDLTGQAVYAFVTMKPEFDLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAG 666
Cdd:PRK12316 4981 VVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAS 5060
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
131-666 |
1.30e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYeadepSESReVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:PLN03102 28 PNRTSIIY-----GKTR-FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLIttdegrrggktiatkqiVDAALQqcPLVENVLVLRRTGNKVP------------MTEGRDKWWDE 278
Cdd:PLN03102 102 SIAAILRHAKPKILF-----------------VDRSFE--PLAREVLHLLSSEDSNLnlpvifiheidfPKRPSSEELDY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 279 EC---AKMPAYCPCERM----ASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLkyvfdahpddrfacmadIGWITG 351
Cdd:PLN03102 163 ECliqRGEPTPSLVARMfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI-----------------IGWEMG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 352 --HSYIIYGPL--ANGIT----TAVFESTPV---YPTPSRYWDFVDKWKATQLYTAPTAIRLLRRmGEDHVKNHDLSSLR 420
Cdd:PLN03102 226 tcPVYLWTLPMfhCNGWTftwgTAARGGTSVcmrHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 421 VLGSVGEPinPEAwhwyndFAGKNQ---CAIVDTYWMTE-TGSISIA---------PLPGAISTKPGSATFPFFGMDVDI 487
Cdd:PLN03102 305 VLTGGSPP--PAA------LVKKVQrlgFQVMHAYGLTEaTGPVLFCewqdewnrlPENQQMELKARQGVSILGLADVDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 488 IDPQTGQ-VLEGNDVEGVLVARRPwpSIARTVYRDHKRYLETYMKpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGH 566
Cdd:PLN03102 377 KNKETQEsVPRDGKTMGEIVIKGS--SIMKGYLKNPKATSEAFKH---GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 567 RLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMK-------PEFDLKATKEADLSKelaiQVRKVIGPFAAPK 639
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgettkeDRVDKLVTRERDLIE----YCRENLPHFMCPR 527
|
570 580
....*....|....*....|....*..
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVLRKIVAG 666
Cdd:PLN03102 528 KVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
415-673 |
2.03e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 85.97 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 415 DLSSLRVLGSVGEPINPEAWHWYNDFAGknqCAIVDTYWMTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQ 494
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTETSPVVSVNPSQAI--QVGTIGIPVPSTLCKVIDDDGNE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 495 VLEGND----VEGVLVARRPWP---SIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHR 567
Cdd:PRK05677 399 LPLGEVgelcVKGPQVMKGYWQrpeATDEILDSD-------------GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFN 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 568 LSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkaTKEadlskELAIQVRKVIGPFAAPKKIYLVSDL 647
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETL--TKE-----QVMEHMRANLTGYKVPKAVEFRDEL 538
|
250 260
....*....|....*....|....*.
9C8S_C 648 PKTRSGKIMRRVLRKivaGEGDQLGD 673
Cdd:PRK05677 539 PTTNVGKILRRELRD---EELKKAGL 561
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
535-661 |
3.90e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.28 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 535 GYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDlkA 614
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVD--K 507
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
9C8S_C 615 TKEADLSKELAIQVRKVIGPFAAPKKIyLVSDLPKTRSGKIMRRVLR 661
Cdd:PLN02479 508 SDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
284-660 |
4.25e-17 |
|
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: 84.44 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 284 PAYcPCERMA--------------SEDPLFILYTSGSTGKPKGVVHSTAGYL-LGTALTLKYVFDAHPDdRFACMADIGW 348
Cdd:cd17650 69 PDY-PAERLQymledsgakllltqPEDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPV-RLLQMASFSF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 349 itghsYIIYGPLANGIT---TAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVL--G 423
Cdd:cd17650 147 -----DVFAGDFARSLLnggTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPV--MAYVYRNGLDLSAMRLLivG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 424 SVGEPINPEAWHwYNDFAGKNQcaIVDTYWMTETgSISIAPLPGAISTKPGSATFP----FFGMDVDIIDPQTGQVLEGn 499
Cdd:cd17650 220 SDGCKAQDFKTL-AARFGQGMR--IINSYGVTEA-TIDSTYYEEGRDPLGDSANVPigrpLPNTAMYVLDERLQPQPVG- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 500 dVEGVL------VAR----RPWPSiartvyrdHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLS 569
Cdd:cd17650 295 -VAGELyiggagVARgylnRPELT--------AERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 570 TAEVESALILHKGVAEtAVVGCADDLTGQA-VYAFVTMKPEFDLKATKEAdLSKELAiqvrkvigPFAAPKKIYLVSDLP 648
Cdd:cd17650 366 LGEIESQLARHPAIDE-AVVAVREDKGGEArLCAYVVAAATLNTAELRAF-LAKELP--------SYMIPSYYVQLDALP 435
|
410
....*....|..
9C8S_C 649 KTRSGKIMRRVL 660
Cdd:cd17650 436 LTPNGKVDRRAL 447
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
299-661 |
4.45e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.47 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPddrfacmADIGWITGHSYIIYG-------PLANGiTTAVFES 371
Cdd:PRK06060 149 YATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTP-------EDTGLCSARMYFAYGlgnsvwfPLATG-GSAVINS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 372 TPVYPTPSRYwdFVDKWKATQLYTAPTAI-RLLRRMGEDHVKnhdlsSLRVLGSVGEPINPEAWHWYNDFAGKnqCAIVD 450
Cdd:PRK06060 221 APVTPEAAAI--LSARFGPSVLYGVPNFFaRVIDSCSPDSFR-----SLRCVVSAGEALELGLAERLMEFFGG--IPILD 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 451 TYWMTETGSISIAPL-----PGAIstkpGSATFPFfgmDVDIIDPQTGQVleGNDVEGVLVARRPwpSIARTVYRDHKRY 525
Cdd:PRK06060 292 GIGSTEVGQTFVSNRvdewrLGTL----GRVLPPY---EIRVVAPDGTTA--GPGVEGDLWVRGP--AIAKGYWNRPDSP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 526 LETymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVT 605
Cdd:PRK06060 361 VAN-----EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 606 MKPEFDLKATKEADLSKELAIQvrkvIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK06060 436 ATSGATIDGSVMRDLHRGLLNR----LSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
123-660 |
5.81e-17 |
|
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: 84.30 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIyeadepSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIhsA 202
Cdd:cd05920 21 LARSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFS--AESLRDRVNDCECKVLITTDEGRRggktiatkqiVD-AALQQcplvenvlvlrrtgnkvpmtegrdkwwdEE 279
Cdd:cd05920 93 VLALPShrRSELSAFCAHAEAVAYIVPDRHAG----------FDhRALAR----------------------------EL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 280 CAKMPaycpcermaseDPLFILYTSGSTGKPKGVVHSTAGYLlgtaltlkYVFDA-------HPDDRFACMADIGwitgH 352
Cdd:cd05920 135 AESIP-----------EVALFLLSGGTTGTPKLIPRTHNDYA--------YNVRAsaevcglDQDTVYLAVLPAA----H 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 353 SYI-----IYGPLANGiTTAVFESTPvypTPSRYWDFVDKWKATQLYTAPTAIRLLrrMGEDHVKNHDLSSLRVLGSVGE 427
Cdd:cd05920 192 NFPlacpgVLGTLLAG-GRVVLAPDP---SPDAAFPLIEREGVTVTALVPALVSLW--LDAAASRRADLSSLRLLQVGGA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 428 PINPEAWHWYNDFAGknqCAIVDTYWMTEtGSISIAPL---PGAISTKPGSATFPffGMDVDIIDPQTGQVLEGNdvEGV 504
Cdd:cd05920 266 RLSPALARRVPPVLG---CTLQQVFGMAE-GLLNYTRLddpDEVIIHTQGRPMSP--DDEIRVVDEEGNPVPPGE--EGE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 505 LVARRPWpsIARTVYR--DHKRYLETYmkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKG 582
Cdd:cd05920 338 LLTRGPY--TIRGYYRapEHNARAFTP----DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 583 VAETAVVGCADDLTGQAVYAFVTMKPEfdlkATKEADLSKELAiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd05920 412 VHDAAVVAMPDELLGERSCAFVVLRDP----PPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
147-670 |
6.29e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TDEGRrggktiatkqivdaalqqCPLVENVLVLrrtgnkvpMTEGRDKWWDEECakmpaycPCERMASEDPLFILYTSGS 306
Cdd:PRK12316 3161 QSHLR------------------LPLAQGVQVL--------DLDRGDENYAEAN-------PAIRTMPENLAYVIYTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGYLLGTALTLKyVFDAHPDDRFACMADIGWiTGHSYIIYGPLANGiTTAVFESTPVYPTPSRYWDFVD 386
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQQ-AYGLGVGDRVLQFTTFSF-DVFVEELFWPLMSG-ARVVLAGPEDWRDPALLVELIN 3284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 387 KWKATQLYTAPTAIRllrrMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYNdfagkNQCAIVDTYWMTETgsiSIAPLP 466
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQ----AFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF-----AGLPLYNLYGPTEA---TITVTH 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 467 GAISTKPGSATF---PFFGMDVDIIDPQTGQVLEGNDVE----GVLVARRPWPSIARTVyrdhKRYLETYMKPYPGYFFF 539
Cdd:PRK12316 3353 WQCVEEGKDAVPigrPIANRACYILDGSLEPVPVGALGElylgGEGLARGYHNRPGLTA----ERFVPDPFVPGERLYRT 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 540 GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVgcadDLTGQAVYAFVTMKPEfdlkatkEAD 619
Cdd:PRK12316 3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDE-------AGD 3497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
9C8S_C 620 LSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEGDQ 670
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
147-662 |
1.12e-16 |
|
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: 83.24 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 tdegrrggktiatkQIVDAALQQCPLVENVLVLRrtgnkvpmtEGRDKwwdeecakmpaycpcermasedpLFILYTSGS 306
Cdd:cd05939 82 --------------NLLDPLLTQSSTEPPSQDDV---------NFRDK-----------------------LFYIYTSGT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGYLLGTALTlKYVFDAHPDDRF-ACMAdigwitghsyiIYGPLAN--GITTAV-FESTPVYP---TPS 379
Cdd:cd05939 116 TGLPKAAVIVHSRYYRIAAGA-YYAFGMRPEDVVyDCLP-----------LYHSAGGimGVGQALlHGSTVVIRkkfSAS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 380 RYWDFVDKWKATQL-YTAPTAIRLLRRMGEDHVKNHdlsslRVLGSVGEPINPEAWhwyNDFAGK-NQCAIVDTYWMTEt 457
Cdd:cd05939 184 NFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLAVGNGLRPQIW---EQFVRRfGIPQIGEFYGATE- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 458 GSISIAPLP---GAISTKP--GSATFPffgmdVDII--DPQTGQVLEGNDveGVLVARRPWPS---IARTVYRDHKRYLE 527
Cdd:cd05939 255 GNSSLVNIDnhvGACGFNSriLPSVYP-----IRLIkvDEDTGELIRDSD--GLCIPCQPGEPgllVGKIIQNDPLRRFD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 528 TYM-------KPYPGYFFFGDGA-------ARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGC-A 592
Cdd:cd05939 328 GYVnegatnkKIARDVFKKGDSAflsgdvlVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVeV 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 593 DDLTGQAVYAFVTMKpefdlkaTKEADLSKeLAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05939 408 PGVEGRAGMAAIVDP-------ERKVDLDR-FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
284-665 |
2.09e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.97 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 284 PAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKyvFDAH------PDDRFACMADIGWITGHSYIIY 357
Cdd:PLN02574 187 FDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVR--FEASqyeypgSDNVYLAALPMFHIYGLSLFVV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GPLANGITTAVFESTPVyptpSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNhdlsSLRVLGSVGEPINPEAWHWY 437
Cdd:PLN02574 265 GLLSLGSTIVVMRRFDA----SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGE----VLKSLKQVSCGAAPLSGKFI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 438 NDFAGK-NQCAIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLE-GNDVEGVLVArrpwPSIA 515
Cdd:PLN02574 337 QDFVQTlPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPpGNCGELWIQG----PGVM 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 516 RTVYRDHKRYLETYMKPypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDL 595
Cdd:PLN02574 413 KGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKE 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 596 TGQAVYAFVTMKPefdlkatkEADLSKELAIQ-VRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:PLN02574 491 CGEIPVAFVVRRQ--------GSTLSQEAVINyVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
145-657 |
2.15e-16 |
|
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: 82.49 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 145 ESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVL 224
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 225 ITTDEgrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermasEDPLFILYTS 304
Cdd:cd05914 84 FVSDE-----------------------------------------------------------------DDVALINYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 305 GSTGKPKGVVhSTAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTP----------- 373
Cdd:cd05914 99 GTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPsakiialafaq 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 374 VYPT--PSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSL-------------RVLGSVGEPINPEAwhwYN 438
Cdd:cd05914 178 VTPTlgVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKK--INNRKIRKLafkkvheafggniKEFVIGGAKINPDV---EE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFAGKNQCAIVdTYWMTETGSISIAPLPGaiSTKPGSATFPFFGMDVDIIDP----QTGQVLegndVEGvlvarrpwPSI 514
Cdd:cd05914 253 FLRTIGFPYTI-GYGMTETAPIISYSPPN--RIRLGSAGKVIDGVEVRIDSPdpatGEGEII----VRG--------PNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 515 ARTVYRDHKRYLETYMKPypGYFFFGDGAARDYDGYMWIKGRVDDVI-NVSGHRLSTAEVESALILHKGVAETAVVGCAD 593
Cdd:cd05914 318 MKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 594 DLTgqavyAFVTMKPEF-DLKATKEADLSKELAIQVR-KVIGPFAAPKKIYLV----SDLPKTRSGKIMR 657
Cdd:cd05914 396 KLV-----ALAYIDPDFlDVKALKQRNIIDAIKWEVRdKVNQKVPNYKKISKVkivkEEFEKTPKGKIKR 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
104-663 |
2.37e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.06 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 104 EHGDVQWFpegtlnaaynclDRHYYKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMT 183
Cdd:PRK12467 3094 ERLVHQLI------------EAQVARTPEAPALVFG------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERS 3155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 184 WQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDEgrrggktiatkqivdaALQQCPLVENVLVLrrtg 263
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH----------------LLEQLPAPAGDTAL---- 3215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 264 nkvpmTEGRDKWWDEecakmPAYCPCERMASEDPLFILYTSGSTGKPKG--VVHSTAGYLLgTALTLKYVFDAHpdDR-- 339
Cdd:PRK12467 3216 -----TLDRLDLNGY-----SENNPSTRVMGENLAYVIYTSGSTGKPKGvgVRHGALANHL-CWIAEAYELDAN--DRvl 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 340 -FACMAdigwITGHSYIIYGPLANGiTTAVFESTPVYpTPSRYWDFVDKWKATQLYTAPTAirlLRRMGEDHvKNHDLSS 418
Cdd:PRK12467 3283 lFMSFS----FDGAQERFLWTLICG-GCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAY---LQQFAEDA-GGADCAS 3352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 419 LRVLGSVGEPINPEAWH----------WYNDFaGKNQCAIVDTYWMTETGSIsiaplPGAISTKPGSatfPFFGMDVDII 488
Cdd:PRK12467 3353 LDIYVFGGEAVPPAAFEqvkrklkprgLTNGY-GPTEAVVTVTLWKCGGDAV-----CEAPYAPIGR---PVAGRSIYVL 3423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 489 DPQTGQVLEGNDVE----GVLVAR----RPWPSIARTVyrdhkryletyMKPYPG----YFFFGDGAARDYDGYMWIKGR 556
Cdd:PRK12467 3424 DGQLNPVPVGVAGElyigGVGLARgyhqRPSLTAERFV-----------ADPFSGsggrLYRTGDLARYRADGVIEYLGR 3492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 557 VDDVINVSGHRLSTAEVESALILHKGVAEtAVVGCADDLTGQAVYAFVTMKPEfdlkatkEADLSKELAIQVRKVIGPFA 636
Cdd:PRK12467 3493 IDHQVKIRGFRIELGEIEARLLQHPSVRE-AVVLARDGAGGKQLVAYVVPADP-------QGDWRETLRDHLAASLPDYM 3564
|
570 580
....*....|....*....|....*..
9C8S_C 637 APKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK12467 3565 VPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
284-660 |
6.11e-16 |
|
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: 80.76 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 284 PAYcPCERMA--------------SEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFACMADIGWI 349
Cdd:cd17652 69 PAY-PAERIAymladarpalllttPDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPSFD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 350 TGHSYIIYGPLANGittavfesTPVYPTPSRywdfvdkwkatqLYTAPTAIRLLRRMGEDHV----------KNHDLSSL 419
Cdd:cd17652 147 ASVWELLMALLAGA--------TLVLAPAEE------------LLPGEPLADLLREHRITHVtlppaalaalPPDDLPDL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 420 RVLGSVGEPINPE-AWHWYNDfagknqCAIVDTYWMTET--GSISIAPLPGAISTKPGSatfPFFGMDVDIIDPQTGQVL 496
Cdd:cd17652 207 RTLVVAGEACPAElVDRWAPG------RRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARLRPVP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 497 EGNDVE----GVLVARRPWPSIARTVyrdhKRYLetymkPYPgyffFGDGAARDY----------DGYMWIKGRVDDVIN 562
Cdd:cd17652 278 PGVPGElyiaGAGLARGYLNRPGLTA----ERFV-----ADP----FGAPGSRMYrtgdlarwraDGQLEFLGRADDQVK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 563 VSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEfdlkatkEADLSKELAIQVRKVIGPFAAPKKIY 642
Cdd:cd17652 345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG-------AAPTAAELRAHLAERLPGYMVPAAFV 417
|
410
....*....|....*...
9C8S_C 643 LVSDLPKTRSGKIMRRVL 660
Cdd:cd17652 418 VLDALPLTPNGKLDRRAL 435
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
451-665 |
6.12e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.81 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 451 TYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVlegnDVEGvlvarrpwPSIARTVYRDHKryletym 530
Cdd:PRK07445 260 TYGMTETASQIATLKPDDFLAGNNSSGQVLPHAQITIPANQTGNI----TIQA--------QSLALGYYPQIL------- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 531 kPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMK-PE 609
Cdd:PRK07445 321 -DSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKdPS 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 610 FDLKATKEAdLSKELAiqvrkvigPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:PRK07445 400 ISLEELKTA-IKDQLS--------PFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
134-661 |
1.06e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 80.69 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 134 TAIIYEADEPSES---REVSYEELMQETCRVAN-VLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSA 209
Cdd:PRK08751 33 TSVAKFADRPAYHsfgKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 210 ESLRDRVNDCECKVLITTDE-GRRGGKTIA---TKQIVDAAL------QQCPLVEnvLVLRRTGNKVP--MTEGRDKWWD 277
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNfGTTVQQVIAdtpVKQVITTGLgdmlgfPKAALVN--FVVKYVKKLVPeyRINGAIRFRE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 278 EECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHS---------TAGYLLGTALTLK----YVFDAHPddrfacma 344
Cdd:PRK08751 191 ALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLThrnlvanmqQAHQWLAGTGKLEegceVVITALP-------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 345 digwitghSYIIYGPLANGITTAVFES-TPVYPTPSRYWDFVDKWKATQlYTAPTAIR-----LLRRMGEDHVknhDLSS 418
Cdd:PRK08751 263 --------LYHIFALTANGLVFMKIGGcNHLISNPRDMPGFVKELKKTR-FTAFTGVNtlfngLLNTPGFDQI---DFSS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 419 LRVLGSVGEPINPE-AWHWYNdfagKNQCAIVDTYWMTETG-SISIAPLpgAISTKPGSATFPFFGMDVDIIDpQTGQVL 496
Cdd:PRK08751 331 LKMTLGGGMAVQRSvAERWKQ----VTGLTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKD-DAGTVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 497 EGNDVeGVLVARRPwpsiaRTVYRDHKRYLET-YMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVES 575
Cdd:PRK08751 404 AIGEI-GELCIKGP-----QVMKGYWKRPEETaKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 576 ALILHKGVAETAVVGCADDLTGQAVYAFVTMKpefDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKI 655
Cdd:PRK08751 478 VIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK---DPALTAE-----DVKAHARANLTGYKQPRIIEFRKELPKTNVGKI 549
|
....*.
9C8S_C 656 MRRVLR 661
Cdd:PRK08751 550 LRRELR 555
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
123-667 |
1.41e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 80.24 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHYYKNPKKTAIIYeadePSESREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSA 202
Cdd:PRK08315 22 LDRTAARYPDREALVY----RDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAESLRDRVNDCECKVLITTDegrrGGKT-------------IATKQIVDAALQQCPLVENVLVLrrTGNKVPmt 269
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAAD----GFKDsdyvamlyelapeLATCEPGQLQSARLPELRRVIFL--GDEKHP-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 270 eGRDKWwdEECAKMPAYCPCERMAS-------EDPLFILYTSGSTGKPKGVVHS-----TAGYLLGTALTLKyvfdahPD 337
Cdd:PRK08315 170 -GMLNF--DELLALGRAVDDAELAArqatldpDDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEAMKLT------EE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 338 DR----------FAC-MADIGWITgHSyiiygplangittavfeSTPVYPTPSrywdF--------VDKWKATQLYTAPT 398
Cdd:PRK08315 241 DRlcipvplyhcFGMvLGNLACVT-HG-----------------ATMVYPGEG----FdplatlaaVEEERCTALYGVPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 399 A-IRLLrrmgeDH--VKNHDLSSLR---VLGSVGePInpEAWHWYNDFAGKNQCAIVdtYWMTETGSISIA-----PLPG 467
Cdd:PRK08315 299 MfIAEL-----DHpdFARFDLSSLRtgiMAGSPC-PI--EVMKRVIDKMHMSEVTIA--YGMTETSPVSTQtrtddPLEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 468 AISTKpGSAtFPFfgMDVDIIDPQTGQVLEGNdVEGVLVARRP------WPSIARTvyR---DHKRYLETymkpypgyff 538
Cdd:PRK08315 369 RVTTV-GRA-LPH--LEVKIVDPETGETVPRG-EQGELCTRGYsvmkgyWNDPEKT--AeaiDADGWMHT---------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 539 fGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkatKEA 618
Cdd:PRK08315 432 -GDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATL---TEE 507
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
9C8S_C 619 DLsKELAiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGE 667
Cdd:PRK08315 508 DV-RDFC---RGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
138-669 |
2.05e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.83 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 138 YEADEPSESrevSYEELMQETCRVANVLK-SYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRV 216
Cdd:PRK05620 31 WGGAEQEQT---TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 217 NDCECKVLITTdegRRGGKTIATkqivdaALQQCPLVENVLVLRRTGNKVPMTEGRDKW----WDEECAKMPAYCPCERM 292
Cdd:PRK05620 108 NHAEDEVIVAD---PRLAEQLGE------ILKECPCVRAVVFIGPSDADSAAAHMPEGIkvysYEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 293 ASEDPLFILYTSGSTGKPKGVVHS-TAGYLLGTALTLKYVFDAHPDDRFACMADIgwitghsyiiYGPLANGITTAVFES 371
Cdd:PRK05620 179 DETTAAAICYSTGTTGAPKGVVYShRSLYLQSLSLRTTDSLAVTHGESFLCCVPI----------YHVLSWGVPLAAFMS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 372 -TP-VYPTPSRYWDFVDKWKATQL----YTAPTA-IRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHwyndfaGKN 444
Cdd:PRK05620 249 gTPlVFPGPDLSAPTLAKIIATAMprvaHGVPTLwIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWE------ERY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 445 QCAIVDTYWMTETGSI-SIAPLPGAIStkpGSAT---------FPFfGMDVDIIDpqTGQVLEGNDV-EGVLVARRPW-- 511
Cdd:PRK05620 323 GVDVVHVWGMTETSPVgTVARPPSGVS---GEARwayrvsqgrFPA-SLEYRIVN--DGQVMESTDRnEGEIQVRGNWvt 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 512 ------PS----IARTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHK 581
Cdd:PRK05620 397 asyyhsPTeeggGAASTFRGEDVEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 582 GVAETAVVGCADDLTGQAVYAFVTMKPefDLKATKEAdlSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK05620 477 EVVECAVIGYPDDKWGERPLAVTVLAP--GIEPTRET--AERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
....*...
9C8S_C 662 KIVAgEGD 669
Cdd:PRK05620 553 QHLA-DGD 559
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
260-670 |
2.88e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.39 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 260 RRTGNKVPMTEGRDKW-WDEECAKMPAYC---PCERMASEDPLFILYTSGSTGKPKGVV--HSTAGYLLGTALTlKYVFD 333
Cdd:PRK12316 616 SHLGRKLPLAAGVQVLdLDRPAAWLEGYSeenPGTELNPENLAYVIYTSGSTGKPKGAGnrHRALSNRLCWMQQ-AYGLG 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 334 AHpdDRFACMADIGWITGHsYIIYGPLANGiTTAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDhvkn 413
Cdd:PRK12316 695 VG--DTVLQKTPFSFDVSV-WEFFWPLMSG-ARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV---- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 414 HDLSSLRVLGSVGEPINPEAWHWYndFAGKNQCAIVDTYWMTETG---SISIAPLPGAISTKPGSatfPFFGMDVDIIDP 490
Cdd:PRK12316 767 ASCTSLRRIVCSGEALPADAQEQV--FAKLPQAGLYNLYGPTEAAidvTHWTCVEEGGDSVPIGR---PIANLACYILDA 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 491 QTGQVLEGNDVEGVLVARrpwpSIARTVYRDHKRYLETYMkPYPgyffFGDGaARDY----------DGYMWIKGRVDDV 560
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGR----GLARGYHGRPGLTAERFV-PSP----FVAG-ERMYrtgdlaryraDGVIEYAGRIDHQ 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 561 INVSGHRLSTAEVESALILHKGVAETAVVGcaddLTGQAVYAFVTMKPEfdlkatkEADLSKELAIQVRKVIGPFAAPKK 640
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE-------GGDWREALKAHLAASLPEYMVPAQ 980
|
410 420 430
....*....|....*....|....*....|
9C8S_C 641 IYLVSDLPKTRSGKIMRRVLRKIVAGEGDQ 670
Cdd:PRK12316 981 WLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
145-662 |
6.49e-15 |
|
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: 77.86 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 145 ESREVSYEELMQETCRVANVLKS-YGVKKGDAVSIYLP------MTWqaaaafLACARIGAIHSAVFAGFSAESLRDRVN 217
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTnspefvFLW------LGLWSIGAAPAFINYNLSGDPLIHCLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 218 DCECKVLITTDEgrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaseDP 297
Cdd:cd05937 76 LSGSRFVIVDPD------------------------------------------------------------------DP 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 298 LFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRFACMA---DIGWITGHSYIiygpLANGITTAVFESTPV 374
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPlyhGTAAFLGACNC----LMSGGTLALSRKFSA 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 375 yptpSRYWDFVDKWKATQ-LYTAPTAIRLLRRMGEDHVKNHdlsslRVLGSVGEPINPEAWHWYND-FagkNQCAIVDTY 452
Cdd:cd05937 166 ----SQFWKDVRDSGATIiQYVGELCRYLLSTPPSPYDRDH-----KVRVAWGNGLRPDIWERFRErF---NVPEIGEFY 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 453 WMTE---------TGSISIaplpGAISTKpGSATFPFFGMDVDI--IDPQTGQVLEGNDV----------EGVLVAR-RP 510
Cdd:cd05937 234 AATEgvfaltnhnVGDFGA----GAIGHH-GLIRRWKFENQVVLvkMDPETDDPIRDPKTgfcvrapvgePGEMLGRvPF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 WPSIARTVY-----RDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAE 585
Cdd:cd05937 309 KNREAFQGYlhnedATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAE 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 586 TAVVGC-ADDLTGQAVYAFVTMKPEFDLKATKEADLSKELAiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05937 389 ANVYGVkVPGHDGRAGCAAITLEESSAVPTEFTKSLLASLA---RKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
147-662 |
1.92e-14 |
|
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: 76.24 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 tdegrrggktiatkqivdaalqqcplvenvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermaseDPLFILYTSGS 306
Cdd:cd05940 82 ---------------------------------------------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 307 TGKPKGVVHSTAGYLLGTALtLKYVFDAHPDDR-FACMAdIGWITGHSYIIYGPLANGITTAVFESTpvypTPSRYWDFV 385
Cdd:cd05940 93 TGLPKAAIISHRRAWRGGAF-FAGSGGALPSDVlYTCLP-LYHSTALIVGWSACLASGATLVIRKKF----SASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 386 DKWKATQL-YTAPTAIRLLRRMGEDHVKNHdlsSLRVLgsVGEPINPEAWhwyNDFAGKNQCA-IVDTYWMTE--TGSIS 461
Cdd:cd05940 167 RKYQATIFqYIGELCRYLLNQPPKPTERKH---KVRMI--FGNGLRPDIW---EEFKERFGVPrIAEFYAATEgnSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 462 IAPLPGAI----STKPGSATFPFFGMDVDIIDP---QTGQVLEGNDVE-GVLVAR--RPWP------------SIARTVY 519
Cdd:cd05940 239 FFGKPGAIgrnpSLLRKVAPLALVKYDLESGEPirdAEGRCIKVPRGEpGLLISRinPLEPfdgytdpaatekKILRDVF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 520 RDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCA-DDLTGQ 598
Cdd:cd05940 319 KKGDAWFNT-----------GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGR 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C8S_C 599 AVYAFVTMKP--EFDLKAtkeadlskeLAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRK 662
Cdd:cd05940 388 AGMAAIVLQPneEFDLSA---------LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
129-680 |
4.99e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 75.30 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 129 KNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIhsavfAGFS 208
Cdd:PRK08279 49 RHPDRPALLFE------DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV-----VALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 209 AESLRDRV-----NDCECKVLITTDEgrrggktiaTKQIVDAALQQCPLVENVLVLRRTGNKVPMTegrdkwwDEECAKM 283
Cdd:PRK08279 118 NTQQRGAVlahslNLVDAKHLIVGEE---------LVEAFEEARADLARPPRLWVAGGDTLDDPEG-------YEDLAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 284 PAYCP------CERMASEDPLFILYTSGSTGKPKGVVHSTAGYLL---GTALTLkyvfDAHPDDRFACM--------ADI 346
Cdd:PRK08279 182 AAGAPttnpasRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKamgGFGGLL----RLTPDDVLYCClplyhntgGTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 347 GWITGhsyiiygpLANGITTAVFESTPVyptpSRYWDFVDKWKATQ----------LYTAPTairllRRMGEDHvknhdl 416
Cdd:PRK08279 258 AWSSV--------LAAGATLALRRKFSA----SRFWDDVRRYRATAfqyigelcryLLNQPP-----KPTDRDH------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 417 sSLRVLgsVGEPINPEAWH-WYNDFAGKnqcAIVDTYWMTE--TGSISIAPLPGAISTKPGSATFPFfgmdvDII--DPQ 491
Cdd:PRK08279 315 -RLRLM--IGNGLRPDIWDeFQQRFGIP---RILEFYAASEgnVGFINVFNFDGTVGRVPLWLAHPY-----AIVkyDVD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 492 TGQVLEGND-----VE----GVLVAR--RPWP------------SIARTVYRDHKRYLET--YMKPYP-GYFFFGDgaaR 545
Cdd:PRK08279 384 TGEPVRDADgrcikVKpgevGLLIGRitDRGPfdgytdpeasekKILRDVFKKGDAWFNTgdLMRDDGfGHAQFVD---R 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 546 DYDGYMWiKGRvddviNVsghrlSTAEVESALILHKGVAETAVVGCA-DDLTGQAVYAFVTMK--PEFDLKAtkeadlsk 622
Cdd:PRK08279 461 LGDTFRW-KGE-----NV-----ATTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLAdgAEFDLAA-------- 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 623 eLAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKivagEGdqlGDLSSIADP 680
Cdd:PRK08279 522 -LAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK----EG---FDPSKVDDP 571
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
146-671 |
5.15e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.04 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 146 SREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLI 225
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 226 TTDEGRRGGKTIATkqivdaALQQCPLVenvlvlrrtgnKVPMTEGRDKWWDEECAKMPAYCPceRMASEDPLFILYTSG 305
Cdd:PRK05857 119 VAPGSKMASSAVPE------ALHSIPVI-----------AVDIAAVTRESEHSLDAASLAGNA--DQGSEDPLAMIFTSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 306 STGKPKGVvhstagyllgtaLTLKYVFDAHPDD-RFACMADIGWITGHSyiIYGPLA-----------NGITTAVFESTP 373
Cdd:PRK05857 180 TTGEPKAV------------LLANRTFFAVPDIlQKEGLNWVTWVVGET--TYSPLPathigglwwilTCLMHGGLCVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 374 VYPTPSRYWDFVDKWKATQLYTaPTAirLLRRMGEDHVKNHDLSSLRVLGSVGEPInPEAWHWYNDFAGKNQCAIvdtYW 453
Cdd:PRK05857 246 GENTTSLLEILTTNAVATTCLV-PTL--LSKLVSELKSANATVPSLRLVGYGGSRA-IAADVRFIEATGVRTAQV---YG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 454 MTETGSISIApLP---GAIS-TKPGSATFPFFGMDVDIIDPQTGQVLEGNDVE----GVLVARRP------WPSIART-- 517
Cdd:PRK05857 319 LSETGCTALC-LPtddGSIVkIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfGTLWIKSPanmlgyWNNPERTae 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 518 VYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTG 597
Cdd:PRK05857 398 VLID-------------GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C8S_C 598 QAVYAFVTMKPEFDLKATKEadLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEGDQL 671
Cdd:PRK05857 465 ALVGLAVVASAELDESAARA--LKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-624 |
8.17e-14 |
|
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: 74.42 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 294 SEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTLKYVFDAHPDDR-FACMADIGwitghsyiIYGPlANGITTAVFEST 372
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVY-RHGTFAAQIDALRQLYGIRPGEVdLATFPLFA--------LFGP-ALGLTSVIPDMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 373 PVYP---TPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHvkNHDLSSLRVLGSVGEPINPEAWHWYNDFAgKNQCAIV 449
Cdd:cd05910 154 PTRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH--GITLPSLRRVLSAGAPVPIALAARLRKML-SDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 450 DTYWMTEtgSISIAPLPG-------AISTKPGSAT---FPFFGMDVDIID------PQTGQVLEGNDVE-GVLVARRpwP 512
Cdd:cd05910 231 TPYGATE--ALPVSSIGSrellattTAATSGGAGTcvgRPIPGVRVRIIEiddepiAEWDDTLELPRGEiGEITVTG--P 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 513 SIARTVYrdHKRYLETYMK-PYPGYFFF---GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAV 588
Cdd:cd05910 307 TVTPTYV--NRPVATALAKiDDNSEGFWhrmGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330 340 350
....*....|....*....|....*....|....*.
9C8S_C 589 VGCADDLTGQAVyafVTMKPEfDLKATKEADLSKEL 624
Cdd:cd05910 385 VGVGKPGCQLPV---LCVEPL-PGTITPRARLEQEL 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-692 |
1.35e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:PRK12316 2017 PEAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEgrrggktiatkqivdaALQQCPLVENVLVLRRTgnkvpmtegRDKWWdeecAKMPAYCPCE 290
Cdd:PRK12316 2091 RLAYMLEDSGAALLLTQRH----------------LLERLPLPAGVARLPLD---------RDAEW----ADYPDTAPAV 2141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYvFDAHPDDR---FACMADIGWITGhsyiIYGPLANGITTA 367
Cdd:PRK12316 2142 QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCelqFMSFSFDGAHEQ----WFHPLLNGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 368 VFESTpvYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRmgEDHVKNHDLsSLRVLGSVGEPINPE---AWH-------WY 437
Cdd:PRK12316 2217 IRDDE--LWDPEQLYDEMERHGVTILDFPPVYLQQLAE--HAERDGRPP-AVRVYCFGGEAVPAAslrLAWealrpvyLF 2291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 438 NDFaGKNQCAIVDTYWMTETGSISIAPLPgAISTKPGSATFPFFGMDVDIIDPQ-TGQVLEGNdvEGV---------LVA 507
Cdd:PRK12316 2292 NGY-GPTEAVVTPLLWKCRPQDPCGAAYV-PIGRALGNRRAYILDADLNLLAPGmAGELYLGG--EGLargylnrpgLTA 2367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 508 RR----PWPSIARTVYRDhkryletymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGV 583
Cdd:PRK12316 2368 ERfvpdPFSASGERLYRT------------------GDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 584 AETAVVGcADDLTGQAVYAFVtmkpefdLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKI 663
Cdd:PRK12316 2430 REAVVVA-QDGASGKQLVAYV-------VPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP 2501
|
570 580
....*....|....*....|....*....
9C8S_C 664 VAGEGDQLGDLSSIADPQIVEEVKQKVTG 692
Cdd:PRK12316 2502 DVSQLRQAYVAPQEGLEQRLAAIWQAVLK 2530
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
123-665 |
1.84e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 73.49 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 123 LDRHyyKNPKKTAIIYEadepseSREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIhsA 202
Cdd:PRK10946 31 LTRH--AASDAIAVICG------ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 203 VFAGFSAES--LRDRVNDCECKVLIttdeGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGnkvpmTEGRDKWWDEEC 280
Cdd:PRK10946 101 VNALFSHQRseLNAYASQIEPALLI----ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDG-----EHSLDDAINHPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 281 AKMPAY-CPCERMAsedplFILYTSGSTGKPKGV--VHSTAGY-LLGTA----LTlkyvfdahPDDRFACMADigwiTGH 352
Cdd:PRK10946 172 EDFTATpSPADEVA-----FFQLSGGSTGTPKLIprTHNDYYYsVRRSVeicgFT--------PQTRYLCALP----AAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 353 SYIIYGPLANGITTA----VFESTPvypTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVL------ 422
Cdd:PRK10946 235 NYPMSSPGALGVFLAggtvVLAPDP---SATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLqvggar 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 423 --GSVGEPINPEAwhwyndfagknQCAIVDTYWMTEtGSISIAPL---PGAISTKPGSatfPFFGMD-VDIIDPQTGQVL 496
Cdd:PRK10946 312 lsETLARRIPAEL-----------GCQLQQVFGMAE-GLVNYTRLddsDERIFTTQGR---PMSPDDeVWVADADGNPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 497 EGNdvEGVLVARRPW--------PSIARTVYRDHkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRL 568
Cdd:PRK10946 377 QGE--VGRLMTRGPYtfrgyyksPQHNASAFDAN------------GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 569 STAEVESALILHKGVAETAVVGCADDLTGQAVYAF-VTMKPefdLKatkeadlskelAIQVRKV-----IGPFAAPKKIY 642
Cdd:PRK10946 443 AAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFlVVKEP---LK-----------AVQLRRFlreqgIAEFKLPDRVE 508
|
570 580
....*....|....*....|...
9C8S_C 643 LVSDLPKTRSGKIMRRVLRKIVA 665
Cdd:PRK10946 509 CVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
295-660 |
1.86e-13 |
|
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: 73.24 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVV--HSTagyLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGitTAVFEST 372
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMieHQS---LVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGA--TLVLRPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 373 PVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDlSSLRVLGSVGEPINPEAWH-WYNDFAGKNQCaiVDT 451
Cdd:cd17644 181 EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRqWQKNVGNFIQL--INV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 452 YWMTE-TGSISIAPLPGAISTKPGSATF--PFFGMDVDIIDPQTGQVLEGNDVE----GVLVAR----RpwPSIARTVYR 520
Cdd:cd17644 258 YGPTEaTIAATVCRLTQLTERNITSVPIgrPIANTQVYILDENLQPVPVGVPGElhigGVGLARgylnR--PELTAEKFI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 521 DHKRYLETYMKPYPGyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAV 600
Cdd:cd17644 336 SHPFNSSESERLYKT----GDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 601 YAF-VTMKPEFDLKATKEADLSKELAIqvrkvigpFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd17644 412 VAYiVPHYEESPSTVELRQFLKAKLPD--------YMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
146-660 |
3.56e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 73.66 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 146 SREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAihsaVFAGFSAESLRDR----VNDCEC 221
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG----AYVPLDPEYPRERlaymIEDSGI 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 222 KVLITTDegrrggktiatkqivdAALQQCPLVENV--LVLrrtgnkvpmtEGRDKWWDEEcakmPAYCPCERMASEDPLF 299
Cdd:PRK12467 1673 ELLLTQS----------------HLQARLPLPDGLrsLVL----------DQEDDWLEGY----SDSNPAVNLAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 300 ILYTSGSTGKPKGvVHSTAGYLLGTALTLKYVFDAHPDDrfacmadiGWITGHSYI-------IYGPLANGiTTAVFEST 372
Cdd:PRK12467 1723 VIYTSGSTGRPKG-AGNRHGALVNRLCATQEAYQLSAAD--------VVLQFTSFAfdvsvweLFWPLING-ARLVIAPP 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 373 PVYPTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEdHVKNhdLSSLRVLGSVGEPINPEAWH-WYNDFA--------GK 443
Cdd:PRK12467 1793 GAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDE-QVEH--PLSLRRVVCGGEALEVEALRpWLERLPdtglfnlyGP 1869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 444 NQCAIVDTYWmtetgSISIAPLPGAISTKPGSatfPFFGMDVDIIDPQTGQVLEGNDVE----GVLVAR----RPWPSIA 515
Cdd:PRK12467 1870 TETAVDVTHW-----TCRRKDLEGRDSVPIGQ---PIANLSTYILDASLNPVPIGVAGElylgGVGLARgylnRPALTAE 1941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 516 RTVyrdhkryletymkPYPgyffFGDGAARDY----------DGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAE 585
Cdd:PRK12467 1942 RFV-------------ADP----FGTVGSRLYrtgdlaryraDGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVRE 2004
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9C8S_C 586 TAVVGCADDLTGQAVYAFVTMKPEFDLKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK12467 2005 AVVIAQDGANGKQLVAYVVPTDPGLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
290-667 |
8.50e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 71.37 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 290 ERMASEdPLFILYTSGSTGKPKGV-------VHSTAGYLLGTALTLKyvfdahpdDRF----ACMADIGWITGH-SYIIY 357
Cdd:cd05908 102 CELADE-LAFIQFSSGSTGDPKGVmlthenlVHNMFAILNSTEWKTK--------DRIlswmPLTHDMGLIAFHlAPLIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 358 GPLANGITTAVFestpvYPTPSRYWDFVDKWKATQLYTAPTAIR-LLRRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHW 436
Cdd:cd05908 173 GMNQYLMPTRLF-----IRRPILWLKKASEHKATIVSSPNFGYKyFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 YNDFAGK---NQCAIVDTYWMTE-------------TGSISI--------APLPGAISTKPGSATF-----PFFGMDVDI 487
Cdd:cd05908 248 FLDHMSKyglKRNAILPVYGLAEasvgaslpkaqspFKTITLgrrhvthgEPEPEVDKKDSECLTFvevgkPIDETDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 488 IDPQTgQVLEgNDVEGVLVARrpwpsiARTV---YRDHKRYLETYMKPyPGYFFFGD-GAARdyDGYMWIKGRVDDVINV 563
Cdd:cd05908 328 CDEDN-KILP-DGYIGHIQIR------GKNVtpgYYNNPEATAKVFTD-DGWLKTGDlGFIR--NGRLVITGREKDIIFV 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 564 SGHRLSTAEVESALILHKGVAETAVVGCA---DDLTGQAVYAFVtmkpefdLKATKEADLSKeLAIQVRKVIGPFAA--P 638
Cdd:cd05908 397 NGQNVYPHDIERIAEELEGVELGRVVACGvnnSNTRNEEIFCFI-------EHRKSEDDFYP-LGKKIKKHLNKRGGwqI 468
|
410 420 430
....*....|....*....|....*....|
9C8S_C 639 KKIYLVSDLPKTRSGKIMR-RVLRKIVAGE 667
Cdd:cd05908 469 NEVLPIRRIPKTTSGKVKRyELAQRYQSGE 498
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
295-663 |
1.21e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 71.49 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 295 EDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRfacmadigwITG-----HSY----IIYGPLANGIt 365
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHN-ILSNIEQISDVFNLRNDDV---------ILSslpffHSFgltvTLWLPLLEGI- 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 366 TAVFESTPVyptpsrywD------FVDKWKATQLYTAPTAIRLLRRMGEdhVKNHDLSSLRVLGSVGEPINPEAwhwYND 439
Cdd:PRK08633 851 KVVYHPDPT--------DalgiakLVAKHRATILLGTPTFLRLYLRNKK--LHPLMFASLRLVVAGAEKLKPEV---ADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 440 FAGKNQCAIVDTYWMTETGSISIAPLPGA--------ISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDvEGVLVARRP- 510
Cdd:PRK08633 918 FEEKFGIRILEGYGATETSPVASVNLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETFEELPPGE-DGLILIGGPq 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 -----WPSIART--VYRDHKRyletymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESAL--ILHK 581
Cdd:PRK08633 997 vmkgyLGDPEKTaeVIKDIDG---------IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakALGG 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 582 GVAETAVVGCADDLTGQAVyAFVTMKPEFDLKATKEADLSKELAiqvrkvigPFAAPKKIYLVSDLPKTRSGKIMRRVLR 661
Cdd:PRK08633 1068 EEVVFAVTAVPDEKKGEKL-VVLHTCGAEDVEELKRAIKESGLP--------NLWKPSRYFKVEALPLLGSGKLDLKGLK 1138
|
..
9C8S_C 662 KI 663
Cdd:PRK08633 1139 EL 1140
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
131-660 |
4.80e-12 |
|
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: 68.65 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 131 PKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAE 210
Cdd:cd17656 2 PDAVAVVFEN------QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 211 SLRDRVNDCECKVLITTDEgrRGGKTIATKQIVdaalqqcpLVENVLVLRRTGNKVPMTegrdkwwdeecakmpaycpce 290
Cdd:cd17656 76 RRIYIMLDSGVRVVLTQRH--LKSKLSFNKSTI--------LLEDPSISQEDTSNIDYI--------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 rMASEDPLFILYTSGSTGKPKGVV--HSTAGYLLgtaltlKYVFDAHPDDRFAcmadigwitghsyiiygplangittAV 368
Cdd:cd17656 125 -NNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL------HFEREKTNINFSD-------------------------KV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 369 FEstpvYPTPS---RYWDFVDKW-KATQLYTAPTAIRLLRRMGEDHVKNHDLSS-------LRVLGSVGEPINP------ 431
Cdd:cd17656 173 LQ----FATCSfdvCYQEIFSTLlSGGTLYIIREETKRDVEQLFDLVKRHNIEVvflpvafLKFIFSEREFINRfptcvk 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 432 ---------------------EAWHWYNdFAGKNQCAIVDTYWMTETGSISIAPLPGaistKPGSATfpffgmDVDIIDP 490
Cdd:cd17656 249 hiitageqlvitnefkemlheHNVHLHN-HYGPSETHVVTTYTINPEAEIPELPPIG----KPISNT------WIYILDQ 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 491 QTGQVLEGND----VEGVLVARRPWPSIARTvyrdHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGH 566
Cdd:cd17656 318 EQQLQPQGIVgelyISGASVARGYLNRQELT----AEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 567 RLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMkpefdLKATKEADLSKELAIQvrkvIGPFAAPKKIYLVSD 646
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-----EQELNISQLREYLAKQ----LPEYMIPSFFVPLDQ 464
|
570
....*....|....
9C8S_C 647 LPKTRSGKIMRRVL 660
Cdd:cd17656 465 LPLTPNGKVDRKAL 478
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
293-664 |
8.01e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.29 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 293 ASEDPLFILYTSGSTGKPKGVVHSTagyllgTALTLKyvfdahpddRFACMADIGWITGHSYIIYGPLAN--GITTAV-- 368
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISH------SALIVQ---------SLAKIAIVGYGEDDVYLHTAPLCHigGLSSALam 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 369 ------------FESTPVYptpsrywDFVDKWKATQLYTAPTA----IRLLRRMGEDHVKNHDLSSLRVLGSVGEPINPE 432
Cdd:PLN02860 235 lmvgachvllpkFDAKAAL-------QAIKQHNVTSMITVPAMmadlISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 433 AWHWYNdfagknQCAIVDTYWMTET-GSISIAPLpgaisTKPGSATFPFFGMDVDIIDPQTGQVLEGNDV---------- 501
Cdd:PLN02860 308 AKKLFP------NAKLFSAYGMTEAcSSLTFMTL-----HDPTLESPKQTLQTVNQTKSSSVHQPQGVCVgkpaphvelk 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 502 --------EGVLVARRP------WP-SIARTVYRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGH 566
Cdd:PLN02860 377 igldessrVGRILTRGPhvmlgyWGqNSETASVLSNDGWLDT-----------GDIGWIDKAGNLWLIGRSNDRIKTGGE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 567 RLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEF------DLKATKEADLSKE-LAIQVR-KVIGPFAAP 638
Cdd:PLN02860 446 NVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWiwsdneKENAKKNLTLSSEtLRHHCReKNLSRFKIP 525
|
410 420
....*....|....*....|....*..
9C8S_C 639 KKIYLVSD-LPKTRSGKIMRRVLRKIV 664
Cdd:PLN02860 526 KLFVQWRKpFPLTTTGKIRRDEVRREV 552
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
288-590 |
2.07e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.85 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 288 PCERMASEDPLFILYTSGSTGKPKGVVHsTAGYLLGTALTLKYVFDAHPDDR----FACMAdigwitghsyiIYGPlANG 363
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVY-THGMFEAQIEALREDYGIEPGEIdlptFPLFA-----------LFGP-ALG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 364 ITTAVFESTPVYPT---PSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHvkNHDLSSLRVLGSVGEPINPEAWH----W 436
Cdd:PRK09274 234 MTSVIPDMDPTRPAtvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEAN--GIKLPSLRRVISAGAPVPIAVIErfraM 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 YNDFAgknqcAIVDTYWMTETGSIS-IAPLPGAISTKPGSAT-------FPFFGMDVDIIDPQTG--------QVLEGND 500
Cdd:PRK09274 312 LPPDA-----EILTPYGATEALPISsIESREILFATRAATDNgagicvgRPVDGVEVRIIAISDApipewddaLRLATGE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 501 VEGVLVARrpwPSIARTVYRDHKRYLETYMKPYPGYFF--FGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALI 578
Cdd:PRK09274 387 IGEIVVAG---PMVTRSYYNRPEATRLAKIPDGQGDVWhrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFN 463
|
330
....*....|..
9C8S_C 579 LHKGVAETAVVG 590
Cdd:PRK09274 464 THPGVKRSALVG 475
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
479-666 |
7.30e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.11 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 479 PFFGMDVDIIDPQtGQVLEGNDVE-GVLVARRPWpsIARTVYRDHKRYLETymkpypGYFFFGDGAARDYDGYMWIKGRV 557
Cdd:PRK07008 361 VIYGVDMKIVGDD-GRELPWDGKAfGDLQVRGPW--VIDRYFRGDASPLVD------GWFPTGDVATIDADGFMQITDRS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 558 DDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLkaTKEadlskELAIQVRKVIGPFAA 637
Cdd:PRK07008 432 KDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEV--TRE-----ELLAFYEGKVAKWWI 504
|
170 180
....*....|....*....|....*....
9C8S_C 638 PKKIYLVSDLPKTRSGKIMRRVLRKIVAG 666
Cdd:PRK07008 505 PDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-693 |
1.07e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.57 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 292 MASEDPLFILYTSGSTGKPKGVvHSTAGYLLGTALTLKYVF--DAHPDDRFAC----MADIGWITGhsyiIYGPLANGIT 365
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFgiDLNPDDVIVSwlplYHDMGLIGG----LLQPIFSGVP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 366 TAVFESTPVYPTPSRYWDFVDKWKATQLYTAPTAIRLL-RRMGEDHVKNHDLSSLRVLGSVGEPINPEAWHWYND-FA-- 441
Cdd:PRK05691 238 CVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCsERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEkFAac 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 442 GKNQCAIVDTYWMTE-----TGSISIAPLP---------GAISTKPG------SATFPFFGMDVDIIDPQTGQVLEGNDV 501
Cdd:PRK05691 318 GFDPDSFFASYGLAEatlfvSGGRRGQGIPaleldaealARNRAEPGtgsvlmSCGRSQPGHAVLIVDPQSLEVLGDNRV 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 502 EGVLVARrpwPSIA-----------RT-VYRDHKRYLETymkpypgyfffGD-GAARDydGYMWIKGRVDDVINVSGHRL 568
Cdd:PRK05691 398 GEIWASG---PSIAhgywrnpeasaKTfVEHDGRTWLRT-----------GDlGFLRD--GELFVTGRLKDMLIVRGHNL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 569 STAEVESAL-----ILHKG-VAETAVVgcADDLTGQAVYAFVTMKPEfdlKATKEADLSKELaiqvRKVIGPF--AAPKK 640
Cdd:PRK05691 462 YPQDIEKTVereveVVRKGrVAAFAVN--HQGEEGIGIAAEISRSVQ---KILPPQALIKSI----RQAVAEAcqEAPSV 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 641 IYLVSD--LPKTRSGKIMRRVLRKIVAGegdqlGDLSSIA---DPQIVEEVKQKVTGS 693
Cdd:PRK05691 533 VLLLNPgaLPKTSSGKLQRSACRLRLAD-----GSLDSYAlfpALQAVEAAQTAASGD 585
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
62-122 |
1.10e-10 |
|
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: 57.10 E-value: 1.10e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 62 YESYVKEWAKtvgpNSDEWWAAKAREtLDWYDDFKTVRAGGFeHGDVQWFPEGTLNAAYNC 122
Cdd:pfam16177 1 YEALYRRSIE----DPEGFWGEVAKE-LDWFKPFDKVLDGSN-GPFAKWFVGGKLNVCYNC 55
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
272-667 |
1.22e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 64.73 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 272 RDKWWDEECAKMPAYCPCERMAsEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDRFacMADIgwitg 351
Cdd:PRK08043 343 ADKLWIFAHLLMPRLAQVKQQP-EDAALILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRF--MSAL----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 352 hsyiiygPL--ANGITTAVFesTPV--------YPTPSRYW---DFVDKWKATQLYTAPTAIRLLRRMGEDhvknHDLSS 418
Cdd:PRK08043 414 -------PLfhSFGLTVGLF--TPLltgaevflYPSPLHYRivpELVYDRNCTVLFGTSTFLGNYARFANP----YDFAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 419 LRVLGSVGEPINPEAWHWYNDfagKNQCAIVDTYWMTETGSISIAPLPgaISTKPGSATFPFFGMDVDIID----PQTGQ 494
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQD---KFGLRILEGYGVTECAPVVSINVP--MAAKPGTVGRILPGMDARLLSvpgiEQGGR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 495 V-LEG-NDVEGVLVARRPWPSIARTVYRDHKRyLEtymkpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAE 572
Cdd:PRK08043 556 LqLKGpNIMNGYLRVEKPGVLEVPTAENARGE-ME------RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEM 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 573 VESALILHKGVAETAVVGCADDLTGQAVYAFVTmkpefdlkatkEADLSKELAIQVRKVIG--PFAAPKKIYLVSDLPKT 650
Cdd:PRK08043 629 VEQLALGVSPDKQHATAIKSDASKGEALVLFTT-----------DSELTREKLQQYAREHGvpELAVPRDIRYLKQLPLL 697
|
410
....*....|....*..
9C8S_C 651 RSGKIMRRVLRKIVAGE 667
Cdd:PRK08043 698 GSGKPDFVTLKSMVDEP 714
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
275-666 |
2.19e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.22 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 275 WWDEECAKMPAYCP----CERMAsEDPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLKYVFDAHPDDR-FACMADIgwi 349
Cdd:PRK06814 770 LADKIKGLLAGRFPlvyfCNRDP-DDPAVILFTSGSEGTPKGVVLSHRN-LLANRAQVAARIDFSPEDKvFNALPVF--- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 350 tgHSYIIYG----PLANGITTAvfestpVYPTPSRYW---DFVDKWKATQLYTAPTAIRLLRRMGedHvkNHDLSSLRVL 422
Cdd:PRK06814 845 --HSFGLTGglvlPLLSGVKVF------LYPSPLHYRiipELIYDTNATILFGTDTFLNGYARYA--H--PYDFRSLRYV 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 423 GSVGEPINPEAWH-WYNDFAGKnqcaIVDTYWMTETGSISiaplpgAIST----KPGSAtfpffgmdvdiidpqtGQVLE 497
Cdd:PRK06814 913 FAGAEKVKEETRQtWMEKFGIR----ILEGYGVTETAPVI------ALNTpmhnKAGTV----------------GRLLP 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 498 G-----NDVEGVLVARRPW---PSIARTVYRDHKRYleTYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLS 569
Cdd:PRK06814 967 GieyrlEPVPGIDEGGRLFvrgPNVMLGYLRAENPG--VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIS 1044
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 570 TAEVES-ALILHKGvAETAVVGCADDLTGQAVYAFVTMKpefdlKATKEADLSKELAIQVRKVigpfAAPKKIYLVSDLP 648
Cdd:PRK06814 1045 LAAVEElAAELWPD-ALHAAVSIPDARKGERIILLTTAS-----DATRAAFLAHAKAAGASEL----MVPAEIITIDEIP 1114
|
410
....*....|....*...
9C8S_C 649 KTRSGKIMRRVLRKIVAG 666
Cdd:PRK06814 1115 LLGTGKIDYVAVTKLAEE 1132
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
142-658 |
3.18e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.09 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 142 EPSESREVSYEELMQETCRVANVLKSYGVKKGDAVsiylpmtwqaaaaflacarigaihsAVFAGFSAEslrdrvndcec 221
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAV-------------------------AVLAGAPVE----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 222 kvLITTDEG--RRGGK-------------------TIATKQIVDA--ALQQCPLVENVLVLRRTGNKV-PMTEgrdkWWD 277
Cdd:PRK07768 67 --IAPTAQGlwMRGASltmlhqptprtdlavwaedTLRVIGMIGAkaVVVGEPFLAAAPVLEEKGIRVlTVAD----LLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 278 EECAKMPAYCPcermasEDPLFILYTSGSTGKPKGVVHSTAG-YLLGTALTLKYVFDAHpDDR-------FACMADIGWI 349
Cdd:PRK07768 141 ADPIDPVETGE------DDLALMQLTSGSTGSPKAVQITHGNlYANAEAMFVAAEFDVE-TDVmvswlplFHDMGMVGFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 350 TghSYIIYGPLANGITTAVFESTPVYptpsryW-DFVDKWKATQLyTAPT-----AIRLLRRMGEDhvKNHDLSSLRVLG 423
Cdd:PRK07768 214 T--VPMYFGAELVKVTPMDFLRDPLL------WaELISKYRGTMT-AAPNfayalLARRLRRQAKP--GAFDLSSLRFAL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 424 SVGEPINPEAwhwYNDFA------GKNQCAIVDTYWMTETG-SISIAPLPGAI------------------STKPGSATF 478
Cdd:PRK07768 283 NGAEPIDPAD---VEDLLdagarfGLRPEAILPAYGMAEATlAVSFSPCGAGLvvdevdadllaalrravpATKGNTRRL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 479 -----PFFGMDVDIIDpQTGQVLEGNDVeGVLVARRPwpSIARtvyrdhkRYLeTYMKPYP-----GYFFFGDGAARDYD 548
Cdd:PRK07768 360 atlgpPLPGLEVRVVD-EDGQVLPPRGV-GVIELRGE--SVTP-------GYL-TMDGFIPaqdadGWLDTGDLGYLTEE 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 549 GYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDlTGQAVYAF---VTMKPEFDLKATKEadLSKELA 625
Cdd:PRK07768 428 GEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFavaVESNAFEDPAEVRR--IRHQVA 504
|
570 580 590
....*....|....*....|....*....|....*
9C8S_C 626 IQVRKVIGpfAAPKKIYLVS--DLPKTRSGKIMRR 658
Cdd:PRK07768 505 HEVVAEVG--VRPRNVVVLGpgSIPKTPSGKLRRA 537
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
294-660 |
9.20e-10 |
|
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: 61.26 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 294 SEDPLFILYTSGSTGKPKGVVHSTAGYL-LGTALTLKYVFDAHPDDRFACMAD-----------IGWITGHSYIIYGPLA 361
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnLRTSLSERYFGRDNGDEAVLFFSNyvfdffveqmtLALLNGQKLVVPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 362 NGittavfestpvypTPSRYWDFVDKWKATQLYTAPTAIRL--LRRmgedhvknhdLSSLRVLGSVGEPINPEAWH-WYN 438
Cdd:cd17648 173 RF-------------DPDRFYAYINREKVTYLSGTPSVLQQydLAR----------LPHLKRVDAAGEEFTAPVFEkLRS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 439 DFAGKnqcaIVDTYWMTETGSISIAPLPGAISTKPGSATFPFFGMDVDIIDPQTGQVLEGNDVE----GVLVAR----RP 510
Cdd:cd17648 230 RFAGL----IINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGElylgGDGVARgylnRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 WPSIARTV----YRDHKRYLETYMKPYPGyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:cd17648 306 ELTAERFLpnpfQTEQERARGRNARLYKT----GDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVREC 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C8S_C 587 AVVGCADDLTGQAV-----YAFVTMKPEfdlkATKEADLSKELaiqvRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd17648 382 AVVAKEDASQAQSRiqkylVGYYLPEPG----HVPESDLLSFL----RAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
299-655 |
1.19e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 60.95 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVvHSTAGYLLGTALTLKYVFDAHPDD-RFacMADIGWITGHSYIIYGPLANGiTTAVFESTPVYPT 377
Cdd:cd17654 122 YVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDiLF--LTSPLTFDPSVVEIFLSLSSG-ATLLIVPTSVKVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 378 PSRYWDFVDKWKATQLYTAPTAirLLRRMGEDHVKNHDLS---SLRVLGSVGE--PINPEAWHWYNDFagkNQCAIVDTY 452
Cdd:cd17654 198 PSKLADILFKRHRITVLQATPT--LFRRFGSQSIKSTVLSatsSLRVLALGGEpfPSLVILSSWRGKG---NRTRIFNIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 453 WMTETGSISIA-PLPGAISTKPGSatFPFFGMDVDIIDpQTGQVLEGNDVEGvlvarrpwpSIARTVYRD--HKRYLETY 529
Cdd:cd17654 273 GITEVSCWALAyKVPEEDSPVQLG--SPLLGTVIEVRD-QNGSEGTGQVFLG---------GLNRVCILDdeVTVPKGTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 530 MKPypgyfffGDGAARDyDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVaETAVVGCADDltgQAVYAFVTMKPe 609
Cdd:cd17654 341 RAT-------GDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGES- 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
9C8S_C 610 fdlkatKEADLSKELaiqVRKVIGPFAAPKKIYLVSDLPKTRSGKI 655
Cdd:cd17654 408 ------SSSRIHKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
149-590 |
2.41e-09 |
|
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: 60.07 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 149 VSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIttd 228
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 229 egrrggktiatkqivdaalqqcplVENvlvlrrtgnkvpmtegrdkwwdeecakmpaycpcermASEDPLFILYTSGSTG 308
Cdd:cd17640 83 ------------------------VEN-------------------------------------DSDDLATIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 309 KPKGVVHSTAGYLLGTALTLKYVfDAHPDDRFACMADIgWitgHSY---IIYGPLANGITTAvfestpvYPTPSRYWDFV 385
Cdd:cd17640 102 NPKGVMLTHANLLHQIRSLSDIV-PPQPGDRFLSILPI-W---HSYersAEYFIFACGCSQA-------YTSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 386 DKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLG------------SVGEPINPEAWHWYNDFAGKnqcaIVDTYW 453
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLfflsggifkfgiSGGGALPPHVDTFFEAIGIE----VLNGYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 454 MTETGSISIAPLPGAIstKPGSATFPFFGMDVDIIDPQTGQVLEGNDvEGVLVARRpwPSIARTVYRD---HKRYLETym 530
Cdd:cd17640 246 LTETSPVVSARRLKCN--VRGSVGRPLPGTEIKIVDPEGNVVLPPGE-KGIVWVRG--PQVMKGYYKNpeaTSKVLDS-- 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 531 kpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVS-GHRLSTAEVESALILHKGVAETAVVG 590
Cdd:cd17640 319 ---DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
293-660 |
6.71e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 58.51 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 293 ASEDPLFILYTSGSTGKPKGVVHSTAGylLGTALTlKYVfdahpdDRFACMADIGWITG----HSY-IIYGPLAnGITTA 367
Cdd:PRK08308 99 LAEEPSLLQYSSGTTGEPKLIRRSWTE--IDREIE-AYN------EALNCEQDETPIVAcpvtHSYgLICGVLA-ALTRG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 368 vfeSTPVYPTPSRYWDFVDKWKATQ---LYTAPTAIRLLRRMGEDHVKNHdlsslRVLGSvGEPInPEAWhwyndFAG-K 443
Cdd:PRK08308 169 ---SKPVIITNKNPKFALNILRNTPqhiLYAVPLMLHILGRLLPGTFQFH-----AVMTS-GTPL-PEAW-----FYKlR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 444 NQCAIV-DTYWMTETGSISIAPlpgaISTKPGSATFPFFGMDVdiidpQTGQVlEGNDVEGVLVARRpwpsiaRTVY-RD 521
Cdd:PRK08308 234 ERTTYMmQQYGCSEAGCVSICP----DMKSHLDLGNPLPHVSV-----SAGSD-ENAPEEIVVKMGD------KEIFtKD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 522 HkryletymkpypGYFffgdgaarDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVY 601
Cdd:PRK08308 298 L------------GYK--------SERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 602 AFVTMKPEFDLkatkeadlskelaIQVR----KVIGPFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK08308 358 AKVISHEEIDP-------------VQLRewciQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
296-653 |
6.91e-09 |
|
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: 58.08 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 296 DPLFILYTSGSTGKPKGVVHSTAGyLLGTALTLkyvfdahpddrfacmADIGWITGHS-YIIYGPLAN------GITTAV 368
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA-LLAQALVL---------------AVLQAIDEGTvFLNSGPLFHigtlmfTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 369 FESTPVY---PTPSRYWDFVDKWKATQLYTAPTAIRLLRRMGEDhvKNHDLSSLRVLgsvgepinPEAWHWyndfagkNQ 445
Cdd:cd17636 65 AGGTNVFvrrVDAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSS--------PAAPEW-------ND 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 446 CAIVDT---------YWMTE-TGSISIAPLPGaisTKPGSATFPFFGMDVDIIDPqtgqvlEGNDVE----GVLVARRP- 510
Cdd:cd17636 128 MATVDTspwgrkpggYGQTEvMGLATFAALGG---GAIGGAGRPSPLVQVRILDE------DGREVPdgevGEIVARGPt 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 511 -----W--PSIARTVYRDhkryletymkpypGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGV 583
Cdd:cd17636 199 vmagyWnrPEVNARRTRG-------------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAV 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 584 AETAVVGCADDLTGQAVYAFVTMKPefDLKATKEadlskELAIQVRKVIGPFAAPKKIYLVSDLPKTRSG 653
Cdd:cd17636 266 ADAAVIGVPDPRWAQSVKAIVVLKP--GASVTEA-----ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
112-314 |
6.40e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.21 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 112 PEGTLNAaynCLDRHYYKNPKKTAIIYEAdepsesREVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFL 191
Cdd:PRK10252 456 PETTLSA---LVAQQAAKTPDAPALADAR------YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALH 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 192 ACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDE--GRRGGKTIATKQIVDAAlqqcplvenvlvlrrtgnkvpmt 269
Cdd:PRK10252 527 AIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADqlPRFADVPDLTSLCYNAP----------------------- 583
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9C8S_C 270 egrdkWWDeecakmPAYCPCERMASEDPLFILYTSGSTGKPKGVV 314
Cdd:PRK10252 584 -----LAP------QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVM 617
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
147-660 |
6.91e-08 |
|
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: 55.89 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 147 REVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLIT 226
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 227 TDEgrrggktiatkQIVDAALQ---QCPLVENVLV-------------LRRTGNKVPMTEGRDKWWDEECAKMPAycpce 290
Cdd:cd17641 90 EDE-----------EQVDKLLEiadRIPSVRYVIYcdprgmrkyddprLISFEDVVALGRALDRRDPGLYEREVA----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 291 RMASEDPLFILYTSGSTGKPKGVVHStAGYLLGTALTLKYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFE 370
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLS-HGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 371 STP--------VYPT----PSRYWD------------------FVDKWKATQLYTA----------PTAIRLLRRMGEDH 410
Cdd:cd17641 233 EPEtmmedlreIGPTfvllPPRVWEgiaadvrarmmdatpfkrFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 411 V----KNH-DLSSLRVLGSVGEPINPEAWHWYNDFaGKNqcaIVDTYWMTETGSISIAPLPGAIstKPGSATFPFFGMDV 485
Cdd:cd17641 313 LfrplRDRlGFSRLRSAATGGAALGPDTFRFFHAI-GVP---LKQLYGQTELAGAYTVHRDGDV--DPDTVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 486 DIIDpqtgqvlegndvEGVLVARRpwPSIARTVYRDHKRYLETYMKpyPGYFFFGDGAARDYDGYMWIKGRVDDVINVS- 564
Cdd:cd17641 387 RIDE------------VGEILVRS--PGVFVGYYKNPEATAEDFDE--DGWLHTGDAGYFKENGHLVVIDRAKDVGTTSd 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 565 GHRLSTAEVESALILHKGVAETAVVGCADDltgqAVYAFVTMKPEF--------DLKATKEADLSKELAIQ------VRK 630
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLGAGRP----YLTAFICIDYAIvgkwaeqrGIAFTTYTDLASRPEVYelirkeVEK 526
|
570 580 590
....*....|....*....|....*....|....*....
9C8S_C 631 VIGPFAAPKKIYLVSDLPK---------TRSGKIMRRVL 660
Cdd:cd17641 527 VNASLPEAQRIRRFLLLYKeldaddgelTRTRKVRRGVI 565
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
284-660 |
7.12e-08 |
|
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: 55.25 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 284 PAYcPCERMA--------------SEDPLFILYTSGSTGKPKGVV---HStagyLLGTALTLKYVFDAHPDDRFACMADI 346
Cdd:cd17645 80 PDY-PGERIAymladssakilltnPDDLAYVIYTSGSTGLPKGVMiehHN----LVNLCEWHRPYFGVTPADKSLVYASF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 347 GwitghsyiiygplangittavFESTpvyptpsrYWDFVDKWKA-TQLYTAPTAIRL----LRRMGEDH----------- 410
Cdd:cd17645 155 S---------------------FDAS--------AWEIFPHLTAgAALHVVPSERRLdldaLNDYFNQEgitisflptga 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 411 ------VKNHDLSSLRVLGSVGEPINPEAWHWYNDFaGKNQCAIVDTywmtetgSISIAPLPGAIST-KPGSATfpffgm 483
Cdd:cd17645 206 aeqfmqLDNQSLRVLLTGGDKLKKIERKGYKLVNNY-GPTENTVVAT-------SFEIDKPYANIPIgKPIDNT------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 484 DVDIIDPQTGQVLEGNDVEGVLVARrpwpSIART-VYRDH---KRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDD 559
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGE----GLARGyLNRPEltaEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 560 VINVSGHRLSTAEVESALILHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEAdlskelaiqVRKVIGPFAAPK 639
Cdd:cd17645 348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREW---------LKNDLPDYMIPT 418
|
410 420
....*....|....*....|.
9C8S_C 640 KIYLVSDLPKTRSGKIMRRVL 660
Cdd:cd17645 419 YFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
109-660 |
1.64e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 109 QWFPEGtlnaayncLDRHYYKNPKKTAIIYEADEpsesreVSYEELMQETCRVANVLKSYGVKKGDAVSIYLPMTWQAAA 188
Cdd:PRK05691 1131 AWLPEL--------LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLV 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 189 AFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVLITTDegrrggktiatkqivdAALQQCPLVENVLVlrrtgnkVPM 268
Cdd:PRK05691 1197 GLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS----------------HLLERLPQAEGVSA-------IAL 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 269 TEGR-DKWwdeecakmPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGylLGTALTL---KYVFDAhpDDRFACMA 344
Cdd:PRK05691 1254 DSLHlDSW--------PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA--LAERLQWmqaTYALDD--SDVLMQKA 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 345 DIG-----W------ITGHSYIIYGPLAngittavfestpvYPTPSRYWDFVDKWKATQLYTAPTAIRLLRrmgeDHVKN 413
Cdd:PRK05691 1322 PISfdvsvWecfwplITGCRLVLAGPGE-------------HRDPQRIAELVQQYGVTTLHFVPPLLQLFI----DEPLA 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 414 HDLSSLRVLGSVGEPINPE----------AWHWYNDFaGKNQCAIVDTYWMTETGSISIAPLpgaistkpGSatfPFFGM 483
Cdd:PRK05691 1385 AACTSLRRLFSGGEALPAElrnrvlqrlpQVQLHNRY-GPTETAINVTHWQCQAEDGERSPI--------GR---PLGNV 1452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 484 DVDIIDPQTGQVLEGNDVE----GVLVAR----RPWPSIARTVY----RDHKRYLETymkpypgyfffGDGAARDYDGYM 551
Cdd:PRK05691 1453 LCRVLDAELNLLPPGVAGElcigGAGLARgylgRPALTAERFVPdplgEDGARLYRT-----------GDRARWNADGAL 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 552 WIKGRVDDVINVSGHRLSTAEVESALILHKGVAEtAVVGCADDLTGQAVYAFVTMKPEFDLKAtkeADLSKELAIQVRKv 631
Cdd:PRK05691 1522 EYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAVLVREGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAELPE- 1596
|
570 580
....*....|....*....|....*....
9C8S_C 632 igpFAAPKKIYLVSDLPKTRSGKIMRRVL 660
Cdd:PRK05691 1597 ---YMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
279-668 |
1.80e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 279 ECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDAHPDDRfACmadiGWI-----TGHS 353
Cdd:PRK05851 136 TAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDV-GC----SWLplyhdMGLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 354 YIIYGPLAnGITTAVFESTPVYPTPSRYWDFVDKWKATqLYTAPT-AIRLLRRMGeDHVKNHDLSSLRVLGSVGEPINPE 432
Cdd:PRK05851 211 FLLTAALA-GAPLWLAPTTAFSASPFRWLSWLSDSRAT-LTAAPNfAYNLIGKYA-RRVSDVDLGALRVALNGGEPVDCD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 433 AwhwYNDFA------GKNQCAIVDTYWMTETGSISIAPLPGA------ISTKPGSAT-------FPFFGMDVDIIDPQTG 493
Cdd:PRK05851 288 G---FERFAtamapfGFDAGAAAPSYGLAESTCAVTVPVPGIglrvdeVTTDDGSGArrhavlgNPIPGMEVRISPGDGA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 494 QVLEGNDVEGVlvarrpwpSIARTvyrdhkryleTYMKPYPG--------YFFFGDGAardY--DGYMWIKGRVDDVINV 563
Cdd:PRK05851 365 AGVAGREIGEI--------EIRGA----------SMMSGYLGqapidpddWFPTGDLG---YlvDGGLVVCGRAKELITV 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 564 SGHRLSTAEVESALILHKGVAETAVVGCADDltGQAVYAFVTMKPEFdlKATKEADLSKELAIQVRKVIG--P----FAA 637
Cdd:PRK05851 424 AGRNIFPTEIERVAAQVRGVREGAVVAVGTG--EGSARPGLVIAAEF--RGPDEAGARSEVVQRVASECGvvPsdvvFVA 499
|
410 420 430
....*....|....*....|....*....|..
9C8S_C 638 PkkiylvSDLPKTRSGKIMR-RVLRKIVAGEG 668
Cdd:PRK05851 500 P------GSLPRTSSGKLRRlAVKRSLEAADG 525
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
144-361 |
3.88e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.44 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 144 SESREVSYEELMQetcRVANV---LKSYGVKKGDAVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCE 220
Cdd:PTZ00216 117 NETRYITYAELWE---RIVNFgrgLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 221 CKVLITtdegrrGGKTIAT--KQIVDAALQQCPLVENvlvlrrtgNKVPM---TEGRD--KWWD--EECAKMPAYCPCER 291
Cdd:PTZ00216 194 CKAIVC------NGKNVPNllRLMKSGGMPNTTIIYL--------DSLPAsvdTEGCRlvAWTDvvAKGHSAGSHHPLNI 259
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
9C8S_C 292 MASEDPL-FILYTSGSTGKPKGVVHsTAGYLLGTALTLKYVFdahpDDRFACMADigwitGHSYIIYGPLA 361
Cdd:PTZ00216 260 PENNDDLaLIMYTSGTTGDPKGVMH-THGSLTAGILALEDRL----NDLIGPPEE-----DETYCSYLPLA 320
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
145-689 |
6.38e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.21 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 145 ESREVSYEELMQETCRVANVLKSY-GVKKGDAVSIYL---PM---TWqaaaaflacarIGAIHSAVFAGFSAESLRDR-- 215
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLgnePAflwIW-----------LGLAKLGCPVAFLNTNIRSKsl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 216 VNDCECKvlittdegrrGGKTIatkqIVDAALQqcPLVENVLV-LRRTGNKVPM------TEGRDKWWDE-ECA---KMP 284
Cdd:cd05938 71 LHCFRCC----------GAKVL----VVAPELQ--EAVEEVLPaLRADGVSVWYlshtsnTEGVISLLDKvDAAsdePVP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 285 AYCPCERMASEDPLFIlYTSGSTGKPKGVVHSTAGYLLGTALTlkYVFDAHPDDR-FACMA---DIGWITGhsyiIYGPL 360
Cdd:cd05938 135 ASLRAHVTIKSPALYI-YTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDViYITLPlyhSSGFLLG----IGGCI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 361 ANGITTAV---FEStpvyptpSRYWDFVDKWKATQLYTAPTAIRLLRRMGE-DHVKNHdlsslRVLGSVGEPINPEAWHW 436
Cdd:cd05938 208 ELGATCVLkpkFSA-------SQFWDDCRKHNVTVIQYIGELLRYLCNQPQsPNDRDH-----KVRLAIGNGLRADVWRE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 437 YNDFAGKNQcaIVDTYWMTEtGSISIAPLPGaistKPGSA---------TFPFfgmdvDII--DPQTGQVLEGND----- 500
Cdd:cd05938 276 FLRRFGPIR--IREFYGSTE-GNIGFFNYTG----KIGAVgrvsylyklLFPF-----ELIkfDVEKEEPVRDAQgfcip 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 501 VE----GVLVAR----RPWPSIARTVYRDHKRYLETYMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAE 572
Cdd:cd05938 344 VAkgepGLLVAKitqqSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 573 VESALILHKGVAETAVVG-CADDLTGQAVYAFVTMKP--EFDLKATKEadlskelaiQVRKVIGPFAAPKKIYLVSDLPK 649
Cdd:cd05938 424 VADVLGLLDFLQEVNVYGvTVPGHEGRIGMAAVKLKPghEFDGKKLYQ---------HVREYLPAYARPRFLRIQDSLEI 494
|
570 580 590 600
....*....|....*....|....*....|....*....|
9C8S_C 650 TRSGKIMRRVLRKivagEGdqlGDLSSIADPQIVEEVKQK 689
Cdd:cd05938 495 TGTFKQQKVRLVE----EG---FNPSIISDPLYFLDETQK 527
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
294-370 |
6.45e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.14 E-value: 6.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C8S_C 294 SEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVFDA-HPDDRfacmadigwitghsYIIYGPLANgittaVFE 370
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDR--------------YLAYLPLAH-----IFE 145
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
299-660 |
1.44e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 299 FILYTSGSTGKPKGVVHSTAGYLLGTALTLKyVFDAHPDDrfaCMAdigwitgHSYII---------YGPLANG------ 363
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL-------HFYSInfdaaserlLVPLLCGarvvlr 2405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 364 ---------ITTAVFES--TPVYPTPSrYWDFVDKWKATQLYTAPtairllrrmgedhvknhdlssLRVLGSVGEPINPE 432
Cdd:PRK05691 2406 aqgqwgaeeICQLIREQqvSILGFTPS-YGSQLAQWLAGQGEQLP---------------------VRMCITGGEALTGE 2463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 433 awHWYNDFAGKNQCAIVDTYWMTETGSISIAPLPGAiSTKPGSATFPF---------FGMDVDI-IDPQ--TGQVLEGnd 500
Cdd:PRK05691 2464 --HLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPE-QLEEGAASVPIgrvvgarvaYILDADLaLVPQgaTGELYVG-- 2538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 501 veGVLVAR----RPWPSIARTV----YRDHKRYLETymkpypgyfffGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAE 572
Cdd:PRK05691 2539 --GAGLAQgyhdRPGLTAERFVadpfAADGGRLYRT-----------GDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 573 VESALILHKGVAETAVVgcADDLTG--QAVYAFVTMKPEFDLKAtkEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKT 650
Cdd:PRK05691 2606 IESRLLEHPAVREAVVL--ALDTPSgkQLAGYLVSAVAGQDDEA--QAALREALKAHLKQQLPDYMVPAHLILLDSLPLT 2681
|
410
....*....|
9C8S_C 651 RSGKIMRRVL 660
Cdd:PRK05691 2682 ANGKLDRRAL 2691
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
447-652 |
1.56e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 48.56 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 447 AIVDTYWMTETGSISIAPLPGAistKPGSATFPFFG---MDVDIIDPQTGQVLEGND-----VE----GVLVARRPWP-- 512
Cdd:PRK07868 745 AHVVEFFATTDGQAVLANVSGA---KIGSKGRPLPGagrVELAAYDPEHDLILEDDRgfvrrAEvnevGVLLARARGPid 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 513 ---SIARTVYRDHKRYLETymkpypGYFFfgdgaARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAETAVV 589
Cdd:PRK07868 822 ptaSVKRGVFAPADTWIST------EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTY 890
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9C8S_C 590 GCADDLTGQAVYAfVTMKPEFDLKATKEADLSKELAIQVRkvigpfaaPKKIYLVSDLPKTRS 652
Cdd:PRK07868 891 GVEVGGRQLAVAA-VTLRPGAAITAADLTEALASLPVGLG--------PDIVHVVPEIPLSAT 944
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
448-664 |
2.15e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 448 IVDTYWMTET----GSISI--------APLP-GaiSTKPGSATFpffgmdvdIIDPQTGQVLEGNDVEGVLVArrpwPSI 514
Cdd:PRK04813 289 IYNTYGPTEAtvavTSIEItdemldqyKRLPiG--YAKPDSPLL--------IIDEEGTKLPDGEQGEIVISG----PSV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 515 ArtvyrdhKRYLETYMKPYPGYFFF--------GDGAARDyDGYMWIKGRVDDVINVSGHRLSTAEVESALILHKGVAET 586
Cdd:PRK04813 355 S-------KGYLNNPEKTAEAFFTFdgqpayhtGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESA 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C8S_C 587 AVVGCADDLTGQAVYAFVTMKP-EFDlkatKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIV 664
Cdd:PRK04813 427 VVVPYNKDHKVQYLIAYVVPKEeDFE----REFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEV 501
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
509-687 |
8.92e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 45.14 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 509 RPWPSIARTVYRDHKRyletymkpypGYFFFGDGaardydgymwiKGRVDDVINVsGHRLStaeveSALILHKGVAETAV 588
Cdd:PRK09188 208 RIWLATGKKVYNFITR----------GLFSWSDG-----------EGTGDRIDNE-APAIQ-----AALKSDPAVSDVAI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 589 VGCADDLTGQAVYAFVtmkpEFDLKATKEAdLSKELAIQvrkviGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEG 668
Cdd:PRK09188 261 ALFSLPAKGVGLYAFV----EAELPADEKS-LRARLAGA-----KPPKPPEHIQPVAALPRDADGTVRDDILRLIAMNQI 330
|
170
....*....|....*....
9C8S_C 669 DQLGDLssIADPQIVEEVK 687
Cdd:PRK09188 331 DELDDL--LREPEIRGLVE 347
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
275-660 |
2.30e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 275 WWDEECAKMPAYCPCERMASEDPLFILYTSGSTGKPKGVVHSTAGYLLGTALTLKYVfdaHPDDRFAcmadIGWITGHSY 354
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL---ALSEADV----IAQTASQSF 3921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 355 II--YGPLANGITTAVFESTP--VYPTPSRYWDFVDKWKATQLYTAPTAIRllRRMGEDHVKnhdLSSLRVLGSVGEPIN 430
Cdd:PRK05691 3922 DIsvWQFLAAPLFGARVEIVPnaIAHDPQGLLAHVQAQGITVLESVPSLIQ--GMLAEDRQA---LDGLRWMLPTGEAMP 3996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 431 PE-AWHWYNDFAgknQCAIVDTYWMTETGS------ISIAPLPGA---ISTKPGSATFPFFGMDVDIIdPQtGQVLEGNd 500
Cdd:PRK05691 3997 PElARQWLQRYP---QIGLVNAYGPAECSDdvaffrVDLASTRGSylpIGSPTDNNRLYLLDEALELV-PL-GAVGELC- 4070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 501 VEGVLVARRPWPSIART--VYRDHkryletymkPY--PGYFFF--GDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVE 574
Cdd:PRK05691 4071 VAGTGVGRGYVGDPLRTalAFVPH---------PFgaPGERLYrtGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIE 4141
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C8S_C 575 SALILHKGVAEtAVVGCADDLTGQAVYAFVTMKPefdlKATKEADLSKELAIQVRKVIGPFAAPKKIYLVSDLPKTRSGK 654
Cdd:PRK05691 4142 ARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQ----TVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
....*.
9C8S_C 655 IMRRVL 660
Cdd:PRK05691 4217 LDRKAL 4222
|
|
| |
