|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
44-696 |
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: 1168.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 44 RYRELHGRSVLEPREFWGDIAKEFYWKTPCSGPFlqynfDVTKGKIFIEWMKGATTNICYNLLDRNVneKKLGDRVAFYW 123
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHL--KERGDKVAIIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 124 EGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILD 203
Cdd:cd05966 75 EGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 204 SSCTLLITADAFYRGEKLVNLKELVDDALHKCrekgFPVKRCIVVKHLGRAelgtgdspshspplkrpcqdlqdkmkakp 283
Cdd:cd05966 155 AQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE----------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 284 mskrpqIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDV 363
Cdd:cd05966 202 ------VPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 364 FWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASL 443
Cdd:cd05966 276 YWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 444 RVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEA 523
Cdd:cd05966 356 RVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEV 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 524 EGYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHR 603
Cdd:cd05966 436 EGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHP 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 604 AIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 683
Cdd:cd05966 516 AVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAA 595
|
650
....*....|...
gi 2119488996 684 NDHDLGDTSTVAD 696
Cdd:cd05966 596 GEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
29-703 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1105.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 29 PPPELSRTAHVpSMARYRELHGRSVLEPREFWGDIAKEFYWKTPcsgpflqYNFDVTKGKIFIEWMKGATTNICYNLLDR 108
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 109 NVNEKklGDRVAFYWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIV 188
Cdd:PRK00174 76 HLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 189 FAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDALHKCRekgfPVKRCIVVKHLGraelgtGDspshsppl 268
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG------GD-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 269 krpcqdlqdkmkakpmskrpqIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYT 348
Cdd:PRK00174 216 ---------------------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 349 ATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLM 428
Cdd:PRK00174 275 AMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 429 KFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVA 508
Cdd:PRK00174 355 KEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 509 PAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGH 588
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 589 LLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKT 668
Cdd:PRK00174 515 RLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKT 594
|
650 660 670
....*....|....*....|....*....|....*
gi 2119488996 669 RSGKIMRRVLRKIAQNDHDLGDTSTVADQSVISHL 703
Cdd:PRK00174 595 RSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
41-703 |
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: 1026.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 41 SMARYRELHGRSVLEPREFWGDIAKE-FYWKTP------CSGPFlqynfdvtkgkiFIEWMKGATTNICYNLLDRNVneK 113
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFKPftkvldWSFPP------------FYKWFVGGELNVSYNCVDRHL--E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 114 KLGDRVAFYWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFS 193
Cdd:TIGR02188 69 ARPDKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 194 ADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDALHKCREKgfpVKRCIVVKHLGRaelgtgdspshspplkrpcq 273
Cdd:TIGR02188 149 AEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTGN-------------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 274 dlqdkmkakpmskrPQIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFK 353
Cdd:TIGR02188 206 --------------PVVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 354 YVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDE 433
Cdd:TIGR02188 272 YVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 434 PVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 513
Cdd:TIGR02188 352 WVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVD 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 514 ES-GEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLST 592
Cdd:TIGR02188 432 EEgNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGT 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 593 AEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:TIGR02188 512 AEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGK 591
|
650 660 670
....*....|....*....|....*....|..
gi 2119488996 673 IMRRVLRKIAQNDHD-LGDTSTVADQSVISHL 703
Cdd:TIGR02188 592 IMRRLLRKIAAGEAEiLGDTSTLEDPSVVEEL 623
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
29-703 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 883.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 29 PPPELSRTAHVPSMARYRELHGRSVLEPREFWGDIAKEFYWKTPCSG-PFLQYNFDVTKGKIFIEWMKGATTNICYNLLD 107
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGdEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 108 RNVnEKKLGDRVAFYWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSI 187
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 188 VFAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDALHKCREKGFPVKRCIVVKHlgraelgtgdspshspp 267
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYEN----------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 268 lkrpcqdlQDKMKakpmskRPQIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLY 347
Cdd:PLN02654 238 --------QLAMK------REDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 348 TATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLL 427
Cdd:PLN02654 304 TATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 428 MKFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGV 507
Cdd:PLN02654 384 MRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 508 APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSG 587
Cdd:PLN02654 464 QPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 588 HLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPK 667
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623
|
650 660 670
....*....|....*....|....*....|....*..
gi 2119488996 668 TRSGKIMRRVLRKIAQNDHD-LGDTSTVADQSVISHL 703
Cdd:PLN02654 624 TRSGKIMRRILRKIASRQLDeLGDTSTLADPGVVDQL 660
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
92-703 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 865.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 92 EWMKGATTNICYNLLDRNVNEKklGDRVAFYWEGnEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILEL 171
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 172 VVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDALHKCREkgfpVKRCIVVKHL 251
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 252 GRAELGTGDspshspplkrpcqdlqdkmkakpmskrpqipwnqgvdLWWHEILGDAEEECEPEWCDAEDPLFILYTSGST 331
Cdd:COG0365 154 GADVPMEGD-------------------------------------LDWDELLAAASAEFEPEPTDADDPLFILYTSGTT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 332 GKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDK 411
Cdd:COG0365 197 GKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 412 YKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPG 491
Cdd:COG0365 277 YGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 492 aTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDG 571
Cdd:COG0365 354 -LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 572 YYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKIS 651
Cdd:COG0365 433 YFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELG 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2119488996 652 PIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADQSVISHL 703
Cdd:COG0365 513 PYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
45-674 |
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: 702.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 45 YRELHGRSVLEPREFWGDIAKEFYWKTPcsgPFLQYNFDVTKGKIFIEWMKGATTNICYNLLDRNVNEKklGDRVAFYWE 124
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITP---YQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 125 GNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDS 204
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 205 SCTLLITADAFYRGEKLVNLKELVDDALHKcreKGFPVKRCIVVKHLGRAelgtgdspshspplkrpcqdlqdkmkakpm 284
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLKRTGSD------------------------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 285 skrpqIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVF 364
Cdd:cd17634 203 -----IDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 365 WCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLR 444
Cdd:cd17634 278 WCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 445 VLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 524
Cdd:cd17634 358 ILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 525 GYLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRA 604
Cdd:cd17634 438 GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPK 517
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 605 IAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIM 674
Cdd:cd17634 518 VAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
45-703 |
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: 595.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 45 YRELHGRSVLEPREFWGDIAKEFYWKTPcsgpfLQYNFDVTKGKiFIEWMKGATTNICYNLLDRNVnEKKLGDRVAFYWE 124
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKP-----PEKILDNSNPP-FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 125 GNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDS 204
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 205 SCTLLITADAFYRGEKLVNLKELVDDALhkcREKGFPVKRCIVVkhlgraelgtgDSPSHSPPLKRPcqdlqdkmkakpm 284
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKAL---ELSGHKPHHVLVL-----------NRPQVPADLTKP------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 285 skrpqipwnqGVDLWWHEILGDAEEEcEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVF 364
Cdd:cd05967 207 ----------GRDLDWSELLAKAEPV-DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVW 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 365 WCTADIGWITGHSYVTYGPLANGATSVLFEGIPT-YPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKF--GDEPVNKYSRA 441
Cdd:cd05967 276 WAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 442 SLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAILNESGEEL 519
Cdd:cd05967 356 SLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 520 EGEAEGYLVFKQPW-PGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESA 598
Cdd:cd05967 433 GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 599 LVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPA-LAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRV 677
Cdd:cd05967 513 VLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRT 592
|
650 660
....*....|....*....|....*.
gi 2119488996 678 LRKIAQNDhDLGDTSTVADQSVISHL 703
Cdd:cd05967 593 LRKIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
42-700 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 549.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 42 MARYRELHGRSVLEPREFWGDIAKEFYWKTPCSGpFLQYNfdvtkGKIFIEWMKGATTNICYNLLDRNVNEKklGDRVAF 121
Cdd:PRK10524 1 MMSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQ-VLDYS-----NPPFARWFVGGRTNLCHNAVDRHLAKR--PEQLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 122 YWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERI 201
Cdd:PRK10524 73 IAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 202 LDSSCTLLITADAFYRGEKLVNLKELVDDALHKCREKgfPVKRCIVVKHLgraelgtgdspshspplkrpcqdlqDKMka 281
Cdd:PRK10524 153 DDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGL-------------------------APM-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 282 kpmskrpqiPWNQGVDLWW---HEILGDAEEECEpeWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDF 358
Cdd:PRK10524 204 ---------ARVAGRDVDYatlRAQHLGARVPVE--WLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 359 HEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKY 438
Cdd:PRK10524 273 KAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKH 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 439 SRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAILNESG 516
Cdd:PRK10524 353 DLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVT 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 517 EELEGEAEG-YLVFKQPW-PGIMRTVYGNHERFEATYFRKF-PGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTA 593
Cdd:PRK10524 430 GEPCGPNEKgVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTR 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 594 EVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVF-----TPALAEELKKQVREKISPIATPDYIQNAPGLPKT 668
Cdd:PRK10524 510 EIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadreaRLALEKEIMALVDSQLGAVARPARVWFVSALPKT 589
|
650 660 670
....*....|....*....|....*....|..
gi 2119488996 669 RSGKIMRRVLRKIAQnDHDLGDTSTVADQSVI 700
Cdd:PRK10524 590 RSGKLLRRAIQAIAE-GRDPGDLTTIEDPAAL 620
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
45-696 |
2.80e-174 |
|
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: 512.04 E-value: 2.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 45 YRELHGRSVLEPREFWGDIAKEF-YWKTPcsgPFLQyNFDVTKGKIFIEWMKGATTNICYNLLDRNVNEKKlgDRVAFYW 123
Cdd:cd05968 9 LEAFLERSAEDNAWFWGEFVKDVgIEWYE---PPYQ-TLDLSGGKPWAAWFVGGRMNIVEQLLDKWLADTR--TRPALRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 124 EGnEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILD 203
Cdd:cd05968 83 EG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 204 SSCTLLITADAFYRGEKLVNLKELVDDALHKCrekgFPVKRCIVVKHLGRAelgtgdspshspplkrpcqdlqdkmkakp 283
Cdd:cd05968 162 AEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGND----------------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 284 mskrpqIPWNQGVDLWWHEILgdAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDD- 362
Cdd:cd05968 209 ------FTPAKGRDLSYDEEK--ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDl 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 363 VFWCTaDIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRAS 442
Cdd:cd05968 281 LTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSS 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 443 LRVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGE 522
Cdd:cd05968 359 LRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 523 AEGyLVFKQPWPGIMRTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 602
Cdd:cd05968 438 VGE-LVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAH 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 603 RAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKiA 682
Cdd:cd05968 517 PAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-A 595
|
650
....*....|....
gi 2119488996 683 QNDHDLGDTSTVAD 696
Cdd:cd05968 596 YLGKELGDLSSLEN 609
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
91-696 |
3.24e-172 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 505.20 E-value: 3.24e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 91 IEWMKGATTNICYNLLDRNVNEKkLGDRVAFYWEGNEPGEatQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILE 170
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 171 LVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELvddalhkcrekgfpvKRCIVVKH 250
Cdd:PRK04319 111 LYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------KHVLLVGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 251 LGRAELGTgdspshspplkrpcQDLQDKMKAkpmskrpqipwnqgvdlwwheilgdAEEECEPEWCDAEDPLFILYTSGS 330
Cdd:PRK04319 176 DVEEGPGT--------------LDFNALMEQ-------------------------ASDEFDIEWTDREDGAILHYTSGS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 331 TGKPKGVVHTTGGYMLYTATSfKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDVSRLWNIVD 410
Cdd:PRK04319 217 TGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 411 KYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLP 490
Cdd:PRK04319 293 DYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 491 gATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEAtYFRkfPGYYVTGDGCRRDED 570
Cdd:PRK04319 370 -AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDED 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 571 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKI 650
Cdd:PRK04319 446 GYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGL 525
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2119488996 651 SPIATPDYIQNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDTSTVAD 696
Cdd:PRK04319 526 GAHAAPREIEFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
135-682 |
1.76e-133 |
|
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: 401.11 E-value: 1.76e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAda 214
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 fyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcQDLQDKMkakpmskrpqipwnq 294
Cdd:cd05969 80 ----------------------------------------------------------EELYERT--------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWIT 374
Cdd:cd05969 87 ----------------------DPEDPTLLHYTSGTTGTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 375 GHSYVTYGPLANGATSVLFEGiptYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPIN 454
Cdd:cd05969 144 GTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 455 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 534
Cdd:cd05969 221 PEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 GIMRTVYGNHERFEaTYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHP 614
Cdd:cd05969 297 SMFRGIWNDEERYK-NSFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119488996 615 HPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:cd05969 374 DPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
106-586 |
2.43e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 340.44 E-value: 2.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 106 LDRNVneKKLGDRVAFywegnEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALH 185
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 186 SIVFAGFSADSLCERILDSSCTLLITADAFyrgeklvnlkelVDDALHKCREKGFPVKRCIVVKHLGRAELgtgdspshs 265
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDAL------------KLEELLEALGKLEVVKLVLVLDRDPVLKE--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 266 pplkrpcqdlqdkmkakpmskrpqipwnqgvDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTgGYM 345
Cdd:pfam00501 133 -------------------------------EPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 346 LYTATSFKYV----FDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVSRLWNIVDKYKVTKFYTAP 421
Cdd:pfam00501 181 VANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 422 TAIRLLMKFGDEPVNKYSraSLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSA 500
Cdd:pfam00501 260 TLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 501 TFPFFGVAPAILNESGEELEGEAEG-YLVFKQpwPGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRI 579
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRK 410
|
....*..
gi 2119488996 580 DDMLNVS 586
Cdd:pfam00501 411 KDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
135-680 |
3.03e-107 |
|
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: 332.76 E-value: 3.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSsctllitada 214
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 fyrgeklvnlkelvddalhkcrekgfpVKRCIVvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqipwnq 294
Cdd:cd05972 72 ---------------------------GAKAIV----------------------------------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdlwwheilgdaeeecepewCDAEDPLFILYTSGSTGKPKGVVHTTGgYMLYTATSFKYVFDFHEDDVFWCTADIGWIT 374
Cdd:cd05972 78 ---------------------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 375 GHSYVTYGPLANGATSVLFEGIPTypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvnKYSRASLRVLGTVGEPIN 454
Cdd:cd05972 136 GAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 455 PEAWLWYHRVVGAqrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 534
Cdd:cd05972 211 PEVIEWWRAATGL---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 GIMRTVYGNHERFEATyFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHP 614
Cdd:cd05972 286 GLFLGYVGDPEKTEAS-IRG--DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP 362
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119488996 615 HPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05972 363 DPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
105-686 |
2.56e-88 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 284.40 E-value: 2.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 105 LLDRNVneKKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAL 184
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 185 HSIVFAGFSADSLcERIL-DSSCTLLITAdafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdsps 263
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVTA--------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 264 hspplkrpcqdlqdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcdaedplFILYTSGSTGKPKGVVHTTGG 343
Cdd:COG0318 104 -----------------------------------------------------------LILYTSGTTGRPKGVMLTHRN 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 344 yMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVSRLWNIVDKYKVTKFYTAPTA 423
Cdd:COG0318 125 -LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTM 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 424 IRLLMKfgDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFP 503
Cdd:COG0318 200 LARLLR--HPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 504 FFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFEATyFRkfPGYYVTGDGCRRDEDGYYWITGRIDDML 583
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDPEATAEA-FR--DGWLRTGDLGRLDEDGYLYIVGRKKDMI 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 584 NVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAP 663
Cdd:COG0318 350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD---AEELRAFLRERLARYKVPRRVEFVD 426
|
570 580
....*....|....*....|...
gi 2119488996 664 GLPKTRSGKIMRRVLRKIAQNDH 686
Cdd:COG0318 427 ELPRTASGKIDRRALRERYAAGA 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
320-674 |
6.51e-88 |
|
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: 279.17 E-value: 6.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 399
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN-LLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 400 PDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQT 479
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 480 ETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNHErfEATYFRKFPGYY 559
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWNNP--EATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 560 VTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHvftPALA 639
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---DLDA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 2119488996 640 EELKKQVREKISPIATPDYIQNAPGLPKTRSGKIM 674
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
38-681 |
3.23e-87 |
|
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: 286.86 E-value: 3.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 38 HVPSMARYRELHGRSVLEPREFWGDIAKefYWKTPCSGPflqYNFDVTKGKIF--IEWMKGATTNICYNLLDRNVNEkkl 115
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 gDRVAFYweGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:cd05943 84 -DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SLCERILDSSCTLLITADAFYRGEKLVNLKElvddalhKCRE--KGFPVKRCIVVKHLGRAElGTGDSPShspplkrpcq 273
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDVRE-------KVAElvKGLPSLLAVVVVPYTVAA-GQPDLSK---------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 274 dlqdkmkakpmskrpqipwnQGVDLWWHEILGDAEE-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSF 352
Cdd:cd05943 223 --------------------IAKALTLEDFLATGAAgELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KYVFDFHEDDVFWCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGD 432
Cdd:cd05943 283 ILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 433 EPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSATFPFF 505
Cdd:cd05943 361 KPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 506 GVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDM 582
Cdd:cd05943 432 GMAVEAFDEEGKPVWGEKGE-LVCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGT 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 583 LNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNA 662
Cdd:cd05943 510 LNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAV 589
|
650
....*....|....*....
gi 2119488996 663 PGLPKTRSGKIMRRVLRKI 681
Cdd:cd05943 590 PDIPRTLSGKKVEVAVKKI 608
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
134-680 |
2.70e-79 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 260.14 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITaD 213
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AfyrgeklvnlkelvdDALHKCrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqipwn 293
Cdd:cd05973 80 A---------------ANRHKL---------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTT------GGYMlytatsfKYVFDFHEDDVFWCT 367
Cdd:cd05973 87 ------------------------DSDPFVMMFTSGTTGLPKGVPVPLralaafGAYL-------RDAVDLRPEDSFWNA 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 368 ADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVsrlWNIVDKYKVTKFYTAPTAIRLLMKFGdEPVNKYSRASLRVLG 447
Cdd:cd05973 136 ADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVS 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 448 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegyl 527
Cdd:cd05973 212 SAGEPLTPEVIRWFDAALGV---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG----------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 528 vfKQPWPGIMRTVYGNHERFEATYFRKFP---------GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESA 598
Cdd:cd05973 278 --DELGPGEPGRLAIDIANSPLMWFRGYQlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 599 LVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd05973 356 LIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
..
gi 2119488996 679 RK 680
Cdd:cd05973 436 RR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
27-678 |
5.74e-79 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 265.51 E-value: 5.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 27 WSPPPELSRTAHVPSMAR------------YRELHGRSVLEPREFWGDIAkEFY---WKTPCSgpflqynfDVTKGKIFI 91
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYT--------VVLAGRRMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 92 --EWMKGATTNICYNLLdRNvnekKLGDRVAFYWEGnEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMIL 169
Cdd:PRK03584 77 gaRWFPGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 170 ELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYRGEKLVN----LKELVDdalhkcrekGFP-VKR 244
Cdd:PRK03584 151 ETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRA---------ALPsLEH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 245 CIVVKHLGRAELGTGDSPSHSpplkrpcqdlqdkmkakpmskrpqipwnqgvdlwWHEILGDAE-EECEPEWCDAEDPLF 323
Cdd:PRK03584 222 VVVVPYLGPAAAAAALPGALL----------------------------------WEDFLAPAEaAELEFEPVPFDHPLW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 324 ILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDD-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDV 402
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 403 SRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETG 482
Cdd:PRK03584 345 NVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISG 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 483 G-HMLTPLPGATPMKP---GSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMrTVY----GNHERFEATYFRK 554
Cdd:PRK03584 419 GtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDT 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 555 FPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE----VEsALVEhraIAEAAVVSHPHPVKGECLYCFVTLRE 630
Cdd:PRK03584 496 FPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEiyrqVE-ALPE---VLDSLVIGQEWPDGDVRMPLFVVLAE 571
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2119488996 631 GHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIM----RRVL 678
Cdd:PRK03584 572 GVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
55-680 |
5.28e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 262.76 E-value: 5.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 55 EPREFWGDIAKEF-YWKTpcsgpflQYNFDVTKGKIFIEWMKGATTNICYNLLDRNVNEKKLGDRVAFYWEGNEPGEATQ 133
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAD 213
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFYRGEKLV----NLKELVDDALHKcrekgfpvkrcivvkhlgraelgtgdsPSHSPPLKRpcQDLQDKMKAKPMSKRPQ 289
Cdd:PTZ00237 173 YGILNDEIItftpNLKEAIELSTFK---------------------------PSNVITLFR--NDITSESDLKKIETIPT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 IPwnQGVDlWWHEILGDAEEECEP--EWCDAED--PLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVFW 365
Cdd:PTZ00237 224 IP--NTLS-WYDEIKKIKENNQSPfyEYVPVESshPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 366 CTADIGWITGHSYVtYGPLANGATSVLFEGIPTYPDVSR--LWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVN---KYSR 440
Cdd:PTZ00237 301 SHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIirsKYDL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 441 ASLRVLGTVGEPINPEAWLWYHRVVGAqRCPIVdtFWQTETGghMLTPLPGATPMKPGSAT-FPFFGVAPAILNESGEEL 519
Cdd:PTZ00237 380 SNLKEIWCGGEVIEESIPEYIENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 520 EGEAEGYLVFKQPWP-GIMRTVYGNHERFEATyFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESA 598
Cdd:PTZ00237 455 NVNEIGEVAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 599 LVEHRAIAEAAVVSHPHPVKGECLYCFVTLREG----HVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIM 674
Cdd:PTZ00237 534 ILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDqsnqSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIP 613
|
....*.
gi 2119488996 675 RRVLRK 680
Cdd:PTZ00237 614 RQIISK 619
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
103-679 |
4.82e-66 |
|
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: 226.87 E-value: 4.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 103 YN---LLDRNVNEKkLGDRVAFYwegnepGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACA 179
Cdd:cd05959 3 YNaatLVDLNLNEG-RGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 180 RLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYrgeklvnlkELVDDALhkcrEKGFPVKRCIVVKHLGRAELGTg 259
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA---------PVLAAAL----TKSEHTLVVLIVSGGAGPEAGA- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 260 dspshspplkrpcqdlqdkmkakpmskrpqipwnqgvdLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVH 339
Cdd:cd05959 142 --------------------------------------LLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVH 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 340 TTGGyMLYTATSF-KYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvsRLWNIVDKYKVTKFY 418
Cdd:cd05959 184 LHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 419 TAPTAIRLLMKfgDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAtpMKPG 498
Cdd:cd05959 260 GVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 499 SATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtvYGNheRFEATYfRKFPGYYV-TGDGCRRDEDGYYWITG 577
Cdd:cd05959 333 TTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM---YWN--NRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 578 RIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPD 657
Cdd:cd05959 407 RADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPR 486
|
570 580
....*....|....*....|..
gi 2119488996 658 YIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05959 487 WIVFVDELPKTATGKIQRFKLR 508
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
36-683 |
2.06e-65 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 228.61 E-value: 2.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 36 TAHVPSMARYRELHGRSVLEPREFWGDIAKEFywKTPCSGPFLQYnFDVTKGkIFIEWMKGATTNICYNLLdrnvnEKKL 115
Cdd:TIGR01217 28 EHHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWegNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:TIGR01217 99 TEPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SLCERILDSSCTLLITADAFYRGEKlvnlKELVDDALHKCReKGFP-VKRCIVVKHLGRAElgtgdspshspplkrpcqd 274
Cdd:TIGR01217 177 GVLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYLGPRE------------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 275 lqdkmkakpmSKRPQIPwnqGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKY 354
Cdd:TIGR01217 233 ----------TEAPKID---GALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 355 VFDFHEDDVFWCTADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEP 434
Cdd:TIGR01217 300 HCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 435 VNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGATPMKP---GSATFPFFGVAPA 510
Cdd:TIGR01217 378 ARTHDLSALQCVASTGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 511 ILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSG 587
Cdd:TIGR01217 452 SWDPEGKPVTGEVGE-LVCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 588 HLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPK 667
Cdd:TIGR01217 530 VRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPH 609
|
650
....*....|....*.
gi 2119488996 668 TRSGKIMRRVLRKIAQ 683
Cdd:TIGR01217 610 TLTGKRVEVAVKRVLQ 625
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
129-679 |
2.95e-64 |
|
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: 220.00 E-value: 2.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTL 208
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqDLQDkmkakpmskrp 288
Cdd:cd05971 82 LVT--------------------------------------------------------------DGSD----------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwnqgvdlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVVHT-------TGGYMLYtatsfkyvFDF--H 359
Cdd:cd05971 89 -------------------------------DPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpR 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 360 EDDVFWCTADIGWItghsyvtyGPLANGATSVLFEGIP------TYPDVSRLWNIVDKYKVTKFYTAPTAIRLlMKFGDE 433
Cdd:cd05971 130 DGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGE 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 434 PVNKYSRaSLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 513
Cdd:cd05971 201 QLKHAQV-KLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVD 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 514 ESGEELEGEAEGYLVFKQPWPGIMRTVYGNHErfeATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTA 593
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELPDPVAFLGYWNNPS---ATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 594 EVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKI 673
Cdd:cd05971 353 EIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKI 432
|
....*.
gi 2119488996 674 MRRVLR 679
Cdd:cd05971 433 RRRELR 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
100-680 |
9.37e-60 |
|
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: 210.40 E-value: 9.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 100 NICYNLLDRNVNEKKLGDRV---AFYWEgNEPGEATQITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAM 175
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 176 LACARLGAlhsivfagfsadslcerILDSSCTLLITADAFYRgeklvnlkelvddaLHKCREKgfpvkrCIVvkhlgrae 255
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIV-------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 256 lgTGDS-PSHSPPLKRPCQDLQDKMKAKPMSkrpqipWNQGVDLwwHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKP 334
Cdd:cd05928 120 --TSDElAPEVDSVASECPSLKTKLLVSEKS------RDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 335 KGVVHTTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDVSRLWNIVDKYKV 414
Cdd:cd05928 190 KMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 415 TKFYTAPTAIRLLMKfgdEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPLPGATP 494
Cdd:cd05928 268 TTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 495 MKPGS--ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHERFEATYFRKFpgyYVTGDGCRRDEDG 571
Cdd:cd05928 340 IKPGSmgKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 572 YYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVtlreghVFTPA--------LAEELK 643
Cdd:cd05928 417 YFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFV------VLAPQflshdpeqLTKELQ 490
|
570 580 590
....*....|....*....|....*....|....*..
gi 2119488996 644 KQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05928 491 QHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
100-685 |
2.25e-59 |
|
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: 209.27 E-value: 2.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 100 NICYNLLDRNVNEKKlgDRVAFYWeGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACA 179
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 180 RLGALHSIVFAGFSADSLCERILDSSCTLLITADafyrgEKlvNLKELVDDALHKCrekGFPVKRCIVvkhlgraelgtg 259
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA-----ED--NIPEEIEKAAPEC---PSKPKLVWV------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 260 dspsHSPPLKRPCQDLQDKMKAKPMSKRPQipwnqgvdlwwheilgDAEEECepewcdAEDPLFILYTSGSTGKPKGVVH 339
Cdd:cd05970 152 ----GDPVPEGWIDFRKLIKNASPDFERPT----------------ANSYPC------GEDILLVYFSSGTTGMPKMVEH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 340 TTGgYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvsRLWNIVDKYKVTKFYT 419
Cdd:cd05970 206 DFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTTFCA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 420 APTAIRLLMKfgdEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPmKPGS 499
Cdd:cd05970 283 PPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 500 ATFPFFGVAPAILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHERFEATYFrkfPGYYVTGDGCRRDEDGYYWI 575
Cdd:cd05970 355 MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWH---DGYYHTGDAAWMDEDGYLWF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 576 TGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIAT 655
Cdd:cd05970 431 VGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKY 510
|
570 580 590
....*....|....*....|....*....|
gi 2119488996 656 PDYIQNAPGLPKTRSGKImRRVlrKIAQND 685
Cdd:cd05970 511 PRIVEFVDELPKTISGKI-RRV--EIRERD 537
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
103-679 |
6.00e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 207.73 E-value: 6.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 103 YNLLDRNVneKKLGDRVAFYWEGNEpgeatqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLG 182
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDGRR------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 183 A-LHSI-VFagFSADSLcERIL-DSSCTLLITADAFyrgEKLV-NLKELVDDalhkcrekgfpVKRCIVVkhlgraelGT 258
Cdd:PRK06187 81 AvLHPInIR--LKPEEI-AYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------VRTVIVE--------GD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 259 GDSPSHSPPLKRpcqdlqdkmkakpmskrpqipwnqgvdlwWHEILGDAEEEcePEWCDAE--DPLFILYTSGSTGKPKG 336
Cdd:PRK06187 136 GPAAPLAPEVGE-----------------------------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 337 VVHTTGGYMLYTATSfKYVFDFHEDDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegIPTYPDVSRL 405
Cdd:PRK06187 185 VVLSHRNLFLHSLAV-CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV----IPRRFDPENL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 406 WNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGtvGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGG-- 483
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGMTETSPvv 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 484 HMLTPLPGATPM--KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFEATyFRKfpGYY 559
Cdd:PRK06187 323 SVLPPEDQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAET-IDG--GWL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 560 VTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalA 639
Cdd:PRK06187 398 HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLD---A 474
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2119488996 640 EELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK06187 475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
116-675 |
4.26e-58 |
|
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: 203.23 E-value: 4.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWEGNEpgeatqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SLCERILDSSCTLLItadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdl 275
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 276 qdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYV 355
Cdd:cd17631 98 -------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAA 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 FDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptyPDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgDEPV 435
Cdd:cd17631 134 LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALL---QHPR 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 436 -NKYSRASLRVLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNE 514
Cdd:cd17631 207 fATTDLSSLRAVIYGGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDP 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 515 SGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEATyFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:cd17631 283 DGREVPPGEVGEIVVRGP--HVMAGYWNRPEATAAA-FRD--GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAE 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIM 674
Cdd:cd17631 358 VEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELD---EDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
|
.
gi 2119488996 675 R 675
Cdd:cd17631 435 K 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
103-679 |
2.02e-56 |
|
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: 199.33 E-value: 2.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 103 YNLLDRNVneKKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLG 182
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 183 AlhsiVFAGFS----ADSLCERILDSSCTLLITADAFyrgeklvnlkelvddalhkcrekgfpvkrcivvKHLGRAelgt 258
Cdd:cd05936 74 A----VVVPLNplytPRELEHILNDSGAKALIVAVSF---------------------------------TDLLAA---- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 259 gdspshspplkrpcqdlqdkmkAKPMSKRPQIpwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVV 338
Cdd:cd05936 113 ----------------------GAPLGERVAL--------------------------TPEDVAVLQYTSGTTGVPKGAM 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 339 HTTGGyMLYTATSFK--YVFDFHEDDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPDVSRLWNIV 409
Cdd:cd05936 145 LTHRN-LVANALQIKawLEDLLEGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 410 DKYKVTKFYTAPTAIRLLMKFGDepVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETG--GHmLT 487
Cdd:cd05936 213 RKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VN 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 488 PLPGatPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFEAT--YFRKfpGYYVTGDGC 565
Cdd:cd05936 287 PLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMK---GYWNRPEETaeAFVD--GWLRTGDIG 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 566 RRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQ 645
Cdd:cd05936 358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAF 434
|
570 580 590
....*....|....*....|....*....|....
gi 2119488996 646 VREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05936 435 CREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
128-680 |
1.22e-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: 197.92 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 128 PGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSSCT 207
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 208 LLITADAFYRGEKLVNLKELVDDALhkcrEKGFPVKRCIVVkhlGRA-ELGTGDSpshspplkrpcqdlqdkmkAKPMSK 286
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAIL----ELALDVGVLIRA---PSAeSLSNLLA-------------------DKKNAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 287 RPQIPwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGgyMLytATSFKYVFDFHE---DDV 363
Cdd:cd05926 142 SEGVP-------------------------LPDDLALILHTSGTTGRPKGVPLTHR--NL--AASATNITNTYKltpDDR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 364 FWCTADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVSRLWNIVDKYKVTkFYTA-PTAIRLLMKFGDE-PVNKYsrA 441
Cdd:cd05926 193 TLVVMPLFHVHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNRPEPnPESPP--P 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 442 SLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHM-LTPLPgATPMKPGSATFPFfGVAPAILNESGEELE 520
Cdd:cd05926 266 KLRFIRSCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 521 GEAEGYLVFKQPwpGIMRTVYGNHERfEATYFRKFpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALV 600
Cdd:cd05926 341 PGVVGEICLRGP--NVTRGYLNNPEA-NAEAAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 601 EHRAIAEAAVVSHPHPVKGECLYCFVTLREGHvftPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05926 417 SHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
100-680 |
1.34e-52 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 190.05 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 100 NICYNLLDRNVNEKKlGDRVAFYwegnepGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACA 179
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 180 RLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYrgeklvnlkELVDDALHKcrekgFPVKRCIVVkhLGRAELGTG 259
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGK-----SPHLEHRVV--VGRPEAGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 260 DspshspplkrpcqdlqdkmkakpmskrpqipwnqgvdlwWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVH 339
Cdd:TIGR02262 141 Q---------------------------------------LAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 340 TTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVSRLWNivdKYKVTKFYT 419
Cdd:TIGR02262 182 THSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTPDAVFDRLR---RHQPTIFYG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 420 APTAIRLLMkfGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGAtpMKPGS 499
Cdd:TIGR02262 259 VPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 500 ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFEATyfrkFPGYYV-TGDGCRRDEDGYYWITGR 578
Cdd:TIGR02262 332 SGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDT----FQGEWTrSGDKYVRNDDGSYTYAGR 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 579 IDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHP---VKGEclyCFVTLREGHvftPALAEELKKQVREKISPIAT 655
Cdd:TIGR02262 406 TDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQ---TALETELKEHVKDRLAPYKY 479
|
570 580
....*....|....*....|....*
gi 2119488996 656 PDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:TIGR02262 480 PRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
134-679 |
7.72e-52 |
|
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: 186.13 E-value: 7.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITad 213
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 afyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqipwn 293
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVFWCTADI--G 371
Cdd:cd05919 89 -----------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffG 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 WITGHSyvTYGPLANGATSVLFegiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSraSLRVLGTVGE 451
Cdd:cd05919 146 YGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALR--SLRLCVSAGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 452 PInPEAwLWYhRVVGAQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQ 531
Cdd:cd05919 219 AL-PRG-LGE-RWMEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 532 PwpGIMRTVYGNHERFEATyFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVV 611
Cdd:cd05919 294 P--SAAVGYWNNPEKSRAT-FNG--GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVV 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119488996 612 SHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05919 369 AVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-679 |
8.32e-51 |
|
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: 182.88 E-value: 8.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 131 ATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLI 210
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 211 Tadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqi 290
Cdd:cd05934 81 V------------------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 291 pwnqgvdlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSFKYVFDFHEDDVFWCTADI 370
Cdd:cd05934 82 -----------------------------DPASILYTSGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPL 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 GWITGHSYVTYGPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgdEPVNKYSRAS-LRVLGtv 449
Cdd:cd05934 132 FHINAQAVSVLAALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLA---QPPSPDDRAHrLRAAY-- 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 450 GEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLVF 529
Cdd:cd05934 203 GAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 530 K-QPWPGIMRTVYGNHErfeATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEA 608
Cdd:cd05934 278 RgLRGWGFFKGYYNMPE---ATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREA 354
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 609 AVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05934 355 AVVAVPDEVGEDEVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
303-679 |
8.86e-51 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 183.06 E-value: 8.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 303 ILGDAEEE---CEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYV 379
Cdd:cd05958 78 ILDKARITvalCAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 380 TYGPLANGATSVLFEGipTYPDvsRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSraSLRVLGTVGEPINPEAWL 459
Cdd:cd05958 158 LLFPFGVGASGVLLEE--ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLS--SLRKCVSAGEALPAALHR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 460 WYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrT 539
Cdd:cd05958 232 AWKEATGI---PIIDGIGSTEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------T 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 540 VY-GNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVK 618
Cdd:cd05958 301 GCrYLADKRQRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESR 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 619 GECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05958 379 GVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
117-680 |
1.44e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 181.67 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADAFYrgeklvnlkELVDDALHKCREKGFpvkrcivvkhLGRAELGTGDSPShspplkrPCQDLQ 276
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALA---------PTAEAALALLPVDTL----------ILSLVLGGREAPG-------GWLDFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 DkmkakpmskrpqipwnqgvdlwWHEILGDAEEECEPewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMlytatsFKYV- 355
Cdd:PRK08316 154 D----------------------WAEAGSVAEPDVEL---ADDDLAQILYTSGTESLPKGAMLTHRALI------AEYVs 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 ----FDFHEDDVFWCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVSRLWNIVDKYKVTKFYTAPTA-IRL 426
Cdd:PRK08316 203 civaGDMSADDIPLHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 427 LmkfgDEPV-NKYSRASLRVlGTVGEPINPEAWLwyHRVvgAQRCPIVdTFW----QTETGghmltPL-----PGATPMK 496
Cdd:PRK08316 275 L----RHPDfDTRDLSSLRK-GYYGASIMPVEVL--KEL--RERLPGL-RFYncygQTEIA-----PLatvlgPEEHLRR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 497 PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEATyFRKfpGYYVTGDGCRRDEDGYYWIT 576
Cdd:PRK08316 340 PGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP--QLMLGYWDDPEKTAEA-FRG--GWFHSGDLGVMDEEGYITVV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 577 GRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISPIATP 656
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|....
gi 2119488996 657 DYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK08316 492 KRVIFVDELPRNPSGKILKRELRE 515
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
134-682 |
1.58e-49 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 179.69 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsIVFAGfsadslcerildsscTLLITAD 213
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA---VVIPA---------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 afyrgeklvNLKELVDdalhkcrekgfpvkrcivvkhLGRAELGTGDSPSHspplkrpcqdlqdkmkakpmskrpqipwn 293
Cdd:cd05974 63 ---------DLRDRVD---------------------RGGAVYAAVDENTH----------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGYMLyTATSFKYVFDFHEDDVFWCTADIGWi 373
Cdd:cd05974 84 ------------------------ADDPMLLYFTSGTTSKPKLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGW- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 374 TGHSYVT-YGPLANGATSVLFegipTYP--DVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgdEPVNKYsRASLRVLGTVG 450
Cdd:cd05974 138 AKHAWSCfFAPWNAGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASF-DVKLREVVGAG 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 451 EPINPEAwlwYHRVVGAQRCPIVDTFWQTETgghmlTPLPGATP---MKPGSATFPFFGVAPAILNESGEELEGEAEGyL 527
Cdd:cd05974 210 EPLNPEV---IEQVRRAWGLTIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-L 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 528 VFKQPWP-GIMRTVYGNHERFEATYFrkfPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIA 606
Cdd:cd05974 281 DLGDTRPvGLMKGYAGDPDKTAHAMR---GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVA 357
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119488996 607 EAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 682
Cdd:cd05974 358 EAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-674 |
2.25e-46 |
|
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: 172.01 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 132 TQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLIT 211
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 212 AdafyrgeklvnlKELVDDALHKCREKGfPVKRCIVVkhlgraelgtgdsPSHSPPLKRPCQDLQDKMKAkPMSKRPqip 291
Cdd:cd05911 89 D------------PDGLEKVKEAAKELG-PKDKIIVL-------------DDKPDGVLSIEDLLSPTLGE-EDEDLP--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 wnqgvdlwwhEILGDAeeecepewcdAEDPLFILYTSGSTGKPKGVV--HTTGGYMLYTATSFKYVfDFHEDDVFWCTAD 369
Cdd:cd05911 139 ----------PPLKDG----------KDDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 370 IGWITG-HSYVTYgpLANGATSVLFEGiptyPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgDEPVNKYSRASLRVLGT 448
Cdd:cd05911 198 LYHIYGlFTTLAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 449 VGEPINPEAwlwYHRV-VGAQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEaegyl 527
Cdd:cd05911 270 GGAPLSKEL---QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP----- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 528 vfKQP---W---PGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 601
Cdd:cd05911 340 --NEPgeiCvrgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLE 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 602 HRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISpiatpDY------IQNAPGLPKTRSGKIM 674
Cdd:cd05911 416 HPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLT---EKEVKDYVAKKVA-----SYkqlrggVVFVDEIPKSASGKIL 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
113-680 |
3.12e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 169.31 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAfYWEGNEpgeatQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGF 192
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 SADSLCERILDSSCTLLITADAFyrgeklVNLKELVDDALhkcrekgfPVKRCIVVkhlgraeLGTGDSPSHSPPLKRpc 272
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF------LGVDYSATTRL--------PALEHVVI-------CETEEDDPHTEKMKT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 qdlqdkmkakpmskrpqipwnqgvdlwWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSF 352
Cdd:PRK07656 147 ---------------------------FTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KYVFDFHEDD----------VFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPT 422
Cdd:PRK07656 199 AEYLGLTEGDrylaanpffhVFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 423 AIRLLMKFGDEpvNKYSRASLRVLGTVGEPInPEAWLwyHRVVGAQRCPIVDT-FWQTETGG-HMLTPLPGATPMKPGSA 500
Cdd:PRK07656 265 MYNSLLQHPDR--SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGvTTFNRLDDDRKTVAGTI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 501 TFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEATYfrKFPGYYVTGDGCRRDEDGYYWITGRID 580
Cdd:PRK07656 340 GTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKK 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 581 DMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQ 660
Cdd:PRK07656 416 DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELT---EEELIAYCREHLAKYKVPRSIE 492
|
570 580
....*....|....*....|
gi 2119488996 661 NAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK07656 493 FLDELPKNATGKVLKRALRE 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
117-678 |
1.64e-42 |
|
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: 160.00 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsiVFAGFSADS 196
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERIL----DSSCTLLITadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpc 272
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 qdlqdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTAtSF 352
Cdd:cd05930 91 --------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL-WM 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KYVFDFHEDDVFWCTADIGWItGHSYVTYGPLANGATSVLfegIP--TYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKF 430
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 431 GDEPVNkysrASLRVLGTVGEPINPEAW-LWYHRVVGAQ--------RCPIVDTFWQTETGGHMLTPLPGATPMkPGSAT 501
Cdd:cd05930 202 LELAAL----PSLRLVLVGGEALPPDLVrRWRELLPGARlvnlygptEATVDATYYRVPPDDEEDGRVPIGRPI-PNTRV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 502 FpffgvapaILNESGeelegeaegylvfkQPWP------------GIMRTVYGNHE----RFEATYFrkFPG--YYVTGD 563
Cdd:cd05930 277 Y--------VLDENL--------------RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGD 332
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 564 GCRRDEDG--YYwiTGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEE 641
Cdd:cd05930 333 LVRWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEE 407
|
570 580 590
....*....|....*....|....*....|....*..
gi 2119488996 642 LKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd05930 408 LRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
99-678 |
3.21e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 158.58 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 99 TNICYNLldrNVNEKKLGDRVAFYWEGNEpgeatqITYRELLTQVCRCANAL-RKQGIRKGDRVSIYMPMILELVVAMLA 177
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 178 CARLGALHSIVFAGFSADSLCERILDSSCTLLIT-ADAFYRGEKLVNLKELvddalhkcrekgfpvkRCIVVKHLGRAel 256
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgSELAPKVAPAVGNLRL----------------RHVIVAQYSDY-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 257 gTGDSPSHSPPlkrpcqdlqDKMKAKPmskrPQIPWNQGVDLWWHEIL--GDAEEECEPewcDAEDPLFILYTSGSTGKP 334
Cdd:PRK08314 143 -LPAEPEIAVP---------AWLRAEP----PLQALAPGGVVAWKEALaaGLAPPPHTA---GPDDLAVLPYTSGTTGVP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 335 KGVVHTTGGYMlYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiptypdVSRlWN------I 408
Cdd:PRK08314 206 KGCMHTHRTVM-ANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---------MPR-WDreaaarL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 409 VDKYKVTKFYTAPT-AIRLLMKFGdepVNKYSRASLRVLGTVGEPInPEAWlwyhrvvgAQR------CPIVDTFWQTET 481
Cdd:PRK08314 275 IERYRVTHWTNIPTmVVDFLASPG---LAERDLSSLRYIGGGGAAM-PEAV--------AERlkeltgLDYVEGYGLTET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 482 GGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTVYGNHERFEATyFRKFPG-- 557
Cdd:PRK08314 343 MAQTHSNPPDRP--KLQCLGIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkr 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 558 YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPA 637
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT 496
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2119488996 638 lAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK08314 497 -EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
27-680 |
3.82e-40 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 157.55 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 27 WSPPPELSRTAHVPSM--ARYRELHGRSVLEPREFWGDIAK------EFYWKTPCSGpfLQYNFDVTKGKIFIE------ 92
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLleARGKELLGSKYKDPISSFSEFQRfsvenpEVYWSIVLDE--LSLVFSVPPRCILDTsdesnp 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 93 ---WMKGATTNICYNLLdrNVNEKKLGDRVAFYW--EGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPM 167
Cdd:PLN03052 165 ggqWLPGAVLNVAECCL--TPKPSKTDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPM 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 168 ILELVVAMLAcarlgalhsIVFAG---------FSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDAlhkcrek 238
Cdd:PLN03052 243 NVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 239 gfPVKRCIVVKhlgraelGTGDSPShspplkrpcqdlqdkmkakpMSKRPQipwnqgvDLWWHEILGDAE-----EECEP 313
Cdd:PLN03052 307 --KAPKAIVLP-------ADGKSVR--------------------VKLREG-------DMSWDDFLARANglrrpDEYKA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 314 EWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVfDFHEDDVF-WCTaDIGWITGHsYVTYGPLANGATSVL 392
Cdd:PLN03052 351 VEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLAL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 393 FEGIPTYPDVSRLwniVDKYKVTKFYTAPTAIRLLMKFGdePVNKYSRASLRVLGTVGEPINPEAWLWYhrVVGAQRCPI 472
Cdd:PLN03052 428 YNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MSRAGYKPI 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 473 VDTFWQTETGGHMLTplpgATPMKPGS-ATF--PFFGVAPAILNESGeelegeaegylvfkQPWP--------------- 534
Cdd:PLN03052 501 IEYCGGTELGGGFVT----GSLLQPQAfAAFstPAMGCKLFILDDSG--------------NPYPddapctgelalfplm 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 -GIMRTVY-GNHERfeaTYFRKFPGYYVT-----GDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHR 603
Cdd:PLN03052 563 fGASSTLLnADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 604 AIAEAAVVSHPHPVKG-ECLYCFVTLREGHVFTPALaEELKK----QVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PLN03052 637 SVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVL 715
|
..
gi 2119488996 679 RK 680
Cdd:PLN03052 716 RQ 717
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
103-698 |
4.00e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 156.65 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 103 YNLLDRNVNekKLGDRVA--FYWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLAcar 180
Cdd:PRK07529 28 YELLSRAAA--RHPDAPAlsFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 181 lGALHSIVFA---GFSADSLCErILDSSCT-LLITADAFYRgeklVNLKELVDDALHKCrekgfPVKRCIVVKHLGRAEL 256
Cdd:PRK07529 103 -GEAAGIANPinpLLEPEQIAE-LLRAAGAkVLVTLGPFPG----TDIWQKVAEVLAAL-----PELRTVVEVDLARYLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 257 GTGDS--PSHSPPLKRPCQDLQDKMKAKPmskrpqipwnqgvdlwwheilGDAEEECEPEwcDAEDPLFILYTSGSTGKP 334
Cdd:PRK07529 172 GPKRLavPLIRRKAHARILDFDAELARQP---------------------GDRLFSGRPI--GPDDVAAYFHTGGTTGMP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 335 KGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPD---VSRLWNIVD 410
Cdd:PRK07529 229 KLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGpgvIANFWKIVE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 411 KYKVTKFYTAPTAIRLLMkfgDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTE-TGGHMLTPL 489
Cdd:PRK07529 306 RYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 490 PGatPMKPGSA--TFPFFGVAPAILNESGEELEGEAEG---YLVFKQP--WPGIMRTVYGNHERFEATYFRkfpgyyvTG 562
Cdd:PRK07529 380 DG--ERRIGSVglRLPYQRVRVVILDDAGRYLRDCAVDevgVLCIAGPnvFSGYLEAAHNKGLWLEDGWLN-------TG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 563 DGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPA-LAEE 641
Cdd:PRK07529 451 DLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAeLLAF 530
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 642 LKKQVREkisPIATPDYIQNAPGLPKTRSGKI---------MRRVLRK-IAQNDHDLGDTSTVADQS 698
Cdd:PRK07529 531 ARDHIAE---RAAVPKHVRILDALPKTAVGKIfkpalrrdaIRRVLRAaLRDAGVEAEVVDVVEDGR 594
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
117-678 |
2.58e-38 |
|
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: 148.22 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLAcarlgalhsIVFAGfsads 196
Cdd:cd17643 2 EAVAVVDED------RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLA---------ILKAG----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 lcerildssctllitadAFYRGeklvnlkelVDDAlhkcrekgFPVKRCIVVkhlgraelgTGDSpshspplkrpcqdlq 276
Cdd:cd17643 62 -----------------GAYVP---------IDPA--------YPVERIAFI---------LADS--------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 dkmkakpmskRPQIpwnqgvdlwwheILGDAEeecepewcdaeDPLFILYTSGSTGKPKGVVHTTGGYM-LYTATSfkYV 355
Cdd:cd17643 84 ----------GPSL------------LLTDPD-----------DLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RW 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 FDFHEDDVfwctadigWITGHSYV-------TYGPLANGATSVlfegIPTYpDVSR----LWNIVDKYKVTKFYTAPTAI 424
Cdd:cd17643 129 FGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAF 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 425 RLLMKFGDEPVNKYSRASLRVLGtvGEPINPeAWL--WYHRVvGAQRCPIVDTFWQTETGGHM----LTP--LPGATpMK 496
Cdd:cd17643 196 YQLVEAADRDGRDPLALRYVIFG--GEALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-AS 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 497 PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRKfPG--YYVTGDGCRRDEDGYYW 574
Cdd:cd17643 271 PIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELE 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 575 ITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKIspia 654
Cdd:cd17643 350 YLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELL---- 422
|
570 580
....*....|....*....|....*....
gi 2119488996 655 tPDYIQNA-----PGLPKTRSGKIMRRVL 678
Cdd:cd17643 423 -PDYMVPAryvplDALPLTVNGKLDRAAL 450
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
129-683 |
3.70e-37 |
|
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: 146.44 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHsiVFAGFS-----ADSLCERild 203
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrraeISHFAEQ--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 204 SSCTLLITADAfYRGEKLVNL-KELVDDALHkcrekgfpVKRCIVVkhlgraelgtGDSpshspplkRPCQDLQDkmkak 282
Cdd:COG1021 121 SEAVAYIIPDR-HRGFDYRALaRELQAEVPS--------LRHVLVV----------GDA--------GEFTSLDA----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 283 pmskrpqipwnqgvdlwwheILGDAEEECEPEwCDAEDPLFILYTSGSTGKPKGVVHTTGGYmLYTATSFKYVFDFHEDD 362
Cdd:COG1021 169 --------------------LLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 363 VFWCTADIGwitgHSY-----VTYGPLANGATSVLFEGipTYPDVsrLWNIVDKYKVTkfYTA--PTAIRLLMKFGDEpv 435
Cdd:COG1021 227 VYLAALPAA----HNFplsspGVLGVLYAGGTVVLAPD--PSPDT--AFPLIERERVT--VTAlvPPLALLWLDAAER-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 436 NKYSRASLRVLGTVGEPINPEA----------WLW-----------YHR-------VVGAQRCP--------IVDtfwqt 479
Cdd:COG1021 295 SRYDLSSLRVLQVGGAKLSPELarrvrpalgcTLQqvfgmaeglvnYTRlddpeevILTTQGRPispddevrIVD----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 480 ETGghmlTPLPgatpmkPGSAtfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnherfeatYFRKfP--- 556
Cdd:COG1021 370 EDG----NPVP------PGEV-----GE-------------------LLTRGPY-----TIRG--------YYRA-Pehn 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 -------GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGE--CLycFVT 627
Cdd:COG1021 402 araftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVV 479
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 628 LReGHVFTPAlaeELKKQVREKisPIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 683
Cdd:COG1021 480 PR-GEPLTLA---ELRRFLRER--GLAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
134-678 |
2.44e-36 |
|
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: 143.53 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAD 213
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFYrgEKLVNLKE---LVDDAlhkcrekgfpvkrcivVKHLGRAELGTGDSPSHSPPlkrpcqdlqdkmkakpmskRPQI 290
Cdd:cd05904 113 ELA--EKLASLALpvvLLDSA----------------EFDSLSFSDLLFEADEAEPP-------------------VVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 291 PwnqgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATsfkYVFDF----HEDDVFWC 366
Cdd:cd05904 156 K--------------------------QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQ---FVAGEgsnsDSEDVFLC 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 367 TADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgDEPVNKYSRASLRVL 446
Cdd:cd05904 207 VLPMFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINPEAwlwYHRVvgAQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSATFPFFGVAPAILNESGEELe 520
Cdd:cd05904 281 MSGAAPLGKEL---IEAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 521 geaegyLVFKQP---W---PGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:cd05904 353 ------LPPNQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAE 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISP------IATPDYIqnapglPKT 668
Cdd:cd05904 425 LEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE---DEIMDFVAKQVAPykkvrkVAFVDAI------PKS 495
|
570
....*....|
gi 2119488996 669 RSGKIMRRVL 678
Cdd:cd05904 496 PSGKILRKEL 505
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
165-679 |
4.44e-35 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 139.57 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 165 MPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDAlhkcrekgfPVKR 244
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA---------APAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 245 CIVVKHLGRaelgtgdsPSHsPPLkrpcqdlqdkmkakpmskRPQipwnqgvDLWWHEILGDA-------EEECEPEWCD 317
Cdd:PLN03051 72 AIVLPAAGE--------PVA-VPL------------------REQ-------DLSWCDFLGVAaaqgsvgGNEYSPVYAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 318 AEDPLFILYTSGSTGKPKGV--VHTTGgymLYTATSFKYVFDFHEDDVFWCTADIGWITGhSYVTYGPLANGATSVLFEG 395
Cdd:PLN03051 118 VESVTNILFSSGTTGEPKAIpwTHLSP---LRCASDGWAHMDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 396 IPTYPDVSRLwniVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQRcPIVDT 475
Cdd:PLN03051 194 APLGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 476 FWQTETGGHML--TPLpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHErfeAT 550
Cdd:PLN03051 270 CGGTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADHD---KV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 551 YFRKFPGYYVTGDGCRRDED-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HRAIAEAAVVSHPHPVKG-EC 621
Cdd:PLN03051 344 YYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpEL 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119488996 622 LYCFVT---LREGHVFT--PALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PLN03051 424 LVIFLVlgeEKKGFDQArpEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
117-679 |
8.15e-35 |
|
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: 138.63 E-value: 8.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:cd17651 10 DAPALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADAfYRGEKLVnlkELVDDALhkcrekgfpvkrcivvkhLGRAELGTGDSPSHSPPLkrpcqdlq 276
Cdd:cd17651 84 LAFMLADAGPVLVLTHPA-LAGELAV---ELVAVTL------------------LDQPGAAAGADAEPDPAL-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 dkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTA------- 349
Cdd:cd17651 134 ----------------------------------------DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAwqarass 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 350 -------TSFKYV-FD--FHEddvfwctadigwitghsyvTYGPLANGATSVLfegIPTY--PDVSRLWNIVDKYKVTKF 417
Cdd:cd17651 174 lgpgartLQFAGLgFDvsVQE-------------------IFSTLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 418 YTAPTAIRLLMKFGDePVNKYSrASLRVLGTVGEPINPEAWL--WYHRVVGAQrcpIVDTFWQTET---GGHMLTPLPGA 492
Cdd:cd17651 232 FLPTVALRALAEHGR-PLGVRL-AALRYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 493 TPMKPGSATfPFFGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTVYGN----HERFEATYFRKFP 556
Cdd:cd17651 307 WPAPPPIGR-PIDNTRVYVLDAAL--------------RPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTP 636
Cdd:cd17651 372 RMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2119488996 637 AlaeELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd17651 452 A---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
117-685 |
9.38e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 139.42 E-value: 9.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADAFyRGEKLVNLKELVDDALhkcrekgfPVKRCIVVkhlgraeLGTGDSPSHSPPLKRPCQDLQ 276
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGFDHAAMARRLRPEL--------PALRHVVV-------VGGDGADSFEALLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 DKMKAKPMSKRPqipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMlytATSFKYV- 355
Cdd:PRK13295 183 PDAPAILARLRP----------------------------GPDDVTQLIYTSGTTGEPKGVMHTANTLM---ANIVPYAe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 -FDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVSRLWNIVDKYKVTkFYTAPTAIRLLM----KF 430
Cdd:PRK13295 232 rLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTPFLTDLtravKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 431 GDEPVnkysrASLRVLGTVGEPINP----EAWlwyhRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPMKpGSAT--FPF 504
Cdd:PRK13295 307 SGRPV-----SSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDER-ASTTdgCPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 505 FGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLN 584
Cdd:PRK13295 373 PGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVII 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 585 VSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT-PALAEELKKQvreKISPIATPDYIQNAP 663
Cdd:PRK13295 447 RGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQYIPERLVVRD 523
|
570 580
....*....|....*....|..
gi 2119488996 664 GLPKTRSGKIMRRVLRKIAQND 685
Cdd:PRK13295 524 ALPRTPSGKIQKFRLREMLRGE 545
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-680 |
1.56e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 138.64 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWegnepGEATqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsiVFAGf 192
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 sadslcerildssctllitadafyrgeklVNLKELVDDALHKCREKGfpvkrcivvkhlGRAELGTGDSPSHSPPLKRPC 272
Cdd:PRK07470 87 -----------------------------TNFRQTPDEVAYLAEASG------------ARAMICHADFPEHAAAVRAAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 QDLQDKMKAKpmskrpQIPWNQGVDLWWHEILGDAEEECEpewCDAEDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSf 352
Cdd:PRK07470 126 PDLTHVVAIG------GARAGLDYEALVARHLGARVANAA---VDHDDPCWFFFTSGTTGRPKAAV-LTHGQMAFVITN- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 kyvfdfHEDDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVSRLWNIVDKYKVTKF 417
Cdd:PRK07470 195 ------HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 418 YTAPTAIRLLMKfgDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMlTPLPGA----- 492
Cdd:PRK07470 259 FTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdae 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 493 -TPM-KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQpwPGIMRTVYGNHERfEATYFRKfpGYYVTGDGCRRDED 570
Cdd:PRK07470 333 dGPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIG--PAVFAGYYNNPEA-NAKAFRD--GWFRTGDLGHLDAR 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 571 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKI 650
Cdd:PRK07470 408 GFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD---EAELLAWLDGKV 484
|
570 580 590
....*....|....*....|....*....|
gi 2119488996 651 SPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK07470 485 ARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
326-682 |
7.38e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 133.37 E-value: 7.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 326 YTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 401
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 402 VSRLWNIVDKYKVTKFYTAPTAIRLLMKfgdEPVNKySRASLRVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE- 480
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 481 TGGHMLTPlPGaTPMKPGSA--TFPFFGVAPAILNESGEELEGEAEGYLvfkqpWPGIM--RTVYGNHERFE-ATYFRKF 555
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVglRLPYARVRIKVLDGVGRLLRDCAPDEV-----GEICVagPGVFGGYLYTEgNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 PGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT 635
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2119488996 636 PalaEELKKQVREKISP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:cd05944 312 E---EELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
134-680 |
6.07e-33 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 133.75 E-value: 6.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAD 213
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFYRgeklvnlkeLVDDALHKCrekgfpvkrcivvkHLGRAELGTGDSPSHSPPLKRPCQDLQDKMKAKPmskrPQIPWN 293
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGDPAHASEGHPGEEPASWPKLLALG----DADPPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 QGVDlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVV--HTTggyMLYTATSFKYVFDFHEDDVFWCTADIG 371
Cdd:TIGR03098 159 PVID---------------------SDMAAILYTSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 WITGHSYVTYGpLANGATSVLFEGIpTYPDVSRLwniVDKYKVTKFYTAPTairLLMKFGDEPVNKYSRASLRVLGTVGE 451
Cdd:TIGR03098 215 FDYGFNQLTTA-FYVGATVVLHDYL-LPRDVLKA---LEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 452 PInPEAWLWYHRvvgaQRCPIVDTFWQ---TETGGHMLTPlPGATPMKPGS--ATFPFFGVapAILNESGEELEGEAEGY 526
Cdd:TIGR03098 287 AM-PRATLSRLR----SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEEGE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 527 LVFKQPwpgIMRTVYGNHERFEATYFRKFPGYYV----------TGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVE 596
Cdd:TIGR03098 359 LVHRGA---LVAMGYWNDPEKTAERFRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 597 SALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPAlaeELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRR 676
Cdd:TIGR03098 436 EVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRK 512
|
....
gi 2119488996 677 VLRK 680
Cdd:TIGR03098 513 ALAK 516
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
135-680 |
1.09e-32 |
|
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: 131.35 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALhsivfagfsadslcerildsSCTLLitadA 214
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV--------------------TNPIL----P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 FYRGEKLVNLkelvddaLHKCREKGFpvkrcIVVKHLGRAElgtgdspshspplkrpcqdlqdkmkakpmskrpqipwnq 294
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVF-----VVPERFRQFD--------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdlwwHEILGDaeeecepewcdaeDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWIT 374
Cdd:cd05903 88 ------PAAMPD-------------AVALLLFTSGTTGEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQT 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 375 GHSYVTYGPLANGATSVLfegiptypdvSRLWN------IVDKYKVTKFYTAPTAIRLLMK---FGDEPVnkysrASLRV 445
Cdd:cd05903 148 GFVYGFTLPLLLGAPVVL----------QDIWDpdkalaLMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRT 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 446 LGTVGEPINP----EAWlwyhRVVGAQRCPIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEG 521
Cdd:cd05903 213 FVCGGATVPRslarRAA----ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 522 EAEGYLVFKQPwpgimRTVYGNHERFEATyFRKFP-GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALV 600
Cdd:cd05903 286 GVEGELLSRGP-----SVFLGYLDRPDLT-ADAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 601 EHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT-PALAEELKKQvreKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05903 360 GHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYLDRQ---GVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
.
gi 2119488996 680 K 680
Cdd:cd05903 437 E 437
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
135-679 |
1.31e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 132.24 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADA 214
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 FYRGeklvnlkelvddalhkcrekgfpvkRCIVVKhlgraelgtgdspshspplkrpCQDLQDKMKAKPMSKRPQIPwnq 294
Cdd:PRK09088 104 VAAG-------------------------RTDVED----------------------LAAFIASADALEPADTPSIP--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTAD----I 370
Cdd:PRK09088 134 -----------------------PERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhiI 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 GWITGHSYVtygpLANGATSVLFEGIPTYPDVSRLWNIvdKYKVTKFYTAPtaiRLLMKFGDEPvnKYSRASLRVLGTV- 449
Cdd:PRK09088 190 GLITSVRPV----LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQP--GFDAAALRHLTALf 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 450 --GEPiNPE----AWLwyhrvvgAQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGE 522
Cdd:PRK09088 259 tgGAP-HAAedilGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 523 AEGYLVFKQP--WPGIMRTVYGNHERFEATyfrkfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALV 600
Cdd:PRK09088 331 VPGELLLRGPnlSPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLA 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 601 EHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK09088 405 DHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
133-678 |
1.71e-32 |
|
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: 130.68 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsivfagfsadslcerildssctllita 212
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANA----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 dafyrgeklvnlkelvddalhkcrekgfpvkrcIVVkhlgraelgtgdspshspPLKrpcqdlqdkmkakPMSKRPQIPW 292
Cdd:cd05935 52 ---------------------------------VVV------------------PIN-------------PMLKERELEY 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvdlwwheILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGW 372
Cdd:cd05935 68 ----------ILNDSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 373 ITGHSYVTYGPLANGATSVLFegipTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfGDEPVNKYSRASLRVLGTVGEP 452
Cdd:cd05935 137 VTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 453 InPEAWLwyHRVVGAQRCPIVDTFWQTETgghmLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEG-YLVF 529
Cdd:cd05935 211 M-PPAVA--EKLLKLTGLRFVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVgEIVV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 530 KQPwpGIMRTvYGNHERFEATYFRKFPG--YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAE 607
Cdd:cd05935 284 RGP--QIFKG-YWNRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 608 AAVVSHPHPVKGECLYCFVTLREGHVFTpALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd05935 361 VCVISVPDERVGEEVKAFIVLRPEYRGK-VTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
105-680 |
1.89e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.82 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 105 LLDRNVneKKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGA- 183
Cdd:PRK05605 37 LYDNAV--ARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 184 --LHSIVFagfSADSLCERILDSSCTLLITADafyrgeKLVN-LKELVDDAlhkcrekgfPVKRCIVVkhlgraelgtgD 260
Cdd:PRK05605 109 vvEHNPLY---TAHELEHPFEDHGARVAIVWD------KVAPtVERLRRTT---------PLETIVSV-----------N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 261 SPSHSPPLKR-----PCQDLQDKMKAKPMSKRPQIPWNQGVDlwwHEILGDAEEECEPEwCDAEDPLFILYTSGSTGKPK 335
Cdd:PRK05605 160 MIAAMPLLQRlalrlPIPALRKARAALTGPAPGTVPWETLVD---AAIGGDGSDVSHPR-PTPDDVALILYTSGTTGKPK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 336 GVVHTTGGYMLYTATSFKYVFDFHEDD--------VFwctadigwitgHSY-----VTYGPLAnGATSVLFegiPTyPDV 402
Cdd:PRK05605 236 GAQLTHRNLFANAAQGKAWVPGLGDGPervlaalpMF-----------HAYgltlcLTLAVSI-GGELVLL---PA-PDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 403 SRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVlgtvgepinpeawlwyhRVVGAQRCPiVDTF--WQTE 480
Cdd:PRK05605 300 DLILDAMKKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRN-----------------AFSGAMALP-VSTVelWEKL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 481 TGGHM-----LT---PLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVYGNHER 546
Cdd:PRK05605 360 TGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFKGYWNR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 547 FEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFV 626
Cdd:PRK05605 435 PEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAV 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2119488996 627 TLREGHVFTPalaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK05605 515 VLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
93-683 |
2.08e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 132.86 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 93 WMKGATTNICYNLLDRNVNE------KKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMP 166
Cdd:PRK06178 18 WPAGIPREPEYPHGERPLTEylrawaRERPQRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 167 MILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADAFYrgeklvnlkelvddalhkcrekgfPVkrci 246
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLA------------------------PV---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 247 VVKHLGRAELGTGDSPSHSPPL-KRPCQDLQDKMKAKPMSkrpqipwnqgvDLWWHEILG--DAEEECEPEWCDAEDPLF 323
Cdd:PRK06178 144 VEQVRAETSLRHVIVTSLADVLpAEPTLPLPDSLRAPRLA-----------AAGAIDLLPalRACTAPVPLPPPALDALA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 324 IL-YTSGSTGKPKGVVHTTGgYMLYTATSFKYV-FDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPD 401
Cdd:PRK06178 213 ALnYTGGTTGMPKGCEHTQR-DMVYTAAAAYAVaVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLL----ARWD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 402 VSRLWNIVDKYKVTK-FYTAPTAIRLLmkfgDEP-VNKYSRASLRVLGTVG--EPINPEAWLWYHRVVGaqrCPIVDTFW 477
Cdd:PRK06178 288 AVAFMAAVERYRVTRtVMLVDNAVELM----DHPrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTG---SVLAEAAW 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 478 -QTET------------GGHMLT--------PLPGA----TPMKPGsATFPFfGV-------APAILnesgeelegeaeg 525
Cdd:PRK06178 361 gMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefkiCDFETG-ELLPL-GAegeivvrTPSLL------------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 526 ylvfkqpwpgimrTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAI 605
Cdd:PRK06178 426 -------------KGYWNKPEATAEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 606 AEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 683
Cdd:PRK06178 491 LGSAVVGRPDPDKGQVPVAFVQLKPGADLT---AAALQAWCRENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
135-610 |
1.74e-31 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 127.38 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERIL-DSSCTLLITA 212
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 DAFyrgeklvnlkelvddaLHKCREKGFPVKRCivvkhLGRAELGTGDSPSHSPPLKRPcqdlqdkmkakpmskrpqipw 292
Cdd:TIGR01733 80 SAL----------------ASRLAGLVLPVILL-----DPLELAALDDAPAPPPPDAPS--------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVfwctadigW 372
Cdd:TIGR01733 118 ------------------------GPDDLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------V 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 373 ITGHSYV-------TYGPLANGATSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgdePVNKYSRASLRV 445
Cdd:TIGR01733 165 LQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA-----AALPPALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 446 LGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelege 522
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 523 aegylvfkQPWP------------GIMRTVYG----NHERFEATYFRKFPGY--YVTGDGCRRDEDGYYWITGRIDDMLN 584
Cdd:TIGR01733 312 --------RPVPvgvvgelyiggpGVARGYLNrpelTAERFVPDPFAGGDGArlYRTGDLVRYLPDGNLEFLGRIDDQVK 383
|
490 500
....*....|....*....|....*.
gi 2119488996 585 VSGHLLSTAEVESALVEHRAIAEAAV 610
Cdd:TIGR01733 384 IRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
116-680 |
4.00e-31 |
|
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: 128.13 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWEGnePGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGA-LHSI---VFAg 191
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 192 fsadslcERILdssctlLITADAfyrGEKLVnlkeLVDDALHKCREKGFPvkRCIVVKHLgraELGTGDSPSHSPPLKRp 271
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAP--RLPTVEHV---VVMTDDAAMPEPAGVG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 272 cqdlqdkmkakpmskrpqipwnqgvdlWWH--EILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYT- 348
Cdd:cd12119 141 ---------------------------VLAyeELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAm 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 349 ATSFKYVFDFHEDDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvsrLWNIVDKYKVTKF 417
Cdd:cd12119 194 AALLTDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 418 YTAPTAIRLLMKFGDEpvNKYSRASLRVLgtvgepinpeawlwyhrVVGAQRCP----------IVDTF--W-QTETG-- 482
Cdd:cd12119 259 AGVPTVWQGLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSpl 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 483 GHMLTPLPGATPMKPG-------SATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFEAtYFR 553
Cdd:cd12119 320 GTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKNDEESEA-LTE 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 554 KfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHV 633
Cdd:cd12119 397 D--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT 474
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2119488996 634 FTPalaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd12119 475 VTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
117-678 |
3.10e-30 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 124.28 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LcERILD-SSCTLLITADAfyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdl 275
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 276 qdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYv 355
Cdd:cd05945 98 --------------------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 FDFHEDDVFWCTA---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvsrlwnivdkykV 414
Cdd:cd05945 133 FPLGPGDVFLNQApfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------I 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 415 TKFYTAPTAIRLLMkfGDEPVNKYSRASLRVLGTVGEPI-NPEAWLWYHRvvgAQRCPIVDTFWQTET----GGHMLTPL 489
Cdd:cd05945 190 TVWVSTPSFAAMCL--LSPTFTPESLPSLRHFLFCGEVLpHKTARALQQR---FPDARIYNTYGPTEAtvavTYIEVTPE 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 490 PGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHERFeatyFRKFPGY--YVTGDGC 565
Cdd:cd05945 265 VLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDLV 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 566 RRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvFTPALAEELKKQ 645
Cdd:cd05945 339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG--AEAGLTKAIKAE 416
|
570 580 590
....*....|....*....|....*....|...
gi 2119488996 646 VREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd05945 417 LAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
117-681 |
6.56e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 123.92 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhSIVFAG--FSA 194
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 195 DSLCERILDSSCTLLITADAFyrgeklvnlkelvddalhkcREKGFPVKRCIVvkhlgraelgtgdspshspplkrpcQD 274
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF--------------------EAKLIPGISVKF-------------------------AE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 275 LQDKMKAKPmskrpqipwnqgvdlwwheilgdaeeECEPEWcDAEDPLFILYTSGSTGKPKGVVHTTGGYmLYTATSFKY 354
Cdd:PRK03640 124 LMNGPKEEA--------------------------EIQEEF-DLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSAL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 355 VFDFHEDDVFWCTADIGWITGHSYVTygplangaTSVLFeGIPTYP----DVSRLWNIVDKYKVTKFYTAPTAI-RLLMK 429
Cdd:PRK03640 176 NLGLTEDDCWLAAVPIFHISGLSILM--------RSVIY-GMRVVLvekfDAEKINKLLQTGGVTIISVVSTMLqRLLER 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 430 FGDEPVNKYSRASLrvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPF 504
Cdd:PRK03640 247 LGEGTYPSSFRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 505 FGVAPAILNESGEELEGEAEGYLVfKQPwpGIMRTVYGNHERFEATyFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLN 584
Cdd:PRK03640 314 FPCELKIEKDGVVVPPFEEGEIVV-KGP--NVTKGYLNREDATRET-FQD--GWFKTGDIGYLDEEGFLYVLDRRSDLII 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 585 VSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLreGHVFTpalAEELKKQVREKISPIATPDYIQNAPG 664
Cdd:PRK03640 388 SGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKRFYFVEE 462
|
570
....*....|....*..
gi 2119488996 665 LPKTRSGKIMRRVLRKI 681
Cdd:PRK03640 463 LPRNASGKLLRHELKQL 479
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
319-679 |
7.41e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 123.32 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 319 EDPLFILYTSGSTGKPKGVV--HTTggyMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGi 396
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRlsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTND- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 397 pTYPDVSrLWNIVDKYKVTKFYTAPTAIRLL--MKFGDEPVnkysrASLRVLGTVGEPInPEAWLWYHR--VVGAQrcpI 472
Cdd:cd05922 192 -GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ---V 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 473 VDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHERFEATYF 552
Cdd:cd05922 261 YVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRRKEG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 553 RKFPGYYvTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVkGECLYCFVTLREGH 632
Cdd:cd05922 338 RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2119488996 633 VFTPALaeelkKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05922 416 DPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
117-679 |
7.68e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 124.33 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLG----ALHSIVfagf 192
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrtALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 SADSLCERILDSSCTLLITADAFY--RGEKLVnlkelvddalhkcrekgfpvKRCIVVKHLgraeLGTGDSPShspplkr 270
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFveRALALL--------------------ARVPSLKHV----LTLGPVPD------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 271 pcqdlqdkmkakpmskrpqipwnqGVDLWwheILGDAEEECEPEWCDA-EDPLFILYTSGSTGKPKGVVHTTGGYMLYTA 349
Cdd:PRK06188 146 ------------------------GVDLL---AAAAKFGPAPLVAAALpPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 350 tsfkyvfdfheddvfWCTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVSRLWNIVDKYKVTKFYTAP 421
Cdd:PRK06188 199 ---------------IQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLRAIEEQRITATFLVP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 422 TAIRLLMkfgDEPvnKYSRASLRVLGTV---GEPINP----EAwlwyHRVVGaqrcPI-VDTFWQTETGgHMLTPLP--- 490
Cdd:PRK06188 264 TMIYALL---DHP--DLRTRDLSSLETVyygASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrd 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 491 --GATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFEAT--YFRKfpGYYVTGDGCR 566
Cdd:PRK06188 330 hdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVAR 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 567 RDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQV 646
Cdd:PRK06188 403 EDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG---AAVDAAELQAHV 479
|
570 580 590
....*....|....*....|....*....|...
gi 2119488996 647 REKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK06188 480 KERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
116-678 |
9.04e-30 |
|
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: 123.54 E-value: 9.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SLcERILDSS--CTLLITADAFYRGEKLVNLKELVDDALhkcrekgfpvkrcivvkhlgraelgtgDSPSHSPPLKRPcq 273
Cdd:cd17646 86 RL-AYMLADAgpAVVLTTADLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPP-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 274 dlqdkmkakpmskRPqipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGG---YMLYTAT 350
Cdd:cd17646 136 -------------RP------------------------------DNLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 351 sfKYVFDfHEDDVFWCTA---DI-GWitghsyVTYGPLANGATSVLFEgiP-TYPDVSRLWNIVDKYKVTKFYTAPTAIR 425
Cdd:cd17646 173 --EYPLG-PGDRVLQKTPlsfDVsVW------ELFWPLVAGARLVVAR--PgGHRDPAYLAALIREHGVTTCHFVPSMLR 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 426 LLMKFGDEPvnkySRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET----------GGHMLTPLPGATPM 495
Cdd:cd17646 242 VFLAEPAAG----SCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 496 kPGSATFpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFEATYFRKFPGYYV 560
Cdd:cd17646 315 -PNTRLY----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLgrpaltaERFVPDPFGPGSRMYR 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 561 TGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHvfTPALAE 640
Cdd:cd17646 373 TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA--AGPDTA 450
|
570 580 590
....*....|....*....|....*....|....*...
gi 2119488996 641 ELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17646 451 ALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
113-678 |
1.22e-29 |
|
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: 123.08 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGF 192
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 SADSLCERILDSSCTLLITADAFyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpc 272
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSL--------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 qdlqdkmkakpmskrPQIPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSF 352
Cdd:cd12117 105 ---------------AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KYVfDFHEDDVFWCTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVSRLWNIVDKYKVTK-FYTAPTaIRLLMKFG 431
Cdd:cd12117 169 NYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQLADED 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 432 DEpvnkySRASLRVLGTVGEPINPEawlWYHRVVgaQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGSatfP 503
Cdd:cd12117 245 PE-----CFAGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---P 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 504 FFGVAPAILNesgeelegeaegylVFKQPWP------------GIMRTvYGNH-----ERFEATYFrkFPG--YYVTGDG 564
Cdd:cd12117 312 IANTRVYVLD--------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYRTGDL 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 565 CRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPALAEELKK 644
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG-----ALDAAELRA 449
|
570 580 590
....*....|....*....|....*....|....
gi 2119488996 645 QVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd12117 450 FLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
128-679 |
6.93e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 121.34 E-value: 6.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 128 PGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCT 207
Cdd:PRK13391 19 ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 208 LLITADAFYrgeklvnlkELVDDALHKCrekgfP-VKRCIVVkhlgraeLGTGDSPshspplkrPCQDLQDKMKAKPMSK 286
Cdd:PRK13391 99 ALITSAAKL---------DVARALLKQC-----PgVRHRLVL-------DGDGELE--------GFVGYAEAVAGLPATP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 287 RPQipwnqgvdlwwhEILGDAeeecepewcdaedplfILYTSGSTGKPKGV---------VHTTGGYMLytatsFKYVFD 357
Cdd:PRK13391 150 IAD------------ESLGTD----------------MLYSSGTTGRPKGIkrplpeqppDTPLPLTAF-----LQRLWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 358 FHEDDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKF 430
Cdd:PRK13391 197 FRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 431 GDEPVNKYSRASLRVLGTVGEPINPE------AWlWyhrvvgaqrCPIVDTFWQTETGGhmltplpGATPM-------KP 497
Cdd:PRK13391 265 PEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-------GFTACdseewlaHP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 498 GSATFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTVYGNHER-FEatYFR----------KFPGYYVTGDGC 565
Cdd:PRK13391 328 GTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 566 RRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQ 645
Cdd:PRK13391 391 YVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAF 470
|
570 580 590
....*....|....*....|....*....|....
gi 2119488996 646 VREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK13391 471 CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
129-679 |
1.69e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 120.01 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTL 208
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAFyrgekLVNLKELVDDAlhkcrEKGFPVKRcivvkhlgraeLGTGDSPSHspplkRPCQDLQDKMKAKPMSKRP 288
Cdd:PRK08276 87 LIVSAAL-----ADTAAELAAEL-----PAGVPLLL-----------VVAGPVPGF-----RSYEEALAAQPDTPIADET 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 QipwnqGVDLwwheilgdaeeecepewcdaedplfiLYTSGSTGKPKGV--------VHTTGGYMLytaTSFKYVFDFHE 360
Cdd:PRK08276 141 A-----GADM--------------------------LYSSGTTGRPKGIkrplpgldPDEAPGMML---ALLGFGMYGGP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 361 DDVFWCTADIGwitgHSYVT-YG--PLANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNK 437
Cdd:PRK08276 187 DSVYLSPAPLY----HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 438 YSRASLRVLGTVGEPINPE------AWlWyhrvvGaqrcPIVD-TFWQTETGGHMLtplpgATPM----KPGSATFPFFG 506
Cdd:PRK08276 259 YDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSEdwlaHPGSVGKAVLG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 507 VApAILNESGEELEGEAEGYLVFKQPWPGImrTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLnVS 586
Cdd:PRK08276 324 EV-RILDEDGNELPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-IS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 587 GHL-LSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGL 665
Cdd:PRK08276 398 GGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDEL 477
|
570
....*....|....
gi 2119488996 666 PKTRSGKIMRRVLR 679
Cdd:PRK08276 478 PRTPTGKLYKRRLR 491
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
320-680 |
2.61e-28 |
|
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: 118.55 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 399
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHAN-LAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 400 PDVSRLWNIVDKYKVTKFYTAPTA-IRLL-----MKFGDEPVNKYSRASLRVLGTVGEPINP---EAWlwyhRVVGAQRc 470
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVptlEEW----EAITGHT- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 471 pIVDTFWQTETGGHMLTPLPGatPMKPGSATFPFFGVAPAIL--NESGEELEGEAEGYLV-----FKQPWpgimrtvygn 543
Cdd:cd05941 240 -LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdeETGEPLPRGEVGEIQVrgpsvFKEYW---------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 544 hERFEAT--YFRKfPGYYVTGDGCRRDEDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGE 620
Cdd:cd05941 307 -NKPEATkeEFTD-DGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGE 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 621 CLYCFVTLREGHvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05941 385 RVVAVVVLRAGA--AALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
129-683 |
8.66e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 118.31 E-value: 8.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTL 208
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAFyRGEKLVN-LKELVDDALHkcrekgfPVKRCIVVkhlgraELGTGDSPSHSPPLKRPCQDLQDkMKAKPMSKR 287
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV------DDAADATPAPAPGARVQLFALPD-PAPPAAAGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 288 PQipwnqgvdlwwheilgdaeeecepewcDAEDPLFILY-TSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWC 366
Cdd:PRK06164 176 RA---------------------------ADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 367 TADIGWITGHSYVTyGPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNkysRASLRVL 446
Cdd:PRK06164 228 ALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGERAD---FPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGepINPeAWLWYHRVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSATFPFFGVAPAILNESG 516
Cdd:PRK06164 300 GFAS--FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 517 EELEGEAEgylvfkqpwPGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVE 596
Cdd:PRK06164 377 SGEIEIRA---------PSLMRGYLDNPDATARALTDD--GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 597 SALVEHRAIAEAAVVSHPHPVKGEClYCFVTLREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSG---KI 673
Cdd:PRK06164 446 HALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKI 521
|
570
....*....|
gi 2119488996 674 MRRVLRKIAQ 683
Cdd:PRK06164 522 QKHRLREMAQ 531
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
134-678 |
9.09e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.60 E-value: 9.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAD 213
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFYrgEKLVNLKELVDdalhkcrekgfpVKRCIVVKhlgRAELGTGDSPSHSPPLKRPCQDLQDKMKAKPMskrpqipwn 293
Cdd:PRK06710 130 LVF--PRVTNVQSATK------------IEHVIVTR---IADFLPFPKNLLYPFVQKKQSNLVVKVSESET--------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgVDLW---WHEILGDAEEECEPEwcdaEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHE-DDVFWCTAD 369
Cdd:PRK06710 184 --IHLWnsvEKEVNTGVEVPCDPE----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 370 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgDEPVNK-YSRASLRVLGT 448
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 449 VGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAE 524
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 525 G-YLVFKQPwpGIMRTVYGNHERFEATYFrkfPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHR 603
Cdd:PRK06710 403 IgEIVVKGP--QIMKGYWNKPEETAAVLQ---DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119488996 604 AIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK06710 478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
594-672 |
1.16e-27 |
|
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: 106.47 E-value: 1.16e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 594 EVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
117-679 |
1.69e-27 |
|
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: 119.58 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsivfA------ 190
Cdd:COG1020 491 DAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------Ayvpldp 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 191 GFSADSLcERIL-DSSCTLLITADAFyrgeklvnLKELVDDALhkcrekgfpvkRCIVVkhlgrAELGTGDSPSHSPPLK 269
Cdd:COG1020 559 AYPAERL-AYMLeDAGARLVLTQSAL--------AARLPELGV-----------PVLAL-----DALALAAEPATNPPVP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 270 RpcqdlqdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTA 349
Cdd:COG1020 614 V----------------------------------------------TPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLL 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 350 TSFKYVFDFHEDDVF-WCTA---DIGwitghsyVT--YGPLANGATSVLF--EGIptyPDVSRLWNIVDKYKVTKFYTAP 421
Cdd:COG1020 647 AWMQRRYGLGPGDRVlQFASlsfDAS-------VWeiFGALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTP 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 422 TAIRLLMKFGDEPVnkysrASLRVLGTVGEPINPEAWLWYHRVVGAQR---------CPIVDTFWQTETGGHMLTPLP-G 491
Cdd:COG1020 717 SLLRALLDAAPEAL-----PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiG 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 492 aTPMkPGSATFpffgvapaILNEsgeelegeaegylvFKQPWP-GIM-------------------RTVygnhERFEATY 551
Cdd:COG1020 792 -RPI-ANTRVY--------VLDA--------------HLQPVPvGVPgelyiggaglargylnrpeLTA----ERFVADP 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 552 FrKFPG--YYVTGDGCRRDEDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFV 626
Cdd:COG1020 844 F-GFPGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYV 919
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2119488996 627 TLREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:COG1020 920 VPEAG---AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
128-678 |
2.04e-27 |
|
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: 116.45 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 128 PGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERI-LDSSC 206
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 207 TLLITADAF-YRGEKLVNLKELVDDAlhkcrekgfpvkrcivvkhlgraELGTGDSPSHSPPLKRPcqdlqdkmkakpms 285
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLALSD-----------------------LVGLGEPESAGPLIEDP-------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 286 krpqipwnqgvdlwwheilgdaeeECEPEwcdaeDPLFILYTSGSTGKPKGVV---HTTGGYMLYTATSFKYVFDFHEdd 362
Cdd:cd05923 146 ------------------------PREPE-----QPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHN-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 363 VFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSraS 442
Cdd:cd05923 195 VVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLS--S 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 443 LRVLGTVGEPInPEAWLwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsatfpFFG---VAPaILNESGEE 518
Cdd:cd05923 269 LRHVTFAGATM-PDAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 519 LEGEAEGYLVFKQP----WPGIMRtvygnheRFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:cd05923 340 LANGEEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvftPALAEELKKQVREkiSPIAT---PDYIQNAPGLPKTRSG 671
Cdd:cd05923 413 IERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG----TLSADELDQFCRA--SELADfkrPRRYFFLDELPKNAMN 486
|
....*..
gi 2119488996 672 KIMRRVL 678
Cdd:cd05923 487 KVLRRQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
324-680 |
2.05e-27 |
|
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: 115.52 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 324 ILYTSGSTGKPKGVVHTTGGYmLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVS 403
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 404 RLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNkysrASLR--VLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTF 476
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYP----NNLRciLLG--GGPA-PKPLL--------EQCkekgiPVYQSY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 477 WQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTVYGNHERFEATYFRkfp 556
Cdd:cd05912 221 GMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNRPDATEESFEN--- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftP 636
Cdd:cd05912 293 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER-----P 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2119488996 637 ALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05912 368 ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
117-698 |
3.55e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 116.42 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGNEpgeatqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADAfyrgekLVNLKELVDDALhkcrekgfPVKRCIVV-------KHLGRAELGTGDSPSHSPplk 269
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIV--------PLLSTVVVaggssddSVLGYEDLLAEAGPAHAP--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 270 rpcqdlqdkmkakpmskrpqipwnqgVDLwwheilgdaeeecePEwcdaEDPLFILYTSGSTGKPKGVV--HTTggymlY 347
Cdd:PRK07786 169 --------------------------VDI--------------PN----DSPALIMYTSGTTGRPKGAVltHAN-----L 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 348 TATSFKYVFDFH---EDDVFWCTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVSRLWNIVDKYKVTKFY 418
Cdd:PRK07786 200 TGQAMTCLRTNGadiNSDVGFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIF 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 419 TAPTAIRLLMkfgDEPVNKYSRASLRVLGTVGEPiNPEAWL--WYHRVVGAQrcpIVDTFWQTEtgghmLTPLpgaTPM- 495
Cdd:PRK07786 271 LVPAQWQAVC---AEQQARPRDLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMl 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 496 -------KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRD 568
Cdd:PRK07786 336 lgedairKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP---TLMSGYWNNPEATAEAFAG--GWFHSGDLVRQD 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 569 EDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALA-EELKKQVR 647
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLT 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2119488996 648 EKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKI--AQNDHDLGDTSTVADQS 698
Cdd:PRK07786 488 DRLARYKHPKALEIVDALPRNPAGKVLKTELRERygACVNVERRSASAGFTER 540
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
132-678 |
3.59e-27 |
|
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: 115.89 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 132 TQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALhsIVFAGFSadslcerildssctllit 211
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 212 adafyrgeklvnlkelvddalHKCREKGFpvkrciVVKHLGRAELGTGDSpshspplkrpcqdlqdkmkakpmskrpqip 291
Cdd:cd05920 99 ---------------------HRRSELSA------FCAHAEAVAYIVPDR------------------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 wNQGVDlwwHEILGDAEEECEPewcdaeDPLFILYTSGSTGKPKGVVHTTGGYmLYTATSFKYVFDFHEDDVFWCTADIG 371
Cdd:cd05920 122 -HAGFD---HRALARELAESIP------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 witgHSYVTYGP-----LANGATSVLfegiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPvnKYSRASLRVL 446
Cdd:cd05920 191 ----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSAtf 502
Cdd:cd05920 261 QVGGARLSPAL---ARRVPPVLGCTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEE-- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 503 pffgvapailnesgeelegeaeGYLVFKQPWpgimrTVYGnHERFEATYFRKFP--GYYVTGDGCRRDEDGYYWITGRID 580
Cdd:cd05920 336 ----------------------GELLTRGPY-----TIRG-YYRAPEHNARAFTpdGFYRTGDLVRRTPDGYLVVEGRIK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 581 DMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvfTPALAEELKKQVREK-ISPIATPDYI 659
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRERgLAAYKLPDRI 463
|
570
....*....|....*....
gi 2119488996 660 QNAPGLPKTRSGKIMRRVL 678
Cdd:cd05920 464 EFVDSLPLTAVGKIDKKAL 482
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
105-611 |
3.60e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 116.74 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 105 LLDRNVneKKLGDRVAFYWEGNepGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAl 184
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 185 hsiVFAGFSADSL---CERIL-DSSCTLLITADAfyrgeklvnlkELVDDALhKCREKGFPVKRcIVVkhlgraelgtgd 260
Cdd:COG1022 91 ---VTVPIYPTSSaeeVAYILnDSGAKVLFVEDQ-----------EQLDKLL-EVRDELPSLRH-IVV------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 261 spshspplkrpcqdlqdkMKAKPMSKRPQIpwnqgvdLWWHEILGDAEEECEPEW-------CDAEDPLFILYTSGSTGK 333
Cdd:COG1022 143 ------------------LDPRGLRDDPRL-------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 334 PKGVVHTTGGyMLYTATSFKYVFDFHEDDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGIPTYPD------- 401
Cdd:COG1022 198 PKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkp 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 402 -----VSRLWNivdkykvtKFYTA------------------------------------PTAIRLLMKFGDEPVnkYS- 439
Cdd:COG1022 271 tfmlaVPRVWE--------KVYAGiqakaeeagglkrklfrwalavgrryararlagkspSLLLRLKHALADKLV--FSk 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 440 -RASL----RVLGTVGEPINPEAWLWYHrVVGAqrcPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAI--- 511
Cdd:COG1022 341 lREALggrlRFAVSGGAALGPELARFFR-ALGI---PVLEGYGLTETSPVITVNRPGD--NRIGTVGPPLPGVEVKIaed 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 512 --LnesgeelegeaegyLVfKQpwPGIMRTVYGNHerfEAT--------YFRkfpgyyvTGD-GcRRDEDGYYWITGRID 580
Cdd:COG1022 415 geI--------------LV-RG--PNVMKGYYKNP---EATaeafdadgWLH-------TGDiG-ELDEDGFLRITGRKK 466
|
570 580 590
....*....|....*....|....*....|..
gi 2119488996 581 DMLNVS-GHLLSTAEVESALVEHRAIAEAAVV 611
Cdd:COG1022 467 DLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
130-678 |
4.16e-27 |
|
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: 115.47 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERIL-DSSCTL 208
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAfyrgeklvnlkelVDDALHKCrekGFPVKRCIVVKHLGRAELGTGDSPshspplkrpcqdlqdkmkakpmskrp 288
Cdd:cd12116 88 VLTDDA-------------LPDRLPAG---LPVLLLALAAAAAAPAAPRTPVSP-------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDD----VF 364
Cdd:cd12116 126 ------------------------------DDLAYVIYTSGSTGRPKGVVVSHRN-LVNFLHSMRERLGLGPGDrllaVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 365 WCTADIGWITghsyvTYGPLANGATSVLFEGIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPvnkysRASLR 444
Cdd:cd12116 175 TYAFDISLLE-----LLLPLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 445 VL-GtvGEPINPEawlwyhrvVGAQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSATFPffgVAPAILNESGeel 519
Cdd:cd12116 244 ALcG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IGRPLANTQV--- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 520 egeaegYLVFKQ---PWPGIMRTVY--------GNHERfEATYFRKF-------PG--YYVTGDGCRRDEDGYYWITGRI 579
Cdd:cd12116 303 ------YVLDAAlrpVPPGVPGELYiggdgvaqGYLGR-PALTAERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRA 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 580 DDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGEcLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYI 659
Cdd:cd12116 376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAF 451
|
570
....*....|....*....
gi 2119488996 660 QNAPGLPKTRSGKIMRRVL 678
Cdd:cd12116 452 VRLDALPLTANGKLDRKAL 470
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
132-682 |
7.68e-27 |
|
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: 114.74 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 132 TQITYRELLTQVCRCANALRKqGIRKGDRVSIYMPMILELVVAMLACARLGALhsIVFAGFSADslcERILDSSCTL--- 208
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAG---LRELRACIKLagi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 --LITADAFYrgEKLvnlkelvddALHKCREKGFPvKRCIVVKHLgRAELGTGDspshspplkrpcqdlqdKMKAKPMSK 286
Cdd:cd05909 80 ktVLTSKQFI--EKL---------KLHHLFDVEYD-ARIVYLEDL-RAKISKAD-----------------KCKAFLAGK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 287 RPQipwnqgvdLWWHEILGDAEEecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWC 366
Cdd:cd05909 130 FPP--------KWLLRIFGVAPV-------QPDDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDVVFG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 367 TADIGWITGHSYVTYGPLANGAtSVLFEGIPTYPDvsRLWNIVDKYKVTKFYTAPTAIRLLMKFgdepVNKYSRASLRVL 446
Cdd:cd05909 194 ALPFFHSFGLTGCLWLPLLSGI-KVVFHPNPLDYK--KIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINPEAW-LWYHRvvgaQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEG 525
Cdd:cd05909 267 VAGAEKLKDTLRqEFQEK----FGIRILEGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 526 YLVFKQPwPGIMRTVYGNHERFEATYFRkfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAI 605
Cdd:cd05909 342 GLLLVRG-PNVMLGYLNEPELTSFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPE 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 606 -AEAAVVSHPHPVKGECLYCFVTLREGHVftpalaEELKKQVRE-KISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:cd05909 418 dNEVAVVSVPDGRKGEKIVLLTTTTDTDP------SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
130-682 |
9.72e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 115.26 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAFyRGEKLVN-----LKELVDDALHKCREKGFPVKRCIVVkhlgraeLGTGDSPSHspplkrpcqdlqdkmkakpm 284
Cdd:PRK12583 122 ICADAF-KTSDYHAmlqelLPGLAEGQPGALACERLPELRGVVS-------LAPAPPPGF-------------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 285 skrpqipwnqgvdLWWHEILGDAE-------EECEPEwCDAEDPLFILYTSGSTGKPKGVVHT-----TGGYMLYTATSF 352
Cdd:PRK12583 174 -------------LAWHELQARGEtvsrealAERQAS-LDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KyvfdfhEDDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYPDVSrlWNIVDKYKVTKFYTAPTairLLMKFGD 432
Cdd:PRK12583 240 T------EHDRLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 433 EP-VNKYSRASLRVLGTVGEPINPEAwlwYHRVVGAQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSATF----PFF 505
Cdd:PRK12583 308 HPqRGNFDLSSLRTGIMAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 506 GVApaILNESGEELEGEAEGYLVFKqpwpG--IMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDML 583
Cdd:PRK12583 383 EVK--VVDPDGATVPRGEIGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 584 NVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAP 663
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*....
gi 2119488996 664 GLPKTRSGKIMRRVLRKIA 682
Cdd:PRK12583 532 EFPMTVTGKVQKFRMREIS 550
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
117-679 |
1.88e-26 |
|
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: 113.23 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGNEpgeatqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:cd17649 2 DAVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspsHSPplkrpcqdlq 276
Cdd:cd17649 76 LRYMLEDSGAGLLLT----------------------------------------------------HHP---------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 dkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYvF 356
Cdd:cd17649 94 ------------------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-Y 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 357 DFHEDDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVN 436
Cdd:cd17649 131 GLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGD 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 437 KySRASLRVLGTVGEPINPE-AWLWyhrvvGAQRCPIVDTFWQTETgghMLTPL--PGATPMKPGSATFP----FFGVAP 509
Cdd:cd17649 209 G-RPPSLRLYIFGGEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 510 AILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFEATYFRKFPG--------YYVTGDGCRRDEDGYYWITGRIDD 581
Cdd:cd17649 280 YILDADLNPVPVGVTGELYIGGE--GLAR---GYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRVDH 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 582 MLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVkGECLYCFVTLREGHVfTPALAEELKKQVREKISPIATPDYIQN 661
Cdd:cd17649 355 QVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVF 432
|
570
....*....|....*...
gi 2119488996 662 APGLPKTRSGKIMRRVLR 679
Cdd:cd17649 433 LARLPLTPNGKLDRKALP 450
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
114-679 |
2.32e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 113.62 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 114 KLGDRVAFYWEgNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFS 193
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 194 ADSlCERILDSS-CTLLITADAFYRGEKLVNlkelvddalhkcREKGFPVKRCIVVkhlgRAELGTGDSPSHSPPLK--R 270
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFYPMYRQIQ------------QEDATPLRHICLT----RVALPADDGVSSFTQLKaqQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 271 PCQDLQdkmkAKPMSkrpqipwnqgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTT-----GGYm 345
Cdd:PRK08008 161 PATLCY----APPLS--------------------------------TDDTAEILFTSGTTSRPKGVVITHynlrfAGY- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 346 lYTA--TSFKY--VF-----DFHEDdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVSRLWNIVDKYKVTK 416
Cdd:PRK08008 204 -YSAwqCALRDddVYltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 417 FYTAPTAIRLLMKfgdEPVNKYSRA-SLRVLgtvgepinpeawLWYHRVVGAQRcpivDTFWQ------------TETGG 483
Cdd:PRK08008 266 TECIPMMIRTLMV---QPPSANDRQhCLREV------------MFYLNLSDQEK----DAFEErfgvrlltsygmTETIV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 484 HMLTPLPGATPMKPgSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHERFEATYFRKfpGYYVTG 562
Cdd:PRK08008 327 GIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPKATAKVLEAD--GWLHTG 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 563 DGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEEL 642
Cdd:PRK08008 404 DTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEF 480
|
570 580 590
....*....|....*....|....*....|....*..
gi 2119488996 643 KKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK08008 481 FAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
130-681 |
2.33e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 113.87 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAFyrgeklvnlkelvDDALHKCREkgfPVKRCivvkhlgraeLGTGDSPSHSPPLKRPCQDLQDKMKAKPMSKRPQ 289
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPP---DLGRL----------RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 IPWNQGvdlwwheilgdaeeecepewcdaedplFILYTSGSTGKPKGVVHTTggymLYTATSFKYVFD---FHEDDVFWC 366
Cdd:PRK07788 205 PPKPGG---------------------------IVILTSGTTGTPKGAPRPE----PSPLAPLAGLLSrvpFRAGETTLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 367 TADIGWITGHSYVTYGpLANGATSVL---FEGIPTYPDVsrlwnivDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASL 443
Cdd:PRK07788 254 PAPMFHATGWAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 444 RVLGTVGEPINPEAWLWYHRVVGaqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSATFPFFGVAPAILNESGee 518
Cdd:PRK07788 326 KIIFVSGSALSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENG-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 519 legeaegylvfkQPWPG--IMRTVYGNHERFEA-TYFR---KFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLST 592
Cdd:PRK07788 395 ------------NEVPRgvVGRIFVGNGFPFEGyTDGRdkqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 593 AEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:PRK07788 463 AEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD---EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGK 539
|
....*....
gi 2119488996 673 IMRRVLRKI 681
Cdd:PRK07788 540 VLKRELREM 548
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
131-680 |
5.66e-26 |
|
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: 112.01 E-value: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 131 ATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSSCTLLI 210
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI-AFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 211 TADAFYRGEKLVNlkelvddalhkcrekgfpvkrcivvkhlgraelgTGDspshspplkrpcqdlqdkmkakpmskrPQI 290
Cdd:cd12118 106 FVDREFEYEDLLA----------------------------------EGD---------------------------PDF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 291 PWNQGVDlwwheilgdaeeecepEWcdaeDPLFILYTSGSTGKPKGVVHTTGGYMLyTATSFKYVFDFHEDDVFWCTADI 370
Cdd:cd12118 125 EWIPPAD----------------EW----DPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 ----GWItghsyVTYGPLANGATSVLFEGIpTYPDVsrlWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRaslRVL 446
Cdd:cd12118 184 fhcnGWC-----FPWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPH---RVH 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSATFPffGVAPAILNESGEELEGEAEG 525
Cdd:cd12118 252 VMTAGAPPPAAVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 526 YLVFKQ------PWPG------------IMRTVYGNHErfeATY--FRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNV 585
Cdd:cd12118 321 VDVLDPetmkpvPRDGktigeivfrgniVMKGYLKNPE---ATAeaFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIIS 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 586 SGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISPIATPDYIQNAPgL 665
Cdd:cd12118 396 GGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-L 471
|
570
....*....|....*
gi 2119488996 666 PKTRSGKIMRRVLRK 680
Cdd:cd12118 472 PKTSTGKIQKFVLRD 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
299-680 |
1.33e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 111.31 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 299 WWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTG-----GYMLYTAtsfkyvFDFHEDDVFWCTADI--- 370
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVMLAQR------FGLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDVSRlwnivdkYKVTKF--------YTAPTAIRllmkfGDEP 434
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPER-----PDDA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 435 VNkysraSLRVL-GTVGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTEtGGHMLTPLPGaTPmkPGSATFPFFGVA--- 508
Cdd:PRK07867 266 DN-----PLRIVyGNEGAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGVAivd 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 509 --------PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHErfeATYFRKFPGYYVTGDGCRRDEDGYYWITGRID 580
Cdd:PRK07867 329 pdtgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAYFAGRLG 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 581 DMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTP-ALAEELKKQvrEKISPIATPDYI 659
Cdd:PRK07867 405 DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPKQWPSYV 482
|
410 420
....*....|....*....|.
gi 2119488996 660 QNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK07867 483 RVCAELPRTATFKVLKRQLSA 503
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
135-680 |
2.50e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.99 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADA 214
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 FyrgeKLVNLKELVddalHKCREKgfpvkrcivVKHLGRAELGTGDSPSHSpplkrpcqdlqdkmkakpmskrpqipwnq 294
Cdd:PRK06087 131 F----KQTRPVDLI----LPLQNQ---------LPQLQQIVGVDKLAPATS----------------------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvDLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWIT 374
Cdd:PRK06087 165 --SLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 375 GHSYVTYGPLANGATSVLFEGIPtyPDVSrlWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVLGTVGEPIn 454
Cdd:PRK06087 242 GFLHGVTAPFLIGARSVLLDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEK--QPADLSALRFFLCGGTTI- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 455 PEawlwyhRVVgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvf 529
Cdd:PRK06087 315 PK------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEAR------------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 530 kqpwpgimRTVYGNHERFEAT--------YFRKfP----------GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLS 591
Cdd:PRK06087 374 --------KTLPPGCEGEEASrgpnvfmgYLDE-PeltaraldeeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENIS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 592 TAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREgHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSG 671
Cdd:PRK06087 445 SREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKA-PHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASG 523
|
....*....
gi 2119488996 672 KIMRRVLRK 680
Cdd:PRK06087 524 KIQKFLLRK 532
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
117-681 |
5.01e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 109.56 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYwegnepGEATQITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SLCERILDSSCTLLITADAFyrgeklVNLKELVddalhkcrekgfpvKRCIVVKHLGRAElgtgdspshspplkrpcqDL 275
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTF------QNMALSM--------------QKVSYVQRVISIT------------------SL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 276 QDKMKAKPMskrpqipwnqgvdlwwheilgDAEEECEpewcdaEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYV 355
Cdd:PRK06839 133 KEIEDRKID---------------------NFVEKNE------SASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 FDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVSRLWNIVDKYKVTKFYTAPT---AIRLLMKFGd 432
Cdd:PRK06839 185 IDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKFE- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 433 epvnKYSRASLRVLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAIL 512
Cdd:PRK06839 260 ----TTNLQSVRWFYNGGAPC-PEELM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 513 NESGEELEGEAEGYLVFKQPwpGIMrTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLST 592
Cdd:PRK06839 332 DENKNKVEVGEVGELLIRGP--NVM-KEYWNRPDATEETIQD--GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 593 AEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGK 483
|
....*....
gi 2119488996 673 IMRRVLRKI 681
Cdd:PRK06839 484 IQKAQLVNQ 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
115-681 |
5.35e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 109.85 E-value: 5.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 115 LGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSA 194
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 195 DSLcERILDSSCTLLITADAfyrgeklvnlkELVDdALHKCREKGFPVKRCIVVKHLGRAELGTGDSPSHSPPLKRPcqd 274
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEA-----------ALLA-ALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAP--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 275 lqdkmkAKPMSKRPQipwnqgvdlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKy 354
Cdd:PRK06155 172 ------APAAAVQPG------------------------------DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 355 VFDFHEDDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgdEP 434
Cdd:PRK06155 215 DLEIGADDVLYTTLPLFHTNALN-AFFQALLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLS---QP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 435 VNKYSRAS-LRVLGTVGEPINpeawlwYHRVVGAqRC--PIVDTFWQTETGGHMLTPLPGAtpmKPGSATFPFFGVAPAI 511
Cdd:PRK06155 287 ARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEARV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 512 LNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHErfEATY--FRKFpgYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHL 589
Cdd:PRK06155 357 VDEHDQELPDGEPGELLLRADEPFAFATGYFGMP--EKTVeaWRNL--WFHTGDRVVRDADGWFRFVDRIKDAIRRRGEN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 590 LSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISPIATPDYIQNAPGLPKTR 669
Cdd:PRK06155 433 ISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVAALPKTE 509
|
570
....*....|..
gi 2119488996 670 SGKIMRRVLRKI 681
Cdd:PRK06155 510 NGKVQKFVLREQ 521
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
324-679 |
5.69e-25 |
|
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: 109.00 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 324 ILYTSGSTGKPKGVVHTTGGYMLYTAT--SFKYVFDFHEDDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 401
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 402 VSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINP---EAWL-WYHrvvgaqrcPIVDTFW 477
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 478 Q-TETGGhmLTPLPGATPMK-PGSATFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY-GNHERFEATYF-- 552
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfANGPGFEYTNDpe 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 553 -----RKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVT 627
Cdd:cd05929 341 ktaaaRNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2119488996 628 LREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
300-679 |
2.67e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.42 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 300 WHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSFKYVFDFHEDDVFWCTADIgwitGHS-- 377
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTERFGLTRDDVCYVSMPL----FHSna 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 378 -YVTYGP-LANGATSVL---FEGIPTYPDVSRlwnivdkYKVTKFYTAPTAIRLLMKFGDEPVNKYSRasLRV-LGTVGE 451
Cdd:PRK13388 206 vMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERPDDADNP--LRVaFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 452 PINPEAWlwyhrvvgAQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSATFPFFGV-----------APAILNES-GE 517
Cdd:PRK13388 277 PRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVaiynpetltecAVARFDAHgAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 518 ELEGEAEGYLVFKQPwPGIMRTVYGNHerfEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVES 597
Cdd:PRK13388 345 LNADEAIGELVNTAG-AGFFEGYYNNP---EATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 598 ALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTP-ALAEELKKQvrEKISPIATPDYIQNAPGLPKTRSGKIMRR 676
Cdd:PRK13388 421 ILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYVRIAADLPSTATNKVLKR 498
|
...
gi 2119488996 677 VLR 679
Cdd:PRK13388 499 ELI 501
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
130-678 |
4.33e-24 |
|
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: 105.86 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITadafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpq 289
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 ipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGymlytATSFkyvfdfheddVFWCTAD 369
Cdd:cd12115 103 ---------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAF----------LQWAAAA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 370 IG--WITGHSYVT-----------YGPLANGATSVLFEGIPTYPDVSRLwnivdkYKVTKFYTAPTAIRLLMKFGDEPvn 436
Cdd:cd12115 141 FSaeELAGVLASTsicfdlsvfelFGPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP-- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 437 kysrASLRVLGTVGEPINPEAWLWYHRVVGAQRC-----PIVDTFWQTetgGHMLTPLPGATPmkpgSATFPFFGVAPAI 511
Cdd:cd12115 213 ----ASVRVVNLAGEPLPRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYV 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 512 LNEsgeelegeaegylvFKQPWP------------GIMRTvYGNHERFEATYFR---KFPG--YYVTGDGCRRDEDGYYW 574
Cdd:cd12115 282 LDR--------------ALQPVPlgvpgelyiggaGVARG-YLGRPGLTAERFLpdpFGPGarLYRTGDLVRWRPDGLLE 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 575 ITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIA 654
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYM 423
|
570 580
....*....|....*....|....
gi 2119488996 655 TPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd12115 424 VPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
130-679 |
5.82e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 106.38 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PRK13382 65 ELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAFyrgeklvnlKELVDDALHKCrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakPMSKRpQ 289
Cdd:PRK13382 145 IYDEEF---------SATVDRALADC-----------------------------------------------PQATR-I 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 IPWNQGVDLWWHEILGDAEEECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-TGGYMlytatSFKYVFDfheddvfwcta 368
Cdd:PRK13382 168 VAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD----------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 369 DIGWITGHSYVTYGPL--ANGATSVLFEGIPTYPDVSR-------LWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYS 439
Cdd:PRK13382 231 RTPWRAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 440 RASLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSATFPFFGVAPAILNES 515
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 516 geelegeaegylvFKQPWPGIMRTVY-GNHERFEAtYF----RKF-PGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHL 589
Cdd:PRK13382 383 -------------FREVPTGEVGTIFvRNDTQFDG-YTsgstKDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGEN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 590 LSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPalaEELKKQVREKISPIATPDYIQNAPGLPKTR 669
Cdd:PRK13382 449 VYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP---ETLKQHVRDNLANYKVPRDIVVLDELPRGA 525
|
570
....*....|
gi 2119488996 670 SGKIMRRVLR 679
Cdd:PRK13382 526 TGKILRRELQ 535
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
129-611 |
6.16e-24 |
|
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: 105.37 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSlCERIL-DSSCT 207
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 208 LLITADAfyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskr 287
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 288 pqipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVfDFHEDDVFWCT 367
Cdd:cd05907 87 -------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSF 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 368 ADIGWITGHSYVTYGPLANGATSVLFEGIPTYPD------------VSRLWNIVdkYKVTKFYTAPTAIRLLMKFGdepv 435
Cdd:cd05907 135 LPLAHVFERRAGLYVPLLAGARIYFASSAETLLDdlsevrptvflaVPRVWEKV--YAAIKVKAVPGLKRKLFDLA---- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 436 nkySRASLRVLGTVGEPINPEAWLWYHrvvgAQRCPIVDTFWQTETGG-HMLTPLPGATPMKPGSATFPF-FGVAPA--I 511
Cdd:cd05907 209 ---VGGRLRFAASGGAPLPAELLHFFR----ALGIPVYEGYGLTETSAvVTLNPPGDNRIGTVGKPLPGVeVRIADDgeI 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 512 LnesgeelegeaegylvFKQpwPGIMRTVYGNHERFEATYFRkfPGYYVTGDGCRRDEDGYYWITGRIDDML-NVSGHLL 590
Cdd:cd05907 282 L----------------VRG--PNVMLGYYKNPEATAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNI 341
|
490 500
....*....|....*....|.
gi 2119488996 591 STAEVESALVEHRAIAEAAVV 611
Cdd:cd05907 342 SPEPIENALKASPLISQAVVI 362
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
115-672 |
2.40e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.58 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 115 LGDRVAFYWeGNEpgeatQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSA 194
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 195 DSLCERILDSSCTLLITADAFyrGEKLVNLKelvdDALHKcrekgfpvkrcivVKHLgrAELGTGDSPSHSPPlkrpcqd 274
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVL----PRLPK-------------LRTL--VVVEDGSGNDLLPG------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 275 lqdkmkakpmskrpqipwnqGVDlwWHEILGDAEEECEPEWCDAEDpLFILYTSGSTGKPKGVVHTT--------GGYML 346
Cdd:PRK07798 142 --------------------AVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRQedifrvllGGRDF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 347 YTATsfkYVFDfhEDDVfwcTADIGWITGHSYVTYGPLANGAT-----SVLFEG--IPTYPDVS----RLWNIVDKYKVT 415
Cdd:PRK07798 199 ATGE---PIED--EEEL---AKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSGqtVVLLPDVRfdadEVWRTIEREKVN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 416 kfytaptairLLMKFGD----------EPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVgaqrcP---IVDTFWQTETG 482
Cdd:PRK07798 271 ----------VITIVGDamarplldalEARGPYDLSSLFAIASGGALFSPSVKEALLELL-----PnvvLTDSIGSSETG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 483 -GHMLTPLPGATPmkPGSATF---PFFGVAPAILNEsgeelegeaegyLVFKQPWPG-IMRT------VYGNHERFEATy 551
Cdd:PRK07798 336 fGGSGTVAKGAVH--TGGPRFtigPRTVVLDEDGNP------------VEPGSGEIGwIARRghiplgYYKDPEKTAET- 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 552 FRKFPG--YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLR 629
Cdd:PRK07798 401 FPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLR 480
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2119488996 630 EGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:PRK07798 481 EGARPD---LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
130-676 |
1.04e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.58 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsIVFAgfsadslceriLDSSctlL 209
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAFYRGEKLvNLKELVDDALHKCrEKGFPVKRCIVVKhlgrAELGTGDSPSHSPPLKrpcqDLQDKMKAKPMSKRPQ 289
Cdd:PRK05852 103 PIAEQRVRSQAA-GARVVLIDADGPH-DRAEPTTRWWPLT----VNVGGDSGPSGGTLSV----HLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 ipwnqGvdlwwheiLGDaeeecepewcdaeDPLFILYTSGSTGKPKGVVHTTGGymlyTATSFKYV---FDFHEDDVfwC 366
Cdd:PRK05852 173 -----G--------LRP-------------DDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 367 TADIGWITGHSYVT--YGPLANGATSVLfegiPTYPDVS--RLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRAS 442
Cdd:PRK05852 221 VAVMPLYHGHGLIAalLATLASGGAVLL----PARGRFSahTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 443 LRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSATFPFFGVA----- 508
Cdd:PRK05852 297 LRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgsdgl 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 509 ---PAILNesgeelegeaegylvfkQPW---PGIMRTVYGNHERFEATYFRkfpGYYVTGDGCRRDEDGYYWITGRIDDM 582
Cdd:PRK05852 374 plpAGAVG-----------------EVWlrgTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 583 LNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIATPDYIQNA 662
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES---APPTAEELVQFCRERLAAFEIPASFQEA 510
|
570
....*....|....
gi 2119488996 663 PGLPKTRSGKIMRR 676
Cdd:PRK05852 511 SGLPHTAKGSLDRR 524
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-678 |
6.89e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTL 208
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAFyrGEKLvnlkelvddalhkcrekgfPVKRCIVVKHLGRAelgtgdspshspplkrpcqdlqdkmkakpmskrp 288
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRP---------------------------------- 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwnqgvDLWWheilgDAEEECEPEWC-DAEDPLFILYTSGSTGKPKGVVHTTGG---YMLYTATSFK----------- 353
Cdd:PRK12316 637 --------AAWL-----EGYSEENPGTElNPENLAYVIYTSGSTGKPKGAGNRHRAlsnRLCWMQQAYGlgvgdtvlqkt 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 354 -YVFDFHEDDVFWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvsRLWNIVDKYKVTKFYTAPTAIRLLMKFG 431
Cdd:PRK12316 704 pFSFDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDE 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 432 DEPvnkySRASLRVLGTVGEPINPEAWLwyhRVVG-AQRCPIVDTFWQTETGghmlTPLPGATPMKPGSATF----PFFG 506
Cdd:PRK12316 765 DVA----SCTSLRRIVCSGEALPADAQE---QVFAkLPQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPIAN 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 507 VAPAILNESGeelegeaegylvfkQPWP------------GIMRTVYG----NHERFEATYFRKFPGYYVTGDGCRRDED 570
Cdd:PRK12316 834 LACYILDANL--------------EPVPvgvlgelylagrGLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRAD 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 571 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVShphpVKGECLYCFVTLR-EGHVFTPALAEELKKQVREK 649
Cdd:PRK12316 900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLEsEGGDWREALKAHLAASLPEY 975
|
570 580
....*....|....*....|....*....
gi 2119488996 650 IspiaTPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK12316 976 M----VPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
319-679 |
7.42e-21 |
|
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: 94.65 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 319 EDPLFILYTSGSTGKPKGVVHT----------TGGYMLYTatsfkyvfdfhEDDVFWCTADIGWITGHSYVTYGPLANGA 388
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivnngyfIGERLGLT-----------EQDRLCIPVPLFHCFGSVLGVLACLTHGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 389 TSVLFEgiPTYpDVSRLWNIVDKYKVTKFYTAPTA-IRLLmkfGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGA 467
Cdd:cd05917 71 TMVFPS--PSF-DPLAVLEAIEKEKCTALHGVPTMfIAEL---EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 468 QRCPIVdtFWQTETGGHMLTPLPGATPMKP----GSAtFPFFGVApaILNESGEelegeaegylvfKQPWPG-------- 535
Cdd:cd05917 145 KDVTIA--YGMTETSPVSTQTRTDDSIEKRvntvGRI-MPHTEAK--IVDPEGG------------IVPPVGvpgelcir 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 536 ---IMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVS 612
Cdd:cd05917 208 gysVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 613 HPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:cd05917 286 VPDERYGEEVCAWIRLKEGAELT---EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
320-675 |
1.69e-20 |
|
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: 93.24 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGvvhttggyMLYTATSFKYVFDFHEDDVFWCTADIGWITG---HSYVTYGplangATSVLFEG- 395
Cdd:cd17633 1 NPFYIGFTSGTTGLPKA--------YYRSERSWIESFVCNEDLFNISGEDAILAPGplsHSLFLYG-----AISALYLGg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 396 ---IPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFgDEPVNKysrasLRVLGTVGEPINPEAwlwyHRVVGAQ--RC 470
Cdd:cd17633 68 tfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLKNIfpKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 471 PIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHERFEAT 550
Cdd:cd17633 138 NLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMVFSG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 551 YFRKFP----GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLycfV 626
Cdd:cd17633 198 YVRGGFsnpdGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA---V 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 627 TLREGHVFT-PALAEELKKQV-REKIspiatPDYIQNAPGLPKTRSGKIMR 675
Cdd:cd17633 275 ALYSGDKLTyKQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
135-684 |
1.83e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.43 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITADA 214
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 FYrgEKLVNLKElvddalhkcrEKGFPVKrCIvvkhlgraelgtgDSPshspplKRPCqdlqdkmkakpmskrpqipwnq 294
Cdd:PLN02246 132 YV--DKLKGLAE----------DDGVTVV-TI-------------DDP------PEGC---------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdLWWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMlytaTSFKYVFD-------FHEDDVFWCT 367
Cdd:PLN02246 158 ---LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLV----TSVAQQVDgenpnlyFHSDDVILCV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 368 ADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVSRLWNIVDKYKVTkfyTAPTAIRLLMKFGDEP-VNKYSRASLRVL 446
Cdd:PLN02246 231 LPMFHIYSLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINPEawlwYHRVVGAqRCP---IVDTFWQTETGGHMLTPLPGA---TPMKPGSAtfpffgvAPAILNESGEELE 520
Cdd:PLN02246 304 LSGAAPLGKE----LEDAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELKIVD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 521 GEAEGYLVFKQPW------PGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:PLN02246 372 PETGASLPRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELK----KQV--REKISPIATPDYIqnapglPKT 668
Cdd:PLN02246 450 LEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI------PKA 520
|
570
....*....|....*..
gi 2119488996 669 RSGKIMRRVLR-KIAQN 684
Cdd:PLN02246 521 PSGKILRKDLRaKLAAG 537
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
320-675 |
2.33e-20 |
|
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: 92.72 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 399
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 400 pDVSRLWNIVDKYKVTKFYT-APTAIRLLMKFGDEPVnkySRASLRVLGTVGEPINPEAWlwyHRVVGAqrcpivdTFW- 477
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 478 ---QTETGGhMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTV---YGNHERFEATY 551
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGP------LVfqgYWNLPELTAYT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 552 FRKfpGYYVTGDGCRRDEDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLR 629
Cdd:cd17637 213 FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2119488996 630 EGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMR 675
Cdd:cd17637 291 PGATLT---ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
320-682 |
1.29e-19 |
|
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: 90.47 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 399
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 400 PDVSRlwnivdkYKVTKFYTAPTAIRLLMkfgDEPVNKYSRASLRVLGTVGEPINPEAwlwyHRVVGAQRCPIVDTFWQT 479
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 480 ETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHERFEATYFRKfPGYY 559
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 560 VTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPALA 639
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG-----PADP 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2119488996 640 EELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
113-681 |
1.67e-19 |
|
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: 92.59 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWEGNEpgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGalhsiVFAGF 192
Cdd:cd17642 28 ASVPGTIAFTDAHTG----VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIG-----VGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 SADSLCERILDSSCTLlitadafyRGEKLVNLKELVDDALHKCREKGFPVKRCIVVkhlgraelgtgDSPshspplkrpc 272
Cdd:cd17642 99 TNDIYNERELDHSLNI--------SKPTIVFCSKKGLQKVLNVQKKLKIIKTIIIL-----------DSK---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 QDLQDKMKAKPMSKRPQIPwnqgvdlwwheilGDAEEECEPEWCDAEDPL-FILYTSGSTGKPKGVVHT----------- 340
Cdd:cd17642 150 EDYKGYQCLYTFITQNLPP-------------GFNEYDFKPPSFDRDEQVaLIMNSSGSTGLPKGVQLThknivarfsha 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 341 ---TGGYMLYTATSFKYVFDFHEDdvFWCTADIGWITGhsyvtygplanGATSVLfegIPTYPDVSRLWNIVDkYKVTKF 417
Cdd:cd17642 217 rdpIFGNQIIPDTAILTVIPFHHG--FGMFTTLGYLIC-----------GFRVVL---MYKFEEELFLRSLQD-YKVQSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 418 YTAPTAIRLLMKfgDEPVNKYSRASLRVLGTVGEPINPEawlwyhrvVGAQ-----RCPIV-DTFWQTETGGHML-TPlp 490
Cdd:cd17642 280 LLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE--------VGEAvakrfKLPGIrQGYGLTETTSAILiTP-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 491 gATPMKPGSA--TFPFFGvAPAILNESGEELEGEAEGYLVFKQpwPGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRD 568
Cdd:cd17642 348 -EGDDKPGAVgkVVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PMIMKGYVNNPEATKALIDKD--GWLHSGDIAYYD 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 569 EDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVRE 648
Cdd:cd17642 422 EDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT---EKEVMDYVAS 498
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2119488996 649 KISP-------IATPDYIqnapglPKTRSGKIMRRVLRKI 681
Cdd:cd17642 499 QVSTakrlrggVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
319-675 |
3.51e-19 |
|
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: 89.63 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 319 EDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 398
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 399 YpdvSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpVNKYSRaSLRVLGTVGE-PINPEA--WLWYHRVvgaqrcPIVDT 475
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVSELKS-ANATVP-SLRLIGYGGSrAIAADVrfIEATGLT------NTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 476 FWQTETGGHMLTPLpGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFEATYFRkf 555
Cdd:cd17635 149 YGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLID-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 pGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghVFT 635
Cdd:cd17635 224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA--ELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2119488996 636 PALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMR 675
Cdd:cd17635 301 ENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
133-678 |
3.96e-19 |
|
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: 91.18 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsiVFAGFSADSLCERILdssctlLITA 212
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGA----AYVPVDIDQPAARRE------AILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 DAfyrGEKLVnLKELVDDALHKcrekgfpvkRCIVVKHLGRAELGTGDSPSHSPPlkrpcqdlqdkmkakpmskrpqipw 292
Cdd:cd12114 82 DA---GARLV-LTDGPDAQLDV---------AVFDVLILDLDALAAPAPPPPVDV------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYM-LYTATSFKYVFDfHEDDVFWCTA--- 368
Cdd:cd12114 124 ------------------------APDDLAYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG-PDDRVLALSSlsf 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 369 -----DIgwitghsyvtYGPLANGATSVLfegiPTY---PDVSRLWNIVDKYKVTKFYTAPT-----------------A 423
Cdd:cd12114 179 dlsvyDI----------FGALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPAllemlldvleaaqallpS 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 424 IRLLMKFGDE-PVNKYSRasLRVLGTVGEPIN----PEAWLW--YHRVVGA---------------QRCPIVDTfwqtet 481
Cdd:cd12114 245 LRLVLLSGDWiPLDLPAR--LRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP------ 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 482 gghMLTPLPGatpmkpgsatfpffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFEATYFRKFPG- 557
Cdd:cd12114 317 ---RGRDCPD--------------WVPGEL---------------------WiggRGVALGYLGDPELTAARFVTHPDGe 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 558 -YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPvKGECLYCFVTLREGHvfTP 636
Cdd:cd12114 359 rLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG--TP 435
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2119488996 637 ALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd12114 436 IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
130-683 |
4.35e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 91.44 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAFYrgeklvnlkELVDDALH---KCREKGFPVKRCIVVkhlgraELGTGDSPSHSPPLKRPCQDLQDKMKakpmSK 286
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKilaEKKKSSFKPPLLIVI------GDPTCDPKSLQYALGKGAIEYEKFLE----TG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 287 RPQIPWNQGVDLWWHEILGdaeeecepewcdaedplfilYTSGSTGKPKGVV-HTTGGYMLytATSFKYVFDFHEDDVFW 365
Cdd:PLN02479 183 DPEFAWKPPADEWQSIALG--------------------YTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 366 CTADIGWITGHSYvTYGPLANGATSVLFEGIPTypdvSRLWNIVDKYKVTKFYTAPTAIRLL------------------ 427
Cdd:PLN02479 241 WTLPMFHCNGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 428 MKFGDEP----VNKYSRASLRVLGTVG--EPINPE---AWL--WYH---------------RVVGAQRCPIVDTfwqtet 481
Cdd:PLN02479 316 MTAGAAPppsvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT------ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 482 gghmltplpgaTPMKPGSATFPFFGVAPAILNesgeelegeaegyLVFKqpwpGIMRTVYGNHERFEAtyfrkfpGYYVT 561
Cdd:PLN02479 390 -----------KTMKPVPADGKTMGEIVMRGN-------------MVMK----GYLKNPKANEEAFAN-------GWFHS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 562 GDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT--PALA 639
Cdd:PLN02479 435 GDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALA 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2119488996 640 EELKKQVREKISPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 683
Cdd:PLN02479 515 EDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
115-679 |
4.48e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.10 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 115 LGDRVAFyWEGNEPGEAT------QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIV 188
Cdd:PRK06145 4 LSASIAF-HARRTPDRAAlvyrdqEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 189 FAGFSADSLCERILDSSCTLLITADAFYRGEKLVNLKELVDDAlhkcrekgfpvkrcivvkhlgraelgtgdspshsppl 268
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAA------------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 269 krpcqdlqdkmkAKPMSKRpqipwnqgvdlwwheiLGDAEEECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTTGgymly 347
Cdd:PRK06145 126 ------------AQADSRR----------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG----- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 348 tatsfkyvfdfhedDVFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVSRLWNIVDKYK 413
Cdd:PRK06145 173 --------------NLHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 414 VTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVLGTVGEPiNPEAWLW-YHRVVGAQRcpIVDTFWQTET-GGHMLTPlPG 491
Cdd:PRK06145 239 LTCAWMAPVMLSRVLTVPDR--DRFDLDSLAWCIGGGEK-TPESRIRdFTRVFTRAR--YIDAYGLTETcSGDTLME-AG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 492 ATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEATYFrkfPGYYVTGDGCRRDEDG 571
Cdd:PRK06145 313 REIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFY---GDWFRSGDVGYLDEEG 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 572 YYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKIS 651
Cdd:PRK06145 388 FLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLA 464
|
570 580
....*....|....*....|....*...
gi 2119488996 652 PIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
133-684 |
5.13e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 90.61 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGiRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITa 212
Cdd:PRK07638 26 VLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 DAFYRGeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqDLQDkmkakpmSKRPQIPW 292
Cdd:PRK07638 104 ERYKLN-------------------------------------------------------DLPD-------EEGRVIEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 NQgvdlwWHEILGDAEEECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTTGGYMlytaTSFK-YVFDFH---EDDVFwct 367
Cdd:PRK07638 122 DE-----WKRMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL----HSFDcNVHDFHmkrEDSVL--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 368 adigwITG---HSYVTYGplangATSVLFEG-----IPTYPDVSRLWNIvDKYKVTKFYTAPTAIRLLMK---FGDEPVN 436
Cdd:PRK07638 189 -----IAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKMK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 437 ------KYSRASLRVLGTvgepINPEAWLWyhrvvgaqrcpivdTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPA 510
Cdd:PRK07638 258 iissgaKWEAEAKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 511 ILNESGeelegeaegylvfKQPWPGIMRTVYGNHERFEATY------FRKFP--GYYVTGDGCRRDEDGYYWITGRIDDM 582
Cdd:PRK07638 320 ICNEAG-------------EEVQKGEIGTVYVKSPQFFMGYiiggvlARELNadGWMTVRDVGYEDEEGFIYIVGREKNM 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 583 LNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLycfVTLREGHvftpALAEELKKQVREKISPIATPDYIQNA 662
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGS----ATKQQLKSFCLQRLSSFKIPKEWHFV 459
|
570 580
....*....|....*....|..
gi 2119488996 663 PGLPKTRSGKIMRRVLRKIAQN 684
Cdd:PRK07638 460 DEIPYTNSGKIARMEAKSWIEN 481
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
133-684 |
7.51e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.43 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhSIVFAGFSADS--LCERILDSSCTLLI 210
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQRseLNAYASQIEPALLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 211 tADafyRGEKLVNLKELVDDALHKCREKgfpvkrCIVVKHlgraelgtGDSPSHSppLKRPCQDLQDKMKAKPMSkrpqi 290
Cdd:PRK10946 126 -AD---RQHALFSDDDFLNTLVAEHSSL------RVVLLL--------NDDGEHS--LDDAINHPAEDFTATPSP----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 291 pwnqgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGYmLYTATSFKYVFDFHEDDVFWCTADi 370
Cdd:PRK10946 181 ---------------------------ADEVAFFQLSGGSTGTPKLIPRTHNDY-YYSVRRSVEICGFTPQTRYLCALP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 gwiTGHSYVTYGPlanGATSVLFEG----IPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVL 446
Cdd:PRK10946 232 ---AAHNYPMSSP---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 447 GTVGEPINP---------------------EAWLWYHR-------VVGAQRCPIV--DTFWQTETGGHmltPLPGATP-- 494
Cdd:PRK10946 306 QVGGARLSEtlarripaelgcqlqqvfgmaEGLVNYTRlddsderIFTTQGRPMSpdDEVWVADADGN---PLPQGEVgr 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 495 -MKPGSATFPffgvapailnesgeelegeaegylvfkqpwpGIMRTVYGNHERFEATyfrkfpGYYVTGDGCRRDEDGYY 573
Cdd:PRK10946 383 lMTRGPYTFR-------------------------------GYYKSPQHNASAFDAN------GFYCSGDLVSIDPDGYI 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 574 WITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPALAEELKKQVREK-ISP 652
Cdd:PRK10946 426 TVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE-----PLKAVQLRRFLREQgIAE 500
|
570 580 590
....*....|....*....|....*....|..
gi 2119488996 653 IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 684
Cdd:PRK10946 501 FKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
317-678 |
9.79e-19 |
|
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: 89.45 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHTtggYMLYTATSFKYVFDFHEDDVfwcTADIGWITGHSY-VTYGPLA----NGATSV 391
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVE---HRNVAHAAHAWRREYELDSF---PVRLLQMASFSFdVFAGDFArsllNGGTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 392 LfegIP--TYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEAWLwYHRVvgAQR 469
Cdd:cd17650 165 I---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTL-AARF--GQG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 470 CPIVDTFWQTET--------GGhmLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegylvfkQPWP------- 534
Cdd:cd17650 239 MRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL--------------QPQPvgvagel 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 -----GIMRTVYGN----HERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAI 605
Cdd:cd17650 300 yiggaGVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAI 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119488996 606 AEAAVVSHpHPVKGECLYC-FVTLREghvfTPALAeELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17650 380 DEAVVAVR-EDKGGEARLCaYVVAAA----TLNTA-ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
130-685 |
2.61e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 88.85 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGA-LH---------SIVFagfsadslce 199
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 200 rILD-SSCTLLITADAFyrgeklvnlKELVDDALhkcreKGFPVKRCIVVkhlgraelgtgdspshspplkrpcqDLQDk 278
Cdd:PRK08162 110 -MLRhGEAKVLIVDTEF---------AEVAREAL-----ALLPGPKPLVI-------------------------DVDD- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 279 mkakpmskrPQIPWNQGV-DLWWHEILGDAEEECEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTTGGYMLytATSFKYV 355
Cdd:PRK08162 149 ---------PEYPGGRFIgALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLN--ALSNILA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 356 FDFHEDDVF-----------WCTAdigWITGhsyvtygplANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAI 424
Cdd:PRK08162 218 WGMPKHPVYlwtlpmfhcngWCFP---WTVA---------ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 425 RLLmkfgdepVNkySRASLRvlgtvgEPINpeawlwyHRVVG--AQRCPIVDTFWQTETGGHMLTPLPGATPM------- 495
Cdd:PRK08162 282 SAL-------IN--APAEWR------AGID-------HPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvc 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 496 --KPGSATFPFfgVAPAILNESGEELEGEAEGYLVFKqpwPGIMRTVYGNHERFEATYFR---------KFP-------- 556
Cdd:PRK08162 340 awQPEWDALPL--DERAQLKARQGVRYPLQEGVTVLD---PDTMQPVPADGETIGEIMFRgnivmkgylKNPkateeafa 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 -GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHvft 635
Cdd:PRK08162 415 gGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA--- 491
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2119488996 636 PALAEELKKQVREKISPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 685
Cdd:PRK08162 492 SATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
117-698 |
2.61e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.40 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGNEpgeatqITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADafyrgeklvnlkelvddalhkcrekgfpvkrcivvkHLgraelgtgdSPSHSPPLKRPCQDLQ 276
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQS------------------------------------HL---------RLPLAQGVQVLDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 DKmkakpmskrpqipwnqgvdlwwheilgDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKyVF 356
Cdd:PRK12316 3181 DE---------------------------NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ-AY 3232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 357 DFHEDDVFWCTADIGWiTGHSYVTYGPLANGATSVLfEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgdEPVN 436
Cdd:PRK12316 3233 GLGVGDRVLQFTTFSF-DVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEED 3306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 437 KYSRASLRVLGTVGEPINPEAwlwYHRVVGAQrcPIVDTFWQTETgghmlTPLPGATPMKPGSATFPFFGVAPAILNESG 516
Cdd:PRK12316 3307 AHRCTSLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRACYI 3376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 517 EELEGEAEGYLVFKQPWPGIMRTVYGNH-------ERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHL 589
Cdd:PRK12316 3377 LDGSLEPVPVGALGELYLGGEGLARGYHnrpgltaERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFR 3456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 590 LSTAEVESALVEHRAIAEAAVVShphpVKGECLYCFVTLREGhvfTPALAEELKKQVREKIspiatPDYIQNA-----PG 664
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflER 3524
|
570 580 590
....*....|....*....|....*....|....
gi 2119488996 665 LPKTRSGKIMRRVLRKIaqnDHDLGDTSTVADQS 698
Cdd:PRK12316 3525 MPLTPNGKLDRKALPRP---DAALLQQDYVAPVN 3555
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
134-681 |
3.24e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 88.75 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLlita 212
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 dAFYRGEKLVNLKELvddalhkcrekGFPVkrcivvkhlgraeLGTGDSPSHSpplkrpcqdlqdkmkakpmSKRPQIPW 292
Cdd:PLN02574 143 -AFTSPENVEKLSPL-----------GVPV-------------IGVPENYDFD-------------------SKRIEFPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvdlwWHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHE----DDVFWCTA 368
Cdd:PLN02574 179 -------FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 369 DIGWITGHSYVTYGPLANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfGDEPVNKYSRASLRVLGT 448
Cdd:PLN02574 252 PMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 449 VGEPINPEAWLWYhrvvgAQRCPIVDtFWQtetgGHMLTPLPGATPMKPGSATFPFFG----VAPAILNESGEELEGEAE 524
Cdd:PLN02574 327 GAAPLSGKFIQDF-----VQTLPHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSsvglLAPNMQAKVVDWSTGCLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 525 GYLVFKQPW---PGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 601
Cdd:PLN02574 397 PPGNCGELWiqgPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 602 HRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 681
Cdd:PLN02574 475 HPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
138-679 |
1.19e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 86.68 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 138 ELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSSCTLLITADAfyr 217
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEI-AYILEDSGARVLIAHA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 218 geklvnlkelvdDALHKCRE---KGFPVkrcIVVKHLGRAELGTGDSPSHSPPlKRPCQDLQDKMKAKPMSKRPQIPwnq 294
Cdd:PRK12406 92 ------------DLLHGLASalpAGVTV---LSVPTPPEIAAAYRISPALLTP-PAGAIDWEGWLAQQEPYDGPPVP--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 295 gvdlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVVHT--TGGYMLYTATSFKYVFDFHEDDVFWCTADIGw 372
Cdd:PRK12406 153 -------------------------QPQSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLTGPLY- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 373 itgHSyvtyGPLANGATSVLFEGI----PTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRvlgt 448
Cdd:PRK12406 207 ---HS----APNAYGLRAGRLGGVlvlqPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLR---- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 449 vgepinpeawlwyHRVVGAQRCP--------------IVDTFWQTETGGhmltpLPGATP----MKPGSATFPFFGVAPA 510
Cdd:PRK12406 275 -------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGA-----VTFATSedalSHPGTVGKAAPGAELR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 511 ILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLL 590
Cdd:PRK12406 337 FVDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 591 STAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRS 670
Cdd:PRK12406 413 YPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD---EADIRAQLKARLAGYKVPKHIEIMAELPREDS 489
|
....*....
gi 2119488996 671 GKIMRRVLR 679
Cdd:PRK12406 490 GKIFKRRLR 498
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
318-679 |
1.60e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 86.22 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 318 AEDPL--FILYTSGSTGKPKGV--------VHTTGGYMLYTATSFkyvFDFHEDDVFWCTADIGwitgHSyvtyGPL--- 384
Cdd:PRK13390 145 TEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwc 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 385 ----ANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINPEA--- 457
Cdd:PRK13390 214 smvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVkha 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 458 ---WLWyhrvvgaqrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSATFPFFGVA----------PAilnesgeelegea 523
Cdd:PRK13390 290 midWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDLhicdddgnelPA------------- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 524 egylvfkqpwpGIMRTVYGNHERFEATYFRK-----------FPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLST 592
Cdd:PRK13390 346 -----------GRIGTVYFERDRLPFRYLNDpektaaaqhpaHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYP 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 593 AEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:PRK13390 415 QETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGK 494
|
....*..
gi 2119488996 673 IMRRVLR 679
Cdd:PRK13390 495 LVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-680 |
2.31e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITadafyrgeklvnlkelvddalHKCREKGFPVKRCIVVKHLGRAELGTGdSPSHSPPLKrpcqdlqdkmkakpmskrpq 289
Cdd:PRK12316 4653 LT---------------------QSHLLQRLPIPDGLASLALDRDEDWEG-FPAHDPAVR-------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 290 ipwnqgvdlwwheilgdaeeecepewCDAEDPLFILYTSGSTGKPKGV----------VHTTGGYMLYTA-------TSF 352
Cdd:PRK12316 4691 --------------------------LHPDNLAYVIYTSGSTGRPKGVavshgslvnhLHATGERYELTPddrvlqfMSF 4744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 353 KyvFD-FHEddvfwctadiGWitghsyvtYGPLANGAtSVLFEGiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfg 431
Cdd:PRK12316 4745 S--FDgSHE----------GL--------YHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-- 4800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 432 dEPVNKYSRASLRVLGTVGEPINPEAW-LWY--------HRVVGAQRCPIVDTFWQTETGghmltPLPGATPMKPGSatf 502
Cdd:PRK12316 4801 -HAERDGEPPSLRVYCFGGEAVAQASYdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT--- 4871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 503 PFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFEATYFRKFPG--------YYVTGDGCRRDEDGYYW 574
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLPVGVAGELYLGGE--GVAR---GYLERPALTAERFVPDpfgapggrLYRTGDLARYRADGVID 4946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 575 ITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVkGECLYCFVTLREGHV-----FTPALAEELKKQVREK 649
Cdd:PRK12316 4947 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALadadeAQAELRDELKAALRER 5025
|
570 580 590
....*....|....*....|....*....|.
gi 2119488996 650 ISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK12316 5026 LPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
317-680 |
3.74e-17 |
|
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: 85.18 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHT-TGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEg 395
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 396 iptYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpVNKYSRASLRVLGTVGEPinPEAWL-----WYHRVVGAQRC 470
Cdd:cd05915 230 ---RLDPASLVELFDGEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRSLIarferMGVEVRQGYGL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 471 PIV-----DTFWQTEtgghmLTPLPGATPMK-PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNH 544
Cdd:cd05915 304 TETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 545 ERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYC 624
Cdd:cd05915 379 EATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 625 FVTLREGHvftpALAEELKKQVREKISPIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05915 457 VVVPRGEK----PTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
129-644 |
4.50e-17 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 84.83 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSSctl 208
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTI-RYVLEHS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 liTADAFYRGeKLvnlkelvDDalHKCREKGFPvkrcivvkhlgrAELGTGDSPSHSPPlkrPCQDLQDKMKAKpmskrp 288
Cdd:cd05932 78 --ESKALFVG-KL-------DD--WKAMAPGVP------------EGLISISLPPPSAA---NCQYQWDDLIAQ------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwnqgvdlwwHEILGDAEEEcepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMlYTATSFKYVFDFHEDDVFWCTA 368
Cdd:cd05932 125 ------------HPPLEERPTR------FPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 369 DIGWITGHSYVTYGPLANGATSVLFEGIPTYPD------------VSRLW-----NIVDKYKVTKfytaptaIRLLMKFg 431
Cdd:cd05932 186 PLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWtkfqqGVQDKIPQQK-------LNLLLKI- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 432 deP-VNKYSRASL---------RVLGTVGEPINPEAWLWYHRVvgaqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSAT 501
Cdd:cd05932 258 --PvVNSLVKRKVlkglgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 502 FPFFGVAPAIlnesgeelegEAEGYLVFKQpwPGIMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDD 581
Cdd:cd05932 330 NAGPGVEVRI----------SEDGEILVRS--PALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKD 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 582 MLNVS-GHLLSTAEVESALVEHRAIaEAAVVS---HPHPVKGECLYCFVTLREGHVFTPALAEELKK 644
Cdd:cd05932 396 IFKTSkGKYVAPAPIENKLAEHDRV-EMVCVIgsgLPAPLALVVLSEEARLRADAFARAELEASLRA 461
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
113-678 |
4.92e-17 |
|
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: 84.69 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWEGNepgeatQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGF 192
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 193 SADSLcERIL-DSSCTLLITADAFYRGEKLVNLKELVDDalhkcrekgfpvkrcivvkhlGRAELGTGDSpshsppLKRP 271
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQSHLQPPIAFIGLIDLLDE---------------------DTIYHEESEN------LEPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 272 CQdlqdkmkakpmskrpqipwnqgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATS 351
Cdd:cd17655 134 SK--------------------------------------------SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 352 FKYVFDFHEDDVfwctADIGWITGHSYVT--YGPLANGATSVLFEGiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLmk 429
Cdd:cd17655 170 NKVIYQGEHLRV----ALFASISFDASVTeiFASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITIIDLTPAHLKLL-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 430 fgdEPVNKYSRASLRVLGTVGEPINPE-AWLWYHRVVGAqrCPIVDTFWQTETG-GHMLTPLpgaTPMKPGSATFPffgV 507
Cdd:cd17655 243 ---DAADDSEGLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSVP---I 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 508 APAILNESGeelegeaegYLVFK--QPWP------------GIMRTvYGNHERFEAtyfRKF------PG--YYVTGDGC 565
Cdd:cd17655 312 GKPLGNTRI---------YILDQygRPQPvgvagelyiggeGVARG-YLNRPELTA---EKFvddpfvPGerMYRTGDLA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 566 RRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPALAEELKKQ 645
Cdd:cd17655 379 RWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK-----ELPVAQLREF 453
|
570 580 590
....*....|....*....|....*....|...
gi 2119488996 646 VREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17655 454 LARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
116-680 |
1.03e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.16 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSAD 195
Cdd:PRK08279 51 PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 196 SL--CERILDSSctLLITADafyrgeklvnlkELVdDALHKCREkgfpvkrcivvkHLGRAELgtgdSPSHSPPLKRPCQ 273
Cdd:PRK08279 125 VLahSLNLVDAK--HLIVGE------------ELV-EAFEEARA------------DLARPPR----LWVAGGDTLDDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 274 DLQDKMKAkpMSKRPqipwnqgvdlwwheilgdaeeECEPEWCD---AEDPLFILYTSGSTGKPKGVVHTTGGYMLYTAt 350
Cdd:PRK08279 174 GYEDLAAA--AAGAP---------------------TTNPASRSgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 351 SFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVSRLWNIVDKYKVTKFYtaptAI--- 424
Cdd:PRK08279 230 GFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRATAFQ----YIgel 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 425 -RLLMkfgDEPVNKYSRA-SLRVLgtVGEPINPEAW--------------LW--------------YHRVVGaqRCP--- 471
Cdd:PRK08279 299 cRYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFDGTVG--RVPlwl 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 472 -----IVDtfWQTETGghmlTPLPGA----TPMKPGSAtfpffGVAPAILNEsgeelegeaegylvfKQPWPG------- 535
Cdd:PRK08279 372 ahpyaIVK--YDVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD---------------RGPFDGytdpeas 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 536 ---IMRTVygnherfeatyFRKFPGYYVTGDGCRRDEDGYYWITGRIDDML-----NVsghllSTAEVESALVEHRAIAE 607
Cdd:PRK08279 426 ekkILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEE 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119488996 608 AAV--VSHPHpVKGECLYCFVTLREGHVFTPAlaeELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK08279 490 AVVygVEVPG-TDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
534-679 |
1.43e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.56 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 534 PGIMRtvyGNHERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSH 613
Cdd:PRK08974 412 PQVML---GYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 614 PHPVKGECLYCFVTLREghvftPAL-AEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK08974 489 PSEVSGEAVKIFVVKKD-----PSLtEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
133-678 |
2.78e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 81.92 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITa 212
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 dafyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqipw 292
Cdd:cd17652 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKY--------VFDFHE---D 361
Cdd:cd17652 91 ------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAfdvgpgsrVLQFASpsfD 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 362 DVFW--CTAdigwitghsyvtygpLANGATSVLfegIPTYPDVS--RLWNIVDKYKVTkFYTAPTAIRLLMKFGDEPvnk 437
Cdd:cd17652 147 ASVWelLMA---------------LLAGATLVL---APAEELLPgePLADLLREHRIT-HVTLPPAALAALPPDDLP--- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 438 ysraSLRVLGTVGEPINPE-AWLWyhrvvgAQRCPIVDTFWQTET--GGHMLTPLPGATPMKPGSatfPFFGVAPAILNE 514
Cdd:cd17652 205 ----DLRTLVVAGEACPAElVDRW------APGRRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDA 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 515 SGeelegeaegylvfkQPWP------------GIMRTvYGNH-----ERFEATYFRKfPG--YYVTGDGCRRDEDGYYWI 575
Cdd:cd17652 272 RL--------------RPVPpgvpgelyiagaGLARG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEF 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 576 TGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIAT 655
Cdd:cd17652 336 LGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMV 412
|
570 580
....*....|....*....|...
gi 2119488996 656 PDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17652 413 PAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
134-680 |
2.86e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAd 213
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ- 2107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 afyrgeklvnlKELVDDALhkcrekgfpvkrcivvkhlgraelgtgdspshsPPLKRPCQDLQDkmkakpmskrpqipwn 293
Cdd:PRK12316 2108 -----------RHLLERLP---------------------------------LPAGVARLPLDR---------------- 2127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgvDLWWHEIlgdAEEECEPEwCDAEDPLFILYTSGSTGKPKGV----------VHTTGGYMLYTATS-----FKYVFD- 357
Cdd:PRK12316 2128 ---DAEWADY---PDTAPAVQ-LAGENLAYVIYTSGSTGLPKGVavshgalvahCQAAGERYELSPADcelqfMSFSFDg 2200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 358 FHEddvfwctadiGWITghsyvtygPLANGATSVLFEGipTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNk 437
Cdd:PRK12316 2201 AHE----------QWFH--------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGR- 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 438 ysRASLRVLGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSATFPFFGVAPA-----I 511
Cdd:PRK12316 2260 --PPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayI 2332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 512 LNESGEELEGEAEGYLVFKQPwpGIMRTVYG----NHERFEATYFRKFPG-YYVTGDGCRRDEDGYYWITGRIDDMLNVS 586
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIR 2410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 587 GHLLSTAEVESALVEHRAIAEAAVVSHPHPvKGECLYCFVTLREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLP 666
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
570
....*....|....
gi 2119488996 667 KTRSGKIMRRVLRK 680
Cdd:PRK12316 2487 LNPNGKLDRKALPK 2500
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
317-683 |
3.21e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSF---------KYVFDFhedDVFWCTadiGWItghsyVTYGPLANG 387
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIigwemgtcpVYLWTL---PMFHCN---GWT-----FTWGTAARG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 388 ATSVLFEGIpTYPDVSRlwNIvDKYKVTKFYTAPTAIRLLMKfGDEPVNKYSRASLRVLgTVGEPiNPEAWLWYHRVVGA 467
Cdd:PLN03102 253 GTSVCMRHV-TAPEIYK--NI-EMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 468 QrcpIVDTFWQTETGGHML--------TPLPGATPMK-PGSATFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwp 534
Cdd:PLN03102 326 Q---VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS-- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 GIMRTVYGNHErfeATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHP 614
Cdd:PLN03102 401 SIMKGYLKNPK---ATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119488996 615 HPVKGECLYCFVTLREGHVFTPALAEELK-------KQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 683
Cdd:PLN03102 478 HPTWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
130-678 |
4.55e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 82.78 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERIL-DSSCTL 208
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAFyrgeklvnlkelvddalhkcrekgfpvkrcivvkhLGR-AELGTGDSPSHSPPLKRPcqDLQDKMKAKPmskr 287
Cdd:PRK10252 559 LITTADQ-----------------------------------LPRfADVPDLTSLCYNAPLAPQ--GAAPLQLSQP---- 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 288 pqipwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVV--HTT---------GGYML--------YT 348
Cdd:PRK10252 598 -------------------------------HHTAYIIFTSGSTGRPKGVMvgQTAivnrllwmqNHYPLtaddvvlqKT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 349 ATSFKY-VFDFheddvFWctadigwitghsyvtygPLANGATSVLFEgiptyPDVSR----LWNIVDKYKVTKFYTAPTa 423
Cdd:PRK10252 647 PCSFDVsVWEF-----FW-----------------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS- 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 424 irLLMKFGDEPVNK---YSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTE---------TGGHMLTPLPG 491
Cdd:PRK10252 699 --MLAAFVASLTPEgarQSCASLRQVFCSGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRG 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 492 AtPMKPGsatFPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFEATYFRkf 555
Cdd:PRK10252 774 S-SVPIG---YPVWNTGLRILDARM--------------RPVPpGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA-- 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 PG--YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH----RAIAEAAVVSHPHPVKGEC--LYCFVT 627
Cdd:PRK10252 834 PGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLV 913
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 628 LREGhvfTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK10252 914 SQSG---LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
133-681 |
8.03e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITA 212
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 DAfyrgeklvnlkelvddalhkcrekgfpvkrciVVKHLGRAelgTGDspsHSPPLKRpcqdlqdkmkakpmskrpqipw 292
Cdd:PRK12467 3200 AH--------------------------------LLEQLPAP---AGD---TALTLDR---------------------- 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nqgvDLWWHEilgdaEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGY-MLYTATSFKYVFDFHEDDVFWCTADig 371
Cdd:PRK12467 3220 ----LDLNGY-----SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALaNHLCWIAEAYELDANDRVLLFMSFS-- 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 wITGHSYVTYGPLANGATSVLFEGIPTYPDvsRLWNIVDKYKVTKFYTAPTAIRLLMKFGDepVNKYSRASLRVLGtvGE 451
Cdd:PRK12467 3289 -FDGAQERFLWTLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG--GADCASLDIYVFG--GE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 452 PINPEAWLWYHRVV---------GAQRCPIVDTFWQTETGGhmlTPLPGATPMKPGSAtfpffGVAPAILNESGeelege 522
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIYVLDGQL------ 3427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 523 aegylvfkQPWP-GIMRTVY--------GNH-------ERFEATYFRKFPG-YYVTGDGCRRDEDGYYWITGRIDDMLNV 585
Cdd:PRK12467 3428 --------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 586 SGHLLSTAEVESALVEHRAIAEAAVVSHPhPVKGECLYCFVTLregHVFTPALAEELKKQVREKIspiatPDYIQNA--- 662
Cdd:PRK12467 3500 RGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL-----PDYMVPAqll 3570
|
570 580
....*....|....*....|.
gi 2119488996 663 --PGLPKTRSGKIMRRVLRKI 681
Cdd:PRK12467 3571 vlAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
133-678 |
1.77e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.98 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLIT- 211
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTq 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 212 ---ADAFYRGEKLvnlkelvddalhkcrekgfpvkRCIVVkhlgraelgtgDSPshspplkrpcqdlQDKMKAKPMSkrp 288
Cdd:PRK12467 1679 shlQARLPLPDGL----------------------RSLVL-----------DQE-------------DDWLEGYSDS--- 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwNQGVDLwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYM-LYTATsfKYVFDFHEDDVfwct 367
Cdd:PRK12467 1710 ----NPAVNL------------------APQNLAYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV---- 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 368 adigWITGHSYV-------TYGPLANGAtSVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKysr 440
Cdd:PRK12467 1762 ----VLQFTSFAfdvsvweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP--- 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 441 ASLRVLGTVGEPINPEAW-LWYHRVVGAQrcpIVDTFWQTETGGHML------------TPLPGATPMkPGSATFpffgV 507
Cdd:PRK12467 1834 LSLRRVVCGGEALEVEALrPWLERLPDTG---LFNLYGPTETAVDVThwtcrrkdlegrDSVPIGQPI-ANLSTY----I 1905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 508 APAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFEATYFRKFPG-YYVTGDGCRRDEDG 571
Cdd:PRK12467 1906 LDASLNP----------------VP-IGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADG 1968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 572 YYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPvKGECLYCFVT-----LREGHVFTPALAEELKKQV 646
Cdd:PRK12467 1969 VIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHL 2047
|
570 580 590
....*....|....*....|....*....|....*..
gi 2119488996 647 REKIspiatPDYIQNA-----PGLPKTRSGKIMRRVL 678
Cdd:PRK12467 2048 KASL-----PEYMVPAhlvflARMPLTPNGKLDRKAL 2079
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
324-675 |
1.87e-15 |
|
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: 78.31 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 324 ILYTSGSTGKPKGVV--HTTggyMLYTATSFKYVFDFHEDDVFWCTADIgwitghsYVTYGPLAnGATSVLFEGIPTYP- 400
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQ---TLRAAAAWADCADLTEDDRYLIINPF-------FHTFGYKA-GIVACLLTGATVVPv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 401 ---DVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgDEP-VNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAQRcpIVDTF 476
Cdd:cd17638 74 avfDVDAILEAIERERITVLPGPPTLFQSLL---DHPgRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFET--VLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 477 WQTETG-GHMLTPLPGATPMKPGSATfPFFGVAPAILNESGEELEGeaegylvfkqpwPGIMRTVYGNHERFEATYFRKf 555
Cdd:cd17638 149 GLTEAGvATMCRPGDDAETVATTCGR-ACPGFEVRIADDGEVLVRG------------YNVMQGYLDDPEATAEAIDAD- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 pGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT 635
Cdd:cd17638 215 -GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLT 293
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2119488996 636 palAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMR 675
Cdd:cd17638 294 ---EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
319-672 |
2.45e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 78.19 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 319 EDPLFILYTSGSTGKPKGVVHTTG--GYMLYTATSFKYVFDFHEDDVFWCTADIGWIT---------GHSYVTYGPLANG 387
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEdiFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVmfpapplmhGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 388 ATSVLFEGIPTYPDvsRLWNIVDKYKVTKFYTAPTAI-RLLMKFGDEPvNKYSRASLRVLGTVGEPINPEawlwyhrvVG 466
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMTIVGDAMaRPLIDALRDA-GPYDLSSLFAISSGGALLSPE--------VK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 467 AQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSATFPFFGVAPAILNESgeelegeaegyLVFKQPWPGIMRTV 540
Cdd:cd05924 152 QGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSGGVGWI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 541 ----------YGNHERFEATyFRKFPG--YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEA 608
Cdd:cd05924 218 arrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119488996 609 AVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGK 672
Cdd:cd05924 297 LVVGRPDERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
133-680 |
2.70e-15 |
|
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: 78.89 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSS-CTLLIT 211
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgATLLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 212 ADAfyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspshspplkrpcqdlqdkmkakpmskrpqip 291
Cdd:cd17653 101 TDS----------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 wnqgvdlwwheilgdaeeecepewcdAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDV-------F 364
Cdd:cd17653 104 --------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVaqvlsiaF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 365 W-CTADIgwitghsyvtYGPLANGATSVLFEGIPTYPDVSRlwnivdkyKVTKFYTAPTAIRLLmkfgdePVNKYSraSL 443
Cdd:cd17653 158 DaCIGEI----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL------SPQDFP--NL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 444 RVLGTVGEPINP---EAWlWYHRVV----GAQRCPIVDTFWQTETGghmlTPLPGATPMkPGSATFpffgvapaILNESg 516
Cdd:cd17653 212 KTIFLGGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY--------ILDAD- 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 517 eelegeaegylvfKQPWP------------GIMRTVYGNHERfEATYFRKFPGY-----YVTGDGCRRDEDGYYWITGRI 579
Cdd:cd17653 277 -------------LQPVPegvvgeicisgvQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGRE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 580 DDMLNVSGHLLSTAEVESALVEHRAIAEAAVVShphpVKGECLYCFVtlreghvfTPALA--EELKKQVREKISPIATPD 657
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI----VVNGRLVAFV--------TPETVdvDGLRSELAKHLPSYAVPD 410
|
570 580
....*....|....*....|...
gi 2119488996 658 YIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
105-679 |
3.19e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.69 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 105 LLDRNVNEKKLGDRVAFYwegnepgEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAL 184
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 185 HSIVFAGFSADSLCERILDSSCTLLITADAF---YRGEKLVNLKELVDDAlhkcrekgfpvkrcivvkhlGRAElgtgds 261
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 262 PSHSPPLKrpcqdlqdkmkakpmskrpqipwnqgvdlwwheilGDAEEecepewcdaedplFILYTSGSTGKPKGVVHTT 341
Cdd:PRK06060 136 PGGYEPMG-----------------------------------GDALA-------------YATYTSGTTGPPKAAIHRH 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 342 ggymlytATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVSRLwnIVDKYKV 414
Cdd:PRK06060 168 -------ADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAI--LSARFGP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 415 TKFYTAPTAIRLLMkfgdEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrCPIVDTFWQTETGGHMLTPlpGATP 494
Cdd:PRK06060 238 SVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 495 MKPGS--ATFPFFG---VAPAilnesgeelegeaegylvFKQPWPGIMRTVYGNHERFEATYFRKfP-------GYYVTG 562
Cdd:PRK06060 310 WRLGTlgRVLPPYEirvVAPD------------------GTTAGPGVEGDLWVRGPAIAKGYWNR-PdspvaneGWLDTR 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 563 DGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEEL 642
Cdd:PRK06060 371 DRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDL 450
|
570 580 590
....*....|....*....|....*....|....*..
gi 2119488996 643 KKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK06060 451 HRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
105-679 |
2.40e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.21 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 105 LLDRNVneKKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAL 184
Cdd:PRK07059 28 LLEESF--RQYADRPAFICMG------KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 185 HSIVFAGFSADSLCERILDSSCTLLITadafyrgekLVNLKELVDDALHKCrekgfPVKRcIVVKHLGRAeLGtgdspsh 264
Cdd:PRK07059 100 VVNVNPLYTPRELEHQLKDSGAEAIVV---------LENFATTVQQVLAKT-----AVKH-VVVASMGDL-LG------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 265 sppLKRPCQDLQDKmKAKPMSKRPQIPWnqgvdlwwHEILGDAEEE-----CEPEWCDAEDPLFILYTSGSTGKPKGVVH 339
Cdd:PRK07059 157 ---FKGHIVNFVVR-RVKKMVPAWSLPG--------HVRFNDALAEgarqtFKPVKLGPDDVAFLQYTGGTTGVSKGATL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 340 TTGGY---MLYTATSFKYVFDF--HEDDVFWCTA----DIGWITGHSYVTygpLANGATSVLfegIPTYPDVSRLWNIVD 410
Cdd:PRK07059 225 LHRNIvanVLQMEAWLQPAFEKkpRPDQLNFVCAlplyHIFALTVCGLLG---MRTGGRNIL---IPNPRDIPGFIKELK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 411 KYKVTKFYTAPTAIRLLMKFGDepVNKYSRASLRV-LG---TVGEPInPEAWLwyhRVVGaqrCPIVDTFWQTETGGhML 486
Cdd:PRK07059 299 KYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIVaNGggmAVQRPV-AERWL---EMTG---CPITEGYGLSETSP-VA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 487 TPLPGATPMKPGSATFPFFGVAPAILNESGEElegeaegyLVFKQPW------PGIMRtvyGNHERFEATYFRKFP-GYY 559
Cdd:PRK07059 369 TCNPVDATEFSGTIGLPLPSTEVSIRDDDGND--------LPLGEPGeicirgPQVMA---GYWNRPDETAKVMTAdGFF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 560 VTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPAL- 638
Cdd:PRK07059 438 RTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----PALt 512
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2119488996 639 AEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK07059 513 EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
45-104 |
4.06e-14 |
|
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: 67.11 E-value: 4.06e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 45 YRELHGRSVLEPREFWGDIAKEFYWKTPCSgpflqYNFDVTKGkIFIEWMKGATTNICYN 104
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFD-----KVLDGSNG-PFAKWFVGGKLNVCYN 54
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
132-678 |
4.44e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.43 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 132 TQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSA---DSLCErILDSSCTL 208
Cdd:PRK05857 40 SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIaaiERFCQ-ITDPAAAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 litadafyrgeklVNLKELVDDALHKCREKGFPVKRCIVVKhlgraelGTGDSpSHSPPLKRPcqdlqdkmKAKPmskrp 288
Cdd:PRK05857 119 -------------VAPGSKMASSAVPEALHSIPVIAVDIAA-------VTRES-EHSLDAASL--------AGNA----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 qipwNQGVDlwwheilgdaeeecepewcdaeDPLFILYTSGSTGKPKGVvhttggyMLYTATSFKYVFDFHEDDVFWcta 368
Cdd:PRK05857 165 ----DQGSE----------------------DPLAMIFTSGTTGEPKAV-------LLANRTFFAVPDILQKEGLNW--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 369 dIGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLL---MKFGDE 433
Cdd:PRK05857 209 -VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 434 PVnkysrASLRVLGTVG-EPINPEAwlwyhRVVGAQRCPIVDTFWQTETGGHMLTpLP----GATPMKPGSATFPFFGV- 507
Cdd:PRK05857 284 TV-----PSLRLVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVd 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 508 ---APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEATYFRkfpGYYVTGDGCRRDEDGYYWITGRIDDMLN 584
Cdd:PRK05857 353 vylAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMII 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 585 VSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGEC--LYCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNA 662
Cdd:PRK05857 430 CGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALvgLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIV 509
|
570
....*....|....*.
gi 2119488996 663 PGLPKTRSGKIMRRVL 678
Cdd:PRK05857 510 TDIPRTQSGKVMRASL 525
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
113-680 |
5.41e-14 |
|
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: 75.35 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWEGNEPGEATQITYRELLTQVCRCANALRKQGiRKGDRVSIYMPMILELVVAMLACARLGALHSIVFA-- 190
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 191 -GFSADSLCERILDSSCTLLITADAFyrgeklvnlkelvDDALHKcrekgfpvkrcivvkhlgraelgTGDSPSHSPPLK 269
Cdd:cd05931 83 pGRHAERLAAILADAGPRVVLTTAAA-------------LAAVRA-----------------------FAASRPAAGTPR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 270 RPCQDLQDkmkakpmskrpqipwnqgvdlwwheiLGDAEEECEPEwCDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTA 349
Cdd:cd05931 127 LLVVDLLP--------------------------DTSAADWPPPS-PDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 350 TSFKYVFDFHEDD--VFW--CTADIGWITGhsyvTYGPLANGATSVLFEgiPTY----PdvsRLW-NIVDKYKVTkFYTA 420
Cdd:cd05931 179 RQIRRAYGLDPGDvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLMS--PAAflrrP---LRWlRLISRYRAT-ISAA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 421 PTairllmkFG-DEPVNKYSRA--------SLRVLGTVGEPINPEAwlwyhrvvgaqrcpiVDTFwQTETGGHMLTP--- 488
Cdd:cd05931 249 PN-------FAyDLCVRRVRDEdlegldlsSWRVALNGAEPVRPAT---------------LRRF-AEAFAPFGFRPeaf 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 489 LPG-----AT---PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVF-------------------KQP--------- 532
Cdd:cd05931 306 RPSyglaeATlfvSGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARELvscgrplpdqevrivdpetGRElpdgevgei 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 533 W---PGIMRTVYGNHERFEATYFRKFP----GYYVTGD-GCRRdeDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRA 604
Cdd:cd05931 386 WvrgPSVASGYWGRPEATAETFGALAAtdegGWLRTGDlGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 605 ---IAEAAVVSHPHPVkGECLycFVTLREGHVFTPALAEELKKQVREKISP---IATPDYIQNAPG-LPKTRSGKIMRRV 677
Cdd:cd05931 464 alrPGCVAAFSVPDDG-EERL--VVVAEVERGADPADLAAIAAAIRAAVARehgVAPADVVLVRPGsIPRTSSGKIQRRA 540
|
...
gi 2119488996 678 LRK 680
Cdd:cd05931 541 CRA 543
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
557-680 |
6.52e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 74.79 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTP 636
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2119488996 637 alaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
134-679 |
1.17e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 74.03 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITa 212
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 213 dafyrgekLVNLKELVDDALHKCRekgfpvkrcivVKHLGRAELGtgdspSHSPPLKRPCQDLQDKmKAKPMSKRPQIPw 292
Cdd:PRK05677 129 --------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRLLINAVVK-HVKKMVPAYHLP- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 293 nQGVDLwwHEILG-DAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHT--------------------TGGYMLYTATS 351
Cdd:PRK05677 183 -QAVKF--NDALAkGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnlvanmlqcralmgsnlnEGCEILIAPLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 352 FKYVFDFheddVFWCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfg 431
Cdd:PRK05677 260 LYHIYAF----TFHCMA--------------MMLIGNHNIL---ISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCN-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 432 DEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETgghmlTPLPGATPMK---PGSATFPFFGVA 508
Cdd:PRK05677 317 NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPSTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 509 PAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFEAT-YFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSG 587
Cdd:PRK05677 389 CKVIDDDGNELPLGEVGELCVKGP--QVMK---GYWQRPEATdEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 588 HLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPK 667
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTGYKVPKAVEFRDELPT 540
|
570
....*....|..
gi 2119488996 668 TRSGKIMRRVLR 679
Cdd:PRK05677 541 TNVGKILRRELR 552
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
129-684 |
1.29e-13 |
|
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: 73.86 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACarlgalhsiVFAGFSAdslcerildssctL 208
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFVP-------------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITADAFYRG-----EKLVNLKELVDdalhkcrekgfpvkRCIVvkhLGRAELgtgdspshspplkrpcqdlqdKMKAKP 283
Cdd:cd05906 93 PLTVPPTYDEpnarlRKLRHIWQLLG--------------SPVV---LTDAEL---------------------VAEFAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 284 MSKRPQIPwnqGVDLWWHEILGDAEEEcePEW--CDAEDPLFILYTSGSTGKPKGVVHTTGGymLYTATSFKYV-FDFHE 360
Cdd:cd05906 135 LETLSGLP---GIRVLSIEELLDTAAD--HDLpqSRPDDLALLMLTSGSTGFPKAVPLTHRN--ILARSAGKIQhNGLTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 361 DDVF--WCTADigWITGHSYVTYGPLANGATSVlfeGIPTyPDV---SRLW-NIVDKYKVTkfYT-APT-AIRLLMKFGD 432
Cdd:cd05906 208 QDVFlnWVPLD--HVGGLVELHLRAVYLGCQQV---HVPT-EEIladPLRWlDLIDRYRVT--ITwAPNfAFALLNDLLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 433 E-PVNKYSRASLRVLGTVGEPINP---EAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF-----P 503
Cdd:cd05906 280 EiEDGTWDLSSLRYLVNAGEAVVAktiRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 504 FFGVAPAILNESGEELEGEAEGYLVFKqpwpGIMRTV-YGNHERFEATYFRKfPGYYVTGD-GCRRDedGYYWITGRIDD 581
Cdd:cd05906 360 IPGVSMRIVDDEGQLLPEGEVGRLQVR----GPVVTKgYYNNPEANAEAFTE-DGWFRTGDlGFLDN--GNLTITGRTKD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 582 MLNVSGHLLSTAEVESAlVEHRAIAE----AAVVSHPHPVKGECLYCFVTLREGHVF-TPALAEELKKQVREKISpiATP 656
Cdd:cd05906 433 TIIVNGVNYYSHEIEAA-VEEVPGVEpsftAAFAVRDPGAETEELAIFFVPEYDLQDaLSETLRAIRSVVSREVG--VSP 509
|
570 580 590
....*....|....*....|....*....|..
gi 2119488996 657 DYI----QNApgLPKTRSGKIMRRVLRKIAQN 684
Cdd:cd05906 510 AYLiplpKEE--IPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
470-682 |
1.68e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 73.70 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 470 CPIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHE 545
Cdd:PRK12492 359 CTIVEGYGLTET-----SPVASTNPYgelaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMK---GYWQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 546 RFEATY-FRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYC 624
Cdd:PRK12492 429 QPEATAeALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119488996 625 FVTLREGHVFTpalaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:PRK12492 509 FVVARDPGLSV----EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
135-682 |
1.79e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 73.69 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERILDSS-CTLLITAD 213
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSEL-EYALNQSgCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFyrgeKLVNLKELVDDalhkcrekgfpvkrciVVKHLGRAELGTGDSPShSPPLKRPCQdlQDKMKAKPMskrpqipwn 293
Cdd:PRK08315 124 GF----KDSDYVAMLYE----------------LAPELATCEPGQLQSAR-LPELRRVIF--LGDEKHPGM--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 qgvdLWWHEILGDAEEEcEPEWCDA-------EDPLFILYTSGSTGKPKGVVHT----------TGGYMLYTatsfkyvf 356
Cdd:PRK08315 172 ----LNFDELLALGRAV-DDAELAArqatldpDDPINIQYTSGTTGFPKGATLThrnilnngyfIGEAMKLT-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 357 dfHEDDV------FWCtadIGWITGhsyvTYGPLANGATSVL----FE-----------------GIPT-------YPDV 402
Cdd:PRK08315 239 --EEDRLcipvplYHC---FGMVLG----NLACVTHGATMVYpgegFDplatlaaveeerctalyGVPTmfiaeldHPDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 403 srlwnivDKYKVTKFYT-----APTAIRLLMKFGDE----------------PVNKYSRAS----LRVlGTVGepinpea 457
Cdd:PRK08315 310 -------ARFDLSSLRTgimagSPCPIEVMKRVIDKmhmsevtiaygmtetsPVSTQTRTDdpleKRV-TTVG------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 458 wlwyhRVVGAQRCPIVDTfwqtETGghmlTPLPgatpmkPGSatfpffgvapailnesgeelegeaegylvfkqpwPG-- 535
Cdd:PRK08315 375 -----RALPHLEVKIVDP----ETG----ETVP------RGE----------------------------------QGel 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 536 ------IMRTVYGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAA 609
Cdd:PRK08315 402 ctrgysVMKGYWNDPEKTAEAIDAD--GWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQ 479
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119488996 610 VVSHPHPVKGECLYCFVTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:PRK08315 480 VVGVPDEKYGEEVCAWIILRPGATLT---EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
134-680 |
1.87e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.43 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITad 213
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 afyrgeklvnlkelvddalhkcrekgfpvkrcivvkhlgraelgtgdspsHSPPLKRpcQDLQDKMKAkpmskrpqIPWN 293
Cdd:PRK12467 616 --------------------------------------------------QSHLLAQ--LPVPAGLRS--------LCLD 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 294 QGVDLWWHEilgdAEEECEPewcdAEDP---LFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYvFDFHEDDVFWCTADI 370
Cdd:PRK12467 636 EPADLLCGY----SGHNPEV----ALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTF 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 371 GWITGHsYVTYGPLANGATsVLFEGIPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgDEPVNKYSRASLRVLGtvG 450
Cdd:PRK12467 707 AFDLGV-TELFGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--G 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 451 EpINPEAWLWYHRVVGAQrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF--PFFGVAPAILNEsgeelegeaegYLv 528
Cdd:PRK12467 781 E-ALQVDLLARVRALGPG-ARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDH-----------YL- 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 529 fkQPWP-GIMRTVY--------GNHER--FEATYFRKFPG------YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLS 591
Cdd:PRK12467 847 --NPVPvGVVGELYiggaglarGYHRRpaLTAERFVPDPFgadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIE 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 592 TAEVESALVEHRAIAEAAVVSHPHPVKGECL-YCFVTLREGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRS 670
Cdd:PRK12467 925 LGEIEARLLAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPN 1004
|
570
....*....|
gi 2119488996 671 GKIMRRVLRK 680
Cdd:PRK12467 1005 GKLDRKALPK 1014
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
113-682 |
2.61e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 72.99 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 113 KKLGDRVAFYWEGnepgeaTQITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAG 191
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 192 FSADSLCERILDSSCTLLITADafyrgeklvNLKELVDDALhkcreKGFPVKRCIVVkhlgraelGTGDSpshsppLKRP 271
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVID---------NFGTTVQQVI-----ADTPVKQVITT--------GLGDM------LGFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 272 CQDLQDKMKAKPMSKRPQIPWNQGVDLWWHEILGdAEEECEPEWCDAEDPLFILYTSGSTGKPKGVvhttggyMLYTATS 351
Cdd:PRK08751 162 KAALVNFVVKYVKKLVPEYRINGAIRFREALALG-RKHSMPTLQIEPDDIAFLQYTGGTTGVAKGA-------MLTHRNL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 352 FKYVFDFHEddvfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGIPTYPDVSR-LWNIVDKYKVTKFyTAPT 422
Cdd:PRK08751 234 VANMQQAHQ----WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGGCNHLISNPRdMPGFVKELKKTRF-TAFT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 423 AIRLLM-KFGDEP-VNKYSRASLRVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETgghmlTPLPGATPMK---- 496
Cdd:PRK08751 309 GVNTLFnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTET-----SPAACINPLTlkey 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 497 PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfEATYFRKFPGYYVTGDGCRRDEDGYYWIT 576
Cdd:PRK08751 381 NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 577 GRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPAL-AEELKKQVREKISPIAT 655
Cdd:PRK08751 457 DRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALtAEDVKAHARANLTGYKQ 531
|
570 580
....*....|....*....|....*..
gi 2119488996 656 PDYIQNAPGLPKTRSGKIMRRVLRKIA 682
Cdd:PRK08751 532 PRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
317-684 |
2.81e-13 |
|
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: 72.58 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVV--H---TTGgymlytATSFKYVFDFHEDD-VFW--------CTADIgwitghsyvtYG 382
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVieHralSTS------ALAHGRALGLTSESrVLQfasytfdvSILEI----------FT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 383 PLANGATSVlfegIPtyPDVSRLWNIVD---KYKVTkfyTA---PTAIRLLMKfGDEPvnkysraSLRVLGTVGEPINPE 456
Cdd:cd05918 168 TLAAGGCLC----IP--SEEDRLNDLAGfinRLRVT---WAfltPSVARLLDP-EDVP-------SLRTLVLGGEALTQS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 457 AW-LWYHRV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsatf 502
Cdd:cd05918 231 DVdTWADRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 503 pffgVAPAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHERFeatyfrkfpgyYVTGDGCRRDEDG--YYwiTGRID 580
Cdd:cd05918 303 ----LARGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 581 DMLNVSGHLLSTAEVESALVEH---RAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTP--------------ALAEELK 643
Cdd:cd05918 359 TQVKIRGQRVELGEIEHHLRQSlpgAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefrALVAELR 438
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2119488996 644 KQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 684
Cdd:cd05918 439 SKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
557-679 |
3.87e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 72.33 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 GYYVTGDGCRRDEDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvft 635
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD----- 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2119488996 636 PALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
317-675 |
1.00e-12 |
|
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: 70.93 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGI 396
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 397 PT-------------YPDVSRLWNIVDKYKVTKFYTAPTAiRLLMKFGDEPVNKYSRASLR--------------VLGtv 449
Cdd:cd05914 166 PSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLK-KFKFKLAKKINNRKIRKLAFkkvheafggnikefVIG-- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 450 GEPINPEAwLWYHRVVGAqrcPIVDTFWQTETGghmltPLPGATP---MKPGSATFPFFGVAPAIlnesGEELEGEAEGY 526
Cdd:cd05914 243 GAKINPDV-EEFLRTIGF---PYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRI----DSPDPATGEGE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 527 LVFKQPwpGIMRTVYGNHERfEATYFRKfPGYYVTGDGCRRDEDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHRAI 605
Cdd:cd05914 310 IIVRGP--NVMKGYYKNPEA-TAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFV 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 606 AEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKKQVREKISpIATPDY-------IQNAPgLPKTRSGKIMR 675
Cdd:cd05914 386 LESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN-QKVPNYkkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
134-678 |
2.00e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLITAD 213
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 214 AFYRGeklvnLKELVDDALHKCREKgfpvkrcivvkhlgraelgtgDSPShspplkrpcqdlqdkMKAKPMSKRPQI--P 291
Cdd:PRK05691 2294 ALFEA-----LGELPAGVARWCLED---------------------DAAA---------------LAAYSDAPLPFLslP 2332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 WNQGvdlwwheilgdaeeecepewcdaedplFILYTSGSTGKPKGVVHTTGGYMLYTATSFKyVFDFHEDDvfwCTADIG 371
Cdd:PRK05691 2333 QHQA---------------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFY 2381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 WIT--GHSYVTYGPLANGATSVL-FEGiptYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFgdePVNKYSRASLRVLGT 448
Cdd:PRK05691 2382 SINfdAASERLLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRMCIT 2455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 449 VGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSATFPFFGVAPA----ILNESGEELEGE 522
Cdd:PRK05691 2456 GGEALTGEHLQRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALVPQG 2530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 523 AEGYLvfkqpWPGIMRTVYGNH-------ERFEATYFRKFPG-YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:PRK05691 2531 ATGEL-----YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAVVSHPHPvKGECLYCFV---TLREGHVFTPALAEELKKQVREKIspiatPDYIQNA-----PGLP 666
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQL-----PDYMVPAhlillDSLP 2679
|
570
....*....|..
gi 2119488996 667 KTRSGKIMRRVL 678
Cdd:PRK05691 2680 LTANGKLDRRAL 2691
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
319-678 |
2.57e-12 |
|
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: 69.77 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 319 EDPLFILYTSGSTGKPKGVV--------HTTGGYMLYTATSFKYVFDFheddvfwctADIGWITG--HSYVTygpLANGA 388
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVLQF---------ASIAFDVAaeEIYVT---LLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 389 TSVLFEGiPTYPDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGdEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVVGaQ 468
Cdd:cd17644 174 TLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVG-N 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 469 RCPIVDTFWQTE----TGGHMLTPLPGATPMKPGSATfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GIMRTVY-- 541
Cdd:cd17644 251 FIQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPVPvGVPGELHig 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 542 ------G-------NHERFEATYFRKFPG--YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIA 606
Cdd:cd17644 316 gvglarGylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVK 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119488996 607 EAAVVSHPHPVKGECLYCFVTlreGHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17644 396 TAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
127-679 |
4.90e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.75 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 127 EPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsiVFagfsadslcerildssc 206
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VF----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 207 TLLITAdafYRgekLVNLKELVDDA---LHKCREKGFPVKRCIVVKHlGRAELGTGDSPSHSPPLKRpcqdlqdkmkakp 283
Cdd:PRK07514 81 LPLNTA---YT---LAELDYFIGDAepaLVVCDPANFAWLSKIAAAA-GAPHVETLDADGTGSLLEA------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 284 mskrpqipwnqgvdlwwheiLGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDV 363
Cdd:PRK07514 141 --------------------AAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 364 FWCTADIGWITGHSYVTYGPLANGA------------------TSVLFEGIPTypdvsrlwnivdkykvtkFYTaptaiR 425
Cdd:PRK07514 200 LIHALPIFHTHGLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT-----R 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 426 LLmkfGDEPVNKYSRASLRVLGTVGEPINPE---AWlwyhrvvgAQRC--PIVDTFWQTETGghMLTPLPGATPMKPGSA 500
Cdd:PRK07514 257 LL---QEPRLTREAAAHMRLFISGSAPLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGERRAGTV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 501 TFPFFGVAPAILNESGEELEGEAEGYL-------VFKQPWPGIMRTvygnherfeATYFRKfPGYYVTGDGCRRDEDGYY 573
Cdd:PRK07514 324 GFPLPGVSLRVTDPETGAELPPGEIGMievkgpnVFKGYWRMPEKT---------AEEFRA-DGFFITGDLGKIDERGYV 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 574 WITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPAlaeELKKQVREKISPI 653
Cdd:PRK07514 394 HIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA---AILAALKGRLARF 470
|
570 580
....*....|....*....|....*.
gi 2119488996 654 ATPDYIQNAPGLPKTRSGKIMRRVLR 679
Cdd:PRK07514 471 KQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
307-680 |
5.55e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.06 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 307 AEEECEPEWCdAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVfDFHEDDVFWCTADIGWITGHSYVtygpLAN 386
Cdd:PLN02860 161 GTTELDYAWA-PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIV-GYGEDDVYLHTAPLCHIGGLSSA----LAM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 387 ---GATSVLfegIPTYpDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVL----GTVGEPINPEAWL 459
Cdd:PLN02860 235 lmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSRLLPDAKK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 460 WYhrvvgaQRCPIVDTFWQTETGGHMltplpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP------- 532
Cdd:PLN02860 311 LF------PNAKLFSAYGMTEACSSL-------TFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAphvelki 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 533 --------------WPGIMRTVYGNHErfEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESA 598
Cdd:PLN02860 378 gldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 599 LVEHRAIAEAAVVSHPHPVKGECLYCFVTLREG----HVFTPAL-------AEELKKQVREK-ISPIATPD-YIQNAPGL 665
Cdd:PLN02860 456 LSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsDNEKENAkknltlsSETLRHHCREKnLSRFKIPKlFVQWRKPF 535
|
410
....*....|....*
gi 2119488996 666 PKTRSGKIMRRVLRK 680
Cdd:PLN02860 536 PLTTTGKIRRDEVRR 550
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
317-683 |
1.20e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.41 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVhTTGGYMLYTATSFKYVFDFHEDDVfwctadigwITG-----HSY----VTYGPLANG 387
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVM-LSHHNILSNIEQISDVFNLRNDDV---------ILSslpffHSFgltvTLWLPLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 388 ATSVlFEGIPTypDVSRLWNIVDKYKVTKFYTAPTAIRLLMKfgDEPVNKYSRASLRVLgtvgepinpeawlwyhrVVGA 467
Cdd:PRK08633 850 IKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------VAGA 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 468 QRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSATFPFFGVAPAILNESGeele 520
Cdd:PRK08633 908 EKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET---- 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 521 geaegYLVFKQPWPG--------IMRTVYGNHERF-EATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLS 591
Cdd:PRK08633 979 -----FEELPPGEDGliliggpqVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVP 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 592 TAEVESALveHRAIAEA----AVVSHPHPVKGECLYCFVTLREGHVftpalaEELKKQVRE-KISPIATPDYIQNAPGLP 666
Cdd:PRK08633 1054 LGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKLVVLHTCGAEDV------EELKRAIKEsGLPNLWKPSRYFKVEALP 1125
|
410
....*....|....*..
gi 2119488996 667 KTRSGKIMRRVLRKIAQ 683
Cdd:PRK08633 1126 LLGSGKLDLKGLKELAL 1142
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
317-680 |
1.29e-11 |
|
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: 67.46 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHTTGgyMLY-TATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYGPLANGATSVL--- 392
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWR--RTLvTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsrk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 393 FEgiptypdVSRLWNIVDKYKVTKFYTAPTAIRLLMkfgDEPVNKYSRASlRVLGTVGEPINPEAWLWYHRVVGAqrcPI 472
Cdd:cd05937 163 FS-------ASQFWKDVRDSGATIIQYVGELCRYLL---STPPSPYDRDH-KVRVAWGNGLRPDIWERFRERFNV---PE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 473 VDTFWQ-TETGGHMLTPLPGAtpmkpgsatfpfFGvAPAILNESGEELEGEAEGYLVFK------QPW------------ 533
Cdd:cd05937 229 IGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQVVLVKmdpetdDPIrdpktgfcvrap 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 534 ---PG--IMRTVYGNHERF-------EAT-------YFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAE 594
Cdd:cd05937 296 vgePGemLGRVPFKNREAFqgylhneDATesklvrdVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 595 VESALVEHRAIAEAAV--VSHP-HPVKGECLYCfvTLREGH-VFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRS 670
Cdd:cd05937 376 VADVLGAHPDIAEANVygVKVPgHDGRAGCAAI--TLEESSaVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDN 453
|
410
....*....|
gi 2119488996 671 GKIMRRVLRK 680
Cdd:cd05937 454 HKQQKGVLRD 463
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
317-678 |
3.48e-11 |
|
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: 65.96 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVV--HTTGGYMLytATSFKYVFDFHEDDVFW---CTADIGWITGHSYVTYGplanGATSV 391
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQleHKNMVNLL--HFEREKTNINFSDKVLQfatCSFDVCYQEIFSTLLSG----GTLYI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 392 LFEgiPTYPDVSRLWNIVDKYKVTKFYTaPTAIRLLMKFGDEPVNKYSRaSLRVLGTVGEPI---NPeawlwYHRVVGAQ 468
Cdd:cd17656 200 IRE--ETKRDVEQLFDLVKRHNIEVVFL-PVAFLKFIFSEREFINRFPT-CVKHIITAGEQLvitNE-----FKEMLHEH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 469 RCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSATFPFfgvapaILNESgeelegeaegylvfKQPWP-GIMR 538
Cdd:cd17656 271 NVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ILDQE--------------QQLQPqGIVG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 539 TVYGN---------------HERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHR 603
Cdd:cd17656 329 ELYISgasvargylnrqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHP 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119488996 604 AIAEAAVVSHPHPVKGECLYC-FVTLREGHVftpalaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17656 409 GVSEAVVLDKADDKGEKYLCAyFVMEQELNI------SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
317-678 |
3.56e-11 |
|
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: 65.88 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGV-VHTTGGYMLYTATSFK----------------YVFDFHEDDVFwctadIGWITGHSYV 379
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVlVEHGSVVNLRTSLSERyfgrdngdeavlffsnYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 380 tygplangatsVLFEGIPTYPDvsRLWNIVDKYKVTKFYTAPTAIRLLmKFGdepvnkySRASLRVLGTVGEPINPEAwl 459
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 460 wYHRVVGAQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP---- 534
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvgav 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 535 --------GIMRTvYGNH-----ERFEATYFR--------KFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTA 593
Cdd:cd17648 288 gelylggdGVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 594 EVESALVEHRAIAEAAVVSHPHPVKGEC-----LYCFVTLREGHVftpaLAEELKKQVREKISPIATPDYIQNAPGLPKT 668
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHV----PESDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
410
....*....|
gi 2119488996 669 RSGKIMRRVL 678
Cdd:cd17648 443 INGKLDVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-678 |
4.44e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYWEGNepgeatQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADS 196
Cdd:PRK05691 1146 ERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILDSSCTLLITADAfyrgeklvnlkeLVDDalhkcrekgfpVKRCIVVKHLGRAELGTGDSPSHSPplkrpcqdlq 276
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSH------------LLER-----------LPQAEGVSAIALDSLHLDSWPSQAP---------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 277 dkmkakpmskrpqipwnqGVDLwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGG------YMLYTat 350
Cdd:PRK05691 1267 ------------------GLHL------------------HGDNLAYVIYTSGSTGQPKGVGNTHAAlaerlqWMQAT-- 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 351 sfkYVFDfhEDDVFWCTADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDVSRLWNIVDKYKVTKFYTAPTairLLMKF 430
Cdd:PRK05691 1309 ---YALD--DSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLF 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 431 GDEPVNKYSRaSLRVLGTVGEPINPE---------AWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLpgatpmkpGSat 501
Cdd:PRK05691 1379 IDEPLAAACT-SLRRLFSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR-- 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 502 fPFFGVAPAILNESGEELEGEAEGYLVFKQpwPGIMRTVYG----NHERFEATYFRKfPG--YYVTGDGCRRDEDGYYWI 575
Cdd:PRK05691 1448 -PLGNVLCRVLDAELNLLPPGVAGELCIGG--AGLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEY 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 576 TGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHpHPVKGECLYCFVTLREGHVFTP-----ALAEELkkqvreki 650
Cdd:PRK05691 1524 LGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEAerlkaALAAEL-------- 1594
|
570 580 590
....*....|....*....|....*....|...
gi 2119488996 651 spiatPDYIQNA-----PGLPKTRSGKIMRRVL 678
Cdd:PRK05691 1595 -----PEYMVPAqlirlDQMPLGPSGKLDRRAL 1622
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
116-483 |
5.39e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 65.94 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 116 GDRVAFYWEGNEPG--------------EATQITYRELLTQVCRCANALR-KQGIRKGDRVSIYMPMILELVVAMLACAR 180
Cdd:cd17632 36 ADRPALGQRATELVtdpatgrttlrllpRFETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 181 LGALHSIVFAGFSADSLCErILDSSCTLLITADAfyrgeklvnlkELVDDALHKCREkGFPVKRCIVVKHlgRAELGTgd 260
Cdd:cd17632 116 LGAVSVPLQAGASAAQLAP-ILAETEPRLLAVSA-----------EHLDLAVEAVLE-GGTPPRLVVFDH--RPEVDA-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 261 spsHSPPLKrpcqdlqdkmkakpmSKRPQIPwNQGVDLWWHEILGDAEEECEPEWCDAE----DPL-FILYTSGSTGKPK 335
Cdd:cd17632 179 ---HRAALE---------------SARERLA-AVGIPVTTLTLIAVRGRDLPPAPLFRPepddDPLaLLIYTSGSTGTPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 336 GVVHTTggymlYTATSFKYVFDFHEDDVFWCTADIGWI-TGHSY---VTYGPLANGAT---------SVLFEGI----PT 398
Cdd:cd17632 240 GAMYTE-----RLVATFWLKVSSIQDIRPPASITLNFMpMSHIAgriSLYGTLARGGTayfaaasdmSTLFDDLalvrPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 399 -YPDVSRLWNIVDKYkvtkfYTAPTAIRLLMKFGDEPVNKYSRASLR--VLG-------TVGEPINPEAWLWYHRVVGAQ 468
Cdd:cd17632 315 eLFLVPRVCDMLFQR-----YQAELDRRSVAGADAETLAERVKAELRerVLGgrllaavCGSAPLSAEMKAFMESLLDLD 389
|
410
....*....|....*
gi 2119488996 469 rcpIVDTFWQTETGG 483
Cdd:cd17632 390 ---LHDGYGSTEAGA 401
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
117-680 |
6.04e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.39 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 117 DRVAFYwegnEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGAlhsiVFAGFSADS 196
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 197 LCERILD----SSCTLLITADAFYrgeklvnlkelvddalHKCREKGFPVkrcIVvkhLGRAELGTGdspshspplkrpc 272
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV---IV---LGEEKIEGA------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 273 qdlqdkmkakpmskrpqipwnqgvdLWWHEILgDAEEECEPEWCDAE----DPLFILYTSGSTGKPKGVVHT-------- 340
Cdd:PLN02330 160 -------------------------VNWKELL-EAADRAGDTSDNEEilqtDLCALPFSSGTTGISKGVMLThrnlvanl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 341 ------TGGYMLYTATSFKYVFDFHeddvfwctadIGWITGHSYVTygpLANGATSVLFEGIptypDVSRLWNIVDKYKV 414
Cdd:PLN02330 214 csslfsVGPEMIGQVVTLGLIPFFH----------IYGITGICCAT---LRNKGKVVVMSRF----ELRTFLNALITQEV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 415 TKFYTAPTAIRLLMKfgDEPVNKY--SRASLRVLGTVGEPINPEAWLWYH-RVVGAQrcpIVDTFWQTETGGHMLT---P 488
Cdd:PLN02330 277 SFAPIVPPIILNLVK--NPIVEEFdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 489 LPGATPMKPGSATFPFFGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHERFEATYFRKfpGYYV 560
Cdd:PLN02330 352 EKGHGIAKKNSVGFILPNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLH 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 561 TGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGEC-LYCFVTLREGhvftPALA 639
Cdd:PLN02330 421 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIpAACVVINPKA----KESE 496
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2119488996 640 EELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
557-678 |
1.06e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 64.63 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 557 GYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGhvfTP 636
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SG 472
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2119488996 637 ALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
551-688 |
1.11e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.73 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 551 YFRK-----FPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCF 625
Cdd:PRK07008 398 YFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119488996 626 VTLREGHVFTpalAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDL 688
Cdd:PRK07008 478 VVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR-DYVL 536
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
123-680 |
1.46e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 64.42 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 123 WEGNEPgeaTQITYRELLTQVCRCANALRKQ-GIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLcERI 201
Cdd:PRK05620 31 WGGAEQ---EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQI-VHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 202 LDSSCTLLITADAfyrgeklvNLKELVDDALHKCrekgfPVKRCIVVkhlgraelgTGDSPSHSPplkrpcqdlqdkmka 281
Cdd:PRK05620 107 INHAEDEVIVADP--------RLAEQLGEILKEC-----PCVRAVVF---------IGPSDADSA--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 282 kpmskRPQIPwnQGVDLWWHEILGDaEEECEPEWCDAE--DPLFILYTSGSTGKPKGVVHT-----TGGYMLYTATSFKy 354
Cdd:PRK05620 150 -----AAHMP--EGIKVYSYEALLD-GRSTVYDWPELDetTAAAICYSTGTTGAPKGVVYShrslyLQSLSLRTTDSLA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 355 vfdFHEDDVFWCTADIgwitgHSYVTYG-PLAN--GATSVLFEGiptyPDVS--RLWNIVDKYKVTKFYTAPTA-IRLLM 428
Cdd:PRK05620 221 ---VTHGESFLCCVPI-----YHVLSWGvPLAAfmSGTPLVFPG----PDLSapTLAKIIATAMPRVAHGVPTLwIQLMV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 429 KFGDEPVNKYSRASLRVLGTVGEPINPEAWLWYHRVvgaqrcPIVDTFWQTETG--GHMLTPLPGATpmkpGSATFPFF- 505
Cdd:PRK05620 289 HYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGV------DVVHVWGMTETSpvGTVARPPSGVS----GEARWAYRv 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 506 --GVAPAILNESGEELEGEAEGY------LVFKQPW-------------PGIMRTVYGNHERFEATYFRKfPGYYVTGDG 564
Cdd:PRK05620 359 sqGRFPASLEYRIVNDGQVMESTdrnegeIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRFTA-DGWLRTGDV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 565 CRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFTPALAEELKK 644
Cdd:PRK05620 438 GSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRD 517
|
570 580 590
....*....|....*....|....*....|....*.
gi 2119488996 645 QVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK05620 518 QLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
130-393 |
1.86e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 64.23 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 130 EATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLL 209
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITadafyRGEKLVNLKELVddalhkcREKGFPvkRCIVVkHLGraELGTG-DSPSHSpplkrpcqdlqdkmkakpmskrp 288
Cdd:PTZ00216 198 VC-----NGKNVPNLLRLM-------KSGGMP--NTTII-YLD--SLPASvDTEGCR----------------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 QIPWNQGVDLwwheilGDAEEECE----PEWCDAEdpLFILYTSGSTGKPKGVVHTTGgymlyTATSFKYVFDFHEDDVF 364
Cdd:PTZ00216 238 LVAWTDVVAK------GHSAGSHHplniPENNDDL--ALIMYTSGTTGDPKGVMHTHG-----SLTAGILALEDRLNDLI 304
|
250 260 270
....*....|....*....|....*....|...
gi 2119488996 365 WCTADigwitGHSYVTYGPLAN----GATSVLF 393
Cdd:PTZ00216 305 GPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
561-678 |
2.38e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 561 TGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLRegHVFTPAlae 640
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*...
gi 2119488996 641 ELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK08308 370 QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
127-683 |
4.04e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 63.45 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 127 EPGEATQITYRELLTQVCRCANALRKqGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVfaGFSADSlcERILdSSC 206
Cdd:PRK06814 652 EDPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFSAGI--ANIL-SAC 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 207 -----TLLITADAFYrgEKlVNLKELVDdALhkcrEKGFpvkRCIVVKHLgRAELGTGDspshspplkrpcqdlqdKMKA 281
Cdd:PRK06814 726 kaaqvKTVLTSRAFI--EK-ARLGPLIE-AL----EFGI---RIIYLEDV-RAQIGLAD-----------------KIKG 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 282 KPMSKRPQIPWNQGvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVV--HTTggyMLYTATSFKYVFDFH 359
Cdd:PRK06814 777 LLAGRFPLVYFCNR---------------------DPDDPAVILFTSGSEGTPKGVVlsHRN---LLANRAQVAARIDFS 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 360 EDDVFWCTADIGwitgHSYvtyGpLANGATSVLFEGIPTYpdvsrlwnivdkykvtkFYTAPTAIRLL----------MK 429
Cdd:PRK06814 833 PEDKVFNALPVF----HSF---G-LTGGLVLPLLSGVKVF-----------------LYPSPLHYRIIpeliydtnatIL 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 430 FG-DEPVNKYSRA-------SLRVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghmltP-LPGATPM--KPG 498
Cdd:PRK06814 888 FGtDTFLNGYARYahpydfrSLRYVFAGAEKVKEETRQTWMEKFGIR---ILEGYGVTETA-----PvIALNTPMhnKAG 959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 499 SAtfpffG-VAPAIlnesgeelegeaeGYLVfkQPWPGI-------MR--TVYGNHERFEATYFRKFP--GYYVTGDGCR 566
Cdd:PRK06814 960 TV-----GrLLPGI-------------EYRL--EPVPGIdeggrlfVRgpNVMLGYLRAENPGVLEPPadGWYDTGDIVT 1019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 567 RDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftpALAEELKKQV 646
Cdd:PRK06814 1020 IDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTTASD------ATRAAFLAHA 1093
|
570 580 590
....*....|....*....|....*....|....*...
gi 2119488996 647 REK-ISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 683
Cdd:PRK06814 1094 KAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
132-680 |
8.37e-10 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 61.67 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 132 TQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTLLIT 211
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 212 adafyrgeklvNLKelvdDALHKCREKgfpvkrcivvkhlgraelgtgdspshSPPlKRPCQDLQDKmkakpmskrpqip 291
Cdd:cd05939 82 -----------NLL----DPLLTQSST--------------------------EPP-SQDDVNFRDK------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 wnqgvdlwwheilgdaeeecepewcdaedpLFILYTSGSTGKPKGVVHTTGGYMLYTATSFkYVFDFHEDDVFWCTADIg 371
Cdd:cd05939 107 ------------------------------LFYIYTSGTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVVYDCLPL- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 372 WITGHSYVTYGP-LANGATSVLFEGIptypDVSRLWNIVDKYKVTKFYTAPTAIRLLMkfGDEPVNKYSRASLRVLgtVG 450
Cdd:cd05939 155 YHSAGGIMGVGQaLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVQYIGEICRYLL--AQPPSEEEQKHNVRLA--VG 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 451 EPINPEAWlwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSATF-PFFG--VAPAIL---NESGEELEGEAE 524
Cdd:cd05939 227 NGLRPQIW---EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRDSD 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 525 GYLVFKQPW-PGIM--RTVYGNHerfeatyFRKFPGY---------------------YVTGDGCRRDEDGYYWITGRID 580
Cdd:cd05939 300 GLCIPCQPGePGLLvgKIIQNDP-------LRRFDGYvnegatnkkiardvfkkgdsaFLSGDVLVMDELGYLYFKDRTG 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 581 DMLNVSGHLLSTAEVESALVEHRAIAEAAV--VSHPHpVKGECLYCFVTLREGHVFTPALAEELKKqvreKISPIATPDY 658
Cdd:cd05939 373 DTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKVDLDRFSAVLAK----SLPPYARPQF 447
|
570 580
....*....|....*....|..
gi 2119488996 659 IQNAPGLPKTRSGKIMRRVLRK 680
Cdd:cd05939 448 IRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
556-680 |
1.55e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.44 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 PGYYVTGDGCRRDeDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVtLREGHVfT 635
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2119488996 636 PALaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRK 680
Cdd:PRK07824 310 PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
556-686 |
1.64e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.78 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 556 PGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHVFT 635
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL 402
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 636 palaEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 686
Cdd:PRK07445 403 ----EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
312-680 |
1.24e-08 |
|
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: 57.88 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 312 EPEWCDAEDPL-FILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVF--W--CTADIGWITGHsyvtYGPLAN 386
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 387 GATSVLfegIPTYPDVSR--LW-NIVDKYKVTKFYTAPTAIRLLMK-FGDEPVNKYSRASLRVLGTVGEPINPE---AWL 459
Cdd:cd05908 173 GMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYElchEFL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 460 WYHRVVGAQRCPIVDTFWQTET---------GGHMLT------------PLPGATPMKPGSATFPFFGVAPA-----ILN 513
Cdd:cd05908 250 DHMSKYGLKRNAILPVYGLAEAsvgaslpkaQSPFKTitlgrrhvthgePEPEVDKKDSECLTFVEVGKPIDetdirICD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 514 ESGEELEGEAEGYLVF--KQPWPGimrtvYGNHERFEATYFRKfPGYYVTGD-GCRRDEDGYywITGRIDDMLNVSGHLL 590
Cdd:cd05908 330 EDNKILPDGYIGHIQIrgKNVTPG-----YYNNPEATAKVFTD-DGWLKTGDlGFIRNGRLV--ITGREKDIIFVNGQNV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 591 STAEVESALVEHRAIAEAAVVS---HPHPVKGECLYCFVTLREGHVFTPALAEELKKQVRE-------KISPIATpdyiq 660
Cdd:cd05908 402 YPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKrggwqinEVLPIRR----- 476
|
410 420
....*....|....*....|
gi 2119488996 661 napgLPKTRSGKIMRRVLRK 680
Cdd:cd05908 477 ----IPKTTSGKVKRYELAQ 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
283-678 |
1.53e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 283 PMSKRPQIpwnqgvdLWWHEILGDAEEECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHED 361
Cdd:PRK05691 3839 GCANRPRL-------LVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRG-MLNNQLSKVPYLALSEA 3910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 362 DVFWCTA----DIG-WitghsYVTYGPLANGATSVLFEGIPTYPdvSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVN 436
Cdd:PRK05691 3911 DVIAQTAsqsfDISvW-----QFLAAPLFGARVEIVPNAIAHDP--QGLLAHVQAQGITVLESVPSLIQGMLAEDRQALD 3983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 437 kysraSLRVLGTVGEPINPE-AWLWYHR--------VVGAQRCPIVDTFWQTETGGHMLTPLPGATP--------MKPGS 499
Cdd:PRK05691 3984 -----GLRWMLPTGEAMPPElARQWLQRypqiglvnAYGPAECSDDVAFFRVDLASTRGSYLPIGSPtdnnrlylLDEAL 4058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 500 ATFPFFGVAPAILNESgeelegeaegylvfkqpwpGIMRTVYGNHERfEATYFRKFP------GYYVTGDGCRRDEDGYY 573
Cdd:PRK05691 4059 ELVPLGAVGELCVAGT-------------------GVGRGYVGDPLR-TALAFVPHPfgapgeRLYRTGDLARRRSDGVL 4118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 574 WITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHPvKGECLYCFVTLREGHVFTPALAEELKKQVREKISPI 653
Cdd:PRK05691 4119 EYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDY 4197
|
410 420
....*....|....*....|....*
gi 2119488996 654 ATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:PRK05691 4198 MVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
134-680 |
1.63e-08 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 57.82 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALhSIvfaGFSADSLCERI---LD-SSCTLL 209
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL-SL---GIYQDSMAEEVaylLNyTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 210 ITADAfyrgEKLVNLKELVDDALHkcrekgfpVKRCIVVKHLGraelgtgdspshspplkrpcqdlqdkmkakpMSK--R 287
Cdd:cd17641 88 IAEDE----EQVDKLLEIADRIPS--------VRYVIYCDPRG-------------------------------MRKydD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 288 PQIPWNQGVdlwwhEILGDAEEECEPEWCDA-------EDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKyvFDF-H 359
Cdd:cd17641 125 PRLISFEDV-----VALGRALDRRDPGLYERevaagkgEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPlG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 360 EDDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY--------PDV----SRLWN---------IVDKYKVTKFY 418
Cdd:cd17641 198 PGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPETMmedlreigPTFvllpPRVWEgiaadvrarMMDATPFKRFM 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 419 -------------------TAPTAIRLLMKFGDEPVNKYSRASL-----RVLGTVGEPINPEAWLWYHrvvgAQRCPIVD 474
Cdd:cd17641 278 felgmklglraldrgkrgrPVSLWLRLASWLADALLFRPLRDRLgfsrlRSAATGGAALGPDTFRFFH----AIGVPLKQ 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 475 TFWQTETGGhmLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegyLVFKQPwpGIMRTVYGNHERFEATYFRK 554
Cdd:cd17641 354 LYGQTELAG--AYTVHRDGDVDPDTVGVPFPGTEVRIDEVGE----------ILVRSP--GVFVGYYKNPEATAEDFDED 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 555 fpGYYVTGDGCRRDEDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHRAIAEAAVVSHPHPVkgecLYCFVTLREGHV 633
Cdd:cd17641 420 --GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRPY----LTAFICIDYAIV 493
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119488996 634 ----------FT--------PALAEELKKQVREKISPIATPDYIQNAPGLPK---------TRSGKIMRRVLRK 680
Cdd:cd17641 494 gkwaeqrgiaFTtytdlasrPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKeldaddgelTRTRKVRRGVIAE 567
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
320-671 |
1.63e-08 |
|
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: 56.93 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 320 DPLFILYTSGSTGKPKGVVHTTGGYMLYTatsfkyvfdfheddvfWCTADIGWITGHS-YVTYGPLANGATsvLFEGIPT 398
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQA----------------LVLAVLQAIDEGTvFLNSGPLFHIGT--LMFTLAT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 399 Y-----------PDVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVLgtvgepinPEAWLWYHRVvga 467
Cdd:cd17636 63 FhaggtnvfvrrVDAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSS--------PAAPEWNDMA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 468 qrcPIVDTFW--------QTETGGhmLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrT 539
Cdd:cd17636 130 ---TVDTSPWgrkpggygQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGP------T 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 540 V---YGNHERFEATYFRKfpGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHPHP 616
Cdd:cd17636 199 VmagYWNRPEVNARRTRG--GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2119488996 617 VKGECLYCFVTLREGHVFTPAlaeELKKQVREKISPIATPDYIQNAPGLPKTRSG 671
Cdd:cd17636 277 RWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
129-385 |
1.66e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.82 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 129 GEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSLCERILDSSCTL 208
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 209 LITadafyrGEKlvNLKELVDdalhkCREKGFPVKRCIVVKhlgraelgtgDSPSHSPPLkrpcqdlQDKMKAKPMSKRP 288
Cdd:PLN02387 182 VIC------DSK--QLKKLID-----ISSQLETVKRVIYMD----------DEGVDSDSS-------LSGSSNWTVSSFS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 289 QIpwnqgvdlwwhEILGDaEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDVfwcta 368
Cdd:PLN02387 232 EV-----------EKLGK-ENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV----- 294
|
250
....*....|....*..
gi 2119488996 369 digwitghsYVTYGPLA 385
Cdd:PLN02387 295 ---------YLAYLPLA 302
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
108-386 |
2.40e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 57.54 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 108 RNVNEKKLGDRVAfywEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSI 187
Cdd:PLN02861 55 KYPNNQMLGRRQV---TDSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 188 VFAGFSADSLcERILDSSCTLLitadAFYRGEKLvnlkelvdDALHKCrekgfpVKRCivVKHLgRAELGTGDSPShspp 267
Cdd:PLN02861 132 LYDTLGANAV-EFIINHAEVSI----AFVQESKI--------SSILSC------LPKC--SSNL-KTIVSFGDVSS---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 268 lkrpcqdlQDKMKAKpmskrpqipwNQGVDLW-WHEILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVHTTGGYML 346
Cdd:PLN02861 186 --------EQKEEAE----------ELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2119488996 347 YTATSFKYVFdfhEDDVFWCTADigwitghSYVTYGPLAN 386
Cdd:PLN02861 248 EVLSTDHLLK---VTDRVATEED-------SYFSYLPLAH 277
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
317-678 |
3.27e-07 |
|
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: 53.33 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVvhttggyMLYtatsfkyvfdfHEDDVFWCTadigWitGHSYVTYGPLANGA--TSVLFE 394
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGV-------MIE-----------HHNLVNLCE----W--HRPYFGVTPADKSLvyASFSFD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 395 G----IPTYPDVSRLWNIVD---KYKVTK----FYTAPTAIRLLMKFGDEPVNKYSRASLRVLGTVGEPINpeawlwyhr 463
Cdd:cd17645 158 AsaweIFPHLTAGAALHVVPserRLDLDAlndyFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLK--------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 464 VVGAQRCPIVDTFWQTETgghmlTPLPGATPMKPGSATFPFfGVAPA-----ILNESGEELEGEAEGYLVFKQPwpGIMR 538
Cdd:cd17645 229 KIERKGYKLVNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEALQLQPIGVAGELCIAGE--GLAR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 539 TvYGNH-----ERFEATYFRKFPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSH 613
Cdd:cd17645 301 G-YLNRpeltaEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119488996 614 PHPVKGECLYCFVTLREghvftPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKIMRRVL 678
Cdd:cd17645 380 EDADGRKYLVAYVTAPE-----EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
318-684 |
4.60e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.18 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 318 AEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIGwitgHSY-VTYG---PLANGATSVLF 393
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPNDRFMSALPLF----HSFgLTVGlftPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 394 EGIPTYPDVSRLwnIVDKYKVTKFYTApTAIRLLMKFGdepvNKYSRASLRVLgtvgepinpeawlwyhrVVGAQRC-PI 472
Cdd:PRK08043 439 PSPLHYRIVPEL--VYDRNCTVLFGTS-TFLGNYARFA----NPYDFARLRYV-----------------VAGAEKLqES 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 473 VDTFWQTETGGHMLTPLpGAT----------PM--KPGSA----------TFPFFGVA---------PAILNEsgeeleg 521
Cdd:PRK08043 495 TKQLWQDKFGLRILEGY-GVTecapvvsinvPMaaKPGTVgrilpgmdarLLSVPGIEqggrlqlkgPNIMNG------- 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 522 eaegYLVFKQPwpGIMRT-----VYGNHErfeatyfrkfPGYYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVE 596
Cdd:PRK08043 567 ----YLRVEKP--GVLEVptaenARGEME----------RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 597 SALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREGHvftpalAEELKKQVREKISP-IATPDYIQNAPGLPKTRSGKIMR 675
Cdd:PRK08043 631 QLALGVSPDKQHATAIKSDASKGEALVLFTTDSELT------REKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDF 704
|
....*....
gi 2119488996 676 RVLRKIAQN 684
Cdd:PRK08043 705 VTLKSMVDE 713
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
307-393 |
9.65e-07 |
|
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: 51.83 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 307 AEEECEPEWCD--AEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHEDDvfwctadigwitgHSYVTYGPL 384
Cdd:cd17639 74 NETECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAYLPL 140
|
90
....*....|...
gi 2119488996 385 AN----GATSVLF 393
Cdd:cd17639 141 AHifelAAENVCL 153
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
323-673 |
1.38e-06 |
|
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: 51.32 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 323 FILYTSGSTGKPKGVvHTTGGYMLYTATSFKYVFDFHEDDVFWCTadigwitghSYVTYGP--------LANGATSVLfe 394
Cdd:cd17654 122 YVIHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLT---------SPLTFDPsvveiflsLSSGATLLI-- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 395 gIPTYPDV--SRLWNIVDK-YKVTKFYTAPTairLLMKFGDEPVNKY--SR-ASLRVLGTVGE--PINPEAWLWYHRVVG 466
Cdd:cd17654 190 -VPTSVKVlpSKLADILFKrHRITVLQATPT---LFRRFGSQSIKSTvlSAtSSLRVLALGGEpfPSLVILSSWRGKGNR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 467 AQRCPIVDTfwqTETGGHMLT--------PLPGATPMkpgsatfpffgVAPAILNESGEELEGEAEGYLvfkqpwPGIMR 538
Cdd:cd17654 266 TRIFNIYGI---TEVSCWALAykvpeedsPVQLGSPL-----------LGTVIEVRDQNGSEGTGQVFL------GGLNR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 539 TVY--GNHERFEATYfrkfpgyYVTGDGCRRdEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVVSHphp 616
Cdd:cd17654 326 VCIldDEVTVPKGTM-------RATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS--- 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2119488996 617 vKGECLYCFvtlregHVFTPALAEELKKQVREKISPIATPDYIQNAPGLPKTRSGKI 673
Cdd:cd17654 395 -DQQRLIAF------IVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
112-411 |
1.50e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 51.64 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 112 EKKLGDRVAfywEGNEPGEATQITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAG 191
Cdd:PLN02736 60 YKYLGTRIR---VDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 192 FSADSLceRILDSSCTLlitADAFYRGEKLVNLKELVDDalhkcrekgFPVKRCIVVkhlgraeLGTGDSPSHSPPLKRP 271
Cdd:PLN02736 137 LGPDAV--KFIVNHAEV---AAIFCVPQTLNTLLSCLSE---------IPSVRLIVV-------VGGADEPLPSLPSGTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 272 CQ-----DLQDKMKAKPMSKRPQIPwnqgvdlwwheilgdaeeecepewcdaEDPLFILYTSGSTGKPKGVVHTTGGYML 346
Cdd:PLN02736 196 VEivtysKLLAQGRSSPQPFRPPKP---------------------------EDVATICYTSGTTGTPKGVVLTHGNLIA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 347 YTATSfkyvfdfhEDDVFWCTADIgwitghsYVTYGPLAN-------------GATSVLFEG------------IPT-YP 400
Cdd:PLN02736 249 NVAGS--------SLSTKFYPSDV-------HISYLPLAHiyervnqivmlhyGVAVGFYQGdnlklmddlaalRPTiFC 313
|
330
....*....|..
gi 2119488996 401 DVSRLWN-IVDK 411
Cdd:PLN02736 314 SVPRLYNrIYDG 325
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
303-458 |
2.36e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 50.67 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 303 ILGDAEEECEPEWCDAEDPLFILYTSGSTGKPKGVVhttggymlYTATSFKYVFDFHEDDVFWCTADIGWITGHSYVTYG 382
Cdd:PRK09274 158 LRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVV--------YTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFG 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 383 PlANGATSVLFEGIPTYP---DVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEpvNKYSRASLRVLGTVGEPINPEAW 458
Cdd:PRK09274 230 P-ALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLRRVISAGAPVPIAVI 305
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
133-216 |
4.24e-06 |
|
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: 49.66 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 133 QITYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARLGALHSIVFAGFSADSL--CERIldSSCTLLI 210
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLahCLNV--SSAKHLV 80
|
....*.
gi 2119488996 211 TADAFY 216
Cdd:cd05940 81 VDAALY 86
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
598-690 |
1.48e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 47.84 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 598 ALVEHRAIAEAAVVSHPHPVKGECLYCFVTLREghvftPALAEELKKQVREKISPIAtPDYIQNAPGLPKTRSGKIMRRV 677
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFVEAEL-----PADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|...
gi 2119488996 678 LRKIAQNDHDLGD 690
Cdd:PRK09188 322 LRLIAMNQIDELD 334
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
318-611 |
3.19e-05 |
|
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: 47.07 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 318 AEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATsFKYVFDFHEDDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 397
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA-LRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 398 TYP---DVSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSraSLRVLGTVGEPINPEAWLWYHRVVgAQRCPIVD 474
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLP--SLRRVLSAGAPVPIALAARLRKML-SDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 475 TFWQTET------GGHMLTPLPGATPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLVfkQPW---------PGI 536
Cdd:cd05910 232 PYGATEAlpvssiGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGeigeitvtgPTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 537 MRTVYGnheRFEATYFRKFPG-----YYVTGDGCRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAAVV 611
Cdd:cd05910 309 TPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
317-453 |
4.41e-04 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 43.50 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHTTGGyMLYTATSFKYVFDFHEDDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 393
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 394 EGIPTYPD------------VSRLW-----NIVDKYK--------------------------------VTKFYTApTAI 424
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWeslysGIQKQVSksspikqflflfflsggifkfgisgggalpphVDTFFEA-IGI 238
|
170 180 190
....*....|....*....|....*....|..
gi 2119488996 425 RLLMKFG---DEPVNKYSRASLRVLGTVGEPI 453
Cdd:cd17640 239 EVLNGYGlteTSPVVSARRLKCNVRGSVGRPL 270
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
135-364 |
6.04e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.27 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 135 TYRELLTQVCRCANALRKQGIRKGDRVSIYMPMILELVVAMLACARlgalHSIVfagfsadslCERILDsscTLlitada 214
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAA----HSLI---------CVPLYD---TL------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 215 fyrGEKLVNLkeLVDDAlhkcrEKGFPVKRCIVVKHLGRAELGTGDSPSHSPPLKRPCQDLQDK---MKAKPMSkrpqip 291
Cdd:PLN02430 136 ---GPGAVDY--IVDHA-----EIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKasqIGVKTYS------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 292 wnqgvdlwWHEILGDAEEecEPEWCDAEDPL---FILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFHE----DDVF 364
Cdd:PLN02430 200 --------WIDFLHMGKE--NPSETNPPKPLdicTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDkmthDDVY 269
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
532-670 |
7.67e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.78 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 532 PWPGIMRTVYGNHERFEATyfrkfpGYYVtgdgcRRDEDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHRAIAEAavV 611
Cdd:PRK07868 822 PTASVKRGVFAPADTWIST------EYLF-----RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLA--V 888
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 612 SHPHPVKGECL-YCFVTLREGHVFTPA-LAEELkkqvrEKISPIATPDYIQNAPGLPKTRS 670
Cdd:PRK07868 889 TYGVEVGGRQLaVAAVTLRPGAAITAAdLTEAL-----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
561-679 |
1.09e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 561 TGD-GCRRDedGYYWITGRIDDMLNVSGHLLSTAEVESALVEhraiaEAAVVShphpvKGECLYCFVTL--REGhvftPA 637
Cdd:PRK05691 433 TGDlGFLRD--GELFVTGRLKDMLIVRGHNLYPQDIEKTVER-----EVEVVR-----KGRVAAFAVNHqgEEG----IG 496
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2119488996 638 LAEELKKQVREKISPIATPDYIQNA----------------PG-LPKTRSGKIMRRVLR 679
Cdd:PRK05691 497 IAAEISRSVQKILPPQALIKSIRQAvaeacqeapsvvlllnPGaLPKTSSGKLQRSACR 555
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
134-411 |
1.33e-03 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 41.82 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 134 ITYRELLTQVCRCANALRKQGIR--KGDRVSIYMPMILELVVAMLACARlgalHSIV----FAGFSADSLCERILDSSCT 207
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYA----YSLVtvplYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 208 LLITADafyrGEKLVNLKELVDdalhkcrekgfpvkrcivvkhlgraeLGTGDSPSHSPPlkrpcqdlqdkmkakpmskr 287
Cdd:cd05927 82 IVFCDA----GVKVYSLEEFEK--------------------------LGKKNKVPPPPP-------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 288 pqipwnqgvdlwwheilgdaeeecepewcDAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYVFDFH---EDDVf 364
Cdd:cd05927 112 -----------------------------KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDV- 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119488996 365 wctadigwitghsYVTYGPLAN---------------------GATSVLFEGI----PTY-PDVSRLWN-IVDK 411
Cdd:cd05927 162 -------------YISYLPLAHifervvealflyhgakigfysGDIRLLLDDIkalkPTVfPGVPRVLNrIYDK 222
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
130-184 |
3.48e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.79 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2119488996 130 EATQITYRELLTQVCRCANALR-KQGIRKGDRVSIYMPMILELVVAMLACARLGAL 184
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVV 66
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
319-337 |
7.55e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.49 E-value: 7.55e-03
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
317-447 |
9.98e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 39.03 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119488996 317 DAEDPLFILYTSGSTGKPKGVVHTTGGYMLYTATSFKYvFDFHEDDVFWCTADIGWITGHSYVTYGPLANGaTSVLFEGI 396
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF-FSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG-VPVVFAYN 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119488996 397 PTYPdvSRLWNIVDKYKVTKFYTAPTAIRLLMKFGDEPVNKYSRASLRVLG 447
Cdd:PRK06334 259 PLYP--KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIG 307
|
|
| |
