|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
16-660 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1108.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 16 FDPSREmeqkILDQANLTAEKYEQACRMATDSPEEFWADRARDLlHWTRDFRTTLesDPEKHEYKWFSGGRLNASYNCLD 95
Cdd:PRK00174 2 FPPPAE----FAANALIDMEQYKALYQESVEDPEGFWAEQAKRL-DWFKPFDTVL--DWNAPFIKWFEDGELNVSYNCLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 96 RHLENgRRNKAALIWQGEPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVI 175
Cdd:PRK00174 75 RHLKT-RGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 176 FAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEISGP 255
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVDWVEGRDLWWHELVAGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 256 DieDYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLA 335
Cdd:PRK00174 234 S--DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATTLLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHV 415
Cdd:PRK00174 312 NGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 416 GKGKLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDIHNDRA 495
Cdd:PRK00174 392 GGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 496 RYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAY 575
Cdd:PRK00174 472 RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 576 VTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGENDLGDTTTLSDASVIADLIE 655
Cdd:PRK00174 552 VTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKLIE 631
|
....*
gi 1816261920 656 GQKEL 660
Cdd:PRK00174 632 ARQNR 636
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
35-646 |
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: 1067.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 35 EKYEQACRMATDSPEEFWADRARDLlHWTRDFRTTLESDPEKHEYKWFSGGRLNASYNCLDRHLENgRRNKAALIWQGEP 114
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKEL-DWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 115 EEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAK 194
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEIsgPDIEDYCKPESMRSADPLFI 274
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLM--AKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYPRPDR 354
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLDTWWQTETGSI 434
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 LISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDIHNDRARYNRTYFERFPGSYETGDG 514
Cdd:cd05966 397 MITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 515 ARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLRE 594
Cdd:cd05966 477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRK 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 595 WVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGENDLGDTTTLSD 646
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
33-655 |
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: 1032.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 33 TAEKYEQACRMATDSPEEFWADRARDLLHWTRDFRTTLESDPEKHeYKWFSGGRLNASYNCLDRHLENgRRNKAALIWQG 112
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPPF-YKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 113 EPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCD 192
Cdd:TIGR02188 81 DEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 193 AKILIAADGVLRGGKKIPLKRNVDEALFECP-SVEQVIMVKRTGDEID-FIEGRDTWWHEEISGPDieDYCKPESMRSAD 270
Cdd:TIGR02188 161 AKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKAS--AYCEPEPMDSED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 271 PLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYP 350
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 351 RPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLDTWWQTE 430
Cdd:TIGR02188 319 DPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 TGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAE-ANEGGHLLITEPWPGMLTDIHNDRARYNRTYFERFPGSY 509
Cdd:TIGR02188 399 TGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 510 ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMR 589
Cdd:TIGR02188 479 FTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELR 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 590 TVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEND-LGDTTTLSDASVIADLIE 655
Cdd:TIGR02188 559 KELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEiLGDTSTLEDPSVVEELIE 625
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
80-655 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 903.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 80 KWFSGGRLNASYNCLDRHLEnGRRNKAALIWQGEPEEEvRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELV 159
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEGEDGEE-RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 160 ISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEID 239
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 240 FiEGrDTWWHEEISGPDieDYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTAD 319
Cdd:COG0365 159 M-EG-DLDWDELLAAAS--AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 320 IGWITGHSYTVYGPLALGATTLLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSV 399
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 400 GEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILISPLPyVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLI 479
Cdd:COG0365 315 GEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLP-GLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 480 TEPWPGMLTDIHNDRARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAA 559
Cdd:COG0365 391 KGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 560 VVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEnDLG 639
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLG 549
|
570
....*....|....*.
gi 1816261920 640 DTTTLSDASVIADLIE 655
Cdd:COG0365 550 DTSTLEDPEALDEIKE 565
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
37-624 |
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: 732.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 37 YEQACRMATDSPEEFWADRARDL-LHWTRDFRTTLESDPEKHEYKWFSGGRLNASYNCLDRHLENgRRNKAALIWQGEPE 115
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILdWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRE-NGDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 116 EEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKI 195
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 196 LIAADGVLRGGKKIPLKRNVDEAL-FECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEISGPDIEDycKPESMRSADPLFI 274
Cdd:cd17634 160 LITADGGVRAGRSVPLKKNVDDALnPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEH--QPEAMNAEDPLFI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYPRPDR 354
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLDTWWQTETGSI 434
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 LISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDIHNDRARYNRTYFERFPGSYETGDG 514
Cdd:cd17634 398 MITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 515 ARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLRE 594
Cdd:cd17634 478 ARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRN 557
|
570 580 590
....*....|....*....|....*....|
gi 1816261920 595 WVSQKIGPIAVPETIQFSEGLPKTRSGKIM 624
Cdd:cd17634 558 WVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
7-655 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 695.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 7 ENLMSEQRT-FDPSREMEQKILDQanlTAEKYEQACRMATDSPEEFWADRARDLL---HWTRDFRTTLESDPEKHEYK-- 80
Cdd:PLN02654 4 ESLASEENDlVFPSKDFSAQALVS---SPQQYMEMYKRSVDDPAGFWSDIASQFYwkqKWEGDEVCSENLDVRKGPISie 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 81 WFSGGRLNASYNCLDRHLENGRRNKAALIWQG-EPEEEVRVfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELV 159
Cdd:PLN02654 81 WFKGGKTNICYNCLDRNVEAGNGDKIAIYWEGnEPGFDASL-TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 160 ISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFE----------CPSVEQVI 229
Cdd:PLN02654 160 IAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDEsakngvsvgiCLTYENQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 230 MVKRtgDEIDFIEGRDTWWHEEIsgPDIEDYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLR 309
Cdd:PLN02654 240 AMKR--EDTKWQEGRDVWWQDVV--PNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 310 DDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYD 389
Cdd:PLN02654 316 PTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 390 LSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDA 469
Cdd:PLN02654 396 RKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 470 EANEGGHLLITEPWPGMLTDIHNDRARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESAL 549
Cdd:PLN02654 476 EGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 550 IAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PLN02654 556 VSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
650 660
....*....|....*....|....*..
gi 1816261920 630 RIAVGE-NDLGDTTTLSDASVIADLIE 655
Cdd:PLN02654 636 KIASRQlDELGDTSTLADPGVVDQLIA 662
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
37-653 |
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: 649.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 37 YEQACRMATDSPEEFWADRARdLLHWTRDFRTTLESDpEKHEYKWFSGGRLNASYNCLDRHLENGRRNKAALIWQGEPEE 116
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 117 EVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKIL 196
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 197 IAADGVLRGGKKIPLKRNVDEALFECPS-VEQVIMVKRTGDEIDFIE-GRDTWWHEEISGPDIEDyCKPesMRSADPLFI 274
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALELSGHkPHHVLVLNRPQVPADLTKpGRDLDWSELLAKAEPVD-CVP--VAATDPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPT-YPRPD 353
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 RYWEIINRYGVNIFYTTPTALRALRREGTQWT--EKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgklPLLDTWWQTET 431
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKyiKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTET 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 432 GSILISPLPYVGKL--KPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPW-PGMLTDIHNDRARYNRTYFERFPGS 508
Cdd:cd05967 393 GWPITANPVGLEPLpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGL-DEDDE 587
Cdd:cd05967 473 YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVkITAEE 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 588 MRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEnDLGDTTTLSDASVIADL 653
Cdd:cd05967 553 LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
34-651 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 587.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 34 AEKYEQACRMATDSPEEFWADRARdLLHWTRDFRTTLE-SDPEKHeyKWFSGGRLNASYNCLDRHLEnGRRNKAALIWQG 112
Cdd:PRK10524 1 MMSYSEFYQRSIDDPEAFWAEQAR-RIDWQTPFTQVLDySNPPFA--RWFVGGRTNLCHNAVDRHLA-KRPEQLALIAVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 113 EPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCD 192
Cdd:PRK10524 77 TETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 193 AKILIAADGVLRGGKKIPLKRNVDEALFECPSV-EQVIMVKRTGDEIDFIEGRD---TWWHEEISGPDIEdyckPESMRS 268
Cdd:PRK10524 157 PVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKpRHVLLVDRGLAPMARVAGRDvdyATLRAQHLGARVP----VEWLES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 269 ADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPT 348
Cdd:PRK10524 233 NEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 349 YPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgklPLLDTWWQ 428
Cdd:PRK10524 313 RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TETGSILISPLPYVGKL--KPGSTGKPLPGISAKIVN-SDGSDAEANEGGHLLITEPW-PGMLTDIHNDRARYNRTYFER 504
Cdd:PRK10524 390 TETGWPILAIARGVEDRptRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 505 FPGS-YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLR--SG 581
Cdd:PRK10524 470 FGRQvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKdsDS 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 582 LDEDDEMRTV---LREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEnDLGDTTTLSDASVIA 651
Cdd:PRK10524 550 LADREARLALekeIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGR-DPGDLTTIEDPAALQ 621
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
30-646 |
0e+00 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 542.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 30 ANLTAEKYEQACRMATDSPEEFWADRARDLLHWTRD-FRTTLESDPEKHEYKWFSGGRLNASYNCLDRHLENgRRNKAAL 108
Cdd:cd05968 2 ASLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEpPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWLAD-TRTRPAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 109 IWQGEpEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRI 188
Cdd:cd05968 81 RWEGE-DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 189 IDCDAKILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEISGPDIEdyckPESMRS 268
Cdd:cd05968 160 QDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDG----AERTES 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 269 ADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDD-VHWCTaDIGWITGhSYTVYGPLALGATTLLFEGVP 347
Cdd:cd05968 236 EDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 348 TYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLDTWW 427
Cdd:cd05968 314 DHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 428 QTET-----GSILISPLpyvgklKPGSTGKPLPGISAKIVNSDGSDAEANEGgHLLITEPWPGMLTDIHNDRARYNRTYF 502
Cdd:cd05968 394 GTEIsggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPARPEVG-ELVLLAPWPGMTRGFWRDEDRYLETYW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 503 ERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGL 582
Cdd:cd05968 467 SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 583 DEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEnDLGDTTTLSD 646
Cdd:cd05968 547 TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK-ELGDLSSLEN 609
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-646 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 525.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 76 KHEYKWFSGGRLNASYNCLDRHLENGRRNKAALIWQGEpeEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMV 155
Cdd:PRK04319 31 EKEFSWLETGKVNIAYEAIDRHADGGRKDKVALRYLDA--SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 156 PELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLRggkKIPLKrnvdealfECPSVEQVIMVkrtG 235
Cdd:PRK04319 109 PELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE---RKPAD--------DLPSLKHVLLV---G 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 236 DEIDFIEGRDTWWHEEISGPD---IEdYCKPESMrsadplFILH-TSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDD 311
Cdd:PRK04319 175 EDVEEGPGTLDFNALMEQASDefdIE-WTDREDG------AILHyTSGSTGKPKGVLHVHNA-MLQHYQTGKYVLDLHED 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 312 DVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTyprPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLS 391
Cdd:PRK04319 247 DVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 392 TLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILISPLPYVgKLKPGSTGKPLPGISAKIVNSDGSDAEA 471
Cdd:PRK04319 324 SLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAM-DIKPGSMGKPLPGIEAAIVDDQGNELPP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEPWPGMLTDIHNDRARYNRtYFErfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIA 551
Cdd:PRK04319 400 NRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLME 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 552 HPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRri 631
Cdd:PRK04319 477 HPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK-- 554
|
570
....*....|....*..
gi 1816261920 632 aVGENDL--GDTTTLSD 646
Cdd:PRK04319 555 -AWELGLpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-633 |
2.01e-154 |
|
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: 453.11 E-value: 2.01e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAad 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 gvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwHEEISgpdiedyckpESMRSADPLFILHTSGS 280
Cdd:cd05969 79 ------------------------------------------------TEELY----------ERTDPEDPTLLHYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTyprPDRYWEIIN 360
Cdd:cd05969 101 TGTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 361 RYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILISPLP 440
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 441 YVgKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDIHNDRARYNRTYFErfpGSYETGDGARVDED 520
Cdd:cd05969 254 CM-PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFID---GWYLTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 521 GDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKI 600
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKL 409
|
490 500 510
....*....|....*....|....*....|...
gi 1816261920 601 GPIAVPETIQFSEGLPKTRSGKIMRRILRRIAV 633
Cdd:cd05969 410 GAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-629 |
9.95e-129 |
|
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: 386.69 E-value: 9.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIaad 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 gvlrggkkiplkrnvdealfecpsveqvimvkrTGDEidfiegrdtwwheeisgpdiedyckpesmrsaDPLFILHTSGS 280
Cdd:cd05972 78 ---------------------------------TDAE--------------------------------DPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVHsTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYPRpdRYWEIIN 360
Cdd:cd05972 93 TGLPKGVLH-THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 361 RYGVNIFYTTPTALRALRREGTqwtEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGsILISPLP 440
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDL---SSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LTVGNFP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 441 YVgKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDIHNDRARYNRTYFErfpGSYETGDGARVDED 520
Cdd:cd05972 243 DM-PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDED 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 521 GDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKI 600
Cdd:cd05972 319 GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVL 398
|
490 500
....*....|....*....|....*....
gi 1816261920 601 GPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05972 399 APYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
94-632 |
1.18e-102 |
|
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: 320.22 E-value: 1.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENgRRNKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHS 173
Cdd:COG0318 5 LRRAAAR-HPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 174 VIFAGFSAVSLQNRIIDCDAKILIAAdgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeis 253
Cdd:COG0318 78 PLNPRLTAEELAYILEDSGARALVTA------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 254 gpdiedyckpesmrsadplFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWvFDLRDDDVHWCTADIGWITGHSYTVYGP 333
Cdd:COG0318 104 -------------------LILYTSGTTGRPKGVMLTHRNLLANAAAIAAA-LGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 334 LALGATTLLfegvPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPINPEVWIWFHE 413
Cdd:COG0318 164 LLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 HVGkgkLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPgMLTdIHND 493
Cdd:COG0318 238 RFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNV-MKG-YWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RARYNRTYFERFpgsYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVY 573
Cdd:COG0318 313 PEATAEAFRDGW---LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 574 AYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:COG0318 390 AFVVLRPGaeLDAEE-----LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
270-624 |
6.78e-100 |
|
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: 308.83 E-value: 6.78e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWvFDLRDDDVHWCTADIGWItGHSYTVYGPLALGATTLLFEGvpty 349
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 PRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQT 429
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPgMLTdIHNDRARynrTYFERFPGSY 509
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV-MKG-YWNNPEA---TAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 510 ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMr 589
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEE- 303
|
330 340 350
....*....|....*....|....*....|....*
gi 1816261920 590 tvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIM 624
Cdd:cd04433 304 --LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-536 |
1.74e-99 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 310.78 E-value: 1.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 117 EVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKIL 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 197 IAADgvlrggkkIPLKRNVDEALFECPSVEQVIMvkrtgdeIDFIEGRDTWWHEEISGPDIEDYCKPESMRSADPLFILH 276
Cdd:pfam00501 98 ITDD--------ALKLEELLEALGKLEVVKLVLV-------LDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 277 TSGSTGKAKGVVHSTGGY---MTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTyPRPD 353
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 RYWEIINRYGVNIFYTTPTALRALRREGTQWTEkyDLSTLRILGSVGEPINPEVWIWFHEHVGKgklPLLDTWWQTETGS 433
Cdd:pfam00501 242 ALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPPELARRFRELFGG---ALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 434 ILISPLPYVGKL-KPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEpwPGMLTDIHNDRARYNRTYFErfPGSYET 511
Cdd:pfam00501 317 VVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRG--PGVMKGYLNDPELTAEAFDE--DGWYRT 392
|
410 420
....*....|....*....|....*
gi 1816261920 512 GDGARVDEDGDYWIMGRLDDVINVS 536
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
28-628 |
3.29e-98 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 314.81 E-value: 3.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 28 DQANLTAEKYEQACRMATDSPEEFWADrardllhwTRDF--------RTTLESDPEKHEYKWFSGGRLNASYNCLdRHle 99
Cdd:PRK03584 27 ARRGLSFDDYAALWRWSVEDLEAFWQS--------VWDFfgvigstpYTVVLAGRRMPGARWFPGARLNYAENLL-RH-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 100 nGRRNKAALIWQGEPEEEVRVfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGF 179
Cdd:PRK03584 96 -RRDDRPAIIFRGEDGPRREL-SWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 180 SAVSLQNRIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEIDF--IEGRDTWwhEEISGPDI 257
Cdd:PRK03584 174 GVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAaaLPGALLW--EDFLAPAE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 258 EDYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGG----YMTATA-HTtqwvfDLRDDD-VHWCTAdIGWITgHSYTVY 331
Cdd:PRK03584 252 AAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGilleHLKELGlHC-----DLGPGDrFFWYTT-CGWMM-WNWLVS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 GpLALGATTLLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWF 411
Cdd:PRK03584 325 G-LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 412 HEHVGKgklpllDTWWQTETGS-------ILISP-LP-YVGKLKpgstGKPLpGISAKIVNSDGSdAEANEGGHLLITEP 482
Cdd:PRK03584 404 YEHVKA------DVWLASISGGtdicscfVGGNPlLPvYRGEIQ----CRGL-GMAVEAWDEDGR-PVVGEVGELVCTKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 483 WPGMLTDIHND--RARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAV 560
Cdd:PRK03584 472 FPSMPLGFWNDpdGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLV 551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 561 VGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIM----RRIL 628
Cdd:PRK03584 552 IGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
31-636 |
1.42e-96 |
|
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: 309.97 E-value: 1.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 31 NLTAEKYEQACRMATDSPEEFWADrardLLHWT-----RDFRTTLESDPEKHEYKWFSGGRLNASYNCLdRHLENGRrnk 105
Cdd:cd05943 13 GLSLADYAALHRWSVDDPGAFWAA----VWDFSgvrgsKPYDVVVVSGRIMPGARWFPGARLNYAENLL-RHADADD--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 106 AALIWQGEpEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQ 185
Cdd:cd05943 85 PAAIYAAE-DGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 186 NRIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDE--IDFIE-GRDTWWHEEIS-GPDIEDYc 261
Cdd:cd05943 164 DRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAgqPDLSKiAKALTLEDFLAtGAAGELE- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 262 kPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTA--TAHTTQWvfDLRDDDV-HWCTAdIGWITGHsYTVYGpLALGA 338
Cdd:cd05943 243 -FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQhlKEHILHC--DLRPGDRlFYYTT-CGWMMWN-WLVSG-LAVGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 339 TTLLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKg 418
Cdd:cd05943 317 TIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 419 klpllDTWWQTETG-------SILISPLPYVGklkPGSTGKPLPGISAKIVNSDGsDAEANEGGHLLITEPWPGMLTDIH 491
Cdd:cd05943 396 -----DVLLASISGgtdiiscFVGGNPLLPVY---RGEIQCRGLGMAVEAFDEEG-KPVWGEKGELVCTKPFPSMPVGFW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 492 ND--RARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKG 569
Cdd:cd05943 467 NDpdGSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 570 QTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEN 636
Cdd:cd05943 547 ERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRP 613
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-630 |
1.88e-93 |
|
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: 295.97 E-value: 1.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAad 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 gvlrggkkiplkrNVDEAlfecpsveqvimvkrtgDEIDfiegrdtwwheeisgpdiedyckpesmrsADPLFILHTSGS 280
Cdd:cd05973 79 -------------DAANR-----------------HKLD-----------------------------SDPFVMMFTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVH------STGGYMtatahttQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTyprPDR 354
Cdd:cd05973 100 TGLPKGVPVplralaAFGAYL-------RDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFS---VES 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLStLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSI 434
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 LISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLItepwpgmltDIHNDRARYNRTYFER----FPGS-Y 509
Cdd:cd05973 246 LANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAI---------DIANSPLMWFRGYQLPdtpaIDGGyY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 510 ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMR 589
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816261920 590 TVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:cd05973 397 DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
37-628 |
2.92e-90 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 293.96 E-value: 2.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 37 YEQACRMATDSPEEFWADRARDLLHWTRDFRTTLESD---PEkheykWFSGGRLNASYNCLDRHLENG-RRNKAALIWQG 112
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDeiyPD-----WFKGGELNTCYNVLDIHVKNPlKRDQDALIYEC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 113 EPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCD 192
Cdd:PTZ00237 85 PYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 193 AKILIAADGVLRGGKKIPLKRNVDEAL----FEcPSveQVIMVKRTGDEID----FIEGRDTW-----WHEEISGPDiED 259
Cdd:PTZ00237 165 PKLIITTNYGILNDEIITFTPNLKEAIelstFK-PS--NVITLFRNDITSEsdlkKIETIPTIpntlsWYDEIKKIK-EN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 260 YCKP----ESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYtVYGPLA 335
Cdd:PTZ00237 241 NQSPfyeyVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYGSLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATTLLFEGVPTYPR--PDRYWEIINRYGVNIFYTTPTALRALRR---EGTQWTEKYDLSTLRILGSVGEPINPEVWIW 410
Cdd:PTZ00237 320 LGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpEATIIRSKYDLSNLKEIWCGGEVIEESIPEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 411 FHEhvgKGKLPLLDTWWQTETGSILIspLPYVGKLKPGST-GKPLPGISAKIVNSDGSDAEANEGGHLLITEPWP-GMLT 488
Cdd:PTZ00237 400 IEN---KLKIKSSRGYGQTEIGITYL--YCYGHINIPYNAtGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFAT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 DIHNDRARYNRTyFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIK 568
Cdd:PTZ00237 475 TFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDC 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 569 GQTVYAYVTLRSGLDED----DEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PTZ00237 554 YNVPIGLLVLKQDQSNQsidlNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
94-629 |
3.50e-89 |
|
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: 286.96 E-value: 3.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENGRRNKAALIwqgepeEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHS 173
Cdd:cd05959 9 VDLNLNEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 174 VIFAGFSAVSLQNRIIDCDAKILIAADgvlrggkkiPLKRNVDEALFE-CPSVEQVIMVKRTGDEIDFIEGRDTWWHEEI 252
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKsEHTLVVLIVSGGAGPEAGALLLAELVAAEAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 253 SGPdiedyckPESMRSADPLFILHTSGSTGKAKGVVHsTGGYMTATAHT-TQWVFDLRDDDVHWCTADIGWITGHSYTVY 331
Cdd:cd05959 154 QLK-------PAATHADDPAFWLYSSGSTGRPKGVVH-LHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 GPLALGATTLLFEGVPTyprPDRYWEIINRYGVNIFYTTPTALRA-LRREGTQwteKYDLSTLRILGSVGEPINPEVWIW 410
Cdd:cd05959 226 FPLSVGATTVLMPERPT---PAAVFKRIRRYRPTVFFGVPTLYAAmLAAPNLP---SRDLSSLRLCVSAGEALPAEVGER 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 411 FHEHVGkgkLPLLDTWWQTETGSILISPLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDI 490
Cdd:cd05959 300 WKARFG---LDILDGIGSTEMLHIFLSNRP--GRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGP--SSATMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 491 HNDRARYNRTyferFPGS-YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKG 569
Cdd:cd05959 373 WNNRDKTRDT----FQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 570 QTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05959 449 TKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
88-637 |
1.28e-88 |
|
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: 286.31 E-value: 1.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 88 NASYNCLDRhLENGRRNKAALIWQGEPEEEvRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACAR 167
Cdd:cd05970 17 NFAYDVVDA-MAKEYPDKLALVWCDDAGEE-RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 168 IGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGvlrggKKIPlkRNVDEALFECPSVEQVIMVkrtGDEIdfiegRDTW 247
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE-----DNIP--EEIEKAAPECPSKPKLVWV---GDPV-----PEGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 248 --WHEEI--SGPDIEDYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGgYMTATAHTTQWVFDLRDDDVHWCTADIGWI 323
Cdd:cd05970 160 idFRKLIknASPDFERPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 324 TGHSYTVYGPLALGATTLLFEgvptYPR--PDRYWEIINRYGVNIFYTTPTALRALRREGTqwtEKYDLSTLRILGSVGE 401
Cdd:cd05970 239 KAVWGKIYGQWIAGAAVFVYD----YDKfdPKALLEKLSKYGVTTFCAPPTIYRFLIREDL---SRYDLSSLRYCTTAGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVWIWFHEHVGkgkLPLLDTWWQTETgSILISPLPYVgKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLI-- 479
Cdd:cd05970 312 ALNPEVFNTFKEKTG---IKLMEGFGQTET-TLTIATFPWM-EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrt 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 480 TEPWP-GMLTDIHNDRARYNRTYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEA 558
Cdd:cd05970 387 SKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 559 AVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKImrrilRRIAVGEND 637
Cdd:cd05970 464 AVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-----RRVEIRERD 537
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
111-630 |
1.40e-84 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 272.77 E-value: 1.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 111 QGEPEEevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIID 190
Cdd:cd05971 1 KGTPEK----VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 191 CDAKILIAaDGvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmrSAD 270
Cdd:cd05971 77 SGASALVT-DG------------------------------------------------------------------SDD 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 271 PLFILHTSGSTGKAKGVVHstgGYMTATAH--TTQWVFDL--RDDDVHWCTADIGWItghsytvyGPLALGATTLLFEGV 346
Cdd:cd05971 90 PALIIYTSGTTGPPKGALH---AHRVLLGHlpGVQFPFNLfpRDGDLYWTPADWAWI--------GGLLDVLLPSLYFGV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 PTYPR------PDRYWEIINRYGVNIFYTTPTALRALRREGTQwTEKYDLStLRILGSVGEPINPEVWIWFHEHVGkgkL 420
Cdd:cd05971 159 PVLAHrmtkfdPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ-LKHAQVK-LRAIATGGESLGEELLGWAREQFG---V 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQTEtGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWP-GMLTDIHNDRARYnr 499
Cdd:cd05971 234 EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPvAFLGYWNNPSATE-- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 tyfERFPGSY-ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTL 578
Cdd:cd05971 311 ---KKMAGDWlLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 579 RSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:cd05971 388 NPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
99-629 |
1.47e-72 |
|
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: 243.91 E-value: 1.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 99 ENGRRNKAALIWQGEPEEEVRvFTYHMLHRKVCRFANVLKKI-GVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFA 177
Cdd:cd05928 21 AGKRPPNPALWWVNGKGDEVK-WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 178 GFSAVSLQNRIIDCDAKILIAADGVlrggkkIPLkrnVDEALFECPSVEQVIMVKRtgdeidfiEGRDTW--WHEEISGP 255
Cdd:cd05928 100 QLTAKDILYRLQASKAKCIVTSDEL------APE---VDSVASECPSLKTKLLVSE--------KSRDGWlnFKELLNEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 256 DIEDYCKpeSMRSADPLFILHTSGSTGKAKGVVHSTGGY-MTATAHTTQWVfDLRDDDVHWCTADIGWITGHSYTVYGPL 334
Cdd:cd05928 163 STEHHCV--ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWL-DLTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 335 ALGATTLlfegVPTYPR--PDRYWEIINRYGVNIFYTTPTALRALRREGTQwteKYDLSTLRILGSVGEPINPEVWIWFH 412
Cdd:cd05928 240 IQGACVF----VHHLPRfdPLVILKTLSSYPITTFCGAPTVYRMLVQQDLS---SYKFPSLQHCVTGGEPLNPEVLEKWK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 413 EHVGkgkLPLLDTWWQTETGsiLISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLI----TEPWpGMLT 488
Cdd:cd05928 313 AQTG---LDIYEGYGQTETG--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpIRPF-GLFS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 DIHNDRARYNRTYFERFpgsYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIK 568
Cdd:cd05928 387 GYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIR 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 569 GQTVYAYVTLRSG-LDEDDEMRTV-LREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05928 464 GEVVKAFVVLAPQfLSHDPEQLTKeLQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
119-629 |
1.55e-71 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 238.13 E-value: 1.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiEDYCkpesmrsadplFILHTS 278
Cdd:cd05919 89 SA---------------------------------------------------------DDIA-----------YLLYSS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADI--GWITGHSytVYGPLALGATTLLFegvPTYPRPDRYW 356
Cdd:cd05919 101 GTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILI 436
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 437 SPLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGMLTDIHNDRARYNRtyferfpGSYETGDG 514
Cdd:cd05919 251 SNRP--GAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPsaAVGYWNNPEKSRATFNG-------GWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 515 ARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLRE 594
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHR 401
|
490 500 510
....*....|....*....|....*....|....*
gi 1816261920 595 WVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05919 402 HLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
104-629 |
2.57e-70 |
|
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: 235.92 E-value: 2.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGEPeeevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAV---HSVIFagfS 180
Cdd:cd05936 14 DKTALIFMGRK------LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvpLNPLY---T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 181 AVSLQNRIIDCDAKILIAAdgvlrggkkIPLKRNVDEALFECPSVEqvimvkRTGDeidfiegrdtwwheeisgpdiedy 260
Cdd:cd05936 85 PRELEHILNDSGAKALIVA---------VSFTDLLAAGAPLGERVA------LTPE------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 261 ckpesmrsaDPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRD-DDVHWCTADIgwitghsYTVYG------- 332
Cdd:cd05936 126 ---------DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPL-------FHVFGltvalll 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 333 PLALGATTLLfegVPTyPRPDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEVWIWFH 412
Cdd:cd05936 190 PLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 413 EHVGKgklPLLDTWWQTETgsiliSPL----PYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGM 486
Cdd:cd05936 264 ELTGV---PIVEGYGLTET-----SPVvavnPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPqvMKGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 487 LTDIHNDRARYNRTYFErfpgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHE 566
Cdd:cd05936 336 WNRPEETAEAFVDGWLR-------TGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 567 IKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05936 409 YSGEAVKAFVVLKEGasLTEEE-----IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
102-630 |
3.26e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 231.61 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsvifagfsA 181
Cdd:PRK06187 19 HPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV---------L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 182 VSLQNR--------II-DCDAKILIAADGVLrggkkiPLKRNVDEALfecPSVEQVIMVkrtgDEIDFIEGRDTWWH-EE 251
Cdd:PRK06187 84 HPINIRlkpeeiayILnDAEDRVVLVDSEFV------PLLAAILPQL---PTVRTVIVE----GDGPAAPLAPEVGEyEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 252 ISGPDIEDYCKPESmRSADPLFILHTSGSTGKAKGVVHStggYMTATAHT---TQWvFDLRDDDV--------HwcTADI 320
Cdd:PRK06187 151 LLAAASDTFDFPDI-DENDAAAMLYTSGTTGHPKGVVLS---HRNLFLHSlavCAW-LKLSRDDVylvivpmfH--VHAW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 321 GWItghsytvYGPLALGATtllfeGVptYPR---PDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILG 397
Cdd:PRK06187 224 GLP-------YLALMAGAK-----QV--IPRrfdPENLLDLIETERVTFFFAVPTIWQMLLKAPR--AYFVDFSSLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 398 SVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSIL-ISPLP---YVGKLKPGSTGKPLPGISAKIVNSDGSDAEANE 473
Cdd:PRK06187 288 YGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPEdqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 474 G--GHLLITEPW--PGMLTDIH-NDRARYNrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESA 548
Cdd:PRK06187 365 GevGEIIVRGPWlmQGYWNRPEaTAETIDG--------GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 549 LIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRR 626
Cdd:PRK06187 437 LYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGatLDAKE-----LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
|
....
gi 1816261920 627 ILRR 630
Cdd:PRK06187 512 VLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
104-625 |
1.58e-65 |
|
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: 222.10 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:cd17631 10 DRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAadgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckp 263
Cdd:cd17631 84 VAYILADSGAKVLFD----------------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 esmrsaDPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLF 343
Cdd:cd17631 99 ------DLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 344 EGvptyPRPDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEV---WIWFHehvgkgkL 420
Cdd:cd17631 172 RK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPMPERLlraLQARG-------V 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQTETGSiLISPLPYVGKL-KPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRARYNR 499
Cdd:cd17631 239 KFVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVMAGYWNRPEATAA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 TYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLR 579
Cdd:cd17631 316 AFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816261920 580 SG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd17631 393 PGaeLDEDE-----LIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
118-629 |
6.69e-65 |
|
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: 220.24 E-value: 6.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 118 VRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILI 197
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 198 AadgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmrsaDPLFILHT 277
Cdd:cd05934 81 V-----------------------------------------------------------------------DPASILYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 278 SGSTGKAKGVVhSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLfegVPTYpRPDRYWE 357
Cdd:cd05934 90 SGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRFWS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 358 IINRYGVNIFYTTPTALRALRREGTQWTEKYdlSTLRILGsvGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILIS 437
Cdd:cd05934 165 DVRRYGATVTNYLGAMLSYLLAQPPSPDDRA--HRLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 438 PLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLIT-EPWPGMLTDIHNDRARYNrtyfERFP-GSYETGDGA 515
Cdd:cd05934 238 PRD--EPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYYNMPEATA----EAMRnGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 516 RVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLR 593
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGetLDPEE-----LF 386
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816261920 594 EWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05934 387 AFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
114-629 |
3.96e-64 |
|
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: 218.50 E-value: 3.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 114 PEEEVrvfTYHMLHRKVCRFANVLK-KIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsvifagfsAVSLqnriidcd 192
Cdd:cd05958 7 PEREW---TYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI---------AVAT-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 193 akiliaadgvlrggkkIPLKRNvdealfecPSVEQVImvKRTGDEIDFIEGRDTwwheeisgpDIEDYCkpesmrsadpl 272
Cdd:cd05958 67 ----------------MPLLRP--------KELAYIL--DKARITVALCAHALT---------ASDDIC----------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 FILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPtyprP 352
Cdd:cd05958 101 ILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT----P 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 353 DRYWEIINRYGVNIFYTTPTALRA---LRREGTQwtekyDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQT 429
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAmlaHPDAAGP-----DLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGST 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETGSILISPLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpgmlTDIHNDRARYNRTYFERfpGSY 509
Cdd:cd05958 249 EMFHIFISARP--GDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-----TGCRYLADKRQRTYVQG--GWN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 510 ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMR 589
Cdd:cd05958 320 ITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLA 399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1816261920 590 TVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05958 400 RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
119-624 |
3.12e-61 |
|
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: 212.07 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRggkkiplkrNVDEALFECPSVEQVIMVkrtGDEIDFIEGRDTWWHEEISGPDiEDYCKPESMRSADPLFILHTS 278
Cdd:cd05911 89 DPDGLE---------KVKEAAKELGPKDKIIVL---DDKPDGVLSIEDLLSPTLGEED-EDLPPPLKDGKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHStggYMTATAHTTQwVFDLRDDDVHWCTADIG-----WITGHSYTVYGPLaLGATTLLFegvptyPRPD 353
Cdd:cd05911 156 GTTGLPKGVCLS---HRNLIANLSQ-VQTFLYGNDGSNDVILGflplyHIYGLFTTLASLL-NGATVIIM------PKFD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 --RYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEVwiwfHEHVGK--GKLPLLDTWWQT 429
Cdd:cd05911 225 seLFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKEL----QELLAKrfPNATIKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETGSILISPLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEA-NEGGHLLITEP--WPGMLtdiHNDRARyNRTYFERfp 506
Cdd:cd05911 299 ETGGILTVNPD--GDDKPGSVGRLLPNVEAKIVDDDGKDSLGpNEPGEICVRGPqvMKGYY---NNPEAT-KETFDED-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 507 GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDE 584
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGekLTE 450
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1816261920 585 DDemrtvLREWVSQKIGPI-AVPETIQFSEGLPKTRSGKIM 624
Cdd:cd05911 451 KE-----VKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
112-633 |
1.46e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 208.27 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 112 GEPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSV--IFAGFSAVSLQNRii 189
Cdd:PRK07529 50 ADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANPInpLLEPEQIAELLRA-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 190 dCDAKILIAadgvLRGGKKIPLKRNVDEALFECPSVEQVIMV---KRTGDEIDFI--------EGRDTWWHEEISGPDIE 258
Cdd:PRK07529 128 -AGAKVLVT----LGPFPGTDIWQKVAEVLAALPELRTVVEVdlaRYLPGPKRLAvplirrkaHARILDFDAELARQPGD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 259 DYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGA 338
Cdd:PRK07529 203 RLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 339 TTLLfegvPT---YPRP---DRYWEIINRYGVNIFYTTPTALRALRRegtQWTEKYDLSTLRILGSVGEPINPEVWIWFH 412
Cdd:PRK07529 282 HVVL----ATpqgYRGPgviANFWKIVERYRINFLSGVPTVYAALLQ---VPVDGHDISSLRYALCGAAPLPVEVFRRFE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 413 EHVGkgkLPLLDTWWQTEtGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDG-----SDAEANEGGHLLITEP--WPG 485
Cdd:PRK07529 355 AATG---VRIVEGYGLTE-ATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILDDagrylRDCAVDEVGVLCIAGPnvFSG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 486 MLTDIHNDRARYNRTYFErfpgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPH 565
Cdd:PRK07529 431 YLEAAHNKGLWLEDGWLN-------TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 566 EIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIG-PIAVPETIQFSEGLPKTRSGKIMRRILRRIAV 633
Cdd:PRK07529 504 AHAGELPVAYVQLKPGASATEAE---LLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
94-636 |
6.63e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 204.52 E-value: 6.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENgRRNKAALIWQGEPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHS 173
Cdd:PRK13295 30 LDACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 174 VIFAGFSAVSLQNRIIDCDAKILIAADgVLRGGKKIPLKRNVDEALfecPSVEQVIMVKRTGD---EIDFIEGRdtwWHE 250
Cdd:PRK13295 109 PLMPIFRERELSFMLKHAESKVLVVPK-TFRGFDHAAMARRLRPEL---PALRHVVVVGGDGAdsfEALLITPA---WEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 251 EISGPDIEDYCKPesmRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGWITGHSYTV 330
Cdd:PRK13295 182 EPDAPAILARLRP---GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAE-RLGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 331 YGPLALGATTLLFEgvptYPRPDRYWEIINRYGVNifYT---TPTALRALRregTQWTEKYDLSTLRILGSVGEPINPEV 407
Cdd:PRK13295 258 MMPVMLGATAVLQD----IWDPARAAELIRTEGVT--FTmasTPFLTDLTR---AVKESGRPVSSLRTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 408 WIWFHEHVGkgkLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPG 485
Cdd:PRK13295 329 VERARAALG---AKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCsnFGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 486 MLtdihnDRARYNRTYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPH 565
Cdd:PRK13295 406 YL-----KRPQLNGTDAD---GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 566 EIKGQTVYAYVTLRSGLDED-DEMRTVLRewvSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEN 636
Cdd:PRK13295 478 ERLGERACAFVVPRPGQSLDfEEMVEFLK---AQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-632 |
1.85e-57 |
|
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: 200.49 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsVIFAG--FSAVSLQNRiidcdakilia 198
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV--VIPATtlLTPDDLRDR----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgVLRGGKKIPLkrnVDEAlfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesMRSADPLFILHTS 278
Cdd:cd05974 68 ---VDRGGAVYAA---VDEN-----------------------------------------------THADDPMLLYFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGGYMTATAHTTQWVfDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFegvpTYPR--PDRYW 356
Cdd:cd05974 95 GTTSKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYARfdAKRVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTTPTALRALRREgtqwtekyDLST----LRILGSVGEPINPEVWiwfhEHVGKG-KLPLLDTWWQTET 431
Cdd:cd05974 170 AALVRYGVTTLCAPPTVWRMLIQQ--------DLASfdvkLREVVGAGEPLNPEVI----EQVRRAwGLTIRDGYGQTET 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 432 gSILISPLPyvGK-LKPGSTGKPLPGISAKIVNSDGsdAEANEGG-HLLITEPWP-GMLTDIHNDRARynrTYFERFPGS 508
Cdd:cd05974 238 -TALVGNSP--GQpVKAGSMGRPLPGYRVALLDPDG--APATEGEvALDLGDTRPvGLMKGYAGDPDK---TAHAMRGGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEM 588
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPET 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816261920 589 RTVLREWVSQKIGPIAVPETIQFSEgLPKTRSGKIMRRILRRIA 632
Cdd:cd05974 390 ALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-629 |
1.16e-55 |
|
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: 197.15 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAA 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DGvlRGGKKIPLKRNVDEALFEcpSVEQVIMVKRTGDEidfiegrdtwwhEEISGPDIEDYCKPES--MRSADPLFILHT 277
Cdd:cd05926 94 KG--ELGPASRAASKLGLAILE--LALDVGVLIRAPSA------------ESLSNLLADKKNAKSEgvPLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 278 SGSTGKAKGVvHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLlfegVPTYPRPDRYWE 357
Cdd:cd05926 158 SGTTGRPKGV-PLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVV----LPPRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 358 IINRYGVNIFYTTPTALRA-LRREGTQWTEKYdlSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILI 436
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQIlLNRPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFG---APVLEAYGMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 437 S-PLPyVGKLKPGSTGKPLpGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRARyNRTYFERFpGSYETGDGA 515
Cdd:cd05926 308 SnPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNPEA-NAEAAFKD-GWFRTGDLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 516 RVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLR 593
Cdd:cd05926 382 YLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGasVTEEE-----LR 456
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816261920 594 EWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05926 457 AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-629 |
3.97e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 190.50 E-value: 3.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 115 EEEVRVfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAK 194
Cdd:PRK07656 26 FGDQRL-TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADGVLrggkkiPLKRNVDEALfecPSVEQVIMVkRTGDEIDFIEGRDTWwhEEISGPDIEDYCKPEsMRSADPLFI 274
Cdd:PRK07656 105 ALFVLGLFL------GVDYSATTRL---PALEHVVIC-ETEEDDPHTEKMKTF--TDFLAAGDPAERAPE-VDPDDVADI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVvhstggyMTATAHT----TQWV--FDLRDDDVHWC----------TAdiGWITghsytvygPLALGA 338
Cdd:PRK07656 172 LFTSGTTGRPKGA-------MLTHRQLlsnaADWAeyLGLTEGDRYLAanpffhvfgyKA--GVNA--------PLMRGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 339 TTLLfegVPTYpRPDRYWEIINRYGVNIFYTTPTA----LRALRREgtqwteKYDLSTLRILGSVGEPINPEVWIWFHEH 414
Cdd:PRK07656 235 TILP---LPVF-DPDEVFRLIETERITVLPGPPTMynslLQHPDRS------AEDLSSLRLAVTGAASMPVALLERFESE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 415 VGKGKLplLDTWWQTE-TGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLItepwpgmltdihnd 493
Cdd:PRK07656 305 LGVDIV--LTGYGLSEaSGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RArYN--RTYFE---------RFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:PRK07656 369 RG-PNvmKGYYDdpeataaaiDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 563 IPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK07656 448 VPDERLGEVGKAYVVLKPGaeLTEEE-----LIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
104-629 |
1.78e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 183.60 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAADGvlrggkkipLKRNVDEALFECPSVEQVIMVKRTGDEIDfiEGRDTWWHEEISGPDIEDyckP 263
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLILSLVLGGREAP--GGWLDFADWAEAGSVAEP---D 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 ESMRSADPLFILHTSGSTGKAKGVVHSTGG----YMTATAHTtqwvfDLRDDDvhwctadigwITGHSYTVY-------- 331
Cdd:PRK08316 166 VELADDDLAQILYTSGTESLPKGAMLTHRAliaeYVSCIVAG-----DMSADD----------IPLHALPLYhcaqldvf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 -GP-LALGATTLLFEGvptyPRPDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRiLGSVGEPINP-EVW 408
Cdd:PRK08316 231 lGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLR-KGYYGASIMPvEVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 409 IWFHEhvgkgKLPLLDTW---WQTEtgsilISPLPYVGK-----LKPGSTGKPLPGISAKIVNSDGSDAEANEGGHllIT 480
Cdd:PRK08316 304 KELRE-----RLPGLRFYncyGQTE-----IAPLATVLGpeehlRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE--IV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 481 EPWPGMLTDIHNDRARYNrtyfERFPGS-YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAA 559
Cdd:PRK08316 372 HRSPQLMLGYWDDPEKTA----EAFRGGwFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 560 VVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK08316 448 VIGLPDPKWIEAVTAVVVPKAGatVTEDE-----LIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
104-626 |
3.07e-50 |
|
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: 180.80 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAADGvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckp 263
Cdd:cd05930 76 LAYILEDSGAKLVLTDPD-------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 esmrsaDPLFILHTSGSTGKAKGVVHSTGGYmtatAHTTQWV---FDLRDDDVHWCTADIGWItGHSYTVYGPLALGATT 340
Cdd:cd05930 94 ------DLAYVIYTSGSTGKPKGVMVEHRGL----VNLLLWMqeaYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LLfegVP--TYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWtekyDLSTLRILGSVGEPINPEVWIWFHEHVGKG 418
Cdd:cd05930 163 VV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELLPGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 419 KlpLLDTWWQTETgSILISplpyVGKLKPGST-------GKPLPGISAKIVNSDGSDAEANEGGHLLITEpwPGMltdih 491
Cdd:cd05930 236 R--LVNLYGPTEA-TVDAT----YYRVPPDDEedgrvpiGRPIPNTRVYVLDENLRPVPPGVPGELYIGG--AGL----- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 492 ndrAR--YNR---TYfERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEA 558
Cdd:cd05930 302 ---ARgyLNRpelTA-ERFvpnpfgPGErmYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREA 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 559 AVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRR 626
Cdd:cd05930 378 AVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
120-629 |
6.89e-49 |
|
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: 177.19 E-value: 6.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAA 199
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DgVLRGGKKIPLkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgPDiedyckpesmrsaDPLFILHTSG 279
Cdd:cd05903 81 E-RFRQFDPAAM-------------------------------------------PD-------------AVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 280 STGKAKGVVHSTGGYMtATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVptypRPDRYWEII 359
Cdd:cd05903 104 TTGEPKGVMHSHNTLS-ASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 360 NRYGVNIFYTTPT----ALRALRREGTqwtekyDLSTLRILGSVGEPINPEVwiwFHEHVGKGKLPLLDTWWQTETGSIL 435
Cdd:cd05903 179 REHGVTFMMGATPfltdLLNAVEEAGE------PLSRLRTFVCGGATVPRSL---ARRAAELLGAKVCSAYGSTECPGAV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 436 ISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGMLtdihnDRARYNRTYFERfpGSYETGD 513
Cdd:cd05903 250 TSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPsvFLGYL-----DRPDLTADAAPE--GWFRTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 514 GARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDED-DEMRTVL 592
Cdd:cd05903 323 LARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYL 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 1816261920 593 RewvSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05903 403 D---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
119-628 |
7.62e-48 |
|
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: 175.89 E-value: 7.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ----ADGVLRGGKKIPLkrnVDEALFECPSVeqvimvkrtgDEIDFIEgrdtwwheeisgpDIEDYCKPEsMRSADPLFI 274
Cdd:cd05904 111 taelAEKLASLALPVVL---LDSAEFDSLSF----------SDLLFEA-------------DEAEPPVVV-IKQDDVAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGYMTATAHTTQ-WVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFegvptyPRPD 353
Cdd:cd05904 164 LYSSGTTGRSKGVMLTHRNLIAMVAQFVAgEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM------PRFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 --RYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEVwiwfhEHVGKGKLP---LLDTWWQ 428
Cdd:cd05904 238 leELLAAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPLGKEL-----IEAFRAKFPnvdLGQGYGM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TETGSILIS-PLPYVGKLKPGSTGKPLPGISAKIVN-SDGSDAEANEGGHLLITEPwpGMLTDIHNDRARYNRTYfeRFP 506
Cdd:cd05904 311 TESTGVVAMcFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGP--SIMKGYLNNPEATAATI--DKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 507 GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDE 584
Cdd:cd05904 387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGssLTE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816261920 585 DDEMrtvlrEWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd05904 467 DEIM-----DFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
104-630 |
8.99e-47 |
|
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: 171.32 E-value: 8.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGepeeevRVFTYHMLHRKVCRFANVL-KKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAV 182
Cdd:cd05941 1 DRIAIVDDG------DSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 183 SLQNRIIDCDAKILIaadgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyck 262
Cdd:cd05941 75 ELEYVITDSEPSLVL----------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 263 pesmrsaDPLFILHTSGSTGKAKGVVHSTGG-YMTATAHTTQWVFdlRDDD----------VH----------WCTADIG 321
Cdd:cd05941 90 -------DPALILYTSGTTGRPKGVVLTHANlAANVRALVDAWRW--TEDDvllhvlplhhVHglvnallcplFAGASVE 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 322 WITGHSYTVYGPLALGATTLLFEGVPT-YPRPDRYWEiinrygvnifyTTPTALRALRREGtqwtekydLSTLRILGSVG 400
Cdd:cd05941 161 FLPKFDPKEVAISRLMPSITVFMGVPTiYTRLLQYYE-----------AHFTDPQFARAAA--------AERLRLMVSGS 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 401 EPINPEVwiwFHEHVGKGKLPLLDTWWQTETGSILISPLPyvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEG-GHLLI 479
Cdd:cd05941 222 AALPVPT---LEEWEAITGHTLLERYGMTEIGMALSNPLD--GERRPGTVGMPLPGVQARIVDEETGEPLPRGEvGEIQV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 480 TEPwpGMLtdihndrarynRTYFERfP----------GSYETGDGARVDEDGDYWIMGRL-DDVINVSGHRLGTTEIESA 548
Cdd:cd05941 297 RGP--SVF-----------KEYWNK-PeatkeeftddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERV 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 549 LIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG---LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd05941 363 LLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEE-----LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
....*
gi 1816261920 626 RILRR 630
Cdd:cd05941 438 KELRK 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
97-628 |
1.82e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 172.84 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 97 HLE-NGRR--NKAALIWQGepeeevRVFTYHMLHRKVCRFANVLK-KIGVSKGDRVAIYLPMVPELVISMLACARIGAVH 172
Cdd:PRK08314 15 NLEvSARRypDKTAIVFYG------RAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 173 SVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKiplkrnvdeaLFECPSVEQVImVKRTGDEIDfIEGRDT---WWH 249
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAP----------AVGNLRLRHVI-VAQYSDYLP-AEPEIAvpaWLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 250 EEISGPDIED-------------YCKPESMRSADPLFIL-HTSGSTGKAKGVVHSTGGYMTATAHTTQWvFDLRDDDVHW 315
Cdd:PRK08314 157 AEPPLQALAPggvvawkealaagLAPPPHTAGPDDLAVLpYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 316 CTADIGWITGHSYTVYGPLALGATTLLFegvptyPRPDR--YWEIINRYGVNIFYTTPTALRALRreGTQWTEKYDLSTL 393
Cdd:PRK08314 236 AVLPLFHVTGMVHSMNAPIYAGATVVLM------PRWDReaAARLIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 394 RILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGS-ILISPLpyvGKLKPGSTGKPLPGISAKIVNSD-GSDAEA 471
Cdd:PRK08314 308 RYIGGGGAAMPEAVAERLKELTG---LDYVEGYGLTETMAqTHSNPP---DRPKLQCLGIPTFGVDARVIDPEtLEELPP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEP------WpgmltdiHNDRAryNRTYFERFPGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTT 543
Cdd:PRK08314 382 GEVGEIVVHGPqvfkgyW-------NRPEA--TAEAFIEIDGKrfFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 544 EIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG----LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTR 619
Cdd:PRK08314 453 EVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEargkTTEEE-----IIAWAREHMAAYKYPRIVEFVDSLPKSG 527
|
....*....
gi 1816261920 620 SGKIMRRIL 628
Cdd:PRK08314 528 SGKILWRQL 536
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-629 |
1.02e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 168.77 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 128 RKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFagfsaVSLQNRIIDCDAKILIAadgvLRGGK 207
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVF-----VPLNPTLKESVLRYLVA----DAGGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 208 -KIPLKRNVDEALFECPSveqvimvkrTGDEIDFIEGrDTWWHEEISGPDIEdyckpesMRSADPLFILHTSGSTGKAKG 286
Cdd:cd05922 72 iVLADAGAADRLRDALPA---------SPDPGTVLDA-DGIRAARASAPAHE-------VSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 287 VVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGWITGHSyTVYGPLALGATTLLfegVPTYPRPDRYWEIINRYGVNI 366
Cdd:cd05922 135 VRLSHQNLLANARSIAE-YLGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL---TNDGVLDDAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 367 FYTTPTALRALRREGTQWTEkydLSTLRILGSVGEPINPEVWIWFHEHVGKGKLPLLdtWWQTE-TGSILISPlPYVGKL 445
Cdd:cd05922 210 LAGVPSTYAMLTRLGFDPAK---LPSLRYLTQAGGRLPQETIARLRELLPGAQVYVM--YGQTEaTRRMTYLP-PERILE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 446 KPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITepwpGMLTDIHNDRARYNRTYFERFPGSYETGDGARVDEDGDYWI 525
Cdd:cd05922 284 KPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 526 MGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIkGQTVYAYVTLRSGLDEDDEMRTvlrewVSQKIGPIAV 605
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLRS-----LAERLPPYKV 433
|
490 500
....*....|....*....|....
gi 1816261920 606 PETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05922 434 PATVRVVDELPLTASGKVDYAALR 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
98-629 |
1.11e-43 |
|
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: 164.34 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 98 LENGRR-NKAALIWQGEPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAI-------YLpmvpELvisMLACARIG 169
Cdd:cd12119 2 LEHAARlHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATlawnthrHL----EL---YYAVPGMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 170 AVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLrggkkiPLkrnVDEALFECPSVEQVImVKRTGDEIDFIEGRDTWWH 249
Cdd:cd12119 75 AVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFL------PL---LEAIAPRLPTVEHVV-VMTDDAAMPEPAGVGVLAY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 250 EEI--SGPDIEDYckPESmRSADPLFILHTSGSTGKAKGVV--H-STggYMTATAHTTQWVFDLRDDDV--------H-- 314
Cdd:cd12119 145 EELlaAESPEYDW--PDF-DENTAAAICYTSGTTGNPKGVVysHrSL--VLHAMAALLTDGLGLSESDVvlpvvpmfHvn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 315 -WCTADIGWITGHSYTVYGPlalgattllfegvptYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTL 393
Cdd:cd12119 220 aWGLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLE--ANGRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 394 RILGSVGEPINPEVWIWFHEHVgkgkLPLLDTWWQTETgsiliSPLPYVGKLKPG--------------STGKPLPGISA 459
Cdd:cd12119 283 RRVVIGGSAVPRSLIEAFEERG----VRVIHAWGMTET-----SPLGTVARPPSEhsnlsedeqlalraKQGRPVPGVEL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 460 KIVNSDGSDAEA--NEGGHLLITEPWpgmLTDIHNDRARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSG 537
Cdd:cd12119 354 RIVDDDGRELPWdgKAVGELQVRGPW---VTKSYYKNDEESEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 538 HRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPK 617
Cdd:cd12119 429 EWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEE---LLEFLADKVAKWWLPDDVVFVDEIPK 505
|
570
....*....|..
gi 1816261920 618 TRSGKIMRRILR 629
Cdd:cd12119 506 TSTGKIDKKALR 517
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-633 |
2.80e-43 |
|
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: 159.57 E-value: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATtLLFEGVPTYPRP--- 352
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLAGPAGYRNPglf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 353 DRYWEIINRYGVNIFYTTPTALRALrregTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETg 432
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAAL----LQVPVNADISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 433 SILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGS-----DAEANEGGHLLITEP--WPGMLTDIHNDRARYNrtyferf 505
Cdd:cd05944 159 TCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPgvFGGYLYTEGNKNAFVA------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 PGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDED 585
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1816261920 586 DEMrtvLREWVSQKIGP-IAVPETIQFSEGLPKTRSGKIMRRILRRIAV 633
Cdd:cd05944 312 EEE---LLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-560 |
5.93e-43 |
|
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: 159.74 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKI-GVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQnRII-DCDAKILIAA 199
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLA-FILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DgvlrggkkiplkrnvdEALFECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEISGPDiedyckpesmrsaDPLFILHTSG 279
Cdd:TIGR01733 80 S----------------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPD-------------DLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 280 STGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVhwctadigWITGHSYT-------VYGPLALGATTLLFEGVPTYPRP 352
Cdd:TIGR01733 131 STGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 353 DRYWEIINRYGVNIFYTTPTALRALRREGtqwteKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgkLPLLDTWWQTETG 432
Cdd:TIGR01733 202 ALLAALIAEHPVTVLNLTPSLLALLAAAL-----PPALASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTETT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 433 ---SILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRARYNRTYFER-FPGS 508
Cdd:TIGR01733 275 vwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGP--GVARGYLNRPELTAERFVPDpFAGG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 509 -----YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAV 560
Cdd:TIGR01733 353 dgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
119-628 |
1.39e-41 |
|
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: 157.08 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLAcarigavhsVIFAGFSAVSlqnriIDCDAkilia 198
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLA---------ILKAGGAYVP-----IDPAY----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkiPLKRN---VDEAlfecpsveQVIMVkrtgdeidfiegrdtwwheeISGPDiedyckpesmrsaDPLFIL 275
Cdd:cd17643 72 -----------PVERIafiLADS--------GPSLL--------------------LTDPD-------------DLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGVVHSTGGYMTATAHTtQWVFDLRDDDVhwctadigWITGHSYT-------VYGPLALGATTLLfegVPT 348
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAAT-QRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLVV---VPY 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 349 YPR--PDRYWEIINRYGVNIFYTTPTALRAL----RREGTqwtekyDLSTLR--ILGsvGEPINPEVWIWFHEHVGKGKL 420
Cdd:cd17643 168 EVArsPEDFARLLRDEGVTVLNQTPSAFYQLveaaDRDGR------DPLALRyvIFG--GEALEAAMLRPWAGRFGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQTETgSILISPLPYVGKLKPGST----GKPLPGISAKIVNSDGSDAEANEGGHLLITEPW--PGMLtdihndr 494
Cdd:cd17643 240 QLVNMYGITET-TVHVTFRPLDAADLPAAAaspiGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGvaRGYL------- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 495 ARYNRTYfERF-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPH 565
Cdd:cd17643 312 GRPELTA-ERFvanpfggPGSrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRED 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 566 EIKGQTVYAYVTLRSGLDEDdemRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17643 391 EPGDTRLVAYVVADDGAAAD---IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
42-629 |
4.35e-41 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 159.86 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 42 RMATDSPEEFWADRARDL-LHWTRDFRTTLESDPE-KHEYKWFSGGRLNASYNCLdrhLENGRR--NKAALIW--QGEPE 115
Cdd:PLN03052 127 RFSVENPEVYWSIVLDELsLVFSVPPRCILDTSDEsNPGGQWLPGAVLNVAECCL---TPKPSKtdDSIAIIWrdEGSDD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 116 EEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKI 195
Cdd:PLN03052 204 LPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 196 LIAADGVLRGGKKIPLKRNVDEAlfECPsveQVIMVKRTGDEIDF-IEGRDTWWHEEIS---GPDIEDYCKPESMRSADP 271
Cdd:PLN03052 284 IFTQDVIVRGGKSIPLYSRVVEA--KAP---KAIVLPADGKSVRVkLREGDMSWDDFLAranGLRRPDEYKAVEQPVEAF 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 272 LFILHTSGSTGKAKGVVHSTGGYMTATAHTtqWV-FDLRDDDVH-WCTaDIGWITGHsYTVYGPLALGATTLLFEGVPTy 349
Cdd:PLN03052 359 TNILFSSGTTGEPKAIPWTQLTPLRAAADA--WAhLDIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPL- 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 prpDR-YWEIINRYGVNIFYTTPTALRALRRegTQWTEKYDLSTLRILGSVGEPINPEVWIWFhehVGKGKL-PLLDTWW 427
Cdd:PLN03052 434 ---GRgFAKFVQDAKVTMLGTVPSIVKTWKN--TNCMAGLDWSSIRCFGSTGEASSVDDYLWL---MSRAGYkPIIEYCG 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 428 QTETGSILISPLPyvgkLKP---GSTGKPLPGISAKIVNSDG----SDA----EANEGGHLLITEPW-----------PG 485
Cdd:PLN03052 506 GTELGGGFVTGSL----LQPqafAAFSTPAMGCKLFILDDSGnpypDDApctgELALFPLMFGASSTllnadhykvyfKG 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 486 MLTdIHNDRARYNRTYFERFPGSYetgdgarvdedgdYWIMGRLDDVINVSGHRLGTTEIESAL-IAHPDVTEAAVVGIP 564
Cdd:PLN03052 582 MPV-FNGKILRRHGDIFERTSGGY-------------YRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVP 647
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 565 HEIKG--QTVYAYV--TLRSGLDEDDEMRTVLREWVSQKIGPI-AVPETIQFSEgLPKTRSGKIMRRILR 629
Cdd:PLN03052 648 PPGGGpeQLVIAAVlkDPPGSNPDLNELKKIFNSAIQKKLNPLfKVSAVVIVPS-FPRTASNKVMRRVLR 716
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
96-623 |
4.63e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 157.90 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 96 RHLENGRRNKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVI 175
Cdd:PRK06178 40 RAWARERPQRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 176 FAGFSAVSLQNRIIDCDAKILIAADGVLrggkkiPLKRNVDEALfecpSVEQVIMVKRTG-----------DEIDFIEGR 244
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQLA------PVVEQVRAET----SLRHVIVTSLADvlpaeptlplpDSLRAPRLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 245 DTWWHEEISGPDIEDYCKPESMRSADPLFIL-HTSGSTGKAKGVVHSTGG--YMTATAHTTQWVfdLRDDDVHWCTADIG 321
Cdd:PRK06178 184 AAGAIDLLPALRACTAPVPLPPPALDALAALnYTGGTTGMPKGCEHTQRDmvYTAAAAYAVAVV--GGEDSVFLSFLPEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 322 WITGHSYTVYGPLALGATTLLFegvpTYPRPDRYWEIINRYGVNI-FYTTPTALRALrrEGTQWTEkYDLSTLRILGSVG 400
Cdd:PRK06178 262 WIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM--DHPRFAE-YDLSSLRQVRVVS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 401 --EPINPEvwiwfhehvgkgklplLDTWWQTETGSILI-----------SPLPYVG--------KLKPGSTGKPLPGISA 459
Cdd:PRK06178 335 fvKKLNPD----------------YRQRWRALTGSVLAeaawgmtethtCDTFTAGfqdddfdlLSQPVFVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 460 KIVNSD-GSDAEANEGGHLLITEPwpGMLTDIHNdRARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGH 538
Cdd:PRK06178 399 KICDFEtGELLPLGAEGEIVVRTP--SLLKGYWN-KPEATAEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 539 RLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPEtIQFSEGLPKT 618
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYKVPE-IRIVDALPMT 549
|
....*
gi 1816261920 619 RSGKI 623
Cdd:PRK06178 550 ATGKV 554
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
122-628 |
5.80e-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: 154.94 E-value: 5.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIaadg 201
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfecpsveqvimvkrTGDEIDfiegrdtwwheeisgpdiedyckpesmrsaDPLFILHTSGST 281
Cdd:cd05935 79 --------------------------------VGSELD------------------------------DLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVVHSTGGYMTATAHTTQWvFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEgvptypRPDR--YWEII 359
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVW-TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA------RWDRetALELI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 360 NRYGVNIFYTTPTALRALRreGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETGSILISPL 439
Cdd:cd05935 170 EKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTETMSQTHTNP 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 440 PyvGKLKPGSTGKPLPGISAKIVN-SDGSDAEANEGGHLLITEP------WpgmltdihnDRARYNRTYFERFPGS--YE 510
Cdd:cd05935 245 P--LRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPqifkgyW---------NRPEETEESFIEIKGRrfFR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 511 TGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGL----DEDD 586
Cdd:cd05935 314 TGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgkvTEED 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1816261920 587 emrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd05935 394 -----IIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-629 |
1.84e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 154.58 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRGgkkiplkRNVDEALfecpsveqvimvkrtgdeIDFIEGRDTwwheeiSGPDIEDYCKPESmrsadPLFILHTS 278
Cdd:PRK09088 101 DDAVAAG-------RTDVEDL------------------AAFIASADA------LEPADTPSIPPER-----VSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPtyPRPDRYWEI 358
Cdd:PRK09088 145 GTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFE--PKRTLGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 359 INRYGVNIFYTTPTALRALRREGTqwtekYDLSTLRILGSV---GEP-INPEVWIWFHEHVgkgklPLLDTWWQTETGSI 434
Cdd:PRK09088 222 DPALGITHYFCVPQMAQAFRAQPG-----FDAAALRHLTALftgGAPhAAEDILGWLDDGI-----PMVDGFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 LISPL-PYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGMLTDIHND-RARYNRTYFErfpgsye 510
Cdd:PRK09088 292 FGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnlSPGYWRRPQATaRAFTGDGWFR------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 511 TGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMrt 590
Cdd:PRK09088 365 TGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLER-- 442
|
490 500 510
....*....|....*....|....*....|....*....
gi 1816261920 591 vLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK09088 443 -IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
102-629 |
2.57e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 154.76 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISM----LACARIGAVHSVifa 177
Cdd:PRK06188 25 YPDRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqLAGLRRTALHPL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 178 gfsaVSLQNR---IIDCDAKILIAADG--VLRGGkkiplkrnvdEALFECPSVEQVIMVKRTGDEIDFIEGRDTWWHEEI 252
Cdd:PRK06188 96 ----GSLDDHayvLEDAGISTLIVDPApfVERAL----------ALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 253 SGPDiedyckpesmRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAhttqwvfdlrdddvhWCTADIGWITGHSYTVYG 332
Cdd:PRK06188 162 VAAA----------LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ---------------IQLAEWEWPADPRFLMCT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 333 PLALGATTLLfegVPTYPR-----------PDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGE 401
Cdd:PRK06188 217 PLSHAGGAFF---LPTLLRggtvivlakfdPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGAS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVWIWFHEHVGkgklPLL-DTWWQTETGSIlISPLPY-------VGKLkpGSTGKPLPGISAKIVNSDGSDAEANE 473
Cdd:PRK06188 292 PMSPVRLAEAIERFG----PIFaQYYGQTEAPMV-ITYLRKrdhdpddPKRL--TSCGRPTPGLRVALLDEDGREVAQGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 474 GGHLLITEPwpGMLTDIHNdraRYNRTYfERFPGSY-ETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAH 552
Cdd:PRK06188 365 VGEICVRGP--LVMDGYWN---RPEETA-EAFRDGWlHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEH 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 553 PDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK06188 439 PAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAE---LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
122-628 |
4.41e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 154.81 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 VLrggkkiPLKRNVDEAlfecPSVEQVImVKRTGDEIDF--------IEGRDT-------------WWH--EEISGPDIE 258
Cdd:PRK06710 131 VF------PRVTNVQSA----TKIEHVI-VTRIADFLPFpknllypfVQKKQSnlvvkvsesetihLWNsvEKEVNTGVE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 259 DYCKPESmrsaDPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDvhwcTADIGWITghSYTVYGPLALGA 338
Cdd:PRK06710 200 VPCDPEN----DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE----EVVLGVLP--FFHVYGMTAVMN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 339 TTLLfEGVPTY--PRPDR--YWEIINRYGVNIFYTTPTALRALRRegTQWTEKYDLSTLRILGSVGEPINPEVWIWFhEH 414
Cdd:PRK06710 270 LSIM-QGYKMVliPKFDMkmVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACISGSAPLPVEVQEKF-ET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 415 VGKGKLplLDTWWQTETGSILISPLPYVGKLkPGSTGKPLPGISAKIVNSDGSDA-EANEGGHLLITEP------W--PG 485
Cdd:PRK06710 346 VTGGKL--VEGYGLTESSPVTHSNFLWEKRV-PGSIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPqimkgyWnkPE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 486 MLTDIHNDrarynrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPH 565
Cdd:PRK06710 423 ETAAVLQD-------------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 566 EIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK06710 490 PYRGETVKAFVVLKEGTECSEEE---LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
119-637 |
1.41e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 152.99 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 -ADGVlrggkkiPLKRNVDEALFECPSVeqvimvkrtgdeidFIEGRDTWWHEE-----ISGPDIEDYCKPESMRSADPL 272
Cdd:PRK06155 125 eAALL-------AALEAADPGDLPLPAV--------------WLLDAPASVSVPagwstAPLPPLDAPAPAAAVQPGDTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 FILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGWITghSYTVYGPLALGATTLLFEgvptyPR- 351
Cdd:PRK06155 184 AILYTSGTTGPSKGVCCPHAQFYWWGRNSAE-DLEIGADDVLYTTLPLFHTN--ALNAFFQALLAGATYVLE-----PRf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 352 -PDRYWEIINRYGVNIFYTTPTALRALrrEGTQWTEKYDLSTLRILGSVGEPinPEVWIWFHEHVGkgkLPLLDTWWQTE 430
Cdd:PRK06155 256 sASGFWPAVRRHGATVTYLLGAMVSIL--LSQPARESDRAHRVRVALGPGVP--AALHAAFRERFG---VDLLDGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 TGSILISPLPyvgKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLI--TEPWP---GMLTDIHNDRARYNRTYFErf 505
Cdd:PRK06155 329 TNFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLraDEPFAfatGYFGMPEKTVEAWRNLWFH-- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 pgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LD 583
Cdd:PRK06155 404 -----TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGtaLE 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 584 EDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGEND 637
Cdd:PRK06155 479 PVA-----LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADT 527
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
119-628 |
2.63e-39 |
|
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: 151.20 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkiplkrnvDEALFecpsveqvimvKRTGDEIDFIEGRDTWWHEEISGPdiedyckPESMRSADPLFILHTS 278
Cdd:cd12117 101 -----------------DRSLA-----------GRAGGLEVAVVIDEALDAGPAGNP-------AVPVSPDDLAYVMYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVV--HSTggyMTATAHTTQWVfDLRDDDVHWCTADIGWiTGHSYTVYGPLALGATTLLFEGvPTYPRPDRYW 356
Cdd:cd12117 146 GSTGRPKGVAvtHRG---VVRLVKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTTPTALRALRREGTQWtekydLSTLRILGSVGEPINPevwiwfhEHVGK-----GKLPLLDTWWQTE- 430
Cdd:cd12117 220 ALIAEEGVTVLWLTAALFNQLADEDPEC-----FAGLRELLTGGEVVSP-------PHVRRvlaacPGLRLVNGYGPTEn 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 ---TGSILISPLPYVGKLKPgsTGKPLPGISAKIVNSDGSDAEANEGGHLLITEpwPGMLTDIHNDRARYNrtyfERF-- 505
Cdd:cd12117 288 ttfTTSHVVTELDEVAGSIP--IGRPIANTRVYVLDEDGRPVPPGVPGELYVGG--DGLALGYLNRPALTA----ERFva 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 ----PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLR 579
Cdd:cd12117 360 dpfgPGErlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816261920 580 SGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd12117 440 GALDAAE-----LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
119-632 |
4.34e-39 |
|
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: 151.45 E-value: 4.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsVIFA----------GFSAVSlqnri 188
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlpahrraeisHFAEQS----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 189 idcDAKILIAADgVLRGGKKIPLKRNVDEalfECPSVEQVIMVKRTGDEIDFiegrDTWWHEEISGPdiedycKPESmRS 268
Cdd:COG1021 122 ---EAVAYIIPD-RHRGFDYRALARELQA---EVPSLRHVLVVGDAGEFTSL----DALLAAPADLS------EPRP-DP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 269 ADPLFILHTSGSTGKAKGVVHSTGGYM---TATAHttqwVFDLRDDDVHWCTADIGwitgHSYT-----VYGPLALGATT 340
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDDYLysvRASAE----ICGLDADTVYLAALPAA----HNFPlsspgVLGVLYAGGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LLFEGvptyPRPDRYWEIINRYGVNIfyTT---PTALRALrrEGTQWtEKYDLSTLRILGSVGEPINPEVwiwfHEHVGk 417
Cdd:COG1021 256 VLAPD----PSPDTAFPLIERERVTV--TAlvpPLALLWL--DAAER-SRYDLSSLRVLQVGGAKLSPEL----ARRVR- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 418 gklPLLDTWWQ-----TEtGSILISPLPYVGKLKPGSTGKPlpgISA----KIVNSDGSDAEANEGGHLLITEPWpgmlT 488
Cdd:COG1021 322 ---PALGCTLQqvfgmAE-GLVNYTRLDDPEEVILTTQGRP---ISPddevRIVDEDGNPVPPGEVGELLTRGPY----T 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 -------DIHNDRArynrtyferFP--GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAA 559
Cdd:COG1021 391 irgyyraPEHNARA---------FTpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 560 VVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWvsqkiGpIA---VPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRER-----G-LAafkLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
122-629 |
7.20e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 151.69 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAV---HSVIFagfSAVSLQNRIIDCDAKILIA 198
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLY---TAHELEHPFEDHGARVAIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGV------LRGGkkIPLKR----NVDEALfecPSVEQ------VIMVKRTGDEID-FIEGRDTWwhEEI---SGPDIE 258
Cdd:PRK05605 136 WDKVaptverLRRT--TPLETivsvNMIAAM---PLLQRlalrlpIPALRKARAALTgPAPGTVPW--ETLvdaAIGGDG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 259 DYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTAdigWITGHSY--TVYGPLA- 335
Cdd:PRK05605 209 SDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVLAA---LPMFHAYglTLCLTLAv 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 -LGATTLLFegvPTyPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPINPE-VWIWfhE 413
Cdd:PRK05605 286 sIGGELVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMALPVStVELW--E 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 HVGKGKLplLDTWWQTETGSILISPlPYVGKLKPGSTGKPLPGISAKIVNSD--GSDAEANEGGHLLITEP--WPGMLtd 489
Cdd:PRK05605 358 KLTGGLL--VEGYGLTETSPIIVGN-PMSDDRRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPqvFKGYW-- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 490 ihnDRARYNRTYFErfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKG 569
Cdd:PRK05605 433 ---NRPEETAKSFL--DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGS 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 570 QTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK05605 508 EEVVAAVVLEPGaaLDPEG-----LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
107-622 |
1.06e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 150.42 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 107 ALIWqGEpeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQN 186
Cdd:PRK07798 21 ALVC-GD-----RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 187 RIIDCDAKILIAADGvlrggkkipLKRNVDEALFECPSVEQVIMVkrtGDEIDFIEGRDTWWHEEI-----SGPDIEDyc 261
Cdd:PRK07798 95 LLDDSDAVALVYERE---------FAPRVAEVLPRLPKLRTLVVV---EDGSGNDLLPGAVDYEDAlaagsPERDFGE-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 262 kpesmRSADPLFILHTSGSTGKAKGVVHSTG----GYMTATAHTTqwVFDLRDDDVHwcTADIGWITGHSYTVYGPLALG 337
Cdd:PRK07798 161 -----RSPDDLYLLYTGGTTGMPKGVMWRQEdifrVLLGGRDFAT--GEPIEDEEEL--AKRAAAGPGMRRFPAPPLMHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 338 ATTL-----LFEG--VPTYP----RPDRYWEIINRYGVNIFYTTPTA-----LRALRREGTqwtekYDLSTLRILGSVGE 401
Cdd:PRK07798 232 AGQWaafaaLFSGqtVVLLPdvrfDADEVWRTIEREKVNVITIVGDAmarplLDALEARGP-----YDLSSLFAIASGGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVWIWFHEHvgkgkLP---LLDTWWQTETGSILISplpyVGKLKPGSTGKPL--PGISAKIVNSDGSDAEANEGGh 476
Cdd:PRK07798 307 LFSPSVKEALLEL-----LPnvvLTDSIGSSETGFGGSG----TVAKGAVHTGGPRftIGPRTVVLDEDGNPVEPGSGE- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 477 llitepwPGML-------TDIHNDRARYNRTYFERFPGSYE-TGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESA 548
Cdd:PRK07798 377 -------IGWIarrghipLGYYKDPEKTAETFPTIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 549 LIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGK 622
Cdd:PRK07798 450 LKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
102-631 |
3.63e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 148.08 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKAALIwqGEPEEevrvFTYHMLHRKVCRFANVLK-KIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFS 180
Cdd:PRK06839 15 HPDRIAII--TEEEE----MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 181 AVSLQNRIIDCDAKILIAAdgvlrggkkiPLKRNVDEALFECPSVEQVImvkrtgdeidFIEGRdtwwhEEISGPDIEDY 260
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVE----------KTFQNMALSMQKVSYVQRVI----------SITSL-----KEIEDRKIDNF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 261 CKPESmrsADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTqWVFDLRDDDVHWCTADIGWITGhsytvygpLALGATT 340
Cdd:PRK06839 144 VEKNE---SASFIICYTSGTTGKPKGAVLTQENMFWNALNNT-FAIDLTMHDRSIVLLPLFHIGG--------IGLFAFP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LLFEG----VPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPINPEVWIWFHEHvg 416
Cdd:PRK06839 212 TLFAGgviiVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKF--ETTNLQSVRWFYNGGAPCPEELMREFIDR-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 417 kgKLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRAR 496
Cdd:PRK06839 288 --GFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVMKEYWNRPDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 497 YNRTYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYV 576
Cdd:PRK06839 364 TEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFI 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 577 TLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:PRK06839 441 VKKSSsvLIEKD-----VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
104-629 |
4.19e-38 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 148.29 E-value: 4.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQgEPEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGF---- 179
Cdd:PRK08008 22 HKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLlree 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 180 SAVSLQNriidCDAKILIAADGVLrggkkiPLKRNVDEalfECPSVEQVIMVKRTGDEIdfIEGRDTWWHEEISGPDIED 259
Cdd:PRK08008 101 SAWILQN----SQASLLVTSAQFY------PMYRQIQQ---EDATPLRHICLTRVALPA--DDGVSSFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 260 YCKPESmrSADPLFILHTSGSTGKAKGVV--HST---GGYMTAtahttqWVFDLRDDDVHW-----------CTADIGwi 323
Cdd:PRK08008 166 YAPPLS--TDDTAEILFTSGTTSRPKGVVitHYNlrfAGYYSA------WQCALRDDDVYLtvmpafhidcqCTAAMA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 324 tghSYTVygplalGATTLLFEgvpTYpRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYdlSTLRilgsvgepi 403
Cdd:PRK08008 236 ---AFSA------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ--HCLR--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 404 npEVWIWFH-------EHVGKGKLPLLDTWWQTETGSILISPLPYvGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGH 476
Cdd:PRK08008 292 --EVMFYLNlsdqekdAFEERFGVRLLTSYGMTETIVGIIGDRPG-DKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 477 LLIT-EPWPGMLTDIHNDRARYNRTYfeRFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDV 555
Cdd:PRK08008 369 ICIKgVPGKTIFKEYYLDPKATAKVL--EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKI 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 556 TEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK08008 447 QDIVVVGIKDSIRDEAIKAFVVLNEGetLSEEE-----FFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
122-629 |
8.51e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 148.00 E-value: 8.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsvifagfsAVSLQNRII---------DCD 192
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI---------AVPVNFRLTppeiaflvsDCG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 193 AKILIAaDGVLrggkkIPLKRNVDEALfecPSVEQVIMVKRTGDeiDFIEGRDTWWHEEisGPDIEDYCKPESmrsaDPL 272
Cdd:PRK07786 115 AHVVVT-EAAL-----APVATAVRDIV---PLLSTVVVAGGSSD--DSVLGYEDLLAEA--GPAHAPVDIPND----SPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 FILHTSGSTGKAKGVV--HSTggyMTATAHTTQWVFDL-RDDDVHWCTADIGWITGHSYTVYGpLALGATTLLfegvptY 349
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVltHAN---LTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPG-LLLGAPTVI------Y 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 P----RPDRYWEIINRYGVNIFYTTPTALRALRREgtQWTEKYDLStLRILGSVGEPINPEVWIWFHEHVGKGKLplLDT 425
Cdd:PRK07786 248 PlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE--QQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQI--LAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 426 WWQTEtgsilISPLPYV--GK---LKPGSTGKPLPGISAKIVNSDGSDAEANEGGHllITEPWPGMLTDIHNDRArynrT 500
Cdd:PRK07786 323 FGQTE-----MSPVTCMllGEdaiRKLGSVGKVIPTVAARVVDENMNDVPVGEVGE--IVYRAPTLMSGYWNNPE----A 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 501 YFERFPGS-YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLR 579
Cdd:PRK07786 392 TAEAFAGGwFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 580 SGLDE---DDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK07786 472 NDDAAltlED-----LAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
107-628 |
9.44e-38 |
|
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: 147.04 E-value: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 107 ALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQN 186
Cdd:cd17646 16 AVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 187 RIIDCDAKILIAADGVLRGGKKIPLKRNVDEALFEcpsveqvimvkrtgdeidfiegrdtwwHEEISGPDiedyckpESM 266
Cdd:cd17646 90 MLADAGPAVVLTTADLAARLPAGGDVALLGDEALA---------------------------APPATPPL-------VPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSADPLFILHTSGSTGKAKGVV--HstggymTATAHTTQWV---FDLRDDDVHWCTADIG-----WitghsyTVYGPLAL 336
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMvtH------AGIVNRLLWMqdeYPLGPGDRVLQKTPLSfdvsvW------ELFWPLVA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 337 GATTLLfegvptyPRPDRY------WEIINRYGVNIFYTTPTALRALrregTQWTEKYDLSTLRILGSVGEPINPEVWIW 410
Cdd:cd17646 204 GARLVV-------ARPGGHrdpaylAALIREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 411 FHEHVGkgkLPLLDTWWQTETgSILISPLPYVGKLKPGST--GKPLPGISAKIVNSDGSDAEANEGGHLLITepwpgmlt 488
Cdd:cd17646 273 FLALPG---AELHNLYGPTEA-AIDVTHWPVRGPAETPSVpiGRPVPNTRLYVLDDALRPVPVGVPGELYLG-------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 DIHNDRARYNRTYF--ERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEA 558
Cdd:cd17646 341 GVQLARGYLGRPALtaERFvpdpfgPGSrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHA 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 559 AVVGIPHEIKGQTVYAYVTLRSG-LDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17646 421 VVVARAAPAGAARLVGYVVPAAGaAGPDTA---ALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
122-629 |
1.43e-37 |
|
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: 145.59 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTHHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmrsADPLFILHTSGST 281
Cdd:cd17649 94 -------------------------------------------------------------------RQLAYVIYTSGST 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSyTVYGPLALGATTLLfEGVPTYPRPDRYWEIINR 361
Cdd:cd17649 107 GTPKGVAVSHGP-LAAHCQATAERYGLTPGDRELQFASFNFDGAHE-QLLPPLICGACVVL-RPDELWASADELAEMVRE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 362 YGVNIFYTTPTALRALRREGTQWTEKYDLStLRILGSVGEPINPE-VWIWFHEHVGkgklpLLDTWWQTETgsiLISPLP 440
Cdd:cd17649 184 LGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPElLRRWLKAPVR-----LFNAYGPTEA---TVTPLV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 441 YVG----KLKPGST--GKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNdraRYNRTYfERF-------PG 507
Cdd:cd17649 255 WKCeagaARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGE--GLARGYLG---RPELTA-ERFvpdpfgaPG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 508 S--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVyAYVTLRSGlDED 585
Cdd:cd17649 329 SrlYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAA-AAQ 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1816261920 586 DEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd17649 407 PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
114-628 |
2.07e-37 |
|
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: 146.11 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 114 PEEEVRVfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDA 193
Cdd:cd05923 23 PARGLRL-TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 194 KILIAADGvlrggkkiplkRNVDEALFEcpsveQVIMVKRTGDEIDFIEgrdtwwhEEISGPDIED-YCKPEsmrsaDPL 272
Cdd:cd05923 102 TAAVIAVD-----------AQVMDAIFQ-----SGVRVLALSDLVGLGE-------PESAGPLIEDpPREPE-----QPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 FILHTSGSTGKAKGVV---HSTGGYMTATAHTTQWVFDlRDDDVhwctadIGWITghSYTVYGPLALGATTLLFEG---V 346
Cdd:cd05923 154 FVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHG-RHNVV------LGLMP--LYHVIGFFAVLVAALALDGtyvV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 PTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKydLSTLRILGSVGEPINPEVWIWFHEHVgkgKLPLLDTW 426
Cdd:cd05923 225 VEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATMPDAVLERVNQHL---PGEKVNIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 427 WQTETGSILISPLPyvgklKPGSTGKPLPGISAKIVNSDGSDAEA---NEGGHLLIT----EPWPGMLTDIHNDRARYNR 499
Cdd:cd05923 300 GTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEAlanGEEGELIVAaaadAAFTGYLNQPEATAKKLQD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 tyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLR 579
Cdd:cd05923 375 -------GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPR 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816261920 580 SGLDEDDEMRTVLRewvSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd05923 448 EGTLSADELDQFCR---ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
119-629 |
3.89e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.43 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRGgkkiplkrnVDEALFECPS-VEQVIMVkrTGDeidfIEGRDTW--WHEEISGPDIEDyckpESMRSAdplfIL 275
Cdd:PRK08276 90 SAALADT---------AAELAAELPAgVPLLLVV--AGP----VPGFRSYeeALAAQPDTPIAD----ETAGAD----ML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGV--------VHSTGGYMTATAHTTqwvFDLRDDDVHWC------TADIGWITghsyTVygpLALGATTL 341
Cdd:PRK08276 147 YSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGPDSVYLSpaplyhTAPLRFGM----SA---LALGGTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 342 LFEGVptypRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVwiwfhehvgkgKLP 421
Cdd:PRK08276 217 VMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEV-----------KRA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 422 LLDtWW---------QTETGSI-LISPLPYVGKlkPGSTGKPLPGIsAKIVNSDGSDAEANEGGhlLITEPWPGMLTDIH 491
Cdd:PRK08276 282 MID-WWgpiiheyyaSSEGGGVtVITSEDWLAH--PGSVGKAVLGE-VRILDEDGNELPPGEIG--TVYFEMDGYPFEYH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 492 NDRARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVInVSGhrlGTT----EIESALIAHPDVTEAAVVGIPHEI 567
Cdd:PRK08276 356 NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG---GVNiypqEIENLLVTHPKVADVAVFGVPDEE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 568 KGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK08276 430 MGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-628 |
4.45e-37 |
|
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: 144.31 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHsvifagfsavslqnriidcdakilia 198
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAY-------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkIPLKrnvdealFECPsVEQVIMVKRTgdeidfiegrdtwwheeisgpdiedyCKPESMRSA--DPLFILH 276
Cdd:cd05945 69 ----------VPLD-------ASSP-AERIREILDA--------------------------AKPALLIADgdDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 277 TSGSTGKAKGVVHSTGGYMTATAhttqWV---FDLRDDDVHWCTADigwitghsYT-------VYGPLALGATTLLfegV 346
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTN----WMlsdFPLGPGDVFLNQAP--------FSfdlsvmdLYPALASGATLVP---V 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 P--TYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKydLSTLRILGSVGEPI-NPEVWIWfhehvgKGKLP-- 421
Cdd:cd05945 170 PrdATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPES--LPSLRHFLFCGEVLpHKTARAL------QQRFPda 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 422 -LLDTWWQTET----GSILISPLPyVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGMLtdihnDR 494
Cdd:cd05945 242 rIYNTYGPTEAtvavTYIEVTPEV-LDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYL-----NN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 495 ARYNRTYFERFPG--SYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTV 572
Cdd:cd05945 316 PEKTAAAFFPDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 573 YAYVTLRSGLDEDDEMRtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd05945 396 IAFVVPKPGAEAGLTKA--IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
107-629 |
6.77e-37 |
|
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: 144.41 E-value: 6.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 107 ALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQN 186
Cdd:cd17651 13 ALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 187 RIIDCDAKILIAADGVLrggkkiplkrnvdealfecpsveqvimvkrtgDEIDFIEGRDTWWHEEISGPDIEDYCKPESM 266
Cdd:cd17651 87 MLADAGPVLVLTHPALA--------------------------------GELAVELVAVTLLDQPGAAAGADAEPDPALD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSaDPLFILHTSGSTGKAKGVV------------HSTGGYMTATAHTTQWV---FDLrddDVHwctadigwitghsyTVY 331
Cdd:cd17651 135 AD-DLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFAglgFDV---SVQ--------------EIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 GPLALGATTLLfegVPTYPRPD--RYWEIINRYGVNIFYTTPTALRALRREGtqWTEKYDLSTLRILGSVGEP--INPEV 407
Cdd:cd17651 197 STLCAGATLVL---PPEEVRTDppALAAWLDEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLTGGEQlvLTEDL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 408 WIWFHEHVGkgkLPLLDTWWQTETGSI--LISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLItepwpG 485
Cdd:cd17651 272 REFCAGLPG---LRLHNHYGPTETHVVtaLSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYI-----G 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 486 MLTDIHNDRARYNRTYfERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTE 557
Cdd:cd17651 344 GAGLARGYLNRPELTA-ERFvpdpfvPGArmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 558 AAVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd17651 423 AVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
152-629 |
7.16e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 144.57 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 152 LPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKIPLKRNVDEAlfeCPSVEQVIMV 231
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA---APAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 232 KRTGDEIDFIEGRDTW----WHEEISGPDIEDYCKPESMRSADPLFILHTSGSTGKAKGV--VHSTG--GYMTATAHttq 303
Cdd:PLN03051 78 AGEPVAVPLREQDLSWcdflGVAAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIpwTHLSPlrCASDGWAH--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 304 wvFDLRDDDVHWCTADIGWITGhSYTVYGPLALGATTLLFEGVPTYPrpdRYWEIINRYGVNIFYTTPTALRALRREGTQ 383
Cdd:PLN03051 155 --MDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGR---GFGKFVQDAGVTVLGLVPSIVKAWRHTGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 384 WTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKlPLLDTWWQTETGSILISPLPyVGKLKPGSTGKPLPGISAKIVN 463
Cdd:PLN03051 229 AMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTL-LQPQAPGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 464 SDG--SDAEANEGGHLLITEPWPGMLTDIHNdrARYNRTYFERFPGSYETGDGARVDED-------GDYWIMGRLDDVIN 534
Cdd:PLN03051 307 DNGvpYPDDQPCVGEVALAPPMLGASDRLLN--ADHDKVYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 535 VSGHRLGTTEIESALI-AHPDVTEAAVVGIPhEIKGQTVYAYVTLRSGLDED-------DEMRTVLREWVSQKIGPIAVP 606
Cdd:PLN03051 385 LGGIKTSSVEIERACDrAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdqarpEALQKKFQEAIQTNLNPLFKV 463
|
490 500
....*....|....*....|...
gi 1816261920 607 ETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PLN03051 464 SRVKIVPELPRNASNKLLRRVLR 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
122-630 |
4.17e-36 |
|
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: 140.56 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsvifagfsAVSLQNRIidcdakiliaadg 201
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE---------AVLLNTRL------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfecpsveqvimvkrTGDEIDFiegrdtwwheeisgpdiedyckpeSMRSADPLF-----ILH 276
Cdd:cd05912 61 --------------------------------TPNELAF------------------------QLKDSDVKLddiatIMY 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 277 TSGSTGKAKGVVHSTGGYMtATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGpLALGATTLLFEGVptypRPDRYW 356
Cdd:cd05912 85 TSGTTGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAEQVL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTTPTALRALRREGTQwTEKYDLSTLrILGsvGEPINPEVwiwFHEHVGKGkLPLLDTWWQTETGSILI 436
Cdd:cd05912 159 HLINSGKVTIISVVPTMLQRLLEILGE-GYPNNLRCI-LLG--GGPAPKPL---LEQCKEKG-IPVYQSYGMTETCSQIV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 437 SPLPYVGKLKPGSTGKPLPGISAKIVNSDGsdaEANEGGHLLITEPwpgMLTDIHNDRARYNRTYFERfpGSYETGDGAR 516
Cdd:cd05912 231 TLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGP---NVTKGYLNRPDATEESFEN--GWFKTGDIGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 517 VDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDemrtvLREWV 596
Cdd:cd05912 303 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEE-----LIAYC 377
|
490 500 510
....*....|....*....|....*....|....
gi 1816261920 597 SQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
104-631 |
7.45e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 141.25 E-value: 7.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGEPEeevrvfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:PRK03640 17 DRTAIEFEEKKV------TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAADgvlrggkkiplkrNVDEALFECPSVEQVIMVKRTGDEIDFIEgrdTWWHEEISGpdiedyckp 263
Cdd:PRK03640 91 LLWQLDDAEVKCLITDD-------------DFEAKLIPGISVKFAELMNGPKEEAEIQE---EFDLDEVAT--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 esmrsadplfILHTSGSTGKAKGVVHSTGG-YMTATAhtTQWVFDLRDDDVHWCTADIGWITGHSyTVYGPLALGATTLL 342
Cdd:PRK03640 146 ----------IMYTSGTTGKPKGVIQTYGNhWWSAVG--SALNLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 343 ---FEgvptyprPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDlSTLR--ILGsvGEPINPEVwiwFHEHVGK 417
Cdd:PRK03640 213 vekFD-------AEKINKLLQTGGVTIISVVSTMLQRLLERLGE--GTYP-SSFRcmLLG--GGPAPKPL---LEQCKEK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 418 GkLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNsDGSDAEANEGGHLLITEP--WPGMLtdiHNDRA 495
Cdd:PRK03640 278 G-IPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPnvTKGYL---NREDA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 496 ryNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAY 575
Cdd:PRK03640 353 --TRETFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAF 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 576 VTLRSGLDEdDEMRTVLREwvsqKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:PRK03640 429 VVKSGEVTE-EELRHFCEE----KLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
105-629 |
1.11e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 141.37 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 105 KAALIWQGEPEeevrVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSL 184
Cdd:PRK13391 13 KPAVIMASTGE----VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 185 QNRIIDCDAKILI---AADGVLRggkkiplkrnvdEALFECPSVEQVIMVKRTGdEIDFIEGRDTWWHEEISGPdIEDYC 261
Cdd:PRK13391 89 AYIVDDSGARALItsaAKLDVAR------------ALLKQCPGVRHRLVLDGDG-ELEGFVGYAEAVAGLPATP-IADES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 262 KPESMrsadplfiLHTSGSTGKAKGVV----HSTGGYMTATAHTTQWVFDLRDDDVHWCTADIgWITGHSYTVYGPLALG 337
Cdd:PRK13391 155 LGTDM--------LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPL-YHSAPQRAVMLVIRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 338 ATTLLFEGVPtyprPDRYWEIINRYGVNIFYTTPTAL-RALRREGTQwTEKYDLSTLRILGSVGEPINPEVwiwfhehvg 416
Cdd:PRK13391 226 GTVIVMEHFD----AEQYLALIEEYGVTHTQLVPTMFsRMLKLPEEV-RDKYDLSSLEVAIHAAAPCPPQV--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 417 kgKLPLLDtWW---------QTE-TGSILISPLPYVGKlkPGSTGKPLPGIsAKIVNSDGSDAEANEGGHLLITEpwpGM 486
Cdd:PRK13391 292 --KEQMID-WWgpiiheyyaATEgLGFTACDSEEWLAH--PGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG---GR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 487 LTDIHNDRARynrTYFERFP-GSYET-GDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP 564
Cdd:PRK13391 363 PFEYLNDPAK---TAEARHPdGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 565 HEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK13391 440 NEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
121-630 |
1.61e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 141.42 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAAD 200
Cdd:PRK06087 50 YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 GVlrggKKIplkRNVDEAL---FECPSVEQVIMVKRTGDEIDfiegRDTWWHEEISGPDIEDYCkpesMRSADPLF-ILH 276
Cdd:PRK06087 130 LF----KQT---RPVDLILplqNQLPQLQQIVGVDKLAPATS----SLSLSQIIADYEPLTTAI----TTHGDELAaVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 277 TSGSTGKAKGVVhSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVptypRPDRYW 356
Cdd:PRK06087 195 TSGTEGLPKGVM-LTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIF----TPDACL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVN-IFYTTP---TALRALRRegtqwtEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgklpLLDTWWQTETg 432
Cdd:PRK06087 270 ALLEQQRCTcMLGATPfiyDLLNLLEK------QPADLSALRFFLCGGTTIPKKVARECQQRGIK----LLSVYGSTES- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 433 siliSPLPYVGKLKP-----GSTGKPLPGISAKIVNSDGSDA-------EANEGGHLLItepwpGMLtdihNDRARYNRT 500
Cdd:PRK06087 339 ----SPHAVVNLDDPlsrfmHTDGYAAAGVEIKVVDEARKTLppgcegeEASRGPNVFM-----GYL----DEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 501 YFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRs 580
Cdd:PRK06087 406 LDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLK- 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 581 gldeDDEMRTVLREWVS----QKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK06087 483 ----APHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
107-622 |
5.06e-35 |
|
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: 142.69 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 107 ALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHsvifagfsaVSL-- 184
Cdd:COG1020 494 AVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY---------VPLdp 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 185 ---QNRII----DCDAKILIAadgvlrggkkiplkrnvDEALFECPSVEQVIMVkrtgdEIDfiegrdtwwHEEISGPDI 257
Cdd:COG1020 559 aypAERLAymleDAGARLVLT-----------------QSALAARLPELGVPVL-----ALD---------ALALAAEPA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 258 EDyckPESMRSA-DPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVhwctadIGWITGHS-----YTVY 331
Cdd:COG1020 608 TN---PPVPVTPdDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfdasvWEIF 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 GPLALGATTLLfegVPTYPR--PDRYWEIINRYGVNIFYTTPTALRALRREGTQwtekyDLSTLRILGSVGEPINPEVWI 409
Cdd:COG1020 678 GALLSGATLVL---APPEARrdPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVR 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 410 WFHEHVGKgkLPLLD-----------TWWQTETGSILISPLPYvgklkpgstGKPLPGISAKIVNSDGSDAEANEGGHLL 478
Cdd:COG1020 750 RWRARLPG--ARLVNlygptettvdsTYYEVTPPDADGGSVPI---------GRPIANTRVYVLDAHLQPVPVGVPGELY 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 479 ITepwpGM-----------LTDihndrarynrtyfERF-------PGS--YETGDGARVDEDG--DYwiMGRLDDVINVS 536
Cdd:COG1020 819 IG----GAglargylnrpeLTA-------------ERFvadpfgfPGArlYRTGDLARWLPDGnlEF--LGRADDQVKIR 879
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 537 GHR--LGttEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEG 614
Cdd:COG1020 880 GFRieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAA---LLRLALALLLPPYMVPAAVVLLLP 954
|
....*...
gi 1816261920 615 LPKTRSGK 622
Cdd:COG1020 955 LPLTGNGK 962
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
121-631 |
1.45e-34 |
|
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: 138.43 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIG---AVHSVIFAG---FSAVSL-QNRIIDCDA 193
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGvgvAPTNDIYNErelDHSLNIsKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 194 KILiaaDGVLRGGKKIPLkrnvdealfecpsVEQVIMVKRTGDEIDFIEGRDTWWHEEISGPDIEDYCKPESMRSADPLF 273
Cdd:cd17642 125 KGL---QKVLNVQKKLKI-------------IKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 ILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVF-DLRDDDVHWCTAdIGWITGHS-YTVYGPLALGATTLLfegVPTYPR 351
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFgNQIIPDTAILTV-IPFHHGFGmFTTLGYLICGFRVVL---MYKFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 352 pDRYWEIINRYGVNIFYTTPTALRALRRegTQWTEKYDLSTLRILGSVGEPINPEVwiwfHEHVGKG-KLPLL-DTWWQT 429
Cdd:cd17642 265 -ELFLRSLQDYKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKEV----GEAVAKRfKLPGIrQGYGLT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETGS-ILISPlpyVGKLKPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEPwpGMLTDIHNDRARYNRTYFERfpG 507
Cdd:cd17642 338 ETTSaILITP---EGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGP--MIMKGYVNNPEATKALIDKD--G 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 508 SYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDED 585
Cdd:cd17642 411 WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGktMTEK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1816261920 586 DEMrtvlrEWVSQKIGPIA-VPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:cd17642 491 EVM-----DYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
124-629 |
1.46e-34 |
|
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: 137.51 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 124 HMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSvifagfsAVSLQNRIIDCDAKILIAADGVL 203
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPA-------YKSSRAPRAEACAIIEIKAAALV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 204 RGGKKIPLKRNVDEALFECPsveqvimvkrtgdeidfiEGRDTwwheeisgPDIEDyckpesmrSADPLFILHTSGSTGK 283
Cdd:cd05929 94 CGLFTGGGALDGLEDYEAAE------------------GGSPE--------TPIED--------EAAGWKMLYSGGTTGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 284 AKGVVHSTGGYMTATAHTTQWVFDL--RDDDVHWCTADIGWITGHSyTVYGPLALGATTLLFEGVptypRPDRYWEIINR 361
Cdd:cd05929 140 PKGIKRGLPGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----DPEEFLRLIER 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 362 YGVNIFYTTPTAL-RALRREGTQwTEKYDLSTLRILGSVGEPINPEV---WIwfhehvgkgklplldTWW---------Q 428
Cdd:cd05929 215 YRVTFAQFVPTMFvRLLKLPEAV-RNAYDLSSLKRVIHAAAPCPPWVkeqWI---------------DWGgpiiweyygG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TE-TGSILISPLPYVGKlkPGSTGKPLPGiSAKIVNSDGSDAEANEGGHLLITEPWPgmlTDIHNDrarYNRTYFERFPG 507
Cdd:cd05929 279 TEgQGLTIINGEEWLTH--PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG---FEYTND---PEKTAAARNEG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 508 SYET-GDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDD 586
Cdd:cd05929 350 GWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816261920 587 EMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
122-625 |
3.71e-34 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 135.27 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADg 201
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdeaLFEcpsveqvimvKRTGDEIDFiegrdtwwhEEISGPDIEDYCKPESMRSADPLFILHTSGST 281
Cdd:TIGR01923 80 -----------------LLE----------EKDFQADSL---------DRIEAAGRYETSLSASFNMDQIATLMFTSGTT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVVHSTGG-YMTATAHTTQWVFDlrdDDVHWCTA-DIGWITGHSyTVYGPLALGATTLLfegvptyprPDRYWEI- 358
Cdd:TIGR01923 124 GKPKAVPHTFRNhYASAVGSKENLGFT---EDDNWLLSlPLYHISGLS-ILFRWLIEGATLRI---------VDKFNQLl 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 359 --INRYGVNIFYTTPTAL-RALRREGTQWTEKYDLstlriLGsvGEPINPEVwiwFHEHVGKGkLPLLDTWWQTETGSIL 435
Cdd:TIGR01923 191 emIANERVTHISLVPTQLnRLLDEGGHNENLRKIL-----LG--GSAIPAPL---IEEAQQYG-LPIYLSYGMTETCSQV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 436 ISPLPYVGKLKPGStGKPLPGISAKIVNSDGSdaeanEGGHLLITEPwpgMLTDIHNDRARYNRTYFERfpGSYETGDGA 515
Cdd:TIGR01923 260 TTATPEMLHARPDV-GRPLAGREIKIKVDNKE-----GHGEIMVKGA---NLMKGYLYQGELTPAFEQQ--GWFNTGDIG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 516 RVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSgldedDEMRTVLREW 595
Cdd:TIGR01923 329 ELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES-----DISQAKLIAY 403
|
490 500 510
....*....|....*....|....*....|
gi 1816261920 596 VSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:TIGR01923 404 LTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-631 |
5.55e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 136.60 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAAD 200
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 ---GVLRG-----GKKIPLKRNVDEalfECPSVEQVimvkRTGDEIdfIEGRDTwwheeISGPDIEdycKPESmrsadpl 272
Cdd:PRK07788 155 eftDLLSAlppdlGRLRAWGGNPDD---DEPSGSTD----ETLDDL--IAGSST-----APLPKPP---KPGG------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 FILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVfDLRDDDVHWCTADIGWITGHSYTVYGpLALGATTLL---FEgvpty 349
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV-PFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrFD----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 prPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgklPLLDTWWQT 429
Cdd:PRK07788 284 --PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGP---VLYNLYGST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETGSILISPlPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEpwpGMLTDIH-NDRARynrtyfERFPGS 508
Cdd:PRK07788 359 EVAFATIAT-PEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN---GFPFEGYtDGRDK------QIIDGL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEM 588
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDA 508
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1816261920 589 rtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:PRK07788 509 ---IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-628 |
3.42e-33 |
|
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: 133.19 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ----ADGVLRGGKKIPLKRNVDEALFECPsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckPESMRSADPLFI 274
Cdd:cd12116 91 ddalPDRLPAGLPVLLLALAAAAAAPAAP---------------------------------------RTPVSPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDvHWCTA-----DIGWITghsytVYGPLALGATTLLFEGVPTY 349
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHRN-LVNFLHSMRERLGLGPGD-RLLAVttyafDISLLE-----LLLPLLAGARVVIAPRETQR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 pRPDRYWEIINRYGVNIFYTTPTALRALRreGTQWTekyDLSTLRIL-GsvGEPINPEVWIWFHEHVGkgklplldTWWQ 428
Cdd:cd12116 205 -DPEALARLIEAHSITVMQATPATWRMLL--DAGWQ---GRAGLTALcG--GEALPPDLAARLLSRVG--------SLWN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 ----TETgSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRArynrTYFER 504
Cdd:cd12116 269 lygpTET-TIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGD--GVAQGYLGRPA----LTAER 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 505 F-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVyAY 575
Cdd:cd12116 342 FvpdpfagPGSrlYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AY 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 576 VTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd12116 421 VVLKAGaaPDAAA-----LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
270-625 |
8.77e-33 |
|
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: 128.68 E-value: 8.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTAtahttqwvFDLRDDDVHWCTADIGWITG---HSYTVYG---PLALGATTLLF 343
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDAILAPGplsHSLFLYGaisALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 344 EGVptypRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtekydLSTLRILGSVGEPINPEVwiwfHEHVGKG--KLP 421
Cdd:cd17633 73 RKF----NPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFEST----KKKLKNIfpKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 422 LLDTWWQTETGsiLISPLPYVGKLKPGSTGKPLPGISAKIVNSDGsdaeaNEGGHLLITEPwpgMLTDIHNDRARYNRTy 501
Cdd:cd17633 139 LIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE---MVFSGYVRGGFSNPD- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 502 ferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG 581
Cdd:cd17633 208 -----GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKL 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1816261920 582 LDEDdemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd17633 283 TYKQ------LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
102-628 |
1.11e-32 |
|
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: 132.07 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKAALIWQGEPEEEV------------------RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISML 163
Cdd:cd05920 4 RRYRAAGYWQDEPLGDLlarsaarhpdriavvdgdRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 164 ACARIGAVhsVIFAGFSAVSLQ-NRIIDCDAKILIAADGVLRGGKKIPLKRnvdEALFECPsveqvimvkrtgdeidfie 242
Cdd:cd05920 84 ALLRLGAV--PVLALPSHRRSElSAFCAHAEAVAYIVPDRHAGFDHRALAR---ELAESIP------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 243 grdtwwheeisgpdiedyckpesmrsaDPLFILHTSGSTGKAKGV--VHSTGGYM-TATAHttqwVFDLRDDDVHWCTAD 319
Cdd:cd05920 140 ---------------------------EVALFLLSGGTTGTPKLIprTHNDYAYNvRASAE----VCGLDQDTVYLAVLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 320 IGwitgHSYTVYGPLALGatTLLFEG---VPTYPRPDRYWEIINRYGVNIFYTTPTALRalrregtQWT-----EKYDLS 391
Cdd:cd05920 189 AA----HNFPLACPGVLG--TLLAGGrvvLAPDPSPDAAFPLIEREGVTVTALVPALVS-------LWLdaaasRRADLS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 392 TLRILGSVGEPINPEVwiwfHEHVGKGKLPLLDTWWQTETGSILISPLPYVGKLKPGSTGKPL-PGISAKIVNSDGSDAE 470
Cdd:cd05920 256 SLRLLQVGGARLSPAL----ARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNPVP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 471 ANEGGHLLITEPWpgmlT-------DIHNDRArynrtyferFP--GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLG 541
Cdd:cd05920 332 PGEEGELLTRGPY----TirgyyraPEHNARA---------FTpdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 542 TTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREwvsQKIGPIAVPETIQFSEGLPKTRSG 621
Cdd:cd05920 399 AEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRE---RGLAAYKLPDRIEFVDSLPLTAVG 475
|
....*..
gi 1816261920 622 KIMRRIL 628
Cdd:cd05920 476 KIDKKAL 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
270-632 |
2.64e-32 |
|
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: 127.45 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHsTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHsYTVYGPLALGATTLLfegvpty 349
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVH-TAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 prPDRYWEIINRYGVNIFYTT---PTALRAL--RREGTQWtekydLSTLRILGSVGEPINPEVWIWFHEhvgKGkLPLLD 424
Cdd:cd17630 72 --LERNQALAEDLAPPGVTHVslvPTQLQRLldSGQGPAA-----LKSLRAVLLGGAPIPPELLERAAD---RG-IPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 425 TWWQTETGS-ILISPLPYVGKlkpGSTGKPLPGISAKIVNsdgsDAEANEGGHLLITEPWPGMLTDIHNDrarynrtyfe 503
Cdd:cd17630 141 TYGMTETASqVATKRPDGFGR---GGVGVLLPGRELRIVE----DGEIWVGGASLAMGYLRGQLVPEFNE---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 504 rfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLD 583
Cdd:cd17630 204 --DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1816261920 584 EDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:cd17630 282 PAE-----LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
119-562 |
3.38e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 132.15 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRggkkiplkRNVDEALFECPSVEQVIMVKRTGDEID--------FIE-GRDTWWHEEIsgpdiedyckpESMRSA 269
Cdd:COG1022 119 EDQEQL--------DKLLEVRDELPSLRHIVVLDPRGLRDDprllsldeLLAlGREVADPAEL-----------EARRAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 ----DPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVH-----WCtadigWITGHSYTVYGpLALGAT- 339
Cdd:COG1022 180 vkpdDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERTVSYYA-LAAGATv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 340 ------------------TLLFeGVPtyprpdRYWEIInRYGVN------------IF-YTTPTALR--ALRREGTQWTE 386
Cdd:COG1022 253 afaespdtlaedlrevkpTFML-AVP------RVWEKV-YAGIQakaeeagglkrkLFrWALAVGRRyaRARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 387 KYDL----------STLR-ILG-------SVGEPINPEVWIWFHehvGKGkLPLLDTWWQTETGSILISPLPyvGKLKPG 448
Cdd:COG1022 325 LLRLkhaladklvfSKLReALGgrlrfavSGGAALGPELARFFR---ALG-IPVLEGYGLTETSPVITVNRP--GDNRIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 449 STGKPLPGISAKIvnsdgsdAEANEgghLLITEpwPGMLTDIHNDRARYNRTYFErfPGSYETGDGARVDEDGDYWIMGR 528
Cdd:COG1022 399 TVGPPLPGVEVKI-------AEDGE---ILVRG--PNVMKGYYKNPEATAEAFDA--DGWLHTGDIGELDEDGFLRITGR 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816261920 529 LDDVINVSGhrlGT----TEIESALIAHPDVTEAAVVG 562
Cdd:COG1022 465 KKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
94-632 |
6.86e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 130.63 E-value: 6.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLengRRNKAALIWQGEPeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHS 173
Cdd:PRK06164 16 LDAHA---RARPDAVALIDED----RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 174 VIFAGFSAVSLQNRIIDCDAKILIAADGVlrggKKIPLKRNVDEALFEC-PSVEQVIMVKRTGDEI-DFIEGRdtwWHEE 251
Cdd:PRK06164 89 AVNTRYRSHEVAHILGRGRARWLVVWPGF----KGIDFAAILAAVPPDAlPPLRAIAVVDDAADATpAPAPGA---RVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 252 ISGPDIEDY--CKPESMRSADPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSyT 329
Cdd:PRK06164 162 FALPDPAPPaaAGERAADPDAGALLFTTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-T 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 330 VYGPLALGATTLL---FEGVPTYPRPDRYwEIINRYGVNIFYTtptalRALRREGtqwtEKYDLSTLRILGSVG-EPINP 405
Cdd:PRK06164 240 LLGALAGGAPLVCepvFDAARTARALRRH-RVTHTFGNDEMLR-----RILDTAG----ERADFPSARLFGFASfAPALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 406 EVWIWFHEHvgkgKLPLLDTWWQTETGSI-LISPL--PYVGKLKPGstGKPL-PGISAKIVNS-DGSDAEANEGGHLLIT 480
Cdd:PRK06164 310 ELAALARAR----GVPLTGLYGSSEVQALvALQPAtdPVSVRIEGG--GRPAsPEARVRARDPqDGALLPDGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 481 EPwPGMLTDIHNDRAryNRTYFERfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAV 560
Cdd:PRK06164 384 AP-SLMRGYLDNPDA--TARALTD-DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 561 VGIphEIKGQTV-YAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSG---KIMRRILRRIA 632
Cdd:PRK06164 460 VGA--TRDGKTVpVAFVIPTDGASPDEAG---LMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
115-632 |
1.85e-31 |
|
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: 128.60 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 115 EEEVRVFTYHMLHRKVCRFANVLKKIGVSkGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAK 194
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADGVLrggKKIPLKRNVD-EALFECPSVEQVIMVKRTGDEID-FIEGR--DTWWheeisgpDIEDYCKPESmrSAD 270
Cdd:cd05909 81 TVLTSKQFI---EKLKLHHLFDvEYDARIVYLEDLRAKISKADKCKaFLAGKfpPKWL-------LRIFGVAPVQ--PDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 271 PLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVhwctadigwitghsytVYGPL----ALGAT----TLL 342
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDV----------------VFGALpffhSFGLTgclwLPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 343 FEGVPT--YPRPDRYW---EIINRYGVNIFYTTPTALRA-LRRegtqwTEKYDLSTLRILGSVGEPINPEVWIWFHEHVG 416
Cdd:cd05909 212 LSGIKVvfHPNPLDYKkipELIYDKKATILLGTPTFLRGyARA-----AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 417 kgkLPLLDTWWQTETGSILISPLPYVGKlKPGSTGKPLPGISAKIVNSDG-SDAEANEGGHLLITEPwPGMLTDIHNDra 495
Cdd:cd05909 287 ---IRILEGYGTTECSPVISVNTPQSPN-KEGTVGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGP-NVMLGYLNEP-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 496 ryNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAH-PDVTEAAVVGIPHEIKGQTVYA 574
Cdd:cd05909 360 --ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 575 YVTLRSGldEDDEMRTVLREwvsQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:cd05909 438 LTTTTDT--DPSSLNDILKN---AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
119-634 |
2.50e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.56 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILI- 197
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIt 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 198 ---AADGVlrggKKIPLKRNVdealfecpsveqVIMVkrtgdeIDfiEGRDTWWH-EEISGPDiEDYCKPESMRSADPLF 273
Cdd:PLN02246 129 qscYVDKL----KGLAEDDGV------------TVVT------ID--DPPEGCLHfSELTQAD-ENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 ILHTSGSTGKAKGVVHSTGGYMTATAhttQWV------FDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFegvp 347
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIM---- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 348 tyPRPD--RYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPEVwiwfhEHVGKGKLP---L 422
Cdd:PLN02246 257 --PKFEigALLELIQRHKVTIAPFVPPIVLAIAKSPV--VEKYDLSSIRMVLSGAAPLGKEL-----EDAFRAKLPnavL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 423 LDTWWQTETGSILI-------SPLPyvgkLKPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEP--WPGMLtdihN 492
Cdd:PLN02246 328 GQGYGMTEAGPVLAmclafakEPFP----VKSGSCGTVVRNAELKIVDPEtGASLPRNQPGEICIRGPqiMKGYL----N 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 493 DRARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTV 572
Cdd:PLN02246 400 DPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVP 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 573 YAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR-RIAVG 634
Cdd:PLN02246 478 VAFVVRSNGseITEDE-----IKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRaKLAAG 537
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
119-629 |
2.87e-31 |
|
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: 127.80 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIa 198
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkiplkrnVDEALfecpsveqvimvkrtgDEIDFIEGRDTWwhEEISGPDIEDyckpesmrsaDPLFILHTS 278
Cdd:cd12118 107 ----------------VDREF----------------EYEDLLAEGDPD--FEWIPPADEW----------DPIALNYTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHS-TGGYMTATAHTTQWvfDLRDDDVHWCTADI----GWitGHSYTVYgplALGATTLLFEGVptypRPD 353
Cdd:cd12118 143 GTTGRPKGVVYHhRGAYLNALANILEW--EMKQHPVYLWTLPMfhcnGW--CFPWTVA---AVGGTNVCLRKV----DAK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 RYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDlSTLRILgSVGEPinPevwiwfHEHVGKGKLPL----LDTWWQT 429
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLP-HRVHVM-TAGAP--P------PAAVLAKMEELgfdvTHVYGLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETgsiliSPLPYVGKLKPGSTGKPLPGISAKI----VNSDGSDAEANEGGHLLITEPWPG-------------MLTDIHN 492
Cdd:cd12118 282 ET-----YGPATVCAWKPEWDELPTEERARLKarqgVRYVGLEEVDVLDPETMKPVPRDGktigeivfrgnivMKGYLKN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 493 DRAryNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTV 572
Cdd:cd12118 357 PEA--TAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 573 YAYVTLRSGLD--EDDemrtvLREWVSQKIGPIAVPETIQFSEgLPKTRSGKIMRRILR 629
Cdd:cd12118 433 CAFVELKEGAKvtEEE-----IIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
104-632 |
3.89e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 127.59 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIwqgepeEEVRVFTYHMLHRKVCRFANVLKKIGvSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:PRK07638 16 NKIAIK------ENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAADgvlrggkkiPLKRNVDEAlfECPSVEQvimvkrtgDEidfiegrdtwWHEEIS--GPDIEDYC 261
Cdd:PRK07638 89 LKERLAISNADMIVTER---------YKLNDLPDE--EGRVIEI--------DE----------WKRMIEkyLPTYAPIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 262 KPESmrsaDPLFILHTSGSTGKAKGVVHSTGGYMTAtahttqwvFDLRDDDVHWCTADIGWITG---HSYTVYGP---LA 335
Cdd:PRK07638 140 NVQN----APFYMGFTSGSTGKPKAFLRAQQSWLHS--------FDCNVHDFHMKREDSVLIAGtlvHSLFLYGAistLY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATTLLfegVPTYpRPDRYWEIINRYGVNIFYTTPTALRALRREgtqwtEKYDLSTLRILGSVGEpinpevwiWFHEHV 415
Cdd:PRK07638 208 VGQTVHL---MRKF-IPNQVLDKLETENISVMYTVPTMLESLYKE-----NRVIENKMKIISSGAK--------WEAEAK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 416 GKGK-----LPLLDTWWQTETgSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--WPGMLT 488
Cdd:PRK07638 271 EKIKnifpyAKLYEFYGASEL-SFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPqfFMGYII 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 DIHNDRarynrtyfERFPGSYET-GDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEI 567
Cdd:PRK07638 350 GGVLAR--------ELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSY 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 568 KGQTVYAYVtlrsgldEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:PRK07638 422 WGEKPVAII-------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
119-629 |
4.74e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 127.51 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRGGKKIpLKRNVdeALFECPSVEQVIMVKRTGDEIDFI-EGRDTW--W---HEEISGPDIEdycKPESMrsadpl 272
Cdd:PRK12406 90 HADLLHGLASA-LPAGV--TVLSVPTPPEIAAAYRISPALLTPpAGAIDWegWlaqQEPYDGPPVP---QPQSM------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 fiLHTSGSTGKAKGVVHS--TGGYMTATAHTTQWVFDLRDDDVHWCTADIGwitgHSY-TVYGPLA--LGATTLLfegvp 347
Cdd:PRK12406 158 --IYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLY----HSApNAYGLRAgrLGGVLVL----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 348 tYPR--PDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVwiwfhehvgkgKLPLLDt 425
Cdd:PRK12406 227 -QPRfdPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV-----------KRAMIE- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 426 WW---------QTETGSI-LISPLPYVGKlkPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMlTDI--HND 493
Cdd:PRK12406 294 WWgpviyeyygSTESGAVtFATSEDALSH--PGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA--GN-PDFtyHNK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RARynRTYFERfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVY 573
Cdd:PRK12406 369 PEK--RAEIDR-GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALM 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 574 AYVTLRSG--LDEDDeMRTVLREwvsqKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK12406 446 AVVEPQPGatLDEAD-IRAQLKA----RLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
121-562 |
5.21e-31 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 126.56 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAad 200
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 gvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeiSGPDiedyckpesmrsaDPLFILHTSGS 280
Cdd:cd05907 84 ----------------------------------------------------EDPD-------------DLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVHSTGGYM-TATAHTTQWvfDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGV-----------PT 348
Cdd:cd05907 99 TGRPKGVMLSHRNILsNALALAERL--PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAetllddlsevrPT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 349 Y----PRpdrYWE-IINRYGVnifyttpTALRALRREGTQWTEkydLSTLRILGSVGEPINPEVWIWFHeHVGkgkLPLL 423
Cdd:cd05907 177 VflavPR---VWEkVYAAIKV-------KAVPGLKRKLFDLAV---GGRLRFAASGGAPLPAELLHFFR-ALG---IPVY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 424 DTWWQTETGS-ILISPLpyvGKLKPGSTGKPLPGISAKIvnsdgsdAEANEgghLLITEpwPGMLTDIHNDRARYNRTYF 502
Cdd:cd05907 240 EGYGLTETSAvVTLNPP---GDNRIGTVGKPLPGVEVRI-------ADDGE---ILVRG--PNVMLGYYKNPEATAEALD 304
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 503 ErfPGSYETGDGARVDEDGDYWIMGRLDDVI-NVSGHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:cd05907 305 A--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-635 |
6.16e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.97 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 115 EEEVRvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAK 194
Cdd:PRK12583 41 HQALR-YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADGvLRG-------GKKIP-LKRNVDEALF--ECPSVEQVIMVkrtgdEIDFIEGRDTWWH-----EEISGPDIED 259
Cdd:PRK12583 120 WVICADA-FKTsdyhamlQELLPgLAEGQPGALAceRLPELRGVVSL-----APAPPPGFLAWHElqargETVSREALAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 260 ycKPESMRSADPLFILHTSGSTGKAKGVVHS-----TGGYMTATAhttqwvFDLRDDDVHWCTADIGWITGHSYTVYGPL 334
Cdd:PRK12583 194 --RQASLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAES------LGLTEHDRLCVPVPLYHCFGMVLANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 335 ALGATTLlfegvptYP----RPDRYWEIINRYGVNIFYTTPTALRAlRREGTQWTEkYDLSTLRILGSVGEPINPEVwiw 410
Cdd:PRK12583 266 TVGACLV-------YPneafDPLATLQAVEEERCTALYGVPTMFIA-ELDHPQRGN-FDLSSLRTGIMAGAPCPIEV--- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 411 FHEHVGKGKLP-LLDTWWQTETGSILI-----SPLPyvgkLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLlITEPWP 484
Cdd:PRK12583 334 MRRVMDEMHMAeVQIAYGMTETSPVSLqttaaDDLE----RRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL-CTRGYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GMLTDIHNDRARYNRTYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP 564
Cdd:PRK12583 409 VMKGYWNNPEATAESIDED---GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 565 HEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGE 635
Cdd:PRK12583 486 DEKYGEEIVAWVRLHPGhaASEEE-----LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEE 553
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
99-629 |
1.41e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 126.31 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 99 ENGRRN--KAALIWqGEpeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHsvif 176
Cdd:PRK07470 15 QAARRFpdRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 177 agfsaVSLQNRIIDCDAKILIAADG--VLRGGKKIPlkRNVDEALFECPSVEQVIMVKRTGDEIDFiegrdtwwhEEISG 254
Cdd:PRK07470 85 -----VPTNFRQTPDEVAYLAEASGarAMICHADFP--EHAAAVRAASPDLTHVVAIGGARAGLDY---------EALVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 255 PDIEDYCKPESMRSADPLFILHTSGSTGKAKGVVhSTGGYMT--ATAHTTQWVFDLRDDDVHWCTADIGwitgHSYTVYG 332
Cdd:PRK07470 149 RHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAV-LTHGQMAfvITNHLADLMPGTTEQDASLVVAPLS----HGAGIHQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 333 --PLALGATTLLfegvPTYPR--PDRYWEIINRYGVNIFYTTPTALRALRREGTqwTEKYDLSTLRILGSVGEPINPE-- 406
Cdd:PRK07470 224 lcQVARGAATVL----LPSERfdPAEVWALVERHRVTNLFTVPTILKMLVEHPA--VDRYDHSSLRYVIYAGAPMYRAdq 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 407 ---------VWIwfhEHVGKGKLplldtwwqteTGSILISPlPYVGKLKP------GSTGKPLPGISAKIVNSDGSDAEA 471
Cdd:PRK07470 298 kralaklgkVLV---QYFGLGEV----------TGNITVLP-PALHDAEDgpdariGTCGFERTGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEP--WPGMLtdiHNDRAryNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESAL 549
Cdd:PRK07470 364 GETGEICVIGPavFAGYY---NNPEA--NAKAFRD--GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 550 IAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRI 627
Cdd:PRK07470 437 LTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGapVDEAE-----LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKM 511
|
..
gi 1816261920 628 LR 629
Cdd:PRK07470 512 VR 513
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
544-622 |
2.05e-30 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 114.18 E-value: 2.05e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 544 EIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGK 622
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
120-629 |
2.14e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 126.32 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLK-KIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAK-ILI 197
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 198 AADgvlrggkkipLKRNVDEALFECPsVEQVIMVkRTGDEIDFIEG--------------------RDTWWHEEISGPDI 257
Cdd:PRK08974 128 VSN----------FAHTLEKVVFKTP-VKHVILT-RMGDQLSTAKGtlvnfvvkyikrlvpkyhlpDAISFRSALHKGRR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 258 EDYCKPEsMRSADPLFILHTSGSTGKAKGVVhSTGGYMTATAHTTQWVFD--LRDDDVHWCTAdigwitghsYTVYGPLA 335
Cdd:PRK08974 196 MQYVKPE-LVPEDLAFLQYTGGTTGVAKGAM-LTHRNMLANLEQAKAAYGplLHPGKELVVTA---------LPLYHIFA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATTLLF--EGVP----TYPR--PDRYWEIiNRY------GVNIFYTtptALraLRREGTQwteKYDLSTLRILGSVGE 401
Cdd:PRK08974 265 LTVNCLLFieLGGQnlliTNPRdiPGFVKEL-KKYpftaitGVNTLFN---AL--LNNEEFQ---ELDFSSLKLSVGGGM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVWIWFHEHVGKGklpLLDTWWQTETgSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITE 481
Cdd:PRK08974 336 AVQQAVAERWVKLTGQY---LLEGYGLTEC-SPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 482 P------W--PGMLTDIHNDrarynrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHP 553
Cdd:PRK08974 412 PqvmlgyWqrPEATDEVIKD-------------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 554 DVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQkigpIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK08974 479 KVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTG----YKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-622 |
3.93e-30 |
|
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: 122.11 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSADPLFILHTSGSTGKAKGVVHSTG----GYMTATAHTTqwVFDLRDDDVHWCTADIGWIT---------GHSYTVYGP 333
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEdifrMLMGGADFGT--GEFTPSEDAHKAAAAAAGTVmfpapplmhGTGSWTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 334 LALGATTLLFEGVPTypRPDRYWEIINRYGVNIFYTTPTA-----LRALRREGTqwtekYDLSTLRILGSVGEPINPEVW 408
Cdd:cd05924 79 GLLGGQTVVLPDDRF--DPEEVWRTIEKHKVTSMTIVGDAmarplIDALRDAGP-----YDLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 409 IWFHEHVGKgkLPLLDTWWQTETGSILISplpyVGKLKPGSTGK-PLPGISAKIVNSDGSDAEANEGGhllitEPWPGML 487
Cdd:cd05924 152 QGLLELVPN--ITLVDAFGSSETGFTGSG----HSAGSGPETGPfTRANPDTVVLDDDGRVVPPGSGG-----VGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 488 TDI----HNDRARYNRTYFERFPGSYE-TGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:cd05924 221 GHIplgyYGDEAKTAETFPEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 563 IPHEIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGK 622
Cdd:cd05924 301 RPDERWGQEVVAVVQLREGAGVDLEE---LREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-628 |
6.24e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.38 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 7 ENLMSEQRTFDPSREMEQKILD------QANLTAEKYEQACRM------ATDSPEEfwADRARDLLHWTRDFRTTLEsDP 74
Cdd:PRK12316 402 QPLVADIEALDTVAGLEFGQLEwksrttQFDLTLDTYEKGGRLhaaltyATDLFEA--RTVERMARHWQNLLRGMVE-NP 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 75 EKH----------EYK-----WFSGGRLNASYNCLDRHLENG--RRNKAALIWQGEPEeevrvFTYHMLHRKVCRFANVL 137
Cdd:PRK12316 479 QARvdelpmldaeERGqlvegWNATAAEYPLQRGVHRLFEEQveRTPEAPALAFGEET-----LDYAELNRRANRLAHAL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 138 KKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADGVLRggkKIPLKRNVDE 217
Cdd:PRK12316 554 IERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGR---KLPLAAGVQV 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 218 ALFECPSVeqvimvkrtgdeidFIEGRDTwwheeiSGPDIEdyCKPEsmrsaDPLFILHTSGSTGKAKGVVHSTGgymtA 297
Cdd:PRK12316 631 LDLDRPAA--------------WLEGYSE------ENPGTE--LNPE-----NLAYVIYTSGSTGKPKGAGNRHR----A 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 298 TAHTTQWVFDLRDDDVHwctADIGWITGHSYTV-----YGPLALGATTLLfeGVPTYPR-PDRYWEIINRYGVNIFYTTP 371
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVG---DTVLQKTPFSFDVsvwefFWPLMSGARLVV--AAPGDHRdPAKLVELINREGVDTLHFVP 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 372 TALRALRREGtqwtEKYDLSTLRILGSVGEPINPEVwiwfHEHVgKGKLP---LLDTWWQTETgSILISPLPYV--GKLK 446
Cdd:PRK12316 755 SMLQAFLQDE----DVASCTSLRRIVCSGEALPADA----QEQV-FAKLPqagLYNLYGPTEA-AIDVTHWTCVeeGGDS 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 447 PgSTGKPLPGISAKIVNSDGsdaeanegghllitEPWP-GMLTDIHNDRARYNRTYF-------ERFPGS--------YE 510
Cdd:PRK12316 825 V-PIGRPIANLACYILDANL--------------EPVPvGVLGELYLAGRGLARGYHgrpgltaERFVPSpfvagermYR 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 511 TGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGipheIKGQTVYAYVTLRsglDEDDEMRT 590
Cdd:PRK12316 890 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE---SEGGDWRE 962
|
650 660 670
....*....|....*....|....*....|....*...
gi 1816261920 591 VLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK12316 963 ALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
270-625 |
6.54e-30 |
|
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: 121.21 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGhsytvygpLALGATTLLFEGV--- 346
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGG--------LWWILTCLIHGGLcvt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 -PTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwTEKYdLSTLRILGSVGE-PINPE--VWIWFhehvgkGKLPL 422
Cdd:cd17635 74 gGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKS-ANAT-VPSLRLIGYGGSrAIAADvrFIEAT------GLTNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 423 LDTWWQTETGSILIspLPYVGKLKP-GSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWpgMLTDIHNDRARYNRTY 501
Cdd:cd17635 146 AQVYGLSETGTALC--LPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 502 FErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVtLRSG 581
Cdd:cd17635 222 ID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV-VASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1816261920 582 ldEDDEMR-TVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd17635 298 --ELDENAiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
122-628 |
2.23e-29 |
|
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: 121.99 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADg 201
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdEALFECPSVEQVIMVKRTGDEidfiegrdtwwheeisGPDIedyckPESMRSA--DPLFILHTSG 279
Cdd:cd12114 93 ---------------PDAQLDVAVFDVLILDLDALA----------------APAP-----PPPVDVApdDLAYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 280 STGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTA----DIGwitghSYTVYGPLALGATTLLfegvptyPRPDR- 354
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINR-RFAVGPDDRVLALSslsfDLS-----VYDIFGALSAGATLVL-------PDEARr 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 ----YW-EIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLR-ILGSvGEpinpevWIwfhehvgkgKLPLLDTWWQ 428
Cdd:cd12114 204 rdpaHWaELIERHGVTLWNSVPALLEMLLDVLEA--AQALLPSLRlVLLS-GD------WI---------PLDLPARLRA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 -------------TETG--SIL---------ISPLPYvgklkpgstGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwp 484
Cdd:cd12114 266 lapdarlislggaTEASiwSIYhpidevppdWRSIPY---------GRPLANQRYRVLDPRGRDCPDWVPGELWIGGR-- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GMLTDIHNDRARYNRTYFERFPGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:cd12114 335 GVALGYLGDPELTAARFVTHPDGErlYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVV 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 563 IPhEIKGQTVYAYVTLRSGLDEDDEmrTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd12114 415 LG-DPGGKRLAAFVVPDNDGTPIAP--DALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
122-628 |
2.56e-29 |
|
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: 121.27 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHsvifagfsavslqnriidcdakiliaadg 201
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAY----------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkIPLkrnvDEALfecPSveqvimvkrtgDEIDFIegrdtwwheeisgpdIEDY-CKPESMRSADPLFILHTSGS 280
Cdd:cd12115 77 -------VPL----DPAY---PP-----------ERLRFI---------------LEDAqARLVLTDPDDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVV---------------HSTGGYMTATAHTTQWVFDLRdddvhwctadigwitghSYTVYGPLALGATTLLFEG 345
Cdd:cd12115 117 TGRPKGVAiehrnaaaflqwaaaAFSAEELAGVLASTSICFDLS-----------------VFELFGPLATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 346 V---PTYPRPDryweiinryGVNIFYTTPTALRALRREGtqwtekyDL-STLRILGSVGEPINPEVWIWFHEHVGKGKL- 420
Cdd:cd12115 180 VlalPDLPAAA---------EVTLINTVPSAAAELLRHD-------ALpASVRVVNLAGEPLPRDLVQRLYARLQVERVv 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 ----PLLDTWWQTetgsilISPLPyVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMltdihndrar 496
Cdd:cd12115 244 nlygPSEDTTYST------VAPVP-PGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGA--GV---------- 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 497 yNRTYF-------ERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVV 561
Cdd:cd12115 305 -ARGYLgrpgltaERFlpdpfgPGArlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 562 GIPHEIKGQTVYAYVTLRSGLDEDdemRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd12115 384 AIGDAAGERRLVAYIVAEPGAAGL---VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-629 |
1.58e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 120.47 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsviFAGFSAVSLQNRIID----CDAK 194
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESEIKKqaeaAGAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADGVLRGGKKIPLKRNVdeaLFEcPSVEQVIMVKRTGDEIDfiEGRDTWWHEEISGPDIedyCkpesmrsADPLfi 274
Cdd:PLN02330 130 LIVTNDTNYGKVKGLGLPVIV---LGE-EKIEGAVNWKELLEAAD--RAGDTSDNEEILQTDL---C-------ALPF-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 lhTSGSTGKAKGVVHStggYMTATAHTTQWVFDLRDDDVHWCTAdIGWITghSYTVYGPLALGATTLLFEGVPTyprpdr 354
Cdd:PLN02330 192 --SSGTTGISKGVMLT---HRNLVANLCSSLFSVGPEMIGQVVT-LGLIP--FFHIYGITGICCATLRNKGKVV------ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 yweIINRYGVNIFYTT------------PTALRALRREGTqwTEKYDLSTLRI--LGSVGEPINPEVWIWFhehvgKGKL 420
Cdd:PLN02330 258 ---VMSRFELRTFLNAlitqevsfapivPPIILNLVKNPI--VEEFDLSKLKLqaIMTAAAPLAPELLTAF-----EAKF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 P---LLDTWWQTETGSILIS---PLPYVGKLKPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEPWpgMLTDIHND 493
Cdd:PLN02330 328 PgvqVQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQC--VMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVY 573
Cdd:PLN02330 406 KEETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 574 AYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PLN02330 484 ACVVINPKAKESEED---ILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
120-629 |
2.57e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 120.91 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACArigavhsvifagfsavslqnriidcdakiliaA 199
Cdd:PRK06060 30 VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACL--------------------------------A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DGVLRGGKKIPLKRNvDEALFECPSveQVIMVKRTGDEID------FIEGRDTWWHEEISGPdiEDYckpESMRSADPLF 273
Cdd:PRK06060 78 RGVMAFLANPELHRD-DHALAARNT--EPALVVTSDALRDrfqpsrVAEAAELMSEAARVAP--GGY---EPMGGDALAY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 ILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLfEGVPTypRPD 353
Cdd:PRK06060 150 ATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPV--TPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 RYWEIINRYGVNIFYTTPTALRalRREGTQWTEKYdlSTLRILGSVGEPINPEVWIWFHEHVGKgkLPLLDTWWQTETGS 433
Cdd:PRK06060 227 AAAILSARFGPSVLYGVPNFFA--RVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 434 ILISPlpYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP--------WP-GMLTDihndrarynrtyfer 504
Cdd:PRK06060 301 TFVSN--RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPaiakgywnRPdSPVAN--------------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 505 fPGSYETGDGARVDEDGdyWIM--GRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGL 582
Cdd:PRK06060 364 -EGWLDTRDRVCIDSDG--WVTyrCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGA 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1816261920 583 DEDDE-MRTVLREWVSQkIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK06060 441 TIDGSvMRDLHRGLLNR-LSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
116-630 |
2.81e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 119.48 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 116 EEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAvHSVIF-AGFSAVSLQNRIIDCDAK 194
Cdd:PRK13382 64 DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLnTSFAGPALAEVVTREGVD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 195 ILIAADgvlrggKKIPLkrnVDEALFECPSVEQVImvkrtgdeiDFIEGRDTWWHEEISGPDIEDYCKPESMRSAdplFI 274
Cdd:PRK13382 143 TVIYDE------EFSAT---VDRALADCPQATRIV---------AWTDEDHDLTVEVLIAAHAGQRPEPTGRKGR---VI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHS-TGGYMTATAhttqwVFDlrdddvhwctaDIGWITGHSYTVYGPL--ALGATTLLFEGVPTYP- 350
Cdd:PRK13382 202 LLTSGTTGTPKGARRSgPGGIGTLKA-----ILD-----------RTPWRAEEPTVIVAPMfhAWGFSQLVLAASLACTi 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 351 ------RPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgklPLLD 424
Cdd:PRK13382 266 vtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 425 TWWQTETGSILISPlPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPW------PGMLTDIHNdraryn 498
Cdd:PRK13382 343 NYNATEAGMIATAT-PADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTqfdgytSGSTKDFHD------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 499 rtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTL 578
Cdd:PRK13382 416 --------GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 579 RSGLDEDDEmrtVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK13382 488 KPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
119-629 |
6.54e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 118.05 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRGGKKIPLKRNVdealfecPSVEqVIMVKRTGDEIDFIEGRdtwwheeisGPDIEDyckpeSMRSADPLF-ILHT 277
Cdd:PRK07514 107 DPANFAWLSKIAAAAGA-------PHVE-TLDADGTGSLLEAAAAA---------PDDFET-----VPRGADDLAaILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 278 SGSTGKAKGVVHSTGGYMT-ATAHTTQWVFdlRDDDV--------HwctadigwitghsytVYGpLALGATTLLFEGVPT 348
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSnALTLVDYWRF--TPDDVlihalpifH---------------THG-LFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 349 Y--PR--PDRYWEIINR----YGVNIFYTTPTALRALRREGTQwtekydlsTLRILGSVGEPINPEVWIWFHEHVGKgkl 420
Cdd:PRK07514 227 IflPKfdPDAVLALMPRatvmMGVPTFYTRLLQEPRLTREAAA--------HMRLFISGSAPLLAETHREFQERTGH--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQTETGsiLISPLPYVGKLKPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEPwpgmltdihNDRARYNR 499
Cdd:PRK07514 296 AILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGP---------NVFKGYWR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 ----TYFE-RFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYA 574
Cdd:PRK07514 365 mpekTAEEfRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 575 YVTLRSG--LDEDDEMRTVLREWVSQKigpiaVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK07514 445 VVVPKPGaaLDEAAILAALKGRLARFK-----QPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-628 |
1.00e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.27 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRggkKIPLkrnvdealfecPSVEQVIMVKRTGDeidfiegrdtwWHEEISGPDIEDYCKPESMrsadpLFILHTS 278
Cdd:PRK12467 616 QSHLLA---QLPV-----------PAGLRSLCLDEPAD-----------LLCGYSGHNPEVALDPDNL-----AYVIYTS 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGGYMTATAHTTQWvFDLRDDD----VHWCTADIGwitghSYTVYGPLALGATtLLFEGVPTYPRPDR 354
Cdd:PRK12467 666 GSTGQPKGVAISHGALANYVCVIAER-LQLAADDsmlmVSTFAFDLG-----VTELFGALASGAT-LHLLPPDCARDAEA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRYGVNIFYTTPTALRALRREGTQwTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgklpLLDTWWQTETgSI 434
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQASRV-ALPRPQRALVCGGEALQVDLLARVRALGPGAR-----LINHYGPTET-TV 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 LISPLPYVGKLKPGST---GKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNdRARYNRTYFERFPGS--- 508
Cdd:PRK12467 812 GVSTYELSDEERDFGNvpiGQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHR-RPALTAERFVPDPFGadg 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 ---YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVyAYVTLRSGLDE- 584
Cdd:PRK12467 889 grlYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGa 967
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1816261920 585 -----DDEMRTVLREWVSQKIgpiaVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK12467 968 ehqatRDELKAQLRQVLPDYM----VPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
269-630 |
1.28e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 116.63 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 269 ADPLFILHTSGSTGKAKGVV---HSTGGYMTATAHTTQWVfdlrDDD----------VHwctadiGWITGhsytVYGPLA 335
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVlsrRAIAADLDALAEAWQWT----ADDvlvhglplfhVH------GLVLG----VLGPLR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATtLLFEGVPTyprPDRYWEIINR-----YGVNIFYT----TPTALRALRREgtqwtekydlstlRILGSVGEPINPE 406
Cdd:PRK07787 194 IGNR-FVHTGRPT---PEAYAQALSEggtlyFGVPTVWSriaaDPEAARALRGA-------------RLLVSGSAALPVP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 407 VwiwFHEHVGKGKLPLLDTWWQTETgsiLISPLPYV-GKLKPGSTGKPLPGISAKIVNSDGSDAEANEG--GHLLITEPw 483
Cdd:PRK07787 257 V---FDRLAALTGHRPVERYGMTET---LITLSTRAdGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGP- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 484 pgMLTDIHNDRARYNRTYFeRFPGSYETGDGARVDEDGDYWIMGRLD-DVINVSGHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:PRK07787 330 --TLFDGYLNRPDATAAAF-TADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 563 IPHEIKGQTVYAYVTLRSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK07787 407 VPDDDLGQRIVAYVVGADDVAADE-----LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-633 |
3.63e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.52 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLrggKKIPLKRNVDEALFEcpsveqvimvkrtgdeidfiegRDTWWHEEISGpdiedycKPESMRSADPL-FILHT 277
Cdd:PRK12316 2107 QRHLL---ERLPLPAGVARLPLD----------------------RDAEWADYPDT-------APAVQLAGENLaYVIYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 278 SGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSyTVYGPLALGATTLLfegvptypRPDRYW- 356
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGA-LVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLI--------RDDELWd 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 -----EIINRYGVNIFYTTPTALRAL----RREGTQwtekydlSTLRILGSVGEPINPEVWIWFHEHVGKGKLplLDTWW 427
Cdd:PRK12316 2225 peqlyDEMERHGVTILDFPPVYLQQLaehaERDGRP-------PAVRVYCFGGEAVPAASLRLAWEALRPVYL--FNGYG 2295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 428 QTETgsiLISPLPY-VGKLKPGST-----GKPLPGISAKIVNSDGsdaeaneggHLLItepwPGMLTDIHNDRARYNRTY 501
Cdd:PRK12316 2296 PTEA---VVTPLLWkCRPQDPCGAayvpiGRALGNRRAYILDADL---------NLLA----PGMAGELYLGGEGLARGY 2359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 502 F-------ERF-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIpH 565
Cdd:PRK12316 2360 LnrpgltaERFvpdpfsaSGErlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-D 2438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 566 EIKGQTVYAYVTLRSGLDEDdemRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAV 633
Cdd:PRK12316 2439 GASGKQLVAYVVPDDAAEDL---LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDV 2503
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
102-629 |
8.33e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 114.60 E-value: 8.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRN--KAALIWQGEPeeevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGF 179
Cdd:PRK06145 13 RRTpdRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 180 SAVSLQNRIIDCDAKILIaadgvlrggkkiplkrnVDEALFECPSVEQVIMVkrtgdeIDFIEGRDTwwhEEISGPDIEd 259
Cdd:PRK06145 87 AADEVAYILGDAGAKLLL-----------------VDEEFDAIVALETPKIV------IDAAAQADS---RRLAQGGLE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 260 yCKPESMRSADPLF-ILHTSGSTGKAKGVVHSTGgymtatahttqwvfdlrddDVHWCTAD----IGWITGHSYTVYGPL 334
Cdd:PRK06145 140 -IPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLVVGPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 335 -ALGATTL-----LFEG----VPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPiN 404
Cdd:PRK06145 200 yHVGAFDLpgiavLWVGgtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DRFDLDSLAWCIGGGEK-T 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 405 PEVWIW-FHEHVGKGKLplLDTWWQTET--GSILISPLPYVGKLkpGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITE 481
Cdd:PRK06145 277 PESRIRdFTRVFTRARY--IDAYGLTETcsGDTLMEAGREIEKI--GSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 482 PwpGMLTDIHNDRARYNRTYFErfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVV 561
Cdd:PRK06145 353 P--KVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 562 GIPHEIKGQTVYAYVTLRSG----LDEddemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGatltLEA-------LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-630 |
1.31e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 VlrggkKIPLKRNVdealfecpsveQVIMVKRtgdeidfiegrdtwwheeisGPDIEDYCKPESMRSADPL-FILHTSGS 280
Cdd:PRK12316 3164 L-----RLPLAQGV-----------QVLDLDR--------------------GDENYAEANPAIRTMPENLaYVIYTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVHSTGgymtATAHTTQWVFDLRDDDVHWCTADIGWIT--GHSYTVYGPLALGATTLLfEGVPTYPRPDRYWEI 358
Cdd:PRK12316 3208 TGKPKGVGIRHS----ALSNHLCWMQQAYGLGVGDRVLQFTTFSfdVFVEELFWPLMSGARVVL-AGPEDWRDPALLVEL 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 359 INRYGVNIFYTTPTALRALRREgtqwTEKYDLSTLRILGSVGEPINPEVwiwfhEHVGKGKLPLLDTWWQTETGSILISP 438
Cdd:PRK12316 3283 INSEGVDVLHAYPSMLQAFLEE----EDAHRCTSLKRIVCGGEALPADL-----QQQVFAGLPLYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 439 LPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNDRA----RYNRTYFERFPGSYETGDG 514
Cdd:PRK12316 3354 QCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNRPGltaeRFVPDPFVPGERLYRTGDL 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 515 ARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVgiphEIKGQTVYAYVTLRsglDEDDEMRTVLRE 594
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPE---DEAGDLREALKA 3504
|
490 500 510
....*....|....*....|....*....|....*.
gi 1816261920 595 WVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK12316 3505 HLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-631 |
1.50e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLrggKKIPLkrnvdealfecPSVEQVIMVKRtgdeidfiegrDTWWHEEISGPDIedYCKPESMRsadplFILHTS 278
Cdd:PRK12467 3199 QAHLL---EQLPA-----------PAGDTALTLDR-----------LDLNGYSENNPST--RVMGENLA-----YVIYTS 3246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGgymtATAHTTQWVFDLRDDDVHwcTADIGWIT----GHSYTVYGPLALGATTLLFEGvpTYPRPDR 354
Cdd:PRK12467 3247 GSTGKPKGVGVRHG----ALANHLCWIAEAYELDAN--DRVLLFMSfsfdGAQERFLWTLICGGCLVVRDN--DLWDPEE 3318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRYGVNIFYTTPTALRALRREGtqwtEKYDLSTLRILGSVGEPINPEVWiwfhEHVgKGKLP---LLDTWWQTET 431
Cdd:PRK12467 3319 LWQAIHAHRISIACFPPAYLQQFAEDA----GGADCASLDIYVFGGEAVPPAAF----EQV-KRKLKprgLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 432 gSILISPLPYVGKLKPGST----GKPLPGISAKIVNSDGsdaeanegghllitEPWP-GMLTDIHNDRARYNRTYFER-- 504
Cdd:PRK12467 3390 -VVTVTLWKCGGDAVCEAPyapiGRPVAGRSIYVLDGQL--------------NPVPvGVAGELYIGGVGLARGYHQRps 3454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 505 ----------FPGS----YETGDGARVDEDG--DYwiMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEiK 568
Cdd:PRK12467 3455 ltaerfvadpFSGSggrlYRTGDLARYRADGviEY--LGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-G 3531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 569 GQTVYAYVTLRsglDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:PRK12467 3532 GKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
122-629 |
1.66e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 113.57 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAA-- 199
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASaa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 -DGVL-RGGKKIPLKRNVdealfecpsveqvimvkrtGDEID-FIEGRDTWwheEISGPDI-EDYCKPesmrsadplFIL 275
Cdd:PRK13390 106 lDGLAaKVGADLPLRLSF-------------------GGEIDgFGSFEAAL---AGAGPRLtEQPCGA---------VML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGV--------VHSTGGYMTATAHTtqwVFDLRDDDVHWCTADIGwitgHSytvyGPL-------ALGATT 340
Cdd:PRK13390 155 YSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARA---FYDISESDIYYSSAPIY----HA----APLrwcsmvhALGGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LL---FEGVPTYprpdRYweiINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEP------------INP 405
Cdd:PRK13390 224 VLakrFDAQATL----GH---VERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdvkhamidwLGP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 406 EVWIWFHEHVGKGkLPLLDT-WWQTEtgsilisplpyvgklkPGSTGKPLPGiSAKIVNSDGSDAEANEGGHLLITEPwp 484
Cdd:PRK13390 297 IVYEYYSSTEAHG-MTFIDSpDWLAH----------------PGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERD-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GMLTDIHNDRARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP 564
Cdd:PRK13390 357 RLPFRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 565 HEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK13390 437 DPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
120-626 |
1.84e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 113.83 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhsvifagfsAVSLQNRIIDCDAKILIAA 199
Cdd:PRK05852 43 AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV---------VVPLDPALPIAEQRVRSQA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DGVlrggkkiplkrnvdealfecpsveQVIMVKRTGdEIDFIEGRDTWWHEEIS-GPDIE------------------DY 260
Cdd:PRK05852 114 AGA------------------------RVVLIDADG-PHDRAEPTTRWWPLTVNvGGDSGpsggtlsvhldaateptpAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 261 CKPESMRSADPLfILHTSGSTGKAKgVVHSTGGYMTATAHTTQWVFDLRDDDVhwCTADIGWITGHsytvyGPLALGATT 340
Cdd:PRK05852 169 STPEGLRPDDAM-IMFTGGTTGLPK-MVPWTHANIASSVRAIITGYRLSPRDA--TVAVMPLYHGH-----GLIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LLFEGVPTYPRPDRY-----WEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHV 415
Cdd:PRK05852 240 LASGGAVLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 416 GKgklPLLDTWWQTE-TGSILISPLPYVGKLK-PGSTGKPLP---GISAKIVNSDGSDAEANEGGHLLITEPW--PGMLT 488
Cdd:PRK05852 320 AA---PVVCAFGMTEaTHQVTTTQIEGIGQTEnPVVSTGLVGrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTvvRGYLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 489 DIHNDRARYNRTYFErfpgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIK 568
Cdd:PRK05852 397 DPTITAANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLY 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 569 GQTVYAYVTLR-SGLDEDDEMRTVLREwvsqKIGPIAVPETIQFSEGLPKTRSGKIMRR 626
Cdd:PRK05852 470 GEAVAAVIVPReSAPPTAEELVQFCRE----RLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
122-630 |
1.90e-26 |
|
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: 112.79 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgPDiedyckpesmrsaDPLFILHTSGST 281
Cdd:cd17653 104 -----------------------------------------------------PD-------------DLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVV--HStggymtATAHTTQWV---FDLRDDDVHWCTADIGW--ITGhsyTVYGPLALGATTLLFEgvptyprPDR 354
Cdd:cd17653 118 GIPKGVMvpHR------GVLNYVSQPparLDVGPGSRVAQVLSIAFdaCIG---EIFSTLCNGGTLVLAD-------PSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 355 YWEIINRyGVNIFYTTPTALRALRREgtqwtekyDLSTLRILGSVGEPINPevwiwfhehvgkgklPLLDTWWQ------ 428
Cdd:cd17653 182 PFAHVAR-TVDALMSTPSILSTLSPQ--------DFPNLKTIFLGGEAVPP---------------SLLDRWSPgrrlyn 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 ----TETgSILISplpyVGKLKPG---STGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpgMLTD--IHNDRARYNR 499
Cdd:cd17653 238 aygpTEC-TISST----MTELLPGqpvTIGKPIPNSTCYILDADLQPVPEGVVGEICISGV---QVARgyLGNPALTASK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 TYFERF-PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIA-HPDVTEAAVVgipheIKGQTVYAY 575
Cdd:cd17653 310 FVPDPFwPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI-----VVNGRLVAF 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 576 VTlRSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:cd17653 385 VT-PETVDVDG-----LRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-625 |
1.48e-25 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 108.13 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTtQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLL--FEgvp 347
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQL-IHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMekFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 348 typrPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGepiNPEVWIWFHEHVGKgklplldTWW 427
Cdd:cd17637 77 ----PAEALELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLD---APETIQRFEETTGA-------TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 428 ----QTETgSILISPLPYVGKlkPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP------WpgmltdihNDRARY 497
Cdd:cd17637 141 slygQTET-SGLVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPlvfqgyW--------NLPELT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 498 NRTYFErfpGSYETGDGARVDEDGDYWIMGRL--DDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAY 575
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 576 VTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd17637 287 CVLKPGatLTADE-----LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
119-628 |
7.71e-25 |
|
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: 107.94 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedycKPEsmrsaDPLFILHTS 278
Cdd:cd17650 91 ---------------------------------------------------------------QPE-----DLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTGKAKGVVHSTGGYMTAtAHTTQWVFDLRDDDVHWCTadigwITGHSYTVY-GPLALgatTLLFEGVpTYPRPD---- 353
Cdd:cd17650 103 GTTGKPKGVMVEHRNVAHA-AHAWRREYELDSFPVRLLQ-----MASFSFDVFaGDFAR---SLLNGGT-LVICPDevkl 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 ---RYWEIINRYGVNIFYTTPTALRALRREgTQWtEKYDLSTLRILgSVGEPINPEVW-IWFHEHVGKGkLPLLDTWWQT 429
Cdd:cd17650 173 dpaALYDLILKSRITLMESTPALIRPVMAY-VYR-NGLDLSAMRLL-IVGSDGCKAQDfKTLAARFGQG-MRIINSYGVT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 ETgsiLISPLPYVGKLKPGST------GKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHND----RARYNR 499
Cdd:cd17650 249 EA---TIDSTYYEEGRDPLGDsanvpiGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpeltAERFVE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 500 TYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVgIPHEIKGQT-VYAYVTL 578
Cdd:cd17650 324 NPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVVA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1816261920 579 RSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17650 403 AATLNTAE-----LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-628 |
8.92e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT 4654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADGVLRGgkkIPLKRNVDeALFecpsveqvimVKRTGDeidfiegrdtwWheeisgpdiEDYCKPESMRSADP---LFIL 275
Cdd:PRK12316 4655 QSHLLQR---LPIPDGLA-SLA----------LDRDED-----------W---------EGFPAHDPAVRLHPdnlAYVI 4700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDD--VHWCTADIgwiTGHSYTVYGPLALGATTLLFEgvPTYPRPD 353
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGS-LVNHLHATGERYELTPDDrvLQFMSFSF---DGSHEGLYHPLINGASVVIRD--DSLWDPE 4774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 RYWEIINRYGVNIFYTTPTALRALRREGTqwtEKYDLSTLRILGSVGEPINPE---VWIWFHEHVGkgklpLLDTWWQTE 430
Cdd:PRK12316 4775 RLYAEIHEHRVTVLVFPPVYLQQLAEHAE---RDGEPPSLRVYCFGGEAVAQAsydLAWRALKPVY-----LFNGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 TgSILISPLPYVGKLKPGST----GKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGmltdihndrarynRTYF---- 502
Cdd:PRK12316 4847 T-TVTVLLWKARDGDACGAAympiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVA-------------RGYLerpa 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 503 ---ERF-------PGS--YETGDGARVDEDG--DYwiMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIK 568
Cdd:PRK12316 4913 ltaERFvpdpfgaPGGrlYRTGDLARYRADGviDY--LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG 4990
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 569 GQTVYAYVTLRSGLDEDD----EMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK12316 4991 KQLVGYVVPQDPALADADeaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
102-630 |
2.67e-24 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 107.32 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKAALIWQGEPEEEVRVFTYHMLHRKVCRFANVLKKIGvSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFA---G 178
Cdd:cd05931 6 RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptpG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 179 FSAVSLQNRIIDCDAKILIAADGVLRGgkkiplkrnVDEALFECPSVeqvimvkrtgdeidfieGRDTWWHEEISGPDIE 258
Cdd:cd05931 85 RHAERLAAILADAGPRVVLTTAAALAA---------VRAFAASRPAA-----------------GTPRLLVVDLLPDTSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 259 DYCKPESMRSADPLFILHTSGSTGKAKGVVHSTGGyMTATAHTTQWVFDLRDDD--VHW--CTADIGWITGhsytVYGPL 334
Cdd:cd05931 139 ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDvvVSWlpLYHDMGLIGG----LLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 335 ALGATTLLFEGVPTYPRPDRYWEIINRYGVNIfyttpTA---------LRALRREGtqwTEKYDLSTLRILGSVGEPINP 405
Cdd:cd05931 214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATI-----SAapnfaydlcVRRVRDED---LEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 406 EVWIWFHE--------------------------HVGKGKLPLLDtwwqTETGSILISPLPYVGKLKPG-----STGKPL 454
Cdd:cd05931 286 ATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVL----RVDRDALAGRAVAVAADDPAarelvSCGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 455 PGISAKIVNSDGSdAEANEGGhllITEPW---PGMLTDIHNDRARYNRTyFERFPGSYE-----TGD-GARVdeDGDYWI 525
Cdd:cd05931 362 PDQEVRIVDPETG-RELPDGE---VGEIWvrgPSVASGYWGRPEATAET-FGALAATDEggwlrTGDlGFLH--DGELYI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 526 MGRLDDVINVSGHRLGTTEIESALIAHPDV---TEAAVVGIPHEIKGQTVYAYVTLRSGLDED-DEMRTVLREWVSQKIG 601
Cdd:cd05931 435 TGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERLVVVAEVERGADPADlAAIAAAIRAAVAREHG 514
|
570 580 590
....*....|....*....|....*....|
gi 1816261920 602 pIAVPETIQFSEG-LPKTRSGKIMRRILRR 630
Cdd:cd05931 515 -VAPADVVLVRPGsIPRTSSGKIQRRACRA 543
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
104-628 |
3.45e-24 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 106.64 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGEPeeevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:cd17655 12 DHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIAAdgvlrggKKIPLKRNVDEalfecpsveqvimvkrtgdEIDFIEGRDTWWHEEISgpdiedyCKP 263
Cdd:cd17655 86 IQYILEDSGADILLTQ-------SHLQPPIAFIG-------------------LIDLLDEDTIYHEESEN-------LEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 ESmRSADPLFILHTSGSTGKAKGV----------VHSTGGYMTATAHTT-----QWVFDLRdddvhwctadigwitghSY 328
Cdd:cd17655 133 VS-KSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWANKVIYQGEHLRvalfaSISFDAS-----------------VT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 329 TVYGPLALGATTLLfegvptYPRPDRYW-----EIINRYGVNIFYTTPTALRALRREGtqwteKYDLSTLRILGSVGEPI 403
Cdd:cd17655 195 EIFASLLSGNTLYI------VRKETVLDgqaltQYIRQNRITIIDLTPAHLKLLDAAD-----DSEGLSLKHLIVGGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 404 NPEVWIWFHEHVGKGKLpLLDTWWQTETgSILISPLPYVGKLKPG---STGKPLPGISAKIVNSDGSDAEANEGGHLLIT 480
Cdd:cd17655 264 STELAKKIIELFGTNPT-ITNAYGPTET-TVDASIYQYEPETDQQvsvPIGKPLGNTRIYILDQYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 481 epwpGMLTDihndRARYNRTYF--ERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALI 550
Cdd:cd17655 342 ----GEGVA----RGYLNRPELtaEKFvddpfvPGErmYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLL 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 551 AHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDemrtvLREWVSQKIGPIAVPET-IQFSEgLPKTRSGKIMRRIL 628
Cdd:cd17655 414 QHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ-----LREFLARELPDYMIPSYfIKLDE-IPLTPNGKVDRKAL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
122-631 |
4.03e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 106.85 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVL-KKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAA- 199
Cdd:PLN02574 68 SYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSp 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 DGVlrgGKKIPLKRnvdealfecpsveQVIMVKRTGDeIDFIEGRDTWWHEEISGPDieDYCKPESMRSADPLFILHTSG 279
Cdd:PLN02574 148 ENV---EKLSPLGV-------------PVIGVPENYD-FDSKRIEFPKFYELIKEDF--DFVPKPVIKQDDVAAIMYSSG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 280 STGKAKGVVhSTGGYMTATAHT------TQWVFDlRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEgvptypRPD 353
Cdd:PLN02574 209 TTGASKGVV-LTHRNLIAMVELfvrfeaSQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMR------RFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 --RYWEIINRYGVNIFYTTPTALRALRREgTQWTEKYDLSTLRILGSVGEPINPEVWIWFHE---HVGkgklpLLDTWWQ 428
Cdd:PLN02574 281 asDMVKVIDRFKVTHFPVVPPILMALTKK-AKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQtlpHVD-----FIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TETGSILISPLPYVGKLKPGSTGKPLPGISAKIVN-SDGSDAEANEGGHLLITEPwpGMLTDIHNDRARYNRTYFERfpG 507
Cdd:PLN02574 355 TESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGP--GVMKGYLNNPKATQSTIDKD--G 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 508 SYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDED 585
Cdd:PLN02574 431 WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGstLSQE 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816261920 586 DEMrtvlrEWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRI 631
Cdd:PLN02574 511 AVI-----NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
121-632 |
6.28e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 105.70 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLAcarigavhsVIFAGFSAVSL---------QNRIIDC 191
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLA---------VLKAGGAFVPLdpshplqrlQEILQDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 192 DAKILIAadgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeiSGPDiedyckpesmrsaDP 271
Cdd:cd05918 96 GAKVVLT------------------------------------------------------SSPS-------------DA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 272 LFILHTSGSTGKAKGVV--H---STG--GYMTATAHTTQW--------VFDLrdddvhwCTADIgwitghsytvYGPLAL 336
Cdd:cd05918 109 AYVIFTSGSTGKPKGVVieHralSTSalAHGRALGLTSESrvlqfasyTFDV-------SILEI----------FTTLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 337 GATTLlfegVPT-YPRPDRYWEIINRYGVNIFYTTPTALRALRREgtqwtekyDLSTLRILGSVGEPINPEVwiwfhehv 415
Cdd:cd05918 172 GGCLC----IPSeEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLRTLVLGGEALTQSD-------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 416 gkgklplLDTWWQ----------TET--GSILISPLPyvgKLKPGSTGKPLPGiSAKIVNSDGSDAEANEG--GHLLITE 481
Cdd:cd05918 232 -------VDTWADrvrlinaygpAECtiAATVSPVVP---STDPRNIGRPLGA-TCWVVDPDNHDRLVPIGavGELLIEG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 482 PW--PGMLTD--------IHN--DRARYNRTYFERFpgsYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESAL 549
Cdd:cd05918 301 PIlaRGYLNDpektaaafIEDpaWLKQEGSGRGRRL---YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 550 IAHPDVTEAAVVGI-----------------PHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKIGPIAVPETIQFS 612
Cdd:cd05918 378 RQSLPGAKEVVVEVvkpkdgssspqlvafvvLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPL 457
|
570 580
....*....|....*....|
gi 1816261920 613 EGLPKTRSGKIMRRILRRIA 632
Cdd:cd05918 458 SHLPLTASGKIDRRALRELA 477
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
421-629 |
8.17e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.00 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQTETGSIL-ISPLPYVgklKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEP------W--PGMLTDIH 491
Cdd:PRK05677 353 AICEGYGMTETSPVVsVNPSQAI---QVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPqvmkgyWqrPEATDEIL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 492 NDRarynrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQT 571
Cdd:PRK05677 430 DSD------------GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 572 VYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQ---VMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
107-628 |
1.23e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.18 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 107 ALIWQGEPeeevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQN 186
Cdd:PRK05691 1149 ALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAY 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 187 RIIDCDAKILIAADGVLrggkkiplkrnvdEALfecPSVEQVIMVKRtgDEIDFiegrDTWwheeisgPDiedyCKPESM 266
Cdd:PRK05691 1223 MLADSGVELLLTQSHLL-------------ERL---PQAEGVSAIAL--DSLHL----DSW-------PS----QAPGLH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSADPL-FILHTSGSTGKAKGVvhstGGYMTATAHTTQWV---FDLRDDDVHWCTADIGWITGhSYTVYGPLALGATtLL 342
Cdd:PRK05691 1270 LHGDNLaYVIYTSGSTGQPKGV----GNTHAALAERLQWMqatYALDDSDVLMQKAPISFDVS-VWECFWPLITGCR-LV 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 343 FEGVPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREgtqwTEKYDLSTLRILGSVGEPINPEV---------WIWFHE 413
Cdd:PRK05691 1344 LAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE----PLAAACTSLRRLFSGGEALPAELrnrvlqrlpQVQLHN 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 HVGKGKLPLLDTWWQTETGSILISPLpyvgklkpgstGKPLPGISAKIVNSDGSDAEANEGGHLLITepwpgmltDIHND 493
Cdd:PRK05691 1420 RYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELNLLPPGVAGELCIG--------GAGLA 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RARYNRTYF--ERF-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVg 562
Cdd:PRK05691 1481 RGYLGRPALtaERFvpdplgeDGArlYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL- 1559
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816261920 563 IPHEIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK05691 1560 VREGAAGAQLVGYYTGEAGQEAEAER---LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
272-628 |
3.34e-23 |
|
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: 103.28 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 272 LFILHTSGSTGKAKGVV--HSTggyMTATAHTTQWVFDLRDDDVHWCTADIGWITGhSYTVYGPLALGATTLLfegVPTY 349
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMieHQS---LVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVL---RPEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 PRPD--RYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDL-STLRILGSVGEPINPEVWIWFHEHVGKgKLPLLDTW 426
Cdd:cd17644 182 MRSSleDFVQYIQQWQLTVLSLPPAYWHLLVLELLL--STIDLpSSLRLVIVGGEAVQPELVRQWQKNVGN-FIQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 427 WQTE---TGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDgsdaeanegghlLITEPwPGMLTDIHNDRARYNRTYFE 503
Cdd:cd17644 259 GPTEatiAATVCRLTQLTERNITSVPIGRPIANTQVYILDEN------------LQPVP-VGVPGELHIGGVGLARGYLN 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 504 R------------FPGS-----YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHE 566
Cdd:cd17644 326 RpeltaekfishpFNSSeserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 567 IKGQTVYAYVTLRSgldEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17644 406 PGNKRLVAYIVPHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
270-629 |
3.77e-23 |
|
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: 101.20 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHS-----TGGYMTATAhttqwvFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLL-- 342
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLThhnivNNGYFIGER------LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 343 --FEGVPTYprpdrywEIINRYGVNIFYTTPTALRALRreGTQWTEKYDLSTLR--ILGsvGEPINPEVWIWFHE----- 413
Cdd:cd05917 77 psFDPLAVL-------EAIEKEKCTALHGVPTMFIAEL--EHPDFDKFDLSSLRtgIMA--GAPCPPELMKRVIEvmnmk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 --HVGKGklplldtwwQTETGSILISPLPYVG-KLKPGSTGKPLPGISAKIVNSDGSdaeanegghlliTEPWPGMLTDI 490
Cdd:cd05917 146 dvTIAYG---------MTETSPVSTQTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGG------------IVPPVGVPGEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 491 -----------HNDRARYNRTYFERfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAA 559
Cdd:cd05917 205 cirgysvmkgyWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQ 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 560 VVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05917 283 VVGVPDERYGEEVCAWIRLKEGaeLTEED-----IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
105-630 |
6.68e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 102.89 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 105 KAALIWQGEPEEEVRvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSL 184
Cdd:cd05915 10 RKEVVSRLHTGEVHR-TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 185 QNRIIDCDAKILIAADGVLR-GGKKIPLKRNVDEALFECPSVEQVIMVKRTGDeidfiegrdtwwheeisgPDIedycKP 263
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLLPlVEAIRGELKTVQHFVVMDEKAPEGYLAYEEAL------------------GEE----AD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 264 -ESMRSADPLFILHTSGSTGKAKGVVHS-TGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYtVYGPLALGATTL 341
Cdd:cd05915 147 pVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCL-PYAATLVGAKQV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 342 LFEGVPTyprPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLsTLRILGSVGEPinPEVWIWFH--------- 412
Cdd:cd05915 226 LPGPRLD---PASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKT-LRRLVVGGSAA--PRSLIARFermgvevrq 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 413 -----EHVGKGKLPLLDTWWQT--ETGSILISP-------LPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEAnegghll 478
Cdd:cd05915 300 gygltETSPVVVQNFVKSHLESlsEEEKLTLKAktglpipLVRLRVADEEGRPVPKDGKALGEVQLKGPWITG------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 479 itepwpGMLTDIHNDRARYNRTyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEA 558
Cdd:cd05915 373 ------GYYGNEEATRSALTPD------GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEA 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 559 AVVGIPHEIKGQTVYAYVTLRSGLDEDDEmrtvLREWVSQKIGPIA-VPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:cd05915 441 AVVAIPHPKWQERPLAVVVPRGEKPTPEE----LNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
268-630 |
1.06e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 102.45 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 268 SADPLFIL-HTSGSTGKAKGVVhSTGGYMTATAHTTQWVFDLRDDDVHWCTADI--------GWITGhsytvygpLALGA 338
Cdd:PRK07867 150 DPDDLFMLiFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPLfhsnavmaGWAVA--------LAAGA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 339 TTLLfegvptyPR--------PDryweiINRYGVNIF--------YTTPTALRALRREgtqwtekydlSTLRIL-GSVGE 401
Cdd:PRK07867 221 SIAL-------RRkfsasgflPD-----VRRYGATYAnyvgkplsYVLATPERPDDAD----------NPLRIVyGNEGA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVwiwFHEHVGkgkLPLLDTWWQTETGsILISPLPyvgKLKPGSTGKPLPGIsaKIVNSDGSD----AEANEGGHL 477
Cdd:PRK07867 279 PGDIAR---FARRFG---CVVVDGFGSTEGG-VAITRTP---DTPPGALGPLPPGV--AIVDPDTGTecppAEDADGRLL 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 478 --------LITEPWPGMLTDIHNDRArynrTYFERF-PGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESA 548
Cdd:PRK07867 347 nadeaigeLVNTAGPGGFEGYYNDPE----ADAERMrGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERI 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 549 LIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDED-DEMRTVLREwvSQKIGPIAVPETIQFSEGLPKTRSGKIMRRI 627
Cdd:PRK07867 423 LLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDpDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQ 500
|
...
gi 1816261920 628 LRR 630
Cdd:PRK07867 501 LSA 503
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
429-632 |
2.42e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 101.44 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TETgSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpgmltdihndraRYNRTYFERfP-- 506
Cdd:PRK12492 368 TET-SPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP-------------QVMKGYWQQ-Pea 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 507 --------GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTL 578
Cdd:PRK12492 433 taealdaeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 579 RSGLDEDDEMRTVLREwvsqKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:PRK12492 513 RDPGLSVEELKAYCKE----NFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
241-631 |
3.03e-22 |
|
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: 100.82 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 241 IEGRDTWW-HEEISGPDIEDYCKPES------MRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDV 313
Cdd:cd05906 132 FAGLETLSgLPGIRVLSIEELLDTAAdhdlpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 314 --HWCTADigWITGHSYTVYGPLALGATTLlfeGVPT---YPRPDRYWEIINRYGV------NIFYTTptaLRALRREGT 382
Cdd:cd05906 211 flNWVPLD--HVGGLVELHLRAVYLGCQQV---HVPTeeiLADPLRWLDLIDRYRVtitwapNFAFAL---LNDLLEEIE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 383 qwTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGKLP---LLDTWWQTETGS-ILISPLPYVGKLKPGST----GKPL 454
Cdd:cd05906 283 --DGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETCSgVIYSRSFPTYDHSQALEfvslGRPI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 455 PGISAKIVNSDGSDAEANEGGHLLITEPwpgMLTDIHNDRARYNRTYFeRFPGSYETGDGARVDeDGDYWIMGRLDDVIN 534
Cdd:cd05906 361 PGVSMRIVDDEGQLLPEGEVGRLQVRGP---VVTKGYYNNPEANAEAF-TEDGWFRTGDLGFLD-NGNLTITGRTKDTII 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 535 VSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQ-TVYAYVTLRSGLDEDDEMRTVLRE---WVSQKIG--PIAV--- 605
Cdd:cd05906 436 VNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAeTEELAIFFVPEYDLQDALSETLRAirsVVSREVGvsPAYLipl 515
|
410 420
....*....|....*....|....*..
gi 1816261920 606 -PETIqfseglPKTRSGKIMRRILRRI 631
Cdd:cd05906 516 pKEEI------PKTSLGKIQRSKLKAA 536
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
94-635 |
3.24e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 100.85 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENG-RRNKAALIWQGEPEEEVRvftYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVH 172
Cdd:PRK05857 17 LDRVFEQArQQPEAIALRRCDGTSALR---YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 173 SVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGKKIPlkrnvdEALFECPSveqvIMVKRTGDEIDFIEGRDTwwheei 252
Cdd:PRK05857 94 VMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVP------EALHSIPV----IAVDIAAVTRESEHSLDA------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 253 sgpdieDYCKPESMRSAD-PLFILHTSGSTGKAKGVVHSTGGYMTatahttqwVFD-LRDDDVHWctadIGWITGHsyTV 330
Cdd:PRK05857 158 ------ASLAGNADQGSEdPLAMIFTSGTTGEPKAVLLANRTFFA--------VPDiLQKEGLNW----VTWVVGE--TT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 331 YGPLAlgAT---------TLLFEG---VPTYPRPDRYWEIINRYGVNIFYTTPTALRALRRE----GTqwtekyDLSTLR 394
Cdd:PRK05857 218 YSPLP--AThigglwwilTCLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSElksaNA------TVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 395 ILGSVG-EPINPEVWiwFHEHVGkgkLPLLDTWWQTETGSILISpLPY----VGKLKPGSTGKPLPGISAKIVNSDGSDA 469
Cdd:PRK05857 290 LVGYGGsRAIAADVR--FIEATG---VRTAQVYGLSETGCTALC-LPTddgsIVKIEAGAVGRPYPGVDVYLAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 470 EANEG------GHLLITEPwPGMLTDIHNDRarynRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTT 543
Cdd:PRK05857 364 TAPGAgpsasfGTLWIKSP-ANMLGYWNNPE----RTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 544 EIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDD--EMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSG 621
Cdd:PRK05857 439 EVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAarALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSG 518
|
570
....*....|....
gi 1816261920 622 KIMRRILRRIAVGE 635
Cdd:PRK05857 519 KVMRASLAAAATAD 532
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
119-632 |
3.40e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 100.79 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 aD----GVLRggkkiplkrnvdEALFECPsvEQVIMVkrtgdeIDFIEGRDTWwHEEISGPDIEDYckpesMRSADPLFI 274
Cdd:PRK08162 122 -DtefaEVAR------------EALALLP--GPKPLV------IDVDDPEYPG-GRFIGALDYEAF-----LASGDPDFA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LH-------------TSGSTGKAKGVV-HSTGGYMTATAHTTQWvfDLRDDDVH-W------CTadiGWitGHSYTVygp 333
Cdd:PRK08162 175 WTlpadewdaialnyTSGTTGNPKGVVyHHRGAYLNALSNILAW--GMPKHPVYlWtlpmfhCN---GW--CFPWTV--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 334 LALGATTLLFEGVptypRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLstlRILGSVGEPINPEVWIWFHE 413
Cdd:PRK08162 245 AARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDH---PVHAMVAGAAPPAAVIAKME 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 HVGkgkLPLLDTWWQTETgsilisplpY----VGKLKPGSTGKPLPGiSAKIVNSDGSDAEANEGGHLLITE-----PWP 484
Cdd:PRK08162 318 EIG---FDLTHVYGLTET---------YgpatVCAWQPEWDALPLDE-RAQLKARQGVRYPLQEGVTVLDPDtmqpvPAD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 G-------------MLTDIHNDRARYnrtyfERFPGS-YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALI 550
Cdd:PRK08162 385 GetigeimfrgnivMKGYLKNPKATE-----EAFAGGwFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 551 AHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGL--DEDDemrtvLREWVSQKIGPIAVPETIQFSEgLPKTRSGKIMRRIL 628
Cdd:PRK08162 460 RHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAsaTEEE-----IIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVL 533
|
....
gi 1816261920 629 RRIA 632
Cdd:PRK08162 534 REQA 537
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
121-634 |
5.19e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 97.40 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAAD 200
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 GVLrggkkiPLKRnvdEALFECPSVE-----QVIMVkrtgDEIDFIEGRDTwwhEEISGPDIEDYCKPESMRSA------ 269
Cdd:PLN03102 120 SFE------PLAR---EVLHLLSSEDsnlnlPVIFI----HEIDFPKRPSS---EELDYECLIQRGEPTPSLVArmfriq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 ---DPLFILHTSGSTGKAKGVVHS-TGGYMTATAHTTQWvfDLRDDDVHWCTADIGWITGHSYTvYGPLALGATTLLFEG 345
Cdd:PLN03102 184 dehDPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGW--EMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 346 VPTyprPDRYwEIINRYGVNIFYTTPTALRALRrEGTQWTEKYDLSTLRILGSVGEPinPEVWIWFHEHVG--------- 416
Cdd:PLN03102 261 VTA---PEIY-KNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGfqvmhaygl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 417 -KGKLPLLDTWWQTETGSIlisPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEG---GHLLITEpwpgmlTDIHN 492
Cdd:PLN03102 334 tEATGPVLFCEWQDEWNRL---PENQQMELKARQGVSILGLADVDVKNKETQESVPRDGktmGEIVIKG------SSIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 493 DRARYNRTYFERFP-GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQT 571
Cdd:PLN03102 405 GYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 572 VYAYVTLRSGLD--EDDEMRTVLRE-----WVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVG 634
Cdd:PLN03102 485 PCAFVVLEKGETtkEDRVDKLVTRErdlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
122-630 |
5.48e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.69 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADg 201
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS- 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdEALFECPSVEqvimvkrtGDEIDFIEGRDTWwheeISGPDIEDyckPESMRSADPL-FILHTSGS 280
Cdd:PRK12467 1680 ---------------HLQARLPLPD--------GLRSLVLDQEDDW----LEGYSDSN---PAVNLAPQNLaYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVVHSTGGyMTATAHTTQWVFDLRDDDVhwctadigWITGHSYT-------VYGPLALGATTLLfegVP--TYPR 351
Cdd:PRK12467 1730 TGRPKGAGNRHGA-LVNRLCATQEAYQLSAADV--------VLQFTSFAfdvsvweLFWPLINGARLVI---APpgAHRD 1797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 352 PDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKydlSTLRILGSVGEPINPEVW-IWFHehvgkgKLP---LLDTWW 427
Cdd:PRK12467 1798 PEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP---LSLRRVVCGGEALEVEALrPWLE------RLPdtgLFNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 428 QTETgSILISPLPYVGKLKPGST----GKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpGMLTDIHNdraRYNRTYfE 503
Cdd:PRK12467 1869 PTET-AVDVTHWTCRRKDLEGRDsvpiGQPIANLSTYILDASLNPVPIGVAGELYLGGV--GLARGYLN---RPALTA-E 1941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 504 RF-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVvgIPHE-IKGQTVY 573
Cdd:PRK12467 1942 RFvadpfgtVGSrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgANGKQLV 2019
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 574 AY-VTLRSGLDEDDE----MRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK12467 2020 AYvVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
122-628 |
6.49e-21 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 95.78 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAadg 201
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmRSADPLFILHTSGST 281
Cdd:cd17652 91 -----------------------------------------------------------------TPDNLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVV--HSTGGYMTATAHTTqwvFDLRDDDVhwctadigWITGHSYT-------VYGPLALGATTLLfegVPTYPR- 351
Cdd:cd17652 106 GRPKGVVvtHRGLANLAAAQIAA---FDVGPGSR--------VLQFASPSfdasvweLLMALLAGATLVL---APAEELl 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 352 -PDRYWEIINRYGVNIFYTTPTALRALrregtqwtEKYDLSTLRILGSVGEPINPEvwiwfhehvgkgklpLLDTWWQ-- 428
Cdd:cd17652 172 pGEPLADLLREHRITHVTLPPAALAAL--------PPDDLPDLRTLVVAGEACPAE---------------LVDRWAPgr 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 --------TET--GSILISPLPYVGKLkpgSTGKPLPGISAKIVnsdgsDAEAnegghllitEPWP-GMLTDIHNDRARY 497
Cdd:cd17652 229 rminaygpTETtvCATMAGPLPGGGVP---PIGRPVPGTRVYVL-----DARL---------RPVPpGVPGELYIAGAGL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 498 NRTYF-------ERF-------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVV 561
Cdd:cd17652 292 ARGYLnrpgltaERFvadpfgaPGSrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 562 GIPHEIKGQTVYAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17652 372 VRDDRPGDKRLVAYVVPAPGAAPTAAE---LRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
94-633 |
6.64e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 96.60 E-value: 6.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENgrrNKAALIwQGEpeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhs 173
Cdd:PRK10946 31 LTRHAAS---DAIAVI-CGE-----RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 174 VIFAGFS--AVSLQNRIIDCDAKILIAAdgvlRGGKKIPLKRNVDEALFECPSVEQVIMVKRTGDEidfieGRDTWwhee 251
Cdd:PRK10946 100 PVNALFShqRSELNAYASQIEPALLIAD----RQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEH-----SLDDA---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 252 ISGPDiEDYcKPESMRSADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADigwiTGHSYTVY 331
Cdd:PRK10946 167 INHPA-EDF-TATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP----AAHNYPMS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 332 GPLALGAttlLFEG----VPTYPRPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILgsvgepinpev 407
Cdd:PRK10946 240 SPGALGV---FLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 408 wiwfheHVGKGKLPlldtwwqtETGSILISP-----LPYVGKLKPG----------------STGKPL-PGISAKIVNSD 465
Cdd:PRK10946 306 ------QVGGARLS--------ETLARRIPAelgcqLQQVFGMAEGlvnytrlddsderiftTQGRPMsPDDEVWVADAD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 466 GSDAEANEGGHLLITEPWpgmltdihNDRARY-----NRTYFERfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRL 540
Cdd:PRK10946 372 GNPLPQGEVGRLMTRGPY--------TFRGYYkspqhNASAFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 541 GTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLdEDDEMRTVLREwvsQKIGPIAVPETIQFSEGLPKTRS 620
Cdd:PRK10946 443 AAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPL-KAVQLRRFLRE---QGIAEFKLPDRVECVDSLPLTAV 518
|
570
....*....|...
gi 1816261920 621 GKIMRRILRRIAV 633
Cdd:PRK10946 519 GKVDKKQLRQWLA 531
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
119-629 |
1.67e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.71 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFAN-VLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILI 197
Cdd:PRK08751 49 KTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 198 AADGvlrggkkipLKRNVDEALFECPsVEQVIMVKrTGDEIDFIEGRDTWWHEEISGPDIEDYCKPESMRSADPL----- 272
Cdd:PRK08751 129 VIDN---------FGTTVQQVIADTP-VKQVITTG-LGDMLGFPKAALVNFVVKYVKKLVPEYRINGAIRFREALalgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 --------------FILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVfdlrdddvhwctADIGWIT-GHSYTV-----YG 332
Cdd:PRK08751 198 hsmptlqiepddiaFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWL------------AGTGKLEeGCEVVItalplYH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 333 PLALGATTLLFEGVPtyprpdryweiinryGVNIFYTTPTALRALRRE--GTQWT------------------EKYDLST 392
Cdd:PRK08751 266 IFALTANGLVFMKIG---------------GCNHLISNPRDMPGFVKElkKTRFTaftgvntlfngllntpgfDQIDFSS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 393 LRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTETG-SILISPLPYvgKLKPGSTGKPLPGISAKIVNSDGSDAEA 471
Cdd:PRK08751 331 LKMTLGGGMAVQRSVAERWKQVTG---LTLVEAYGLTETSpAACINPLTL--KEYNGSIGLPIPSTDACIKDDAGTVLAI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEPwpgmltdihndraRYNRTYFER---------FPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGT 542
Cdd:PRK08751 406 GEIGELCIKGP-------------QVMKGYWKRpeetakvmdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 543 TEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTlrsgldEDDEMRTV--LREWVSQKIGPIAVPETIQFSEGLPKTRS 620
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDPALTAedVKAHARANLTGYKQPRIIEFRKELPKTNV 546
|
....*....
gi 1816261920 621 GKIMRRILR 629
Cdd:PRK08751 547 GKILRRELR 555
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
274-628 |
5.55e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 93.91 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 ILHTSGSTGKAKGV-----VHSTGGYMTATAHTTQwvfdLRdddvhwctadigwiTGHSYTVYGPL-------------A 335
Cdd:PRK13383 179 VLLTSGTTGKPKGVprapqLRSAVGVWVTILDRTR----LR--------------TGSRISVAMPMfhglglgmlmltiA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 336 LGATTLL---FEGVPTYPRPDryweiINRygVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFH 412
Cdd:PRK13383 241 LGGTVLThrhFDAEAALAQAS-----LHR--ADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 413 EHVGKgklPLLDTWWQTETGsilISPLPYVGKLK--PGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGMLTDI 490
Cdd:PRK13383 314 DTYGD---ILYNGYGSTEVG---IGALATPADLRdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 491 HNDRARYNrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQ 570
Cdd:PRK13383 388 GGGKAVVD--------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGH 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 571 TVYAYVTLRSGLDED-DEMRTVLREWVSQkigpIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK13383 460 RLAAFVVLHPGSGVDaAQLRDYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
274-625 |
9.96e-20 |
|
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: 90.64 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 ILHTSGSTGKAKGVVHSTGGYMTATAhttQW--VFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTL---LFEgvpt 348
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAA---AWadCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVpvaVFD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 349 yprPDRYWEIINRYGVNIFYTTPTALRALRREGTQwtEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKgkLPLLDTWWQ 428
Cdd:cd17638 78 ---VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGF--ETVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 429 TETGSILISPLPYVGKLKPGSTGKPLPGISAKIVNSdgsdaeanegGHLLITEPwpGMLTDIHNDRARYNRTYFERfpGS 508
Cdd:cd17638 151 TEAGVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGY--NVMQGYLDDPEATAEAIDAD--GW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDD 586
Cdd:cd17638 217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvtLTEED 296
|
330 340 350
....*....|....*....|....*....|....*....
gi 1816261920 587 emrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMR 625
Cdd:cd17638 297 -----VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
121-628 |
1.23e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 93.96 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAAD 200
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 GVLrggkkiplkrnvdeALFecpsveqvimvkrTGDEIDFIEGRDTWWheeiSGPDIEDYCKPesmRSADPLFILHTSGS 280
Cdd:PRK10252 564 DQL--------------PRF-------------ADVPDLTSLCYNAPL----APQGAAPLQLS---QPHHTAYIIFTSGS 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVV--HstggymTATAHTTQWVFD---LRDDDVHW----CTADIG-WitghsyTVYGPLALGATTLLFEgvPTYP 350
Cdd:PRK10252 610 TGRPKGVMvgQ------TAIVNRLLWMQNhypLTADDVVLqktpCSFDVSvW------EFFWPFIAGAKLVMAE--PEAH 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 351 R-PDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQT 429
Cdd:PRK10252 676 RdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTG---APLHNLYGPT 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 430 EtGSILISPLPYVGKLKPGSTGKPLP--------GIsaKIVNSDGSDAEANEGGHLlitepwpgMLTDIHNDRARYNRTY 501
Cdd:PRK10252 753 E-AAVDVSWYPAFGEELAAVRGSSVPigypvwntGL--RILDARMRPVPPGVAGDL--------YLTGIQLAQGYLGRPD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 502 F--ERF------PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEA---AVVGIPHEIK 568
Cdd:PRK10252 822 LtaSRFiadpfaPGErmYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAAT 901
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 569 G----QTVyAYVTLRSGLDEDDEMrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK10252 902 GgdarQLV-GYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-628 |
7.29e-19 |
|
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: 89.84 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 VlrggkKIPLKRNVDEALFECPSVEQVimvkrTGDEIDFIEGRDtwwheeisgpdiedyckpesmrsaDPLFILHTSGST 281
Cdd:cd17656 95 L-----KSKLSFNKSTILLEDPSISQE-----DTSNIDYINNSD------------------------DLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVVHSTGGYMTATAHTTQWVFDLRDDDV---HWCTADIGWitghsYTVYGPLALGATTLLfegVPTYPRPD--RYW 356
Cdd:cd17656 141 GKPKGVQLEHKNMVNLLHFEREKTNINFSDKVlqfATCSFDVCY-----QEIFSTLLSGGTLYI---IREETKRDveQLF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTtPTALRALRREGTQWTEKYdLSTLRILGSVGEP--INPEVWIWFHEHvgkgKLPLLDTWWQTETGSI 434
Cdd:cd17656 213 DLVKRHNIEVVFL-PVAFLKFIFSEREFINRF-PTCVKHIITAGEQlvITNEFKEMLHEH----NVHLHNHYGPSETHVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 435 ---LISPLPYVGKLKPgsTGKPLPGISAKIVNSDGSDAEANEGGHLLITepwpgmltDIHNDRARYNRTYF--ERF---- 505
Cdd:cd17656 287 ttyTINPEAEIPELPP--IGKPISNTWIYILDQEQQLQPQGIVGELYIS--------GASVARGYLNRQELtaEKFfpdp 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 --PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG 581
Cdd:cd17656 357 fdPNErmYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1816261920 582 LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17656 437 LNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
270-630 |
8.16e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.09 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGwitgHSYTVY---GP-LALGATTLLfeg 345
Cdd:PRK13388 151 DPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTE-RFGLTRDDVCYVSMPLF----HSNAVMagwAPaVASGAAVAL--- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 346 VPTYpRPDRYWEIINRYGVNIFYTTPTALRALRREgtqwTEKYDLS--TLRIlgSVGEPINPEVWIWFHEHVGkgkLPLL 423
Cdd:PRK13388 223 PAKF-SASGFLDDVRRYGATYFNYVGKPLAYILAT----PERPDDAdnPLRV--AFGNEASPRDIAEFSRRFG---CQVE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 424 DTWWQTETGSILISP--LPyvgklkPGSTGKPLPGISakIVNSDG----SDAEANEGGHLLITEPWPGMLTDIHNdrARY 497
Cdd:PRK13388 293 DGYGSSEGAVIVVREpgTP------PGSIGRGAPGVA--IYNPETltecAVARFDAHGALLNADEAIGELVNTAG--AGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 498 NRTYF-------ERFP-GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKG 569
Cdd:PRK13388 363 FEGYYnnpeataERMRhGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 570 QTVYAYVTLRSGLDED-DEMRTVLREwvSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK13388 443 DQVMAALVLRDGATFDpDAFAAFLAA--QPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
270-634 |
2.17e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 89.98 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVV---HSTGGYMTATAHttqwVFDLRDDDVhwctadigwITG-----HS--YTV--YGPLALG 337
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSfgLTVtlWLPLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 338 AttllfeGVPTYPRPDRYWEI---INRYGVNIFYTTPTALRALRRegTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEH 414
Cdd:PRK08633 850 I------KVVYHPDPTDALGIaklVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 415 VGKgklPLLDTWWQTETGSILISPLPYV---------GKlKPGSTGKPLPGISAKIVNSD-GSDAEANEGGHLLITEP-- 482
Cdd:PRK08633 922 FGI---RILEGYGATETSPVASVNLPDVlaadfkrqtGS-KEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPqv 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 483 WPGMLTD-------IHN-DRARYnrtyferfpgsYETGDGARVDEDGDYWIMGRLDDVINVSGHR--LGTTEIESALIAH 552
Cdd:PRK08633 998 MKGYLGDpektaevIKDiDGIGW-----------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMvpLGAVEEELAKALG 1066
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 553 PDVTEAAVVGIPHEIKGQTVyayVTLRSGLDEDDEmrTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:PRK08633 1067 GEEVVFAVTAVPDEKKGEKL---VVLHTCGAEDVE--ELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
..
gi 1816261920 633 VG 634
Cdd:PRK08633 1142 LA 1143
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
93-630 |
7.09e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.55 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 93 CLDRhLENGRRNKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVH 172
Cdd:PLN02860 12 CLTR-LATLRGNAVVTISGN------RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 173 SVIFAGFSAVSLQNRIIDCDAKILIAADGVLRGGkkIPLKRNvdealfECPSVEQVIMVKRTGDEIDF----IEGRDTWW 248
Cdd:PLN02860 85 APLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWY--EELQND------RLPSLMWQVFLESPSSSVFIflnsFLTTEMLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 249 HEEISGPDIeDYC-KPEsmrsaDPLFILHTSGSTGKAKGVVhstggyMTATAHTTQWVFDLR-----DDDVHWCTADIGW 322
Cdd:PLN02860 157 QRALGTTEL-DYAwAPD-----DAVLICFTSGTTGRPKGVT------ISHSALIVQSLAKIAivgygEDDVYLHTAPLCH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 323 ITGHSyTVYGPLALGATTLLFegvptyPRPDR--YWEIINRYGVNIFYTTPTALRAL----RREGTQWTEKYDLSTLRIL 396
Cdd:PLN02860 225 IGGLS-SALAMLMVGACHVLL------PKFDAkaALQAIKQHNVTSMITVPAMMADLisltRKSMTWKVFPSVRKILNGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 397 GSVGEPINPEVWIWFhehvgkGKLPLLDTWWQTETGSIL-------------ISPLPYVGKLKPGST--------GKPLP 455
Cdd:PLN02860 298 GSLSSRLLPDAKKLF------PNAKLFSAYGMTEACSSLtfmtlhdptlespKQTLQTVNQTKSSSVhqpqgvcvGKPAP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 456 GISAKIvNSDGSDAEAN---EGGHLLITEpW---PGMLTDIHNDrarynrtyferfpGSYETGDGARVDEDGDYWIMGRL 529
Cdd:PLN02860 372 HVELKI-GLDESSRVGRiltRGPHVMLGY-WgqnSETASVLSND-------------GWLDTGDIGWIDKAGNLWLIGRS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 530 DDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLD-EDDEMRT----------VLREWVSQ 598
Cdd:PLN02860 437 NDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIwSDNEKENakknltlsseTLRHHCRE 516
|
570 580 590
....*....|....*....|....*....|....
gi 1816261920 599 K-IGPIAVPETI-QFSEGLPKTRSGKIMRRILRR 630
Cdd:PLN02860 517 KnLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
122-564 |
7.64e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 87.26 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAadg 201
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkIPlKRNVDEALF--ECPSVEQVIMVkrtgdeidfieGRDTWW-----HEEISGPDIEDYcKPESMRSADPLFI 274
Cdd:PRK09274 120 -------IP-KAHLARRLFgwGKPSVRRLVTV-----------GGRLLWggttlATLLRDGAAAPF-PMADLAPDDMAAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 275 LHTSGSTGKAKGVVHSTGGYmTATAHTTQWVFDLRDDDVHWCTADIgwitghsYTVYGPlALGATTLLFEGVPTYP---R 351
Cdd:PRK09274 180 LFTSGSTGTPKGVVYTHGMF-EAQIEALREDYGIEPGEIDLPTFPL-------FALFGP-ALGMTSVIPDMDPTRPatvD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 352 PDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKydLSTLRILGSVGEPINPEVWIWFHE--------HVGKGK---L 420
Cdd:PRK09274 251 PAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIK--LPSLRRVISAGAPVPIAVIERFRAmlppdaeiLTPYGAteaL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 P---------LLDTWWQTETGS-ILIsplpyvgklkpgstGKPLPGISAKIVN---------SDGSDAEANEGGHLLITE 481
Cdd:PRK09274 329 PissiesreiLFATRAATDNGAgICV--------------GRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 482 PwpgMLTD--IHNDRA-------RYNRTYFERfpgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAH 552
Cdd:PRK09274 395 P---MVTRsyYNRPEAtrlakipDGQGDVWHR------MGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465
|
490
....*....|..
gi 1816261920 553 PDVTEAAVVGIP 564
Cdd:PRK09274 466 PGVKRSALVGVG 477
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
421-628 |
1.20e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 85.86 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 421 PLLDTWWQT---------------ETGSILISPlpyvgKLK-PGSTGKPLPGISAKIvnsdGSDAEANEggHLLITEpwp 484
Cdd:PRK08308 223 PLPEAWFYKlrerttymmqqygcsEAGCVSICP-----DMKsHLDLGNPLPHVSVSA----GSDENAPE--EIVVKM--- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 gmltdihNDRARYnrtyferfpgsyeTGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP 564
Cdd:PRK08308 289 -------GDKEIF-------------TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGK 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 565 HEIKGQTVYAYVTLRSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK08308 349 DPVAGERVKAKVISHEEIDPVQ-----LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-635 |
2.36e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 85.63 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAAD 200
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 GV-----------LRGGKKIPLKRNVDEALFecPSVEQVImvkRTGDEIdfIEGRDTW--WHEEISGPDIEDYCKPESMR 267
Cdd:PRK08315 124 GFkdsdyvamlyeLAPELATCEPGQLQSARL--PELRRVI---FLGDEK--HPGMLNFdeLLALGRAVDDAELAARQATL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 268 SA-DPLFILHTSGSTGKAKGVVHS-----TGGYMTATAhttqwvFDLRDDD-----V---HwC----TADIGWITGHSYT 329
Cdd:PRK08315 197 DPdDPINIQYTSGTTGFPKGATLThrnilNNGYFIGEA------MKLTEEDrlcipVplyH-CfgmvLGNLACVTHGATM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 330 VY-----GPLALGAT------TLLFeGVPT-----YPRPDRyweiinrygvnifyttptalralrregtqwtEKYDLSTL 393
Cdd:PRK08315 270 VYpgegfDPLATLAAveeercTALY-GVPTmfiaeLDHPDF-------------------------------ARFDLSSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 394 R--IL-GSVGePIN-----------PEVWIwfhehvGKGklplldtwwQTETGsilisplpyvgklkPGST--------- 450
Cdd:PRK08315 318 RtgIMaGSPC-PIEvmkrvidkmhmSEVTI------AYG---------MTETS--------------PVSTqtrtddple 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 451 ------GKPLPGISAKIVNSD-GSDAEANEGGHLLiTEPWPGMLtDIHNDRARYNRTYFERfpGSYETGDGARVDEDGDY 523
Cdd:PRK08315 368 krvttvGRALPHLEVKIVDPEtGETVPRGEQGELC-TRGYSVMK-GYWNDPEKTAEAIDAD--GWMHTGDLAVMDEEGYV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 524 WIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIG 601
Cdd:PRK08315 444 NIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGatLTEED-----VRDFCRGKIA 518
|
570 580 590
....*....|....*....|....*....|....
gi 1816261920 602 PIAVPETIQFSEGLPKTRSGKIMRRILRRIAVGE 635
Cdd:PRK08315 519 HYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
108-625 |
3.28e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 84.80 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 108 LIWQGEPeeevrvFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNR 187
Cdd:cd05914 1 LYYGGEP------LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 188 IIDCDAKILIAADgvlrggkkiplkrNVDEALfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmr 267
Cdd:cd05914 75 LNHSEAKAIFVSD-------------EDDVAL------------------------------------------------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 268 sadplfILHTSGSTGKAKGVVhSTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVP 347
Cdd:cd05914 94 ------INYTSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 348 T----------------YPRP----DRY-WEIINRYGVNIF----YTTPTALRALRREGTQWTEKYDlSTLRILGSVGEP 402
Cdd:cd05914 167 SakiialafaqvtptlgVPVPlvieKIFkMDIIPKLTLKKFkfklAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 403 INPEVWIWFHehvgKGKLPLLDTWWQTETGSILISPLPyvGKLKPGSTGKPLPGISAKIvnsDGSDAEANEGGhlLITEP 482
Cdd:cd05914 246 INPDVEEFLR----TIGFPYTIGYGMTETAPIISYSPP--NRIRLGSAGKVIDGVEVRI---DSPDPATGEGE--IIVRG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 483 WPGMLTDIHNDRARYnrtyfERFP--GSYETGDGARVDEDGDYWIMGRLDDVI-NVSGHRLGTTEIESALIAHPDVTEAA 559
Cdd:cd05914 315 PNVMKGYYKNPEATA-----EAFDkdGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESL 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816261920 560 VVgiPHEIKGQ-TVYAYVTLR--SGLDEDDEMRTVL---REWVSQKIGPIA-VPETIQFSEGLPKTRSGKIMR 625
Cdd:cd05914 390 VV--VQEKKLVaLAYIDPDFLdvKALKQRNIIDAIKwevRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
102-628 |
3.77e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 102 RRNKA-ALIWQGEpeeevrVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFS 180
Cdd:PRK05691 2200 RTPQApALTFAGQ------TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 181 AVSLQNRIIDCDAKILIAadgvlrggkkiplKRNVDEALFECPSveqviMVKRtgdeidfiegrdtwWHEEISGPDIEDY 260
Cdd:PRK05691 2274 LERLHYMIEDSGIGLLLS-------------DRALFEALGELPA-----GVAR--------------WCLEDDAAALAAY 2321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 261 ckpesmrSADPL----------FILHTSGSTGKAKGVVHSTGgymtATAHTTQWV---FDLRDDD--VHWCTADIGWITG 325
Cdd:PRK05691 2322 -------SDAPLpflslpqhqaYLIYTSGSTGKPKGVVVSHG----EIAMHCQAVierFGMRADDceLHFYSINFDAASE 2390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 326 HSYTvygPLALGATTLLfegvptypRPDRYW------EIINRYGVNIFYTTPTALRALrregTQWTEK-YDLSTLRILGS 398
Cdd:PRK05691 2391 RLLV---PLLCGARVVL--------RAQGQWgaeeicQLIREQQVSILGFTPSYGSQL----AQWLAGqGEQLPVRMCIT 2455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 399 VGEPINPEVWiwfhEHVGKGKLP--LLDTWWQTETGSI-LISPLPyvGKLKPGSTGKPLPGI----SAKIVNSDGSDAEA 471
Cdd:PRK05691 2456 GGEALTGEHL----QRIRQAFAPqlFFNAYGPTETVVMpLACLAP--EQLEEGAASVPIGRVvgarVAYILDADLALVPQ 2529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEPwpGMLTDIHnDRARYNRtyfERF---PGS------YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGT 542
Cdd:PRK05691 2530 GATGELYVGGA--GLAQGYH-DRPGLTA---ERFvadPFAadggrlYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIEL 2603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 543 TEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDED--DEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRS 620
Cdd:PRK05691 2604 GEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTAN 2683
|
....*...
gi 1816261920 621 GKIMRRIL 628
Cdd:PRK05691 2684 GKLDRRAL 2691
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-593 |
8.13e-17 |
|
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: 83.66 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSADPLFILHTSGSTGKAKGVVHsTGGYMTATAHTTQWVFDLRDDDVHWCTADIgwitghsYTVYGPlALGATTLLFEGV 346
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVY-RHGTFAAQIDALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 PTYP---RPDRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKydLSTLRILGSVGEPINPEVWIWFHEHVGKGkLPLL 423
Cdd:cd05910 154 PTRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLSDE-AEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 424 DTWWQTET------GS--ILISPLPYVGKLKPGSTGKPLPGISAKIVNSD-------GSDAEANEG--GHLLITEPwpgM 486
Cdd:cd05910 231 TPYGATEAlpvssiGSreLLATTTAATSGGAGTCVGRPIPGVRVRIIEIDdepiaewDDTLELPRGeiGEITVTGP---T 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 487 LTDIHNDRARYNR-----TYFERFpgSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVV 561
Cdd:cd05910 308 VTPTYVNRPVATAlakidDNSEGF--WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
330 340 350
....*....|....*....|....*....|..
gi 1816261920 562 GIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLR 593
Cdd:cd05910 386 GVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
268-628 |
8.37e-17 |
|
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: 83.60 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 268 SADPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLF---E 344
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSE-RYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVppdE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 345 GVPTyprPDRYWEIINRYGVNIFYTTPTALralrregtqwtEKYDLS---TLRILGSVGEPINPEVwiwFHEHVGKGKLP 421
Cdd:cd17648 172 MRFD---PDRFYAYINREKVTYLSGTPSVL-----------QQYDLArlpHLKRVDAAGEEFTAPV---FEKLRSRFAGL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 422 LLDTWWQTETgSI--LISPLPYVGKLKpGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPW--PGMLT--DIHNDRA 495
Cdd:cd17648 235 IINAYGPTET-TVtnHKRFFPGDQRFD-KSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGvaRGYLNrpELTAERF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 496 RYNRTYFE------RFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKG 569
Cdd:cd17648 313 LPNPFQTEqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQA 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 570 QT------VYAYVTLRSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17648 393 QSriqkylVGYYLPEPGHVPESD-----LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
119-629 |
1.70e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 83.15 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARigavhsvifAGFSAVS---------LQNRII 189
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR---------AGYVVVNvnplytpreLEHQLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 190 DCDAKILIA----ADGVLRGGKKIPLKRNVDEALFECPSVEQVI----------MV--------KRTGDEIDfiEGRDTW 247
Cdd:PRK07059 118 DSGAEAIVVlenfATTVQQVLAKTAVKHVVVASMGDLLGFKGHIvnfvvrrvkkMVpawslpghVRFNDALA--EGARQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 248 WHEEISGPDiedyckpesmrsaDPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQW---VFDLRDDDVHWCTadigwIT 324
Cdd:PRK07059 196 FKPVKLGPD-------------DVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWlqpAFEKKPRPDQLNF-----VC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 325 G----HSY--TVYGPLAL--GATTLLfegVPTyPR--PDRYWEIiNRYGVNIFYTTPTALRAL-RREGTQwteKYDLSTL 393
Cdd:PRK07059 258 AlplyHIFalTVCGLLGMrtGGRNIL---IPN-PRdiPGFIKEL-KKYQVHIFPAVNTLYNALlNNPDFD---KLDFSKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 394 RI-LG---SVGEPInPEVWiwfHEHVGkgkLPLLDTWWQTETGSILISPLPYVGKLKpGSTGKPLPGISAKIVNSDGSDA 469
Cdd:PRK07059 330 IVaNGggmAVQRPV-AERW---LEMTG---CPITEGYGLSETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 470 EANEGGHLLITEP------WpgmltdihndrARYNRTYFERFP-GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGT 542
Cdd:PRK07059 402 PLGEPGEICIRGPqvmagyW-----------NRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 543 TEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRS-GLDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSG 621
Cdd:PRK07059 471 NEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDpALTEED-----VKAFCKERLTNYKRPKFVEFRTELPKTNVG 545
|
....*...
gi 1816261920 622 KIMRRILR 629
Cdd:PRK07059 546 KILRRELR 553
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
426-629 |
1.73e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.88 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 426 WWQTETgsiliSPLPYVGKLKPG--------------STGKPLPGISAKIVNSDGSDA--EANEGGHLLITEP-----WP 484
Cdd:PRK06018 325 WGMTEM-----SPLGTLAALKPPfsklpgdarldvlqKQGYPPFGVEMKITDDAGKELpwDGKTFGRLKVRGPavaaaYY 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GMLTDIHNDRarynrtyferfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP 564
Cdd:PRK06018 400 RVDGEILDDD------------GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 565 HEIKGQTVYAYVTLRSGldeddemRTVLREWVSQ----KIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:PRK06018 468 HPKWDERPLLIVQLKPG-------ETATREEILKymdgKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
263-623 |
1.94e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 83.48 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 263 PESMRSA-DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIgwitGHSYTVYGplalGATTL 341
Cdd:PRK06814 786 YFCNRDPdDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAA-RIDFSPEDKVFNALPV----FHSFGLTG----GLVLP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 342 LFEGVPT--YPRPDRYW---EIInrYGVN--IFYTTPTALRALRRegtqWTEKYDLSTLRILGSVGEPINPE---VWIwf 411
Cdd:PRK06814 857 LLSGVKVflYPSPLHYRiipELI--YDTNatILFGTDTFLNGYAR----YAHPYDFRSLRYVFAGAEKVKEEtrqTWM-- 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 412 hEHVGkgkLPLLDTWWQTETGSILISPLPYVGklKPGSTGKPLPGISAKIVNSDGSDaeanEGGHLLITEPwPGMLTDIH 491
Cdd:PRK06814 929 -EKFG---IRILEGYGVTETAPVIALNTPMHN--KAGTVGRLLPGIEYRLEPVPGID----EGGRLFVRGP-NVMLGYLR 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 492 NDRaryNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIEsALIAH--PDvTEAAVVGIPHEIKG 569
Cdd:PRK06814 998 AEN---PGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE-ELAAElwPD-ALHAAVSIPDARKG 1072
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 570 QTVyAYVTLRSGLDeddemRTVLREWVSQK-IGPIAVPETIQFSEGLPKTRSGKI 623
Cdd:PRK06814 1073 ERI-ILLTTASDAT-----RAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
37-93 |
2.18e-16 |
|
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: 73.28 E-value: 2.18e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816261920 37 YEQACRMATDSPEEFWADRARDLlHWTRDFRTTLESDPEKHeYKWFSGGRLNASYNC 93
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKEL-DWFKPFDKVLDGSNGPF-AKWFVGGKLNVCYNC 55
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
103-562 |
3.45e-16 |
|
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: 82.09 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 103 RNKAALIWQgepeeevrVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAV 182
Cdd:cd17641 2 REKDFGIWQ--------EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 183 SLQNRIIDCDAKILIAADgvlrggkkiplKRNVD---EALFECPSVEQVIMVKRTG----------DEIDFIE-GRdtww 248
Cdd:cd17641 74 EVAYLLNYTGARVVIAED-----------EEQVDkllEIADRIPSVRYVIYCDPRGmrkyddprliSFEDVVAlGR---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 249 heEISGPDIEDYCKPESMRSADPLFIL-HTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVhWCTADIGWITGHS 327
Cdd:cd17641 139 --ALDRRDPGLYEREVAAGKGEDVAVLcTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEY-VSVLPLPWIGEQM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 328 YTVYGPLALG--------ATTL---LFEGVPTYP-RPDRYWE-IINRYGVNIFYTTP-----------TALRAL------ 377
Cdd:cd17641 216 YSVGQALVCGfivnfpeePETMmedLREIGPTFVlLPPRVWEgIAADVRARMMDATPfkrfmfelgmkLGLRALdrgkrg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 378 RREGTQWTEKYDL---------------STLRILGSVGEPINPEVWIWFHEhVGkgkLPLLDTWWQTET-GSILISPlpy 441
Cdd:cd17641 296 RPVSLWLRLASWLadallfrplrdrlgfSRLRSAATGGAALGPDTFRFFHA-IG---VPLKQLYGQTELaGAYTVHR--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 442 VGKLKPGSTGKPLPGISAKIvnsdgsdaeANEGGHLLITepwPGMLTDIHNDRARYNRTYFERfpGSYETGDGARVDEDG 521
Cdd:cd17641 369 DGDVDPDTVGVPFPGTEVRI---------DEVGEILVRS---PGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1816261920 522 DYWIMGRLDDVINVS-GHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:cd17641 435 HLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-562 |
4.69e-16 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 81.36 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAad 200
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 GVLRGGKKipLKRNVDEALFECPSVEQvimvkrtgdeiDFIEGRDTWWHEEISGPDIEDyckpESMRSADPLF-ILHTSG 279
Cdd:cd05932 85 GKLDDWKA--MAPGVPEGLISISLPPP-----------SAANCQYQWDDLIAQHPPLEE----RPTRFPEQLAtLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 280 STGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTYP------RPD 353
Cdd:cd05932 148 TTGQPKGVMLTFGSFAWAAQAGIE-HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVedvqraRPT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 ------RYW-----EIINRYGV---NIFYTTPTALRALRRegtQWTEKYDLSTLRILGSVGEPINPEVWIWFHEhVGkgk 419
Cdd:cd05932 227 lffsvpRLWtkfqqGVQDKIPQqklNLLLKIPVVNSLVKR---KVLKGLGLDQCRLAGCGSAPVPPALLEWYRS-LG--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 420 LPLLDTWWQTEtgSILISPLPYVGKLKPGSTGKPLPGISAKIvnsdgsdaeaNEGGHLLITEPwpGMLTDIHNDRARYNR 499
Cdd:cd05932 300 LNILEAYGMTE--NFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSP--ALMMGYYKDPEATAE 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 500 TYFErfPGSYETGDGARVDEDGDYWIMGRLDDVINVS-GHRLGTTEIESALIAHPDVTEAAVVG 562
Cdd:cd05932 366 AFTA--DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
506-630 |
5.96e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 77.01 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 PGSYETGDGARVDeDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQ-TVYAYVTLRSGLDE 584
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQrVVAAVVGDGGPAPT 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1816261920 585 DDEmrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK07824 312 LEA----LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
94-638 |
6.95e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.90 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 94 LDRHLENG---RRNKAALIWQGEPEEEVrvfTYHMLHRKVCRFANVLK-KIGVSKGDRVAIYLPMVPELVISMLACARIG 169
Cdd:PRK05620 12 LTRILEYGstvHGDTTVTTWGGAEQEQT---TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 170 AVHSVIFAGFSAVSLQNRIIDCDAKILIAaDGVLrggkkiplKRNVDEALFECPSVEQVIMVkrTGDEID---------- 239
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVIVA-DPRL--------AEQLGEILKECPCVRAVVFI--GPSDADsaaahmpegi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 240 -------FIEGRDTwwheEISGPDIEDyckpesmrsADPLFILHTSGSTGKAKGVVHSTGG-YMTATAHTTQWVFDLRDD 311
Cdd:PRK05620 158 kvysyeaLLDGRST----VYDWPELDE---------TTAAAICYSTGTTGAPKGVVYSHRSlYLQSLSLRTTDSLAVTHG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 312 DVHWCTADIGWITghSYTVygPLA--LGATTLLFEGVPTypRPDRYWEIINrygvnifyttpTAL-RALRREGTQWT--- 385
Cdd:PRK05620 225 ESFLCCVPIYHVL--SWGV--PLAafMSGTPLVFPGPDL--SAPTLAKIIA-----------TAMpRVAHGVPTLWIqlm 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 386 --------EKYDLSTLRILGSVGEPINPEVWiwfHEHVGkgkLPLLDTWWQTETGSILISPLPYVG------KLKPGSTG 451
Cdd:PRK05620 288 vhylknppERMSLQEIYVGGSAVPPILIKAW---EERYG---VDVVHVWGMTETSPVGTVARPPSGvsgearWAYRVSQG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 452 KPLPGISAKIVNsDGSDAEANE--GGHLLITEPW----------------PGMLTDIHNDRARynrtyfERFP--GSYET 511
Cdd:PRK05620 362 RFPASLEYRIVN-DGQVMESTDrnEGEIQVRGNWvtasyyhspteegggaASTFRGEDVEDAN------DRFTadGWLRT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 512 GDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTV 591
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAER 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1816261920 592 LREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRR-IAVGENDL 638
Cdd:PRK05620 515 LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhLADGDFEI 562
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
507-629 |
1.01e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.58 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 507 GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDD 586
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSD 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1816261920 587 EMRTV--LREWVSQKIGPIAVPETIQFSEgLPKTRSGKIMRRILR 629
Cdd:PLN02479 510 EAALAedIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLR 553
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
270-621 |
2.40e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.65 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMTATAHTtqwvfdlrdddvhwctADIGWITGHS-YTVYGPL------ALGATTLL 342
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVL----------------AVLQAIDEGTvFLNSGPLfhigtlMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 343 FEGVPTYPR---PDRYWEIINRYGVN-IFYTTPT--ALRALRREGtqwteKYDLSTLRILGSVGE---PINPEVWIWFHE 413
Cdd:cd17636 65 AGGTNVFVRrvdAEEVLELIEAERCThAFLLPPTidQIVELNADG-----LYDLSSLRSSPAAPEwndMATVDTSPWGRK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 414 HVGKGklplldtwwQTETGSILIspLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPwpgmltDIHN- 492
Cdd:cd17636 140 PGGYG---------QTEVMGLAT--FAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGP------TVMAg 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 493 --DRARYN--RTYFerfpGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIK 568
Cdd:cd17636 203 ywNRPEVNarRTRG----GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRW 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1816261920 569 GQTVYAYVTLRSG--LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSG 621
Cdd:cd17636 279 AQSVKAIVVLKPGasVTEAE-----LIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
117-629 |
3.93e-14 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 75.16 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 117 EVRVFTYHMLHRKVCRFANVLKKI-GVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKI 195
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 196 LIAADgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmrsADPLFIL 275
Cdd:cd05937 82 VIVDP--------------------------------------------------------------------DDPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 276 HTSGSTGKAKGVVHSTG-GYMTATAHTTqwVFDLRDDDVHWCTADIGWITGHSytvygplaLGATTLLFEGVPTYPRPD- 353
Cdd:cd05937 94 YTSGTTGLPKAAAISWRrTLVTSNLLSH--DLNLKNGDRTYTCMPLYHGTAAF--------LGACNCLMSGGTLALSRKf 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 354 ---RYWEIINRYGVNIFYTTPTALRALRREGTqwtEKYDlSTLRILGSVGEPINPEVWIWFHEHVGkgkLPLLDTWWQTe 430
Cdd:cd05937 164 sasQFWKDVRDSGATIIQYVGELCRYLLSTPP---SPYD-RDHKVRVAWGNGLRPDIWERFRERFN---VPEIGEFYAA- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 TGSILISPLPYVGKLKPGSTGKPLPGISAK------IVNSDGSD--------------AEANEGGHLLIT------EPWP 484
Cdd:cd05937 236 TEGVFALTNHNVGDFGAGAIGHHGLIRRWKfenqvvLVKMDPETddpirdpktgfcvrAPVGEPGEMLGRvpfknrEAFQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GMLtdiHNDRA---RYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVV 561
Cdd:cd05937 316 GYL---HNEDAtesKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 562 GI--PHEiKGQTVYAYVTLR-SGLDEDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILR 629
Cdd:cd05937 393 GVkvPGH-DGRAGCAAITLEeSSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
115-629 |
2.26e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 73.20 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 115 EEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAiylpmvpelvismlACARIGAVHSVIF---AGFSAV--SLQNRII 189
Cdd:PRK07008 34 EGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVG--------------TLAWNGYRHLEAYygvSGSGAVchTINPRLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 190 -DCDAKILIAADG--VLRGGKKIPLkrnVDEALFECPSVEQVIMV----KRTGDEIDFIEgrdtwwHEEISGPDIEDYCK 262
Cdd:PRK07008 100 pEQIAYIVNHAEDryVLFDLTFLPL---VDALAPQCPNVKGWVAMtdaaHLPAGSTPLLC------YETLVGAQDGDYDW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 263 PE-SMRSADPLfiLHTSGSTGKAKGVVHStggYMTATAHTtqwvFDLRDDDVHWCTA-DI-----------GWitGHSYT 329
Cdd:PRK07008 171 PRfDENQASSL--CYTSGTTGNPKGALYS---HRSTVLHA----YGAALPDAMGLSArDAvlpvvpmfhvnAW--GLPYS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 330 VygplALGATTLLFEGvptyPRPD--RYWEIINRYGVNIFYTTPTA----LRALRREGTQwtekydLSTLR--ILGsvGE 401
Cdd:PRK07008 240 A----PLTGAKLVLPG----PDLDgkSLYELIEAERVTFSAGVPTVwlglLNHMREAGLR------FSTLRrtVIG--GS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 402 PINPEVWIWFHEHVGkgkLPLLDTWWQTEtgsilISPLPYVGKLK------PGST--------GKPLPGISAKIVNSDGS 467
Cdd:PRK07008 304 ACPPAMIRTFEDEYG---VEVIHAWGMTE-----MSPLGTLCKLKwkhsqlPLDEqrkllekqGRVIYGVDMKIVGDDGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 468 DA--EANEGGHLLITEPWpgmLTDihndraRYNRTyfERFP---GSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGT 542
Cdd:PRK07008 376 ELpwDGKAFGDLQVRGPW---VID------RYFRG--DASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 543 TEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLdedDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGK 622
Cdd:PRK07008 445 IDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGK 521
|
....*..
gi 1816261920 623 IMRRILR 629
Cdd:PRK07008 522 LQKLKLR 528
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
121-628 |
3.15e-13 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 72.20 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 121 FTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAad 200
Cdd:cd17645 24 LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 201 gvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmRSADPLFILHTSGS 280
Cdd:cd17645 102 ------------------------------------------------------------------NPDDLAYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 281 TGKAKGVV--HStggymtATAHTTQW---VFDLRDDDVHWCTADIGWiTGHSYTVYGPLALGATTLLfegVPTYPRPDry 355
Cdd:cd17645 116 TGLPKGVMieHH------NLVNLCEWhrpYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALHV---VPSERRLD-- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 356 WEIINRY----GVNIFYTtPTALralrreGTQWTEkYDLSTLRILGSVGEPINPEVwiwfhehvgKGKLPLLDTWWQTET 431
Cdd:cd17645 184 LDALNDYfnqeGITISFL-PTGA------AEQFMQ-LDNQSLRVLLTGGDKLKKIE---------RKGYKLVNNYGPTEN 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 432 gSILISPLPYVGKLKPGSTGKPLPGISAKIVNSDGSDAEANEGGHLLITEPWPGmltdihndRARYNRTYF--ERF---- 505
Cdd:cd17645 247 -TVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLA--------RGYLNRPELtaEKFivhp 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 --PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSG 581
Cdd:cd17645 318 fvPGErmYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEE 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1816261920 582 LDEDDemrtvLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:cd17645 398 IPHEE-----LREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
119-634 |
4.32e-12 |
|
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: 68.53 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIa 198
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 adgvlrggkkiplkrnvdealfecpsveqvimvkrtgdeidfiegrdtwwheeisgpdiedyckpesmrsADPLFILHTS 278
Cdd:cd05940 81 ----------------------------------------------------------------------VDAALYIYTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 279 GSTG--KAKGVVHSTGGYMTATAhttQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVPTyprpDRYW 356
Cdd:cd05940 91 GTTGlpKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSA----SNFW 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 357 EIINRYGVNIFYTTPTALRALRREGTQWTEKyDLSTLRILGSvgePINPEVWIWFHEHVGKGKlpLLDTWWQTE------ 430
Cdd:cd05940 164 DDIRKYQATIFQYIGELCRYLLNQPPKPTER-KHKVRMIFGN---GLRPDIWEEFKERFGVPR--IAEFYAATEgnsgfi 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 431 -----TGSILISP--LPYVGKLK----PGSTGKPlpgisakIVNSDGSDAEANEG--GHLL--ITEPWP--GMlTDIHND 493
Cdd:cd05940 238 nffgkPGAIGRNPslLRKVAPLAlvkyDLESGEP-------IRDAEGRCIKVPRGepGLLIsrINPLEPfdGY-TDPAAT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 494 RARYNRTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIP---HEikGQ 570
Cdd:cd05940 310 EKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTD--GR 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816261920 571 TVYAYVTLRSGLDEDdemRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVG 634
Cdd:cd05940 388 AGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
104-630 |
1.16e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 67.59 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 104 NKAALIWQGepeeevRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVS 183
Cdd:PRK08279 52 DRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 184 LQNRIIDCDAKILIaadgvlrggkkiplkrnVDEALFECpsveqvimVKRTGDEIDfiEGRDTWWHEEISGPDIEDY--- 260
Cdd:PRK08279 126 LAHSLNLVDAKHLI-----------------VGEELVEA--------FEEARADLA--RPPRLWVAGGDTLDDPEGYedl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 261 ---------CKPES---MRSADPLFILHTSGSTGKAKGVVHSTGGYMTAT---AHTTqwvfDLRDDDVHWCTADIGWITG 325
Cdd:PRK08279 179 aaaaagaptTNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMggfGGLL----RLTPDDVLYCCLPLYHNTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 326 HSYTVYGPLALGATTLLfegvptypRP----DRYWEIINRYGVNIF--------YTTPTALRALRREgtqwtekydlSTL 393
Cdd:PRK08279 255 GTVAWSSVLAAGATLAL--------RRkfsaSRFWDDVRRYRATAFqyigelcrYLLNQPPKPTDRD----------HRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 394 RILgsVGEPINPEVWIWFHEHVGKGKlpLLDTWWQTET-----------GSILISPLPyvgKLKPGS-------TGKPlp 455
Cdd:PRK08279 317 RLM--IGNGLRPDIWDEFQQRFGIPR--ILEFYAASEGnvgfinvfnfdGTVGRVPLW---LAHPYAivkydvdTGEP-- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 456 gisakIVNSDG--SDAEANEGGHLL--ITEPWP--GMlTDIHNDRARYNRTYFErfPGS--YETGDGARVDEDGDYWIMG 527
Cdd:PRK08279 388 -----VRDADGrcIKVKPGEVGLLIgrITDRGPfdGY-TDPEASEKKILRDVFK--KGDawFNTGDLMRDDGFGHAQFVD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 528 RLDDVI-----NVSghrlgTTEIESALIAHPDVTEAAVVG--IP-HEikGQTVYAYVTLRSGLDEDdemRTVLREWVSQK 599
Cdd:PRK08279 460 RLGDTFrwkgeNVA-----TTEVENALSGFPGVEEAVVYGveVPgTD--GRAGMAAIVLADGAEFD---LAALAAHLYER 529
|
570 580 590
....*....|....*....|....*....|.
gi 1816261920 600 IGPIAVPETIQFSEGLPKTRSGKIMRRILRR 630
Cdd:PRK08279 530 LPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
239-633 |
2.13e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.56 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 239 DFIEGRDTWwheEISGPDIEDYCKPeSMRSADPLFILHTSGSTGKAKGVVHS--TggyMTATAHTTQWVFDLrdDDVH-W 315
Cdd:PRK07445 94 DQIWGLDQL---KLSHPPPLPSQGI-LPNLETGWIMIPTGGSSGQIRFAIHTweT---LTASVQGFQRYFQL--QQVNsF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 316 CTADIGWITG-----HSYTVYGPLALGATTLLFEGVPTYPRPDRYWeiinrygvniFYTTPTALRALRREGTQWtekydL 390
Cdd:PRK07445 165 CVLPLYHVSGlmqfmRSFLTGGKLVILPYKRLKSGQELPPNPSDFF----------LSLVPTQLQRLLQLRPQW-----L 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 391 STLRI--LGsvGEPinpeVWIWFHEHVGKGKLPLLDTWWQTETGSilisplpYVGKLKPG-------STGKPLPGisAKI 461
Cdd:PRK07445 230 AQFRTilLG--GAP----AWPSLLEQARQLQLRLAPTYGMTETAS-------QIATLKPDdflagnnSSGQVLPH--AQI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 462 vnsdgsDAEANEGGHLLITEP------WPgmltdihndrarynrtYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINV 535
Cdd:PRK07445 295 ------TIPANQTGNITIQAQslalgyYP----------------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 536 SGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYA-YVTLRSGLDEDDemrtvLREWVSQKIGPIAVPETIQFSEG 614
Cdd:PRK07445 353 GGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAiYVPKDPSISLEE-----LKTAIKDQLSPFKQPKHWIPVPQ 427
|
410
....*....|....*....
gi 1816261920 615 LPKTRSGKIMRRILRRIAV 633
Cdd:PRK07445 428 LPRNPQGKINRQQLQQIAV 446
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-635 |
2.59e-11 |
|
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: 66.36 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 267 RSADPL-FILHTSGSTGKAKGVV--HSTGGY-MTATAHTTQWvfDLRDDDVHW--CTADIGWITGHsytvYGPLALGATT 340
Cdd:cd05908 103 ELADELaFIQFSSGSTGDPKGVMltHENLVHnMFAILNSTEW--KTKDRILSWmpLTHDMGLIAFH----LAPLIAGMNQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 341 LLFEGVPTYPRPDRYWEIINRYGVNIFYTTPTALR-ALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVGKGK 419
Cdd:cd05908 177 YLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKyFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 420 L--------------------PLLDTWWQTET----GSILISPLPYVGKLKPG-----STGKPLPGISAKIVNSDGSDAE 470
Cdd:cd05908 257 LkrnailpvyglaeasvgaslPKAQSPFKTITlgrrHVTHGEPEPEVDKKDSEcltfvEVGKPIDETDIRICDEDNKILP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 471 ANEGGHLLIT--EPWPGMltdiHNDRARYNRTYFErfPGSYETGDGARVdEDGDYWIMGRLDDVINVSGHRLGTTEIESA 548
Cdd:cd05908 337 DGYIGHIQIRgkNVTPGY----YNNPEATAKVFTD--DGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 549 LIAHPDVTEAAVVGI---PHEIKGQTVYAYVTLRSGLDE----DDEMRTVLRE---WVSQKIGPIAVpetiqfsegLPKT 618
Cdd:cd05908 410 AEELEGVELGRVVACgvnNSNTRNEEIFCFIEHRKSEDDfyplGKKIKKHLNKrggWQINEVLPIRR---------IPKT 480
|
410
....*....|....*...
gi 1816261920 619 RSGKIMR-RILRRIAVGE 635
Cdd:cd05908 481 TSGKVKRyELAQRYQSGE 498
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
118-625 |
4.07e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.80 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 118 VRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHS-----VIFAGFSA--VSLQNRIID 190
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpMGFGGRESyiAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 191 CDAKILIAADGvlrggkkipLKRNVDEALFECPSVEQVimvkrTGDEIDFIEGRDTwwheEISGPDIEDYCkpesmrsad 270
Cdd:PRK09192 127 AQPAAIITPDE---------LLPWVNEATHGNPLLHVL-----SHAWFKALPEADV----ALPRPTPDDIA--------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 271 plFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDD--VHWCT--ADIGWITghsyTVYGPLALGATTLLfegV 346
Cdd:PRK09192 180 --YLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDrcVSWLPfyHDMGLVG----FLLTPVATQLSVDY---L 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 347 PTYP---RPDRYWEIINRYGVNIFYTTPTALR-ALRREGTQWTEKYDLSTLRILGSVGEPINPEVWIWFHEHVG------ 416
Cdd:PRK09192 251 PTRDfarRPLQWLDLISRNRGTISYSPPFGYElCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFApagfdd 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 417 KGKLPL--------------LDTWWQTETgsILISPLPYVGKLKPGST-----------GKPLPGISAKIVNSDGSDAEA 471
Cdd:PRK09192 331 KAFMPSyglaeatlavsfspLGSGIVVEE--VDRDRLEYQGKAVAPGAetrrvrtfvncGKALPGHEIEIRNEAGMPLPE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 472 NEGGHLLITEPwPGMltdihndrarynRTYFERfpgsYETGDGARVD-----------EDGDYWIMGRLDDVINVSGHRL 540
Cdd:PRK09192 409 RVVGHICVRGP-SLM------------SGYFRD----EESQDVLAADgwldtgdlgylLDGYLYITGRAKDLIIINGRNI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 541 GTTEIESALIAHPDVT--EAAVVGIPHEiKGQTVYAYVTLRSGldeDDEMRTVLREWVSQKIGPI-AVPETIQF--SEGL 615
Cdd:PRK09192 472 WPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLVQCRIS---DEERRGQLIHALAALVRSEfGVEAAVELvpPHSL 547
|
570
....*....|
gi 1816261920 616 PKTRSGKIMR 625
Cdd:PRK09192 548 PRTSSGKLSR 557
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
111-626 |
5.73e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.40 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 111 QGEPEEEVRVfTYHMLHRKVCRFANVLKKIGVSKGDRVAIyLPMVPELVISmlacarigAVHSVIFAGFSAVSLQN---- 186
Cdd:PRK07768 21 TGEPDAPVRH-TWGEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPVEIAP--------TAQGLWMRGASLTMLHQptpr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 187 -----------RIIDcdakiLIAADGVLRGgkkiplkrnvdeALFE--CPSVEQVIMvkrTGDEIDfiegrDTWWHEEIS 253
Cdd:PRK07768 91 tdlavwaedtlRVIG-----MIGAKAVVVG------------EPFLaaAPVLEEKGI---RVLTVA-----DLLAADPID 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 254 GPDIEDyckpesmrsADPLFILHTSGSTGKAKGV------VHSTGGYMTATAHttqwvFDLRDD-DVHW--CTADIGWIT 324
Cdd:PRK07768 146 PVETGE---------DDLALMQLTSGSTGSPKAVqithgnLYANAEAMFVAAE-----FDVETDvMVSWlpLFHDMGMVG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 325 GhsYTVygPLALGATTLLFEGVPTYPRPDRYWEIINRY------GVNIFYTTptALRALRREGTQwtEKYDLSTLRILGS 398
Cdd:PRK07768 212 F--LTV--PMYFGAELVKVTPMDFLRDPLLWAELISKYrgtmtaAPNFAYAL--LARRLRRQAKP--GAFDLSSLRFALN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 399 VGEPINPEVWIWFHEHVGKGKLP---LLDTWWQTETG-SILISPLP------YV----------------GKLKPGST-G 451
Cdd:PRK07768 284 GAEPIDPADVEDLLDAGARFGLRpeaILPAYGMAEATlAVSFSPCGaglvvdEVdadllaalrravpatkGNTRRLATlG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 452 KPLPGISAKIVNSDGSDAEANEGGHLLI----------TEPWPGMLTDIHndrarynrtyferfpGSYETGDGARVDEDG 521
Cdd:PRK07768 364 PPLPGLEVRVVDEDGQVLPPRGVGVIELrgesvtpgylTMDGFIPAQDAD---------------GWLDTGDLGYLTEEG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 522 DYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDDEMRTVLREWVSQKI- 600
Cdd:PRK07768 429 EVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVv 508
|
570 580 590
....*....|....*....|....*....|....*
gi 1816261920 601 -----GPIAV----PETIqfseglPKTRSGKIMRR 626
Cdd:PRK07768 509 aevgvRPRNVvvlgPGSI------PKTPSGKLRRA 537
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
270-632 |
7.84e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.12 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 270 DPLFILHTSGSTGKAKGVVHSTGGYMtATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLfegvptY 349
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLL-ANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL------Y 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 350 PRPDRYW---EIINRYGVNIFYTTPTALRALRRegtqWTEKYDLSTLRILGSVGEPINPEV-WIWFHehvgKGKLPLLDT 425
Cdd:PRK08043 439 PSPLHYRivpELVYDRNCTVLFGTSTFLGNYAR----FANPYDFARLRYVVAGAEKLQESTkQLWQD----KFGLRILEG 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 426 WWQTETGSILISPLPYVGKlkPGSTGKPLPGISAKIVNSDGSDaeanEGGHLLITEP----------WPGMLTDIHNDRA 495
Cdd:PRK08043 511 YGVTECAPVVSINVPMAAK--PGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPnimngylrveKPGVLEVPTAENA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 496 RYNRTyferfPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIES-ALIAHPDVTEAAVVgIPHEIKGQTVYA 574
Cdd:PRK08043 585 RGEME-----RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEALVL 658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816261920 575 YVTlRSGLDEdDEMRTVLREwvsQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIA 632
Cdd:PRK08043 659 FTT-DSELTR-EKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
506-634 |
8.16e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.57 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 506 PGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAvVGIPHEIKGQTVYAYVTLRSGLD 583
Cdd:PRK05691 4099 PGErlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVL 4177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 584 EDDEMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRILRRIAVG 634
Cdd:PRK05691 4178 AQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIG 4228
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
119-581 |
3.75e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 60.12 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 119 RVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVhSVIFAGFSAVSLQNRIIDCDAkilIA 198
Cdd:PRK07868 471 RVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV-AVLMPPDTDLAAAVRLGGVTE---II 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADgvlrggkkiplKRNVDEALFECPSVeqviMVKRTGD--EIDFIEGRDTWWHEEISgPD---IEDYCKPESMRSADPLF 273
Cdd:PRK07868 547 TD-----------PTNLEAARQLPGRV----LVLGGGEsrDLDLPDDADVIDMEKID-PDaveLPGWYRPNPGLARDLAF 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 274 IL-HTSGSTGKAKGVvhsTGGYMTATAHTTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGATTLLFEGVptypRP 352
Cdd:PRK07868 611 IAfSTAGGELVAKQI---TNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL----DP 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 353 DRYWEIINRYGVNIFYTTPTALRalrregtqwtEKYDLSTLRILGS------VGEPINPEVWiwfhEHVGKGKLP--LLD 424
Cdd:PRK07868 684 DRFVQEVRQYGVTVVSYTWAMLR----------EVVDDPAFVLHGNhpvrlfIGSGMPTGLW----ERVVEAFAPahVVE 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 425 TWWQTETGSILISplpyVGKLKPGSTGKPLPG-----------ISAKIV-NSDG--SDAEANEGGhLLITEPWPGMltdi 490
Cdd:PRK07868 750 FFATTDGQAVLAN----VSGAKIGSKGRPLPGagrvelaaydpEHDLILeDDRGfvRRAEVNEVG-VLLARARGPI---- 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 491 hNDRARYNRTYFErfPGS--YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIphEIK 568
Cdd:PRK07868 821 -DPTASVKRGVFA--PADtwISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGV--EVG 895
|
490
....*....|....
gi 1816261920 569 GQTV-YAYVTLRSG 581
Cdd:PRK07868 896 GRQLaVAAVTLRPG 909
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
122-343 |
7.60e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.97 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIAADG 201
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 VLrggKKIPlkrNVDEALfecPSVEQVIMVKRTGDEIDFIEGRDTWWHEEiSGPDIEDYCK-----PESMRSADPLFILH 276
Cdd:PLN02387 188 QL---KKLI---DISSQL---ETVKRVIYMDDEGVDSDSSLSGSSNWTVS-SFSEVEKLGKenpvdPDLPSPNDIAVIMY 257
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816261920 277 TSGSTGKAKGVVHSTGGYMTATAHTTQWVFDLRDDDVhwctadigwitghsYTVYGPLA----LGATTLLF 343
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLAhileLAAESVMA 314
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
116-466 |
1.15e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.45 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 116 EEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFA--GFSAVSLQNRIIDCDA 193
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYAnlGEDALAYALRETECKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 194 kiliaadgVLRGGKKIP-LKRNVDEALFECPSVeqvIMVkrtgDEIDfiEGRDTWWHEEISGPDIEDycKPESMRSADPL 272
Cdd:PTZ00216 197 --------IVCNGKNVPnLLRLMKSGGMPNTTI---IYL----DSLP--ASVDTEGCRLVAWTDVVA--KGHSAGSHHPL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 273 ----------FILHTSGSTGKAKGVVHsTGGYMTATAHT-TQWVFDLrdddvhwctadIGWIT-GHSYTVYGPLA----L 336
Cdd:PTZ00216 258 nipennddlaLIMYTSGTTGDPKGVMH-THGSLTAGILAlEDRLNDL-----------IGPPEeDETYCSYLPLAhimeF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 337 GATTLLFE-------GVP-----TYPRP--D-------------RYWEIINRyGV------------NIF---YTTPtaL 374
Cdd:PTZ00216 326 GVTNIFLArgaligfGSPrtltdTFARPhgDltefrpvfligvpRIFDTIKK-AVeaklppvgslkrRVFdhaYQSR--L 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 375 RALR--REGTQWTEK-YDL------STLRILGSVGEPINPEVWIWFHEHVGkgklPLLDTWWQTET---GSILISplpyv 442
Cdd:PTZ00216 403 RALKegKDTPYWNEKvFSApravlgGRVRAMLSGGGPLSAATQEFVNVVFG----MVIQGWGLTETvccGGIQRT----- 473
|
410 420
....*....|....*....|....
gi 1816261920 443 GKLKPGSTGKPLPGISAKIVNSDG 466
Cdd:PTZ00216 474 GDLEPNAVGQLLKGVEMKLLDTEE 497
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
438-628 |
7.86e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 55.29 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 438 PLPyVGKLKPGSTgkplpgisAKIVNSDGSDAEANEGGHLLITEPW--PGMLtdihNDRARYNRTYFErFPG--SYETGD 513
Cdd:PRK04813 317 RLP-IGYAKPDSP--------LLIIDEEGTKLPDGEQGEIVISGPSvsKGYL----NNPEKTAEAFFT-FDGqpAYHTGD 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 514 GARVDeDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEDD-EMRTVL 592
Cdd:PRK04813 383 AGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREfELTKAI 461
|
170 180 190
....*....|....*....|....*....|....*.
gi 1816261920 593 REWVSQKIGPIAVPETIQFSEGLPKTRSGKIMRRIL 628
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
120-585 |
2.49e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 53.83 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 120 VFTYHMLHRKVCRFANVLKK-IGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIA 198
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 199 ADgvlrggkkiPLKRNVDEALfecPSVEQ----VIMVKRT---------GDEIDfiegrdtwwhEEISGPdiedycKPES 265
Cdd:cd05938 85 AP---------ELQEAVEEVL---PALRAdgvsVWYLSHTsntegvislLDKVD----------AASDEP------VPAS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 266 MRSA----DPLFILHTSGSTG--KAKGVVHSTGGYMTAtahtTQWVFDLRDDDVHWCTADIGWITGHSYTVYGPLALGAT 339
Cdd:cd05938 137 LRAHvtikSPALYIYTSGTTGlpKAARISHLRVLQCSG----FLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGAT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 340 TLLfegvptypRP----DRYWEIINRYGVNIFYTTPTALRALRREGTQWTEKYdlSTLRIlgSVGEPINPEVWIWFHEHV 415
Cdd:cd05938 213 CVL--------KPkfsaSQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRD--HKVRL--AIGNGLRADVWREFLRRF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 416 gkGKLPLLDTWWQTEtGSilISPLPYVGklKPGSTGKplpgISA--------KIVNSDGSDAEA--NEGGHLLITEPW-P 484
Cdd:cd05938 281 --GPIRIREFYGSTE-GN--IGFFNYTG--KIGAVGR----VSYlykllfpfELIKFDVEKEEPvrDAQGFCIPVAKGeP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 485 GML-TDIHN---------DRARYN----RTYFERFPGSYETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALI 550
Cdd:cd05938 350 GLLvAKITQqspflgyagDKEQTEkkllRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLG 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816261920 551 AHPDVTEAAVVGIP---HEikGQTVYAYVTLRSGLDED 585
Cdd:cd05938 430 LLDFLQEVNVYGVTvpgHE--GRIGMAAVKLKPGHEFD 465
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
266-623 |
5.23e-07 |
|
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: 52.47 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 266 MRSADPL-FILHTSGSTGKAKGVVHSTGGYMTATAHTTQwVFDLRDDDVHWCTadigwitghSYTVYGP--------LAL 336
Cdd:cd17654 114 IRTDECLaYVIHTSGTTGTPKIVAVPHKCILPNIQHFRS-LFNITSEDILFLT---------SPLTFDPsvveiflsLSS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 337 GATTLLfegVPTYPR--PDRYWEII-NRYGVNIFYTTPTALRALRREGTQWTEKYDLSTLRILGSVGE--PINPEVWIWF 411
Cdd:cd17654 184 GATLLI---VPTSVKvlPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEpfPSLVILSSWR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 412 HEhvgKGKLPLLDTWWQTETGS--------ILISPLPyvgklkpgsTGKPLPGISAKIVNSDGSDAEANEGGHLLITepw 483
Cdd:cd17654 261 GK---GNRTRIFNIYGITEVSCwalaykvpEEDSPVQ---------LGSPLLGTVIEVRDQNGSEGTGQVFLGGLNR--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 484 pGMLTDIHNDRArynrtyferFPGSYETGDGARVdEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTEAAVVgi 563
Cdd:cd17654 326 -VCILDDEVTVP---------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-- 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 564 pHEIKGQTVYAYVTLRSGLDEDDEMRTVLREwvsqkigPIAVPETIQFSEGLPKTRSGKI 623
Cdd:cd17654 393 -LSDQQRLIAFIVGESSSSRIHKELQLTLLS-------SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
545-660 |
5.73e-07 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 52.07 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 545 IESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDEddemrTVLREWVSQKIGPIAvPETIQFSEGLPKTRSGKIM 624
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELPADE-----KSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|....*...
gi 1816261920 625 RRILRRIAVGENDLGDT--TTLSDASVIADLIEGQKEL 660
Cdd:PRK09188 319 DDILRLIAMNQIDELDDllREPEIRGLVEAIAAHRLNL 356
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
122-429 |
5.60e-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: 49.52 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAVSLQNRIIDCDAKILIaadg 201
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 202 vlrggkkiplkrnvdealfeCPSveqvimvkrtgdeidfiegrdtwwheeisgpdiedycKPEsmrsaDPLFILHTSGST 281
Cdd:cd17639 83 --------------------TDG-------------------------------------KPD-----DLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 282 GKAKGVVHsTGGYMTATAHT-TQWVFD-LRDDDVhwctadigwitghsYTVYGPLA----LGATTLLFegvptyprpdrY 355
Cdd:cd17639 101 GNPKGVML-THGNLVAGIAGlGDRVPElLGPDDR--------------YLAYLPLAhifeLAAENVCL-----------Y 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 356 WeiinryGVNIFYTTPTAL--RALRRegtqwtEKYDLSTLR--ILGSVgepinPEVWiwfhEHVGKG---KLPLLDTWWQ 428
Cdd:cd17639 155 R------GGTIGYGSPRTLtdKSKRG------CKGDLTEFKptLMVGV-----PAIW----DTIRKGvlaKLNPMGGLKR 213
|
.
gi 1816261920 429 T 429
Cdd:cd17639 214 T 214
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
96-299 |
7.51e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 49.25 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 96 RHLENGRRNKaaLIWQgepeeevrvfTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVI 175
Cdd:PLN02614 67 REIVDGKPGK--YVWQ----------TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 176 FAGFSAVSLQNRIIDCDAKILIAADgvlrggKKIPlkrnvdEALFECPSVEQVI--MVKRTGDEIDFIEGRDTW------ 247
Cdd:PLN02614 135 YDTLGAGAVEFIISHSEVSIVFVEE------KKIS------ELFKTCPNSTEYMktVVSFGGVSREQKEEAETFglviya 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1816261920 248 WHEEISGPDIEDYCKPESMRSaDPLFILHTSGSTGKAKGVVHSTGGYMTATA 299
Cdd:PLN02614 203 WDEFLKLGEGKQYDLPIKKKS-DICTIMYTSGTTGDPKGVMISNESIVTLIA 253
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
114-371 |
1.61e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.52 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 114 PEEEVRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGF-------------- 179
Cdd:TIGR03443 264 PSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYpparqtiylsvakp 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 180 -------SAVSLQNRIIDCDAKIL----------IAADGVLRGGKkiplkrnVDEALFECPSVEQVIMVKRTGdeidfie 242
Cdd:TIGR03443 344 ralivieKAGTLDQLVRDYIDKELelrteipalaLQDDGSLVGGS-------LEGGETDVLAPYQALKDTPTG------- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 243 grdtwwheEISGPDiedyckpesmrSADPL-FilhTSGSTGKAKGVVhstgGYMTATAHTTQWV---FDLRDDDVHWCTA 318
Cdd:TIGR03443 410 --------VVVGPD-----------SNPTLsF---TSGSEGIPKGVL----GRHFSLAYYFPWMakrFGLSENDKFTMLS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 319 DIgwitGH---SYTVYGPLALGATTLlfegVPTYP---RPDRYWEIINRYGVNIFYTTP 371
Cdd:TIGR03443 464 GI----AHdpiQRDMFTPLFLGAQLL----VPTADdigTPGRLAEWMAKYGATVTHLTP 514
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
122-306 |
3.35e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 47.14 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 122 TYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIF--AGFSAVSLqnrIIDcDAKILIAa 199
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYdtLGANAVEF---IIN-HAEVSIA- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 200 dgvLRGGKKIPlkrNVDEALFECPSVEQVI--------MVKRTGDEIdfieGRDTWWHEEISGPDIEDYCKPESmRSADP 271
Cdd:PLN02861 154 ---FVQESKIS---SILSCLPKCSSNLKTIvsfgdvssEQKEEAEEL----GVSCFSWEEFSLMGSLDCELPPK-QKTDI 222
|
170 180 190
....*....|....*....|....*....|....*
gi 1816261920 272 LFILHTSGSTGKAKGVVHSTGGYMTATAHTTQWVF 306
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK 257
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
118-210 |
4.78e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 43.28 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 118 VRVFTYHMLHRKVCRFANVLKKIGVSKGDRVAIYLPMVPELVISMLACARIGAVHSVIFAGFSAvSLQNRIIDCdAK--- 194
Cdd:cd17647 18 TRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP-ARQNIYLGV-AKprg 95
|
90
....*....|....*..
gi 1816261920 195 -ILIAADGVLRGGKKIP 210
Cdd:cd17647 96 lIVIRAAGVVVGPDSNP 112
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
389-633 |
9.22e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.45 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 389 DLSTLRILGSVGEPINPEVWIWFHEH---VGKGKLPLLDTWWQTETGSILISPLPYVGKL------KPGST-------GK 452
Cdd:PRK05851 270 DLGALRVALNGGEPVDCDGFERFATAmapFGFDAGAAAPSYGLAESTCAVTVPVPGIGLRvdevttDDGSGarrhavlGN 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 453 PLPGISAKIVNSDGS-DAEANEGGHLLI--TEPWPGMLTDIHNDRArynrtyfERFPgsyeTGD-GARVDedGDYWIMGR 528
Cdd:PRK05851 350 PIPGMEVRISPGDGAaGVAGREIGEIEIrgASMMSGYLGQAPIDPD-------DWFP----TGDlGYLVD--GGLVVCGR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 529 LDDVINVSGHRLGTTEIESALIAHPDVTEAAVVGIPHEIKGqtvyayvtLRSGL---------DEDDEMRTVLREWVSQk 599
Cdd:PRK05851 417 AKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--------ARPGLviaaefrgpDEAGARSEVVQRVASE- 487
|
250 260 270
....*....|....*....|....*....|....*.
gi 1816261920 600 IGpiAVPETIQFSE--GLPKTRSGKimrriLRRIAV 633
Cdd:PRK05851 488 CG--VVPSDVVFVApgSLPRTSSGK-----LRRLAV 516
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
277-617 |
2.88e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 40.52 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 277 TSGSTGKAKGVvhstgGYmtaTAH---TTQWVF-------DLRDDD-VHWCTAdIGWITGHSYTVYGPLALGATTllfeg 345
Cdd:COG1541 91 SSGTTGKPTVV-----GY---TRKdldRWAELFarslraaGVRPGDrVQNAFG-YGLFTGGLGLHYGAERLGATV----- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 346 VPTYP-RPDRYWEIINRYGVNIFYTTPT-ALR---ALRREGTQWTEkydlSTLR--ILGsvGEPInPEVWI-WFHEHVGk 417
Cdd:COG1541 157 IPAGGgNTERQLRLMQDFGPTVLVGTPSyLLYlaeVAEEEGIDPRD----LSLKkgIFG--GEPW-SEEMRkEIEERWG- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 418 gkLPLLDTWWQTETGsilisplPYVG---KLKPGS---------------TGKPLPgisakivnsDGsdaeanEGGHLLI 479
Cdd:COG1541 229 --IKAYDIYGLTEVG-------PGVAyecEAQDGLhiwedhflveiidpeTGEPVP---------EG------EEGELVV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 480 TepwpgMLTD-----IhndraRYNrtyferfpgsyeTGDGARVDEDGDYW---------IMGRLDDVINVSGHRLGTTEI 545
Cdd:COG1541 285 T-----TLTKeamplI-----RYR------------TGDLTRLLPEPCPCgrthprigrILGRADDMLIIRGVNVFPSQI 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 546 ESALIAHPDVTEAAVVGIPHEIKGQTVYAYVTLRSGLDED-------DEMRTVLRewVSQKIGpIAVPETIQFSEGLPK 617
Cdd:COG1541 343 EEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEalaeaiaAALKAVLG--LRAEVE-LVEPGSLPRSEGKAK 418
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
509-623 |
6.33e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 39.42 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261920 509 YETGDGARVDEDGDYWIMGRLDDVINVSGHRLGTTEIESALIAHPDVTE------------AAVVG--IPHEIKGQTVYA 574
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrrdkdeePTLVSyiVPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1816261920 575 YVTLRSGLDEDD----------EMRTVLREWVSQKIGPIAVPETIQFSEGLPKTRSGKI 623
Cdd:cd17647 454 AQEDVPKEVSTDpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| |
