|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-721 |
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: 1172.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFlrynfDVTKGKIFIEWMKGATTNICYNVLDRNVHekKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 125 WstsgnssyrytcrEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVF 204
Cdd:cd05966 74 W-------------EGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 205 AGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAelgmgdstsqsppik 284
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE--------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 285 rscpdvqgklkekskrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVA 364
Cdd:cd05966 202 --------------------VPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 365 TTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMK 444
Cdd:cd05966 262 TTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 445 FGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAP 524
Cdd:cd05966 342 FGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 525 AILNESGEELEGEAEGYLllrtetswleVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRI 604
Cdd:cd05966 422 AILDEEGNEVEGEVEGYL----------VIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRV 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 605 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYI 684
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKI 571
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462580884 685 QNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVAD 721
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-728 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1097.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 31 PPPEVSRSAHVpSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPcpgpflrYNFDVTKGKIFIEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 111 NVHEKklGDKVAFYWstsgnssyrytcrEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM 190
Cdd:PRK00174 76 HLKTR--GDKVAIIW-------------EGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 191 LACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQekgfPVRCCIVVKHLGrae 270
Cdd:PRK00174 141 LACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 271 lgmGDstsqsppikrscpdvqgklkekskrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPK 350
Cdd:PRK00174 214 ---GD-----------------------------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPK 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 351 GVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVT 430
Cdd:PRK00174 262 GVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 431 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPM 510
Cdd:PRK00174 342 IFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 511 KPGSATFPFFGVAPAILNESGEELEGEAEGYLllrtetswleVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGC 590
Cdd:PRK00174 422 KPGSATRPLPGIQPAVVDEEGNPLEGGEGGNL----------VIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGA 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 591 QRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQ 670
Cdd:PRK00174 492 RRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNW 571
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580884 671 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHL 728
Cdd:PRK00174 572 VRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
43-728 |
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: 1016.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 43 SLQRYRELHRRSVEEPREFWGDIAKE-FYWKTPcpgpflrynFDVTK---GKIFIEWMKGATTNICYNVLDRnvHEKKLG 118
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFKP---------FTKVLdwsFPPFYKWFVGGELNVSYNCVDR--HLEARP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 119 DKVAFYWstsgnssyrytcrEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA 198
Cdd:TIGR02188 72 DKVAIIW-------------EGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 199 LHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfpVRCCIVVKHLGraelgmgdsts 278
Cdd:TIGR02188 139 IHSVVFGGFSAEALADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 279 qsppikrscpdvqgklkekskrvQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGG 358
Cdd:TIGR02188 205 -----------------------NPVVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 359 YMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTA 438
Cdd:TIGR02188 262 YLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 439 IRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFP 518
Cdd:TIGR02188 342 IRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 519 FFGVAPAILNESGEELEGEAEGYLLlrtetswleVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYY 598
Cdd:TIGR02188 422 FFGIEPAVVDEEGNPVEGPGEGGYL---------VIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYI 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 599 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPI 678
Cdd:TIGR02188 493 WITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPI 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 679 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD-LGDMSTVADPSVISHL 728
Cdd:TIGR02188 573 AKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEiLGDTSTLEDPSVVEEL 623
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-728 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 878.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 31 PPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTP-CPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 110 RNVhEKKLGDKVAFYWstsgnssyrytcrEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVA 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYW-------------EGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 190 MLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVkhlgra 269
Cdd:PLN02654 162 MLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTY------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 270 elgmgdstsqsppikrscpDVQGKLKEKSKRvqpqisWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 349
Cdd:PLN02654 236 -------------------ENQLAMKREDTK------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 350 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKV 429
Cdd:PLN02654 291 KGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 430 TKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATP 509
Cdd:PLN02654 371 TIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 510 MKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLrtetswlevfKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDG 589
Cdd:PLN02654 451 QKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCV----------KKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDG 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 590 CQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKK 669
Cdd:PLN02654 521 CSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLIL 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 670 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD-LGDMSTVADPSVISHL 728
Cdd:PLN02654 601 TVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDeLGDTSTLADPGVVDQL 660
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
94-728 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 855.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 94 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWStsgnssyrytcregNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKG 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWE--------------GEDGEERTLTYAELRREVNRFANALRALGVKKG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 174 DRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEk 253
Cdd:COG0365 65 DRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 254 gfpVRCCIVVKHLGrAELGMGDstsqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDA 333
Cdd:COG0365 144 ---LEHVIVVGRTG-ADVPMEG------------------------------------DLDWDELLAAASAEFEPEPTDA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPT 413
Cdd:COG0365 184 DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 414 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQ 493
Cdd:COG0365 264 FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 494 TETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLllrtetswleVFKQPWPGIMRTVYGNHERFE 573
Cdd:COG0365 341 TETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGEL----------VIKGPWPGMFRGYWNDPERYR 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 574 TTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 653
Cdd:COG0365 410 ETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVL 489
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580884 654 CDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDMSTVADPSVISHL 728
Cdd:COG0365 490 KPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-699 |
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: 693.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCPGpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKklGDKVAFYWs 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIY- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 127 tsgnssyrytcrEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 206
Cdd:cd17634 75 ------------EGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 207 FSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKcqeKGFPVRCCIVVKhlgraelgmgdstsqsppikrs 286
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLK---------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 287 cpdvqgklkekskRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATT 366
Cdd:cd17634 198 -------------RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 367 FKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFG 446
Cdd:cd17634 265 MKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 447 DEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAI 526
Cdd:cd17634 345 DDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 527 LNESGEELEGEAEGYLllrtetswleVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDD 606
Cdd:cd17634 425 VDNEGHPQPGGTEGNL----------VITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDD 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQN 686
Cdd:cd17634 495 VINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHW 574
|
650
....*....|...
gi 2462580884 687 APGLPKTRSGKIM 699
Cdd:cd17634 575 VDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-728 |
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: 585.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 47 YRELHRRSVEEPREFWGDIAKEFYWKTP-------CPGPFLRynfdvtkgkifieWMKGATTNICYNVLDRNVhEKKLGD 119
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPpekildnSNPPFTR-------------WFVGGRLNTCYNALDRHV-EAGRGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 120 KVAFYWSTSgnssyrytcregnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 199
Cdd:cd05967 67 QIALIYDSP-------------VTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 200 HSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCciVVKHLGRAELGMGDStsq 279
Cdd:cd05967 134 HSVVFGGFAAKELASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHV--LVLNRPQVPADLTKP--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 280 sppikrscpdvqgklkekskrvqpqiswnqGIDLWWHELMQEAGdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGY 359
Cdd:cd05967 207 ------------------------------GRDLDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGH 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 360 MLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPT-YPDVNRLWSIVDKYKVTKFYTAPTA 438
Cdd:cd05967 256 AVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 439 IRLLMKF--GDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGS 514
Cdd:cd05967 336 IRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGS 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 515 ATFPFFGVAPAILNESGEElegeaegyllLRTETSWLEVFKQPW-PGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRD 593
Cdd:cd05967 413 PGKPVPGYQVQVLDEDGEP----------VGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKD 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 594 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIR 672
Cdd:cd05967 483 EDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVR 562
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 673 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDMSTVADPSVISHL 728
Cdd:cd05967 563 EQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
45-725 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 560.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPcPGPFLRYNfdvtkGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 125 W-STsgnssyrytcregnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIV 203
Cdd:PRK10524 74 AvST--------------ETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 204 FAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCCIVVKHLGRAElgmgdstsqsppi 283
Cdd:PRK10524 140 FGGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLAPMA------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 284 krscpdvqgklkekskrvqpqisWNQGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLY 362
Cdd:PRK10524 205 -----------------------RVAGRDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 363 VATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL 442
Cdd:PRK10524 262 LATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 443 MKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFF 520
Cdd:PRK10524 342 KKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMY 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 521 GVAPAILNESGEELEGEAEGYLLlrtetswleVFKQPW-PGIMRTVYGNHERFETTYFKKF-PGYYVTGDGCQRDQDGYY 598
Cdd:PRK10524 419 GYNVKLLNEVTGEPCGPNEKGVL---------VIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYY 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 599 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-----PKLTEELKKQIRE 673
Cdd:PRK10524 490 FILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDS 569
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2462580884 674 KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDLGDMSTVADPSVI 725
Cdd:PRK10524 570 QLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAE-GRDPGDLTTIEDPAAL 620
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-722 |
4.22e-173 |
|
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: 509.72 E-value: 4.22e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 44 LQRYRELHRRSVEEPREFWGDIAKEF-YWKTPCPGPFLrynfDVTKGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 123 FYWStsgnssyrytcregNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSI 202
Cdd:cd05968 80 LRWE--------------GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 203 VFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAELgmgdstsqspp 282
Cdd:cd05968 146 IFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 283 ikrscpdvqgklkekskrvqpqisWNQGIDLWWHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLY 362
Cdd:cd05968 211 ------------------------PAKGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 363 VATTFKYVFDFHAED-VFWCTaDIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRL 441
Cdd:cd05968 265 AAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 442 LMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSATFPFFG 521
Cdd:cd05968 343 LKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPG 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 522 VAPAILNESGEElegeaegyllLRTETSWLEVFKqPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWIT 601
Cdd:cd05968 422 MKADVLDESGKP----------ARPEVGELVLLA-PWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYIL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 602 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATP 681
Cdd:cd05968 491 GRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSP 570
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2462580884 682 DYIQNAPGLPKTRSGKIMRRVLRKiAQNDHDLGDMSTVADP 722
Cdd:cd05968 571 ERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
93-721 |
6.57e-172 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 505.20 E-value: 6.57e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 93 IEWMKGATTNICYNVLDRNVHEKkLGDKVAFYWSTsgnssyrytcregnePGETTQITYHQLLVQVCQFSNVLRKQGIQK 172
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLD---------------ASRKEKYTYKELKELSNKFANVLKELGVEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 173 GDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELadealqkcqe 252
Cdd:PRK04319 98 GDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 253 kgfpvrccivvKHLgraeLGMGDSTSQSPPIkrscpdvqgklkekskrvqpqiswnqgIDLWwhELMQEAGDECEPEWCD 332
Cdd:PRK04319 168 -----------KHV----LLVGEDVEEGPGT---------------------------LDFN--ALMEQASDEFDIEWTD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 412
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLH-VHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 tYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFW 492
Cdd:PRK04319 281 -RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWW 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 QTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLrtetswlevfKQPWPGIMRTVYGNHERF 572
Cdd:PRK04319 357 MTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI----------KKGWPSMMRGIWNNPEKY 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 573 ETtYFKkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 652
Cdd:PRK04319 426 ES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 653 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDMSTVAD 721
Cdd:PRK04319 503 LRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
150-707 |
1.40e-134 |
|
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: 404.58 E-value: 1.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDa 229
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 230 fyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgKLKEKSkrvqpqiswnq 309
Cdd:cd05969 81 ---------------------------------------------------------------ELYERT----------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 310 gidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 389
Cdd:cd05969 87 ----------------------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 390 GHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPIN 469
Cdd:cd05969 144 GTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 470 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTEts 549
Cdd:cd05969 221 PEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPG-- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 550 wlevfkqpWPGIMRTVYGNHERFETtYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 629
Cdd:cd05969 295 --------WPSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPA 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580884 630 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:cd05969 364 VAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-611 |
9.32e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.88 E-value: 9.32e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 142 EPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSC 221
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 222 SLLITTDAFYrgeklvnlkelaDEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIkrscpdvqgklkekskrv 301
Cdd:pfam00501 95 KVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADV------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 302 qpqiswnqgidlwwhelmqeagDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVgGYMLYVATTFKYV----FDFHAED 377
Cdd:pfam00501 145 ----------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraS 457
Cdd:pfam00501 202 RVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--S 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 458 LQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSATFPFFGVAPAILNESGEELEG 536
Cdd:pfam00501 279 LRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDETGEPVP 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 537 EAEG-YLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS 611
Cdd:pfam00501 356 PGEPgELCVRG------------PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
150-705 |
6.52e-103 |
|
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: 322.36 E-value: 6.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLIttda 229
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 230 fyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswnq 309
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 310 gidlwwhelmqeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGgYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 389
Cdd:cd05972 78 ---------------------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 390 GHSYVTYGPLANGATSVLFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvtKHSRASLQVLGTVGEPIN 469
Cdd:cd05972 136 GAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 470 PEAWLWYHRVVGAqrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTets 549
Cdd:cd05972 211 PEVIEWWRAATGL---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKL--- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 550 wlevfkqPWPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 629
Cdd:cd05972 283 -------PPPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 630 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05972 353 VAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-706 |
3.50e-83 |
|
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: 276.46 E-value: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 40 HVPSLQRYRELHRRSVEEPREFWGDIAKefYWKTPCPGPflrYNFDVTKGKIF--IEWMKGATTNICYNVLDRNVHEkkl 117
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 118 gDKVAFYWStsgnssyrytcregnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 197
Cdd:cd05943 84 -DPAAIYAA---------------EDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 198 ALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKEladealqKCQE--KGFPVRCCIVVkhlgraelgmgd 275
Cdd:cd05943 148 AIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVRE-------KVAElvKGLPSLLAVVV------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 276 stsqsppIKRSCPDVQGKLKEKSKRVqpqiswnqgidLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT 355
Cdd:cd05943 209 -------VPYTVAAGQPDLSKIAKAL-----------TLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 356 VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTA 435
Cdd:cd05943 271 AGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 436 PTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGGhmlTPLPGA-------T 508
Cdd:cd05943 349 AKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 509 PMKPGSATFPFFGVAPAILNESGEElegeaegyllLRTETSWLeVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYV 585
Cdd:cd05943 420 PVYRGEIQCRGLGMAVEAFDEEGKP----------VWGEKGEL-VCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWA 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 586 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTE 665
Cdd:cd05943 488 HGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRK 567
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2462580884 666 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 706
Cdd:cd05943 568 RIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
335-699 |
7.06e-83 |
|
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: 266.46 E-value: 7.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 414
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 415 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQT 494
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 495 ETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTEtswlevfkQPWPGimrtvYGNHErfET 574
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP--------SVMKG-----YWNNP--EA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 575 TYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC 654
Cdd:cd04433 215 TAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462580884 655 DGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 699
Cdd:cd04433 295 PGADLDA---EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
149-705 |
3.71e-78 |
|
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: 257.45 E-value: 3.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERiLDSSCSLLITTD 228
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AFYRgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 308
Cdd:cd05973 80 AANR---------------------------------------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 qgidlwwHELmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWI 388
Cdd:cd05973 84 -------HKL--------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWA 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 389 TGHSYVTYGPLANGATSVLFEGIPTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPI 468
Cdd:cd05973 142 YGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 469 NPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTET 548
Cdd:cd05973 218 TPEVIRWFDAALGV---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIAN 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 549 SWLEVFKQPWPGIMRTVYGnherfettyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 628
Cdd:cd05973 295 SPLMWFRGYQLPDTPAIDG--------------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHP 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580884 629 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05973 361 AVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
145-711 |
1.43e-77 |
|
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: 256.28 E-value: 1.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSL 223
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL-AYILeDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqp 303
Cdd:COG0318 100 LVT----------------------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqgidlwwhelmqeagdecepewcdaedpLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 383
Cdd:COG0318 103 ---------------------------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVAL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 384 DIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGT 463
Cdd:COG0318 149 PLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLR--HPEFARYDLSSLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLL 543
Cdd:COG0318 223 GGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 544 LRTetswlevfkqpwPGIMRTVYGNHERFEttyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 622
Cdd:COG0318 300 VRG------------PNVMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEE 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 623 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 702
Cdd:COG0318 364 VLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRA 440
|
....*....
gi 2462580884 703 LRKIAQNDH 711
Cdd:COG0318 441 LRERYAAGA 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-705 |
9.38e-75 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 254.28 E-value: 9.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 57 EPREFWGDIAKEF-YWKTpcpgpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYwstsgnssyrY 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALI----------Y 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 136 TCregneP--GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLC 213
Cdd:PTZ00237 83 EC-----PylKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 214 ERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRcciVVKHLgraelgMGDSTSQSppikrscpdvQGK 293
Cdd:PTZ00237 158 DRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFK--PSN---VITLF------RNDITSES----------DLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 294 LKEKSKRVQPQISWNQGIDLWwHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF 373
Cdd:PTZ00237 217 KIETIPTIPNTLSWYDEIKKI-KENNQSPFYEYVP--VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 374 HAEDVFWCTADIGWITGHSYVtYGPLANGATSVLFEGIPTYPDV--NRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVT 451
Cdd:PTZ00237 294 DIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 452 KHSR---ASLQVLGTVGEPINPEAWLWYHRVVGAqRCPIVdtFWQTETGghMLTPLPGATPMKPGSAT-FPFFGVAPAIL 527
Cdd:PTZ00237 373 IRSKydlSNLKEIWCGGEVIEESIPEYIENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSIL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 528 NESGEElegeaegylLLRTETSWLeVFKQPWP-GIMRTVYGNHERFETTyFKKFPGYYVTGDGCQRDQDGYYWITGRIDD 606
Cdd:PTZ00237 448 SEDGKE---------LNVNEIGEV-AFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP----KLTEELKKQIREKIGPIATPD 682
Cdd:PTZ00237 517 QIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLR 596
|
650 660
....*....|....*....|...
gi 2462580884 683 YIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PTZ00237 597 KIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-703 |
9.37e-74 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 252.02 E-value: 9.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 29 WSPPPEVSRSAHVPSLQR------------YRELHRRSVEEPREFWGDIAkEFY---WKTPCPgpflrynfDVTKGKIFI 93
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYT--------VVLAGRRMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 94 --EWMKGATTNICYNVLdRNvhekKLGDKVAFYwstsgnssYRytcregNEPGETTQITYHQLLVQVCQFSNVLRKQGIQ 171
Cdd:PRK03584 77 gaRWFPGARLNYAENLL-RH----RRDDRPAII--------FR------GEDGPRRELSWAELRRQVAALAAALRALGVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 172 KGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVN----LKELADeal 247
Cdd:PRK03584 138 PGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRA--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 248 qkcqekGFP-VRCCIVVKHLGRAELGmgdstsqsPPIKRSCPdvqgklkekskrvqpqiswnqgidlwWHELMQEAGD-E 325
Cdd:PRK03584 215 ------ALPsLEHVVVVPYLGPAAAA--------AALPGALL--------------------------WEDFLAPAEAaE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 326 CEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAED-VFWCTAdIGWITGHSYVtyGPLANGAT 404
Cdd:PRK03584 255 LEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGAT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 405 SVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqr 484
Cdd:PRK03584 332 LVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 485 cpivDTFWQTETGG-HMLTPLPGATPMKP---GSATFPFFGVAPAILNESGEElegeaegyllLRTETSWLeVFKQPWPG 560
Cdd:PRK03584 410 ----DVWLASISGGtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRP----------VVGEVGEL-VCTKPFPS 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 561 iMrTVY----GNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 636
Cdd:PRK03584 475 -M-PLGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVI 552
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 637 GHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM----RRVL 703
Cdd:PRK03584 553 GQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-708 |
1.03e-62 |
|
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: 221.68 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 39 AHVPSLQRYRELHRRSVEEPREFWGDIAKEFywKTPCPGPFLRYnFDVTKGkIFIEWMKGATTNICYNVLdrnvhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 119 DKVAFYWStsgnssyrytcregnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA 198
Cdd:TIGR01217 100 EPALLYVD---------------ETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 199 LHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKlvnlKELADEALQKCQeKGFP-VRCCIVVKHLgraelgmGDST 277
Cdd:TIGR01217 165 IWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYL-------GPRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 278 SQSPPIKRScpdvqgklkekskrvqpqiswnqgidLWWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTV 356
Cdd:TIGR01217 233 TEAPKIDGA--------------------------LDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 357 GGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAP 436
Cdd:TIGR01217 287 GGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 437 TAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGATPMKP--- 512
Cdd:TIGR01217 365 KYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhi 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 513 GSATFPFFGVAPAILNESGEElegeaegyllLRTETSWLeVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDG 589
Cdd:TIGR01217 439 GEIQAPGLGTAVQSWDPEGKP----------VTGEVGEL-VCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDW 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 590 CQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKK 669
Cdd:TIGR01217 507 ITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKR 586
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462580884 670 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 708
Cdd:TIGR01217 587 TIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQ 625
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-705 |
7.20e-62 |
|
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: 216.56 E-value: 7.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 102 NICYNVLDRNVHEKKLGDKV---AFYWStsgnssyrytcregNEPGETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVA 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV--------------NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 178 IYMPMIPELVVAMLACARIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladeaLQKCQEKgfpv 257
Cdd:cd05928 72 VILPRVPEWWLVNVACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK---- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 258 rcCIVVkhlgraelgmGDSTSQS-PPIKRSCPDVQGKLkekskRVQPQiSWNQGIDLwwHELMQEAGDECEPEWCDAEDP 336
Cdd:cd05928 117 --CIVT----------SDELAPEvDSVASECPSLKTKL-----LVSEK-SRDGWLNF--KELLNEASTEHHCVETGSQEP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 337 LFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpD 416
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-D 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 417 VNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTET 496
Cdd:cd05928 255 PLVILKTLSSYPITTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTET 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 497 GghMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETSwlevfkQPWpGIMRTVYGNHERFETTY 576
Cdd:cd05928 329 G--LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPI------RPF-GLFSGYVDNPEKTAATI 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 577 FKKFpgyYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC-D 655
Cdd:cd05928 400 RGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQ 476
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 656 GHTFSP-KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05928 477 FLSHDPeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
144-704 |
2.86e-61 |
|
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: 212.29 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqp 303
Cdd:cd05971 82 LVT----------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqgidlwwhelmqeagDEcepewcdAEDPLFILYTSGSTGKPKGVVHT-------VGGYMLYvattfkyvFDF--H 374
Cdd:cd05971 85 --------------------DG-------SDDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpR 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 375 AEDVFWCTADIGWItghsyvtyGPLANGATSVLFEGIP------TYPDVNRLWSIVDKYKVTKFYTAPTAIRLlMKFGDE 448
Cdd:cd05971 130 DGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGE 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 449 PVtKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 528
Cdd:cd05971 201 QL-KHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVD 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 529 ESGEElegeaegylLLRTETSWLEVfKQPWPGIMRTVYGNHERFEttyfKKFPG-YYVTGDGCQRDQDGYYWITGRIDDM 607
Cdd:cd05971 276 DNGTP---------LPPGEVGEIAV-ELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 608 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNA 687
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFV 421
|
570
....*....|....*..
gi 2462580884 688 PGLPKTRSGKIMRRVLR 704
Cdd:cd05971 422 NELPRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
105-704 |
3.30e-57 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 202.98 E-value: 3.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 105 YN---VLDRNVhEKKLGDKVAFYwstsgnssyrytcregnepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMP 181
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI-------------------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIML 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 182 MIPELVVAMLACARIGALhSIVFAGFSSESLCERIL-DSSCSLLITTDAFYrgeklvnlkELADEALqkcqEKGFPVRCC 260
Cdd:cd05959 63 DTVDFPTAFLGAIRAGIV-PVPVNTLLTPDDYAYYLeDSRARVVVVSGELA---------PVLAAAL----TKSEHTLVV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 261 IVVkhlgraelgmgdstsqsppikrscpdVQGKLkekskrvqpqiswNQGIDLWWHELMQEAGDECEPEWCDAEDPLFIL 340
Cdd:cd05959 129 LIV--------------------------SGGAG-------------PEAGALLLAELVAAEAEQLKPAATHADDPAFWL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 341 YTSGSTGKPKGVVHTVGGyMLYVATTF-KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnR 419
Cdd:cd05959 170 YSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--A 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 420 LWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGH 499
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 500 MLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwpGIMRTVYGNheRFETTYfKK 579
Cdd:cd05959 321 FLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRG-------------PSSATMYWN--NRDKTR-DT 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 580 FPGYYV-TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 658
Cdd:cd05959 383 FQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE 462
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2462580884 659 FSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05959 463 DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-710 |
3.69e-56 |
|
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: 200.80 E-value: 3.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 102 NICYNVLDRNVHEKKlgDKVAFYWStsgnssyrytcregNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMP 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVWC--------------DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 182 MIPELVVAMLACARIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladealqkCQEKGFPVRCCI 261
Cdd:cd05970 81 RRYEFWYSLLALHKLGA-----------------IAIPATHQLTAKDIVYR-----------------IESADIKMIVAI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 262 vvkhlgrAELGMGDSTSQSPPikrSCPDvqgklkeKSKRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDA---EDPLF 338
Cdd:cd05970 127 -------AEDNIPEEIEKAAP---ECPS-------KPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYpcgEDILL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 339 ILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvn 418
Cdd:cd05970 190 VYFSSGTTGMPKMVEH-DFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 419 RLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGG 498
Cdd:cd05970 267 ALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 499 HMLTpLPGATPmKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETswlevfKQPWpGIMRTVYGNHERFETTYFK 578
Cdd:cd05970 341 TIAT-FPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSK------GKPV-GLFGGYYKDAEKTAEVWHD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 579 kfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 658
Cdd:cd05970 412 ---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYE 488
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2462580884 659 FSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKImRRVlrKIAQND 710
Cdd:cd05970 489 PSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-RRV--EIRERD 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
149-704 |
4.41e-54 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 192.68 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 228
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 afyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 308
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 qgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI--G 386
Cdd:cd05919 89 -----------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffG 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 387 WITGHSyvTYGPLANGATSVLFegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGE 466
Cdd:cd05919 146 YGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 467 PInPEAwLWYhRVVGAQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRT 546
Cdd:cd05919 219 AL-PRG-LGE-RWMEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 547 ETswleVFKQPWpgimrtvygnhERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 626
Cdd:cd05919 294 PS----AAVGYW-----------NNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQ 358
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580884 627 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05919 359 HPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
142-700 |
3.79e-50 |
|
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: 181.65 E-value: 3.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 142 EPGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSC 221
Cdd:cd17631 16 FGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 222 SLLIttdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrv 301
Cdd:cd17631 94 KVLF---------------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 302 qpqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWC 381
Cdd:cd17631 98 --------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLV 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 382 TADIGWITGHSYVTYGPLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVL 461
Cdd:cd17631 145 VAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 462 GTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGY 541
Cdd:cd17631 219 IYGGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 542 LLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 621
Cdd:cd17631 295 IVVRG------------PHVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVE 359
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 622 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 700
Cdd:cd17631 360 DVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-704 |
6.09e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 183.08 E-value: 6.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 105 YNVLDRNVheKKLGDKVAFYWstsgnssyrytcregnepgETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIP 184
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYF-------------------DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 185 ELVVAMLACARIGA-LHSIVFagFSSESLCERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEalqkcqekgfpVRCCI 261
Cdd:PRK06187 68 EYLEAYFAVPKIGAvLHPINI--RLKPEEIAYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------VRTVI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 262 VVKHLGRAELGmgdstsqsppikrscPDVQGklkekskrvqpqiswnqgidlwWHELMQEAGDEcePEWCDAE--DPLFI 339
Cdd:PRK06187 132 VEGDGPAAPLA---------------PEVGE----------------------YEELLAAASDT--FDFPDIDenDAAAM 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 340 LYTSGSTGKPKGVV--------HTVGGymlyvattfKYVFDFHAEDVF-----------WctadiGWitghsyvTYGPLA 400
Cdd:PRK06187 173 LYTSGTTGHPKGVVlshrnlflHSLAV---------CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALM 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 401 NGATSVlfegIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVV 480
Cdd:PRK06187 232 AGAKQV----IPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKF 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 481 GaqrCPIVDTFWQTETGG--HMLTPLPGATPM--KPGSATFPFFGVAPAILNESGEElegeaegylLLRTETSWLEV-FK 555
Cdd:PRK06187 306 G---IDLVQGYGMTETSPvvSVLPPEDQLPGQwtKRRSAGRPLPGVEARIVDDDGDE---------LPPDGGEVGEIiVR 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 556 QPWpgIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 635
Cdd:PRK06187 374 GPW--LMQGYWNRPEATAETIDG---GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAV 448
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 636 VGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK06187 449 IGVPDEKWGERPVAVVVLKPGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
143-705 |
5.46e-49 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 179.82 E-value: 5.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 143 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCS 222
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAFYRGEKLVNLKELAdealqkcqekgfpvrccivvkhLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQ 302
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLG----------------------LAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGV--VHT-VGGYMLYVATTFKYVFD------- 372
Cdd:cd05926 146 PL----------------------------PDDLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvm 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 373 --FHaedvfwctadigwITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTkFYTA-PTAIRLLMKFgDEP 449
Cdd:cd05926 198 plFH-------------VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHM-LTPLPgATPMKPGSATFPFfGVAPAILN 528
Cdd:cd05926 259 NPESPPPKLRFIRSCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 529 ESGEELEGEAEGYLLLRTETswlevfkqpwpgIMRTVYGNHE-RFEttYFKKFpGYYVTGDGCQRDQDGYYWITGRIDDM 607
Cdd:cd05926 334 EDGEILPPGVVGEICLRGPN------------VTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKEL 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 608 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHtfsPKLTEELKKQIREKIGPIATPDYIQNA 687
Cdd:cd05926 399 INRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFV 475
|
570
....*....|....*...
gi 2462580884 688 PGLPKTRSGKIMRRVLRK 705
Cdd:cd05926 476 DELPKTATGKIQRRKVAE 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
333-704 |
1.12e-47 |
|
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: 174.97 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 412
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 TYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFW 492
Cdd:cd05958 174 ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 QTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETSWlevfkqpwpgimrtvYGNHERF 572
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGC---------------RYLADKR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 573 ETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 652
Cdd:cd05958 310 QRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462580884 653 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05958 388 LRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-704 |
6.11e-47 |
|
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: 173.52 E-value: 6.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 105 YNVLDRNVheKKLGDKVAFYWstsgnssyrytcregnePGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIP 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIF-----------------MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 185 ELVVAMLACARIGAlhsIVfagfsseslcerildsscsllITTDAFYRGEklvnlkELAdEALQKCQEKGfpvrccIVVk 264
Cdd:cd05936 61 QFPIAYFGALKAGA---VV---------------------VPLNPLYTPR------ELE-HILNDSGAKA------LIV- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 265 hlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSG 344
Cdd:cd05936 103 -----------------------------------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSG 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 345 STGKPKGVVHTVGGYMLYVATTFKYVFDFH-AEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPD 416
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FR 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 417 VNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTET 496
Cdd:cd05936 205 PIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTET 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 497 G--GHmLTPLPGatPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERFET 574
Cdd:cd05936 280 SpvVA-VNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRG------------PQVMKGYWNRPEETAE 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 575 TyFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC 654
Cdd:cd05936 345 A-FVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK 421
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2462580884 655 DGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05936 422 EGASLTE---EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
324-704 |
1.06e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 171.71 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 324 DECEPEWCDAeDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLAN 401
Cdd:cd05934 72 DHSGAQLVVV-DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 402 GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgTVGEPINPEAWLWYHRVVG 481
Cdd:cd05934 148 GATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFEERFG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 482 aqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTEtswlevfkQPWpGI 561
Cdd:cd05934 220 ---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGL--------RGW-GF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 562 MRTVYGNHErfETTyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 640
Cdd:cd05934 286 FKGYYNMPE--ATA--EAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPD 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462580884 641 PVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05934 362 EVGEDEVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
333-707 |
4.33e-45 |
|
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: 167.36 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFkYVFDFHAEDVFWCTADIGWiTGHSYVT-YGPLANGATSVLFegi 411
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 412 pTYP--DVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHRVVGAQRCPIVD 489
Cdd:cd05974 159 -NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQVRRAWGLTIRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 490 TFWQTETgghmlTPLPGATP---MKPGSATFPFFGVAPAILNESGEELegeaegylllrTETSWLEVFKQPWP-GIMRTV 565
Cdd:cd05974 231 GYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPA-----------TEGEVALDLGDTRPvGLMKGY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 566 YGNHERfetTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 645
Cdd:cd05974 295 AGDPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLS 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462580884 646 CLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 707
Cdd:cd05974 372 VPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
131-705 |
3.01e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 163.95 E-value: 3.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 131 SSYRYTCREGNEPGETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 210
Cdd:PRK08316 20 SARRYPDKTALVFGDRS-WTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 211 SLCeRILDSSCSLLITTDAfyrgeklvNLKELADEALQKCQEKGFPVRCcivVKHLGRAELGMGDstsqsppikrscpdv 290
Cdd:PRK08316 99 ELA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL---VLGGREAPGGWLD--------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 291 qgklkekskrvqpqiswnqgIDLWwhelmQEAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----VGGYMLYVAT 365
Cdd:PRK08316 152 --------------------FADW-----AEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 366 TfkyvfDFHAEDVFWCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTA-IR 440
Cdd:PRK08316 207 G-----DMSADDIPLHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwIS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 441 LLmkfgdepvtKH---SRASLQVL--GTVGEPINPEAWLwyHRVvgAQRCPIVdTFW----QTETGghmltplPGATPM- 510
Cdd:PRK08316 274 LL---------RHpdfDTRDLSSLrkGYYGASIMPVEVL--KEL--RERLPGL-RFYncygQTEIA-------PLATVLg 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 511 ------KPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETSWLEVFKQPwpgimrtvygnhERFETTyFKKfpGYY 584
Cdd:PRK08316 333 peehlrRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDP------------EKTAEA-FRG--GWF 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 585 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPklt 664
Cdd:PRK08316 398 HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE--- 474
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2462580884 665 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK08316 475 DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
145-699 |
2.28e-42 |
|
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: 160.84 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITTDAFYrgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSqsppikrscpdvqgklkekskrvqpq 304
Cdd:cd05911 87 FTDPDGL-------------EKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLS-------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 isWNQGIDLWWHELMQEAGDEcepewcdaeDPLFILYTSGSTGKPKGVV--HTVGGYMLYVATTFKYVfDFHAEDVFWCT 382
Cdd:cd05911 128 --PTLGEEDEDLPPPLKDGKD---------DTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 383 ADIGWITG-HSYVTYgpLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVL 461
Cdd:cd05911 196 LPLYHIYGlFTTLAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 462 GTVGEPINPEAwlwYHRV-VGAQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELegeaeg 540
Cdd:cd05911 268 LSGGAPLSKEL---QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDS------ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 541 ylLLRTETSWLEV-FKQPWPGimrtVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 619
Cdd:cd05911 337 --LGPNEPGEICVrGPQVMKG----YYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 620 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsPKLTE-ELKKQIREKIgpiatPDY------IQNAPGLPK 692
Cdd:cd05911 409 LEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPK 479
|
....*..
gi 2462580884 693 TRSGKIM 699
Cdd:cd05911 480 SASGKIL 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
102-705 |
1.80e-40 |
|
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: 155.77 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 102 NICYNVLDRNVHEKKlGDKVAFYWSTSgnssyrytcregnepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMP 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFIDDIS-------------------SLSYGELEAQVRRLAAALRRLGVKREERVLLLML 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 182 MIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkeladealqkcqekgfpvrcci 261
Cdd:TIGR02262 64 DGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL------------------------------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 262 vvkhlgraelgmgdstsqsPPIKrscpDVQGKLKEKSKRVQPQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILY 341
Cdd:TIGR02262 114 -------------------PVIK----AALGKSPHLEHRVVVGRPEAGEVQL--AELLATESEQFKPAATQADDPAFWLY 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 342 TSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLW 421
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVF 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 422 SIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHML 501
Cdd:TIGR02262 246 DRLRRHQPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 502 TPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETSwlevfkqpwpGIMrtVYGNHERFETTYFKkfp 581
Cdd:TIGR02262 321 SNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSS----------ATM--YWNNRAKSRDTFQG--- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHT 658
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT 460
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2462580884 659 fspKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:TIGR02262 461 ---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
149-723 |
9.90e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 146.64 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAcariGALHSIVFA---GFSSESLCErildsscsLLI 225
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TTDAfyrgEKLVNLKELAD-EALQKCQEKgfpVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQGKLkekskrvqpq 304
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGtDIWQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARI---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 ISWNQgidlwwhELMQEAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 383
Cdd:PRK07529 190 LDFDA-------ELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 384 DIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPD---VNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQ 459
Cdd:PRK07529 262 PLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 460 VLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTE-TGGHMLTPLPGatPMKPGSA--TFPFFGVAPAILNESGEELEG 536
Cdd:PRK07529 337 YALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 537 EAEG---YLLLRTETswleVFkqpwPGIMRTVYGNHERFEttyfkkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 613
Cdd:PRK07529 412 CAVDevgVLCIAGPN----VF----SGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 614 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREkigPIATPDYIQNAPGLPK 692
Cdd:PRK07529 477 NIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEaELLAFARDHIAE---RAAVPKHVRILDALPK 553
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2462580884 693 TRSGKI---------MRRVLRK-IAQNDHDLGDMSTVADPS 723
Cdd:PRK07529 554 TAVGKIfkpalrrdaIRRVLRAaLRDAGVEAEVVDVVEDGR 594
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
145-703 |
1.82e-36 |
|
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: 142.67 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERIL----DSS 220
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 221 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskr 300
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 301 vqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFW 380
Cdd:cd05930 91 -------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVL 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 CTADIGWItGHSYVTYGPLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVtkhsRASL 458
Cdd:cd05930 139 QFTSFSFD-VSVWEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 459 QVLGTVGEPINPEAW-LWYHRVVGAQ--------RCPIVDTFWQTETGGHMLTPLPGATPMkPGSATFpffgvapaILNe 529
Cdd:cd05930 211 RLVLVGGEALPPDLVrRWRELLPGARlvnlygptEATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLD- 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 530 sgeelegeaegylllrtetSWLevfkQPWP------------GIMRTVYGNHE----RFETTYFkkFPG--YYVTGD-GC 590
Cdd:cd05930 281 -------------------ENL----RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGDlVR 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 591 QRDqDG--YYwiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELK 668
Cdd:cd05930 336 WLP-DGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELR 409
|
570 580 590
....*....|....*....|....*....|....*
gi 2462580884 669 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd05930 410 AHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
147-705 |
3.61e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 143.12 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsscslLIT 226
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV------------------------VVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 tdafyrgeklVNLKELADEALQKCQEKGfpVRCCIVVKHLgraeLGMGDSTSQSPP---IKRSCPDVQGK-LKEKSKRvq 302
Cdd:PRK07656 85 ----------LNTRYTADEAAYILARGD--AKALFVLGLF----LGVDYSATTRLPaleHVVICETEEDDpHTEKMKT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqgidlwWHELMQEA-GDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGG-YMLY--VATTFKYVFD------ 372
Cdd:PRK07656 147 ------------FTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAadWAEYLGLTEGdrylaa 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 373 ---FHaedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEp 449
Cdd:PRK07656 214 npfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 vTKHSRASLQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDT-FWQTETGGHM-LTPLPGATPMKPGSATFPFFGVAPAIL 527
Cdd:PRK07656 276 -SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKIV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 528 NESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDM 607
Cdd:PRK07656 352 NELGEEVPVGEVGELLVRG------------PNVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDM 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 608 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspkLTEE-LKKQIREKIGPIATPDYIQN 686
Cdd:PRK07656 418 FIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE----LTEEeLIAYCREHLAKYKVPRSIEF 493
|
570
....*....|....*....
gi 2462580884 687 APGLPKTRSGKIMRRVLRK 705
Cdd:PRK07656 494 LDELPKNATGKVLKRALRE 512
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
29-705 |
6.05e-36 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 145.22 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 29 WSPPPEVSRSAHVPSLQRYR-----------------ELHRRSVEEPREFWGDIAKEF--YWKTPcPGPFLRYNFDVTKG 89
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDELslVFSVP-PRCILDTSDESNPG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 90 KifiEWMKGATTNICYNVLDRNVHEKklGDKVAFYWSTSGNSSYRYTCregnepgettqITYHQLLVQVCQFSNVLRKQG 169
Cdd:PLN03052 166 G---QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWRDEGSDDLPVNR-----------MTLSELRSQVSRVANALDALG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 170 IQKGDRVAIYMPMIPELVVAMLAcarigalhsIVFAG---------FSSESLCERILDSSCSLLITTDAFYRGEKLVNLK 240
Cdd:PLN03052 230 FEKGDAIAIDMPMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 241 ELADEAlqkcqekgfpvrccivvkhlgraelgmgdstsQSP-----PIKRSCPDVQgkLKEKskrvqpqiswnqgiDLWW 315
Cdd:PLN03052 301 SRVVEA--------------------------------KAPkaivlPADGKSVRVK--LREG--------------DMSW 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 316 HELMQEA-----GDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVF-WCTaDIGWIT 389
Cdd:PLN03052 333 DDFLARAnglrrPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 390 GHsYVTYGPLANGATSVLFEGIPTYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGdePVTKHSRASLQVLGTVGEPIN 469
Cdd:PLN03052 411 GP-WLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASS 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 470 PEAWLWYhrVVGAQRCPIVDTFWQTETGGHMLTplpgATPMKPGS-ATF--PFFGVAPAILNESGEELEGEAEGylllrt 546
Cdd:PLN03052 485 VDDYLWL--MSRAGYKPIIEYCGGTELGGGFVT----GSLLQPQAfAAFstPAMGCKLFILDDSGNPYPDDAPC------ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 547 eTSWLEVFKQPWPGIMRTVYGNHERfetTYFKKFPGYYVT-----GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 621
Cdd:PLN03052 553 -TGELALFPLMFGASSTLLNADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIE 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 622 ----SAlveHEAVAEAAVVGHPHPVKG-ECLYCFVTLCDGHTFSPKLtEELKK----QIREKIGPIATPDYIQNAPGLPK 692
Cdd:PLN03052 629 rvcnAA---DESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPR 704
|
730
....*....|...
gi 2462580884 693 TRSGKIMRRVLRK 705
Cdd:PLN03052 705 TASNKVMRRVLRQ 717
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
148-708 |
2.84e-35 |
|
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: 141.05 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHsiVFAGFS---SE--SLCERildSSCS 222
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrrAEisHFAEQ---SEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAfYRGeklVNLKELADEALQKCQEkgfpVRCCIVVkhlgraelgmGDStsqsppikrscpdvqgklkekskrvQ 302
Cdd:COG1021 125 AYIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV----------GDA-------------------------G 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQISWNqgidlwwhELMQEAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCT 382
Cdd:COG1021 162 EFTSLD--------ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 383 ADIGwitgHSY-----VTYGPLANGATSVLfegIPTyPDVNRLWSIVDKYKVTkfYTA--PTAIRLLMKFGDEpvTKHSR 455
Cdd:COG1021 232 LPAA----HNFplsspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 456 ASLQVLGTVGEPINPEA----------WLW-----------Y-------HRVVGAQRCP--------IVDtfwqtETGgh 499
Cdd:COG1021 300 SSLRVLQVGGAKLSPELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 500 mlTPLPgatpmkPGSAtfpffGVapailnesgeelegeaegyLLLRTetswlevfkqpwPGIMRTVYGNHERFETTyfkk 579
Cdd:COG1021 373 --NPVP------PGEV-----GE-------------------LLTRG------------PYTIRGYYRAPEHNARA---- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 580 FP--GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcD 655
Cdd:COG1021 405 FTpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-R 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 656 GHTFSPKlteELKKQIREKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 708
Cdd:COG1021 482 GEPLTLA---ELRRFLRER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
180-704 |
6.65e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 136.48 E-value: 6.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 180 MPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALqkcqekgfPVRC 259
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAA--------PAKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 260 cIVVKHLGRaelgmgdstsqsppikrscpDVQGKLKEKskrvqpqiswnqgiDLWWHELMQEA-------GDECEPEWCD 332
Cdd:PLN03051 73 -IVLPAAGE--------------------PVAVPLREQ--------------DLSWCDFLGVAaaqgsvgGNEYSPVYAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIP 412
Cdd:PLN03051 118 VESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 TYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcPIVDTFW 492
Cdd:PLN03051 196 LGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 QTETGGHML--TPLpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAegylllrTETSWLEVFKQPWPGIMRTVYGNHE 570
Cdd:PLN03051 272 GTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQ-------PCVGEVALAPPMLGASDRLLNADHD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 571 RfetTYFKKFPGYYVTGDGCQRDQD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPV 642
Cdd:PLN03051 342 K---VYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPD 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462580884 643 KG-ECLYCFVTLCD-GHTFSPKLTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PLN03051 419 GGpELLVIFLVLGEeKKGFDQARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
147-703 |
4.30e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 134.70 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVL-RKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 225
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TTDafyrgeklvnlkELADEALQKCQEKGfpVRCCIVVKhlgraelgMGDSTSQSPPIK-----RSCPDVQGKLKEKSkr 300
Cdd:PRK08314 114 VGS------------ELAPKVAPAVGNLR--LRHVIVAQ--------YSDYLPAEPEIAvpawlRAEPPLQALAPGGV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 301 vqpqISWNQGIDlwwhelmqeAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFW 380
Cdd:PRK08314 170 ----VAWKEALA---------AGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 CTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPT-AIRLLMKFGdepVTKHSRASLQ 459
Cdd:PRK08314 236 AVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERYRVTHWTNIPTmVVDFLASPG---LAERDLSSLR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 460 VLGTVGEPInPEAwlwyhrvVgAQR------CPIVDTFWQTETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEE 533
Cdd:PRK08314 309 YIGGGGAAM-PEA-------V-AERlkeltgLDYVEGYGLTETMAQTHSNPPDRP--KLQCLGIPTFGVDARVIDPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 534 LegeaegylLLRTETSWLEVFKqpwPGIMRTVYGNHERFETTyFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVS 611
Cdd:PRK08314 378 E--------LPPGEVGEIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 612 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlTEELKKQIREKIGPIATPDYIQNAPGLP 691
Cdd:PRK08314 446 GFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLP 524
|
570
....*....|..
gi 2462580884 692 KTRSGKIMRRVL 703
Cdd:PRK08314 525 KSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
332-703 |
5.45e-32 |
|
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: 129.74 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGYM-LYVATTfkYVFDFHAEDVfwctadigWITGHSYV-------TYGPLANGA 403
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 404 TSVlfegIPTYpDVNR----LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPeAWL--WYH 477
Cdd:cd17643 161 RLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEA-AMLrpWAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 478 RVvGAQRCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLllrtetswl 551
Cdd:cd17643 233 RF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGVVGELYV--------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 552 evfkqPWPGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 625
Cdd:cd17643 302 -----SGAGVARGYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 626 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMR 700
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADI---AELRALLKELL-----PDYMVPAryvplDALPLTVNGKLDR 447
|
...
gi 2462580884 701 RVL 703
Cdd:cd17643 448 AAL 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
341-707 |
1.82e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 126.44 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 341 YTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 416
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 417 VNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE- 495
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 496 TGGHMLTPlPGaTPMKPGSA--TFPFFGVAPAILNESGEelegeaegyLLLRTETSwlEVFkqpwPGIM--RTVYGNH-- 569
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVglRLPYARVRIKVLDGVGR---------LLRDCAPD--EVG----EICVagPGVFGGYly 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 570 -ERFETTYFKkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 648
Cdd:cd05944 222 tEGNKNAFVA--DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 649 CFVTLCDGHTFSP-KLTEELKKQIREKigpIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:cd05944 300 AYVQLKPGAVVEEeELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
149-703 |
3.45e-31 |
|
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: 128.12 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 228
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AfyrgeklvNLKELADEALQkcqekgfpvrccIVVkhLGRAElgmGDSTSQSPPIKRSCPDvqgklkeksKRVQPQISwn 308
Cdd:cd05904 113 E--------LAEKLASLALP------------VVL--LDSAE---FDSLSFSDLLFEADEA---------EPPVVVIK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 qgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYmlyVATTFKYVFDF----HAEDVFWCTAD 384
Cdd:cd05904 157 ------------------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTV 464
Cdd:cd05904 210 MFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 465 GEPINPEAwlwYHRVvgAQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSATFPFFGVAPAILNesgeelegea 538
Cdd:cd05904 284 AAPLGKEL---IEAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVD---------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 539 egylllrTETSWLEVFKQP---W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 612
Cdd:cd05904 347 -------PETGESLPPNQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKG 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 613 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGP------IATPDYIqn 686
Cdd:cd05904 418 FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTED---EIMDFVAKQVAPykkvrkVAFVDAI-- 492
|
570
....*....|....*..
gi 2462580884 687 apglPKTRSGKIMRRVL 703
Cdd:cd05904 493 ----PKSPSGKILRKEL 505
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
138-705 |
6.82e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 124.77 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 138 REGNEPG---ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGfsseslce 214
Cdd:PRK07470 19 RFPDRIAlvwGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 215 rildsscsllittdafyrgeklVNLKELADEALQKCQEKGfpvrccivvkhlGRAELGMGDSTSQSPPIKRSCPDVQGKL 294
Cdd:PRK07470 87 ----------------------TNFRQTPDEVAYLAEASG------------ARAMICHADFPEHAAAVRAASPDLTHVV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 295 KEKSKRVQPQISwnqgidlwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTfkyvfdfH 374
Cdd:PRK07470 133 AIGGARAGLDYE---------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAFVITN-------H 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 375 AEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVNRLWSIVDKYKVTKFYTAPTAI 439
Cdd:PRK07470 196 LADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNLFTVPTIL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 440 RLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMlTPLPGA------TPM-KP 512
Cdd:PRK07470 266 KMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdaedGPDaRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 513 GSATFPFFGVAPAILNESGEelegeaegyLLLRTETSWLEVFKqpwPGIMRTVYGNHERFEttyfKKF-PGYYVTGDGCQ 591
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGR---------ELPPGETGEICVIG---PAVFAGYYNNPEANA----KAFrDGWFRTGDLGH 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 592 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQI 671
Cdd:PRK07470 404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWL 480
|
570 580 590
....*....|....*....|....*....|....
gi 2462580884 672 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK07470 481 DGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
619-697 |
7.36e-29 |
|
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: 109.94 E-value: 7.36e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 619 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 697
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
147-708 |
9.05e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 121.69 E-value: 9.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLIT 226
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 TDAFYrgeklvnlkELADEALQKCqekgfPVRCCIVVkhlgraelGMGDSTSQSPPIkrSCPD-VQGklkekskrvqPQI 305
Cdd:PRK06178 137 LDQLA---------PVVEQVRAET-----SLRHVIVT--------SLADVLPAEPTL--PLPDsLRA----------PRL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 SWNQGIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTFKYVFDFHAED-VFWCTAD 384
Cdd:PRK06178 183 AAAGAIDLL--PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAAAYAVAVVGGEDsVFLSFLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTK-FYTAPTAIRLLmkfgDEP-VTKHSRASLQVLG 462
Cdd:PRK06178 260 EFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM----DHPrFAEYDLSSLRQVR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 463 TVG--EPINPEAWLWYHRVVGaqrCPIVDTFW-QTET------------GGHMLT--------PLPGA----TPMKPGsA 515
Cdd:PRK06178 332 VVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefkiCDFETG-E 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 516 TFPFfGVAPAILnesgeelegeaegyllLRTETswleVFKQPWpgimrtvygNHERFETTYFKKfpGYYVTGDGCQRDQD 595
Cdd:PRK06178 408 LLPL-GAEGEIV----------------VRTPS----LLKGYW---------NKPEATAEALRD--GWLHTGDIGKIDEQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 596 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKI 675
Cdd:PRK06178 456 GFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENM 532
|
570 580 590
....*....|....*....|....*....|....
gi 2462580884 676 GPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 708
Cdd:PRK06178 533 AVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
144-704 |
4.56e-28 |
|
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: 118.60 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSL 223
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAFYRGEklvnlkeLADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqp 303
Cdd:cd17651 95 LVLTHPALAGE-------LAVEL--------------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqGIDLWWHELMQEAGDECEPEW-CDAEDPLFILYTSGSTGKPKGVV------------HTVGGYMLYVATTFKYV 370
Cdd:cd17651 111 ------VAVTLLDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 371 ---FDFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegIPTY--PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF 445
Cdd:cd17651 185 glgFDVSVQEIF-----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 446 GDEPVTKHsrASLQVLGTVGEPINPEAWL--WYHRVVGAQrcpIVDTFWQTET---GGHMLTPLPGATPMKPGsatfpff 520
Cdd:cd17651 245 GRPLGVRL--AALRYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAAWPAPPP------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 521 gVAPAILNESGeelegeaegYLLLRtetswlevFKQPWP------------GIMRTVYGN----HERFETTYFKKFPGYY 584
Cdd:cd17651 313 -IGRPIDNTRV---------YVLDA--------ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMY 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 585 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLT 664
Cdd:cd17651 375 RTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDA 451
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2462580884 665 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd17651 452 AELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
149-703 |
7.17e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.98 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 228
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AFYrgEKLVNLkeladEALQKCQEkgfpvrccIVVKHLgraelgmgdstSQSPPIKRSC--PDVQgklkEKSKRVQPQIS 306
Cdd:PRK06710 130 LVF--PRVTNV-----QSATKIEH--------VIVTRI-----------ADFLPFPKNLlyPFVQ----KKQSNLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 307 WNQGIDLWwhELMQEAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD-FHAEDVFWCTAD 384
Cdd:PRK06710 180 ESETIHLW--NSVEKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTK-HSRASLQVLGT 463
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEElegeae 539
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGE------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 540 gylLLRTETSWLEVFKQPwpGIMRTVYGNHErfETTYFKKfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 619
Cdd:PRK06710 397 ---ALPPGEIGEIVVKGP--QIMKGYWNKPE--ETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPRE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 620 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 699
Cdd:PRK06710 469 VEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKIL 545
|
....
gi 2462580884 700 RRVL 703
Cdd:PRK06710 546 RRVL 549
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
143-705 |
1.06e-27 |
|
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: 117.73 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 143 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LHSI---VFAgfsseslcERILd 218
Cdd:cd12119 20 EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP--------EQIA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 219 sscslLITTDAfyrGEKLVnlkeLADEALQKCQEkgfpvrccivvkhlgraelgmgdstsqspPIKRSCPDVQGKLKEKS 298
Cdd:cd12119 91 -----YIINHA---EDRVV----FVDRDFLPLLE-----------------------------AIAPRLPTVEHVVVMTD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 299 KRVQPQISWNQGIDlWWHELMQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMlyvattfKYV 370
Cdd:cd12119 130 DAAMPEPAGVGVLA-YEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAALL-------TDG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 371 FDFHAEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvnrLWSIVDKYKVTKFYTAPTAI 439
Cdd:cd12119 201 LGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFAAGVPTVW 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 440 RLLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGAQRCP----------IVDTF--W-QTETG--GHMLTPL 504
Cdd:cd12119 266 QGLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSplGTVARPP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 505 PGATPMKPG-------SATFPFFGVAPAILNESGeelegeaegylllrTETSW-------LEVfKQPWpgIMRTVYGNHE 570
Cdd:cd12119 327 SEHSNLSEDeqlalraKQGRPVPGVELRIVDDDG--------------RELPWdgkavgeLQV-RGPW--VTKSYYKNDE 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 571 rfeTTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 650
Cdd:cd12119 390 ---ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAV 466
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2462580884 651 VTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd12119 467 VVLKEGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-704 |
1.95e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.01 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 119 DKVAFYWstsgnssyrytcregnepGETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM----LACA 194
Cdd:PRK06188 27 DRPALVL------------------GDTR-LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqLAGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 195 RIGALHSIVfagfSSESLCERILDSSCSLLITTDAFYRgeklvnlkELADEALQKCQEkgfpvrccivVKHLgraeLGMG 274
Cdd:PRK06188 88 RRTALHPLG----SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 275 DStsqsppikrscpdvqgklkekskrvqpqiswNQGIDLWwhelmqEAGDECEPE----WCDAEDPLFILYTSGSTGKPK 350
Cdd:PRK06188 142 PV-------------------------------PDGVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 351 GVVHTVGGYmlyvaTTFkyvfdfhaedVFWCTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVNRLWS 422
Cdd:PRK06188 185 GVMGTHRSI-----ATM----------AQIQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 423 IVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPINP----EAwlwyHRVVGaqrcPI-VDTFWQTETG 497
Cdd:PRK06188 250 AIEEQRITATFLVPTMIYALLDHPDLRTRDLS--SLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 498 gHMLTPLP-----GATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRtvyGNHERF 572
Cdd:PRK06188 320 -MVITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRG------------PLVMD---GYWNRP 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 573 ETT--YFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 650
Cdd:PRK06188 384 EETaeAFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2462580884 651 VTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK06188 462 VVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
150-635 |
2.16e-27 |
|
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: 115.44 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLITT 227
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 DAFyrgeklvnlkeladealqkCQEKGFPVRCCIVVkhLGRAELGMGDSTSQSPPIKRSCPDvqgklkekskrvqpqisw 307
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVfwctadigW 387
Cdd:TIGR01733 121 ---------------------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------V 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 388 ITGHSYV-------TYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTkhSRASLQV 460
Cdd:TIGR01733 165 LQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 461 LGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGE 537
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 538 AEGYLLLRTetswlevfkqpwPGIMRtvyGNHERFETT--YFKKFPGY-------YVTGDGCQRDQDGYYWITGRIDDML 608
Cdd:TIGR01733 318 VVGELYIGG------------PGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQV 382
|
490 500
....*....|....*....|....*..
gi 2462580884 609 NVSGHLLSTAEVESALVEHEAVAEAAV 635
Cdd:TIGR01733 383 KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
149-705 |
3.53e-27 |
|
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: 116.42 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 228
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AFYRgeklvnlkeLADEALQKCqekgfpvrccivvkHLGRAELGMGDSTSQSPPIKRSCPdvqgklkekskrvqpqISWN 308
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGDPAHASEGHPGEEP----------------ASWP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 QgidlwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT----VGGymlyvATTFKYVFDFHAEDVFWCTAD 384
Cdd:TIGR03098 147 K---------LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLShrnlVAG-----AQSVATYLENRPDDRLLAVLP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSYVTYGpLANGATSVLFEgiptYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTV 464
Cdd:TIGR03098 213 LSFDYGFNQLTTA-FYVGATVVLHD----YLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 465 GEPInPEAWLWYHRvvgaQRCPIVDTFWQ---TETGGHMLTPlPGATPMKPGSatfpffgVAPAILNESGeelegeaegy 541
Cdd:TIGR03098 285 GGAM-PRATLSRLR----SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDS-------IGKAIPNAEV---------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 542 LLLRTETSWLEVfKQPWPGIMRTV-----YGNHERFETTYFKKFPGYYV----------TGDGCQRDQDGYYWITGRIDD 606
Cdd:TIGR03098 342 LVLREDGSECAP-GEEGELVHRGAlvamgYWNDPEKTAERFRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQN 686
Cdd:TIGR03098 421 MIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHV 497
|
570
....*....|....*....
gi 2462580884 687 APGLPKTRSGKIMRRVLRK 705
Cdd:TIGR03098 498 RQALPRNANGKIDRKALAK 516
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
150-704 |
3.75e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 116.06 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 229
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 230 FYRGE-KLVNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 308
Cdd:PRK09088 104 VAAGRtDVEDLAAFIASA-------------------------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 qgidlwwhelmqEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTAD---- 384
Cdd:PRK09088 122 ------------DALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhi 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSYVtygpLANGATSVLFEGIPTYPDVNRLWSIvdKYKVTKFYTAPtaiRLLMKFGDEPVTKHSR-ASLQVLGT 463
Cdd:PRK09088 189 IGLITSVRPV----LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPiNPE----AWLwyhrvvgAQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGEA 538
Cdd:PRK09088 260 GGAP-HAAedilGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 539 EGYLLLRTETswleVFkqpwPGIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 618
Cdd:PRK09088 332 PGELLLRGPN----LS----PGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPA 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 619 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKI 698
Cdd:PRK09088 398 EIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
....*.
gi 2462580884 699 MRRVLR 704
Cdd:PRK09088 475 QKARLR 480
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
144-710 |
1.41e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 114.77 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK13295 51 GAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAFyRG---EKLVNlkELADE--ALQKcqekgfpvrccIVVkhlgraeLGMGDSTS----QSPPIKRSCPDVQGKL 294
Cdd:PRK13295 131 LVVPKTF-RGfdhAAMAR--RLRPElpALRH-----------VVV-------VGGDGADSfealLITPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 295 KekskRVQPqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHT----VGGYMLYVATtfkyv 370
Cdd:PRK13295 190 A----RLRP----------------------------GPDDVTQLIYTSGTTGEPKGVMHTantlMANIVPYAER----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 371 FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVNRLWSIVDKYKVTkFYTAPTAirLLMKFGDepV 450
Cdd:PRK13295 233 LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP--FLTDLTR--A 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 451 TKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPMKpGSAT--FPFFG 521
Cdd:PRK13295 304 VKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDER-ASTTdgCPLPG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 522 VAPAILNESGEELEGEAEGYLLLRTETSWLEVFKQP-WPGImrtvygnherfettyfkKFPGYYVTGDGCQRDQDGYYWI 600
Cdd:PRK13295 375 VEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPqLNGT-----------------DADGWFDTGDLARIDADGYIRI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 601 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PKLTEELKKQireKIGPIA 679
Cdd:PRK13295 438 SGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQY 514
|
570 580 590
....*....|....*....|....*....|.
gi 2462580884 680 TPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 710
Cdd:PRK13295 515 IPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
148-703 |
2.32e-26 |
|
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: 113.16 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 226
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 TDAfyrgeklvnlkeLADealqkcqekgfPVRCCIVVKHLGRAELGMGDSTSQSPPikrscpdvqgklkekskrvqpqis 306
Cdd:cd12116 91 DDA------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPV------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 307 wnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGY------------------MLYVATtfk 368
Cdd:cd12116 124 -------------------------SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 369 YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE 448
Cdd:cd12116 176 YAFDISLLELLL-----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 449 PvtkhsRASLQVL-GtvGEPINPEawlwyhrvVGAQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSATFPffgVA 523
Cdd:cd12116 238 G-----RAGLTALcG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 524 PAILNesgeelegeaegylllrTETSWLEVFKQPWP-GIMRTVY--------GNHERFETTyFKKF-------PG--YYV 585
Cdd:cd12116 295 RPLAN-----------------TQVYVLDAALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYR 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 586 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSpklTE 665
Cdd:cd12116 357 TGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AA 432
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462580884 666 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd12116 433 ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
335-705 |
2.41e-26 |
|
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: 112.86 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGYMlyvATTFKYV--FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIp 412
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLS---ASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 typDVNRLWSIVDKYKVTKFYTAPTAIRLLMK---FGDEPVtkhsrASLQVLGTVGEPINP----EAWlwyhRVVGAQRC 485
Cdd:cd05903 170 ---DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRslarRAA----ELLGAKVC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 486 PIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETswlevfkqpwpgimrTV 565
Cdd:cd05903 238 SA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPS---------------VF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 566 YGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 645
Cdd:cd05903 300 LGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 646 CLYCFVTLCDGHTFS-PKLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05903 380 RACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
335-705 |
3.07e-26 |
|
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: 112.38 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 414
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 415 PDVNRLWSIVDKYKVTKFYTAPTA-IRLL--MKFGDEPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhRVVGAQR 484
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyYEAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 485 cpIVDTFWQTETGGHMLTPLPGatPMKPGSATFPFFGVAPAIL-NESGEELEGEAEGYLLLRTETswleVFKQPWPGIMR 563
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPS----VFKEYWNKPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 564 TVygnhERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 642
Cdd:cd05941 312 TK----EEFTDD------GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 643 KGECLYCFVTLCDGHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05941 382 WGERVVAVVVLRAGAA--ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
148-703 |
3.79e-26 |
|
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: 111.80 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 227
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 dafyrgeklvnlKELADEALqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqisw 307
Cdd:cd05935 81 ------------SELDDLAL------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqgidlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVHTvGGYMLYVATTFKYVFDFHAEDVFWCTADIGW 387
Cdd:cd05935 89 -------------------------------IPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 388 ITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEP 467
Cdd:cd05935 137 VTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 468 InPEAWLwyHRVVGAQRCPIVDTFWQTETgghmLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEGYLLLr 545
Cdd:cd05935 211 M-PPAVA--EKLLKLTGLRFVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVGEIV- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 546 teTSWLEVFKQPWpgimRTVYGNHERFETTYFKKFpgyYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 625
Cdd:cd05935 283 --VRGPQIFKGYW----NRPEETEESFIEIKGRRF---FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLY 353
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 626 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtFSPKLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd05935 354 KHPAI*EVCVISVPDERVGEEVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
339-705 |
5.22e-26 |
|
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: 111.28 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 339 ILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVN 418
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 419 RLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQ 493
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 494 TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAegyLLLRTetswlevfkqpwPGIMRTVYGNHER-- 571
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKG------------PNVTKGYLNRPDAte 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 572 --FETTYFKkfpgyyvTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 649
Cdd:cd05912 288 esFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVA 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580884 650 FVTLcdghtfSPKLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05912 361 FVVS------ERPISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
147-703 |
5.94e-26 |
|
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: 111.57 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILD-SSCSLLI 225
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI-REILDaAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 Ttdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqi 305
Cdd:cd05945 94 A------------------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 swnqgidlwwhelmqeAGDecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTA-- 383
Cdd:cd05945 95 ----------------DGD----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQApf 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 384 -------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvnrlwsivdkykVTKFYTAPTAIRLLMk 444
Cdd:cd05945 148 sfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------ITVWVSTPSFAAMCL- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 445 fGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRvvgAQRCPIVDTFWQTET----GGHMLTPLPGATpMKPGSATFP 518
Cdd:cd05945 204 -LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQR---FPDARIYNTYGPTEAtvavTYIEVTPEVLDG-YDRLPIGYA 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 519 FFGVAPAILNESGEELEGEAEGYLLLRTETswleVFKqpwpGIMRtVYGNHERFettyFKKFPGY--YVTGDGCQRDQDG 596
Cdd:cd05945 278 KPGAKLVILDEDGRPVPPGEKGELVISGPS----VSK----GYLN-NPEKTAAA----FFPDEGQraYRTGDLVRLEADG 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 597 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFspKLTEELKKQIREKIG 676
Cdd:cd05945 345 LLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA--GLTKAIKAELAERLP 422
|
570 580
....*....|....*....|....*..
gi 2462580884 677 PIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd05945 423 PYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
334-704 |
1.10e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 110.99 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGi 411
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTND- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 412 pTYPDVNrLWSIVDKYKVTKFYTAPTAIRLL--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWLWYHR--VVGAQrcpI 487
Cdd:cd05922 192 -GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ---V 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 488 VDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETSWLEVFKQPwpgimrtvyg 567
Cdd:cd05922 261 YVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDP---------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 568 NHERFETTyfkkFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECL 647
Cdd:cd05922 331 PYRRKEGR----GGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKL 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580884 648 YCFVTLCDGHTFSPklteeLKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05922 406 ALFVTAPDKIDPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
145-706 |
1.69e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.82 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAG--FSSESLCERILDSSCS 222
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSREELLWQLDDAEVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAFyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvQGKLKEkskrvq 302
Cdd:PRK03640 102 CLITDDDF------------------------------------------------------------EAKLIP------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWC 381
Cdd:PRK03640 116 -------GISVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 382 TADIGWITGHSYVTygplangaTSVLFeGIPTY-------PDVNRLwsIVDKyKVTKFYTAPTAI-RLLMKFGDEPVTKH 453
Cdd:PRK03640 188 AVPIFHISGLSILM--------RSVIY-GMRVVlvekfdaEKINKL--LQTG-GVTIISVVSTMLqRLLERLGEGTYPSS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 454 SRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 528
Cdd:PRK03640 256 FRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEK 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 529 ESGEELEGEAEGYLLlrtetswlevfKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCQRDQDGYYWITGRIDD 606
Cdd:PRK03640 323 DGVVVPPFEEGEIVV-----------KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSD 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSpklTEELKKQIREKIGPIATPDYIQN 686
Cdd:PRK03640 385 LIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKRFYF 459
|
570 580
....*....|....*....|
gi 2462580884 687 APGLPKTRSGKIMRRVLRKI 706
Cdd:PRK03640 460 VEELPRNASGKLLRHELKQL 479
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
315-704 |
2.05e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 111.27 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 315 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgyMLYV---ATTFKYvfDFHAEDVFWCTADIGwitgH 391
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 392 S---YVTYGP-LANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQV-LGT 463
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSATFPFFGV-----------APAILNES 530
Cdd:PRK13388 274 EASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVaiynpetltecAVARFDAH 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 531 GEelegeaegylLLRTETSWLEVFKQPWPGIMRTVYGNH----ERFETtyfkkfpGYYVTGDGCQRDQDGYYWITGRIDD 606
Cdd:PRK13388 342 GA----------LLNADEAIGELVNTAGAGFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTAD 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPIATPDYIQ 685
Cdd:PRK13388 405 WMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYVR 482
|
410
....*....|....*....
gi 2462580884 686 NAPGLPKTRSGKIMRRVLR 704
Cdd:PRK13388 483 IAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
334-704 |
6.83e-25 |
|
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: 108.61 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPT 413
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 414 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPINPE-AWLWyhrvvGAQRCPIVDTFW 492
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRW-----LKAPVRLFNAYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 QTETgghMLTPL--PGATPMKPGSATFP----FFGVAPAILNESGEELEGEAEGYLLLRTEtswlevfkqpwpGIMRtvy 566
Cdd:cd17649 245 PTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVGVTGELYIGGE------------GLAR--- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 567 GNHERFETTYfKKF-------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 637
Cdd:cd17649 307 GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580884 638 HPHPVkGECLYCFVTLCDGHTfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd17649 386 LDGAG-GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-705 |
7.73e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.70 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 107 VLDRNVHEkkLGDKVAFYWStsgnssyrytcregnepGETTqiTYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPEL 186
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFF-----------------GATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 187 VVAMLACARIGA---LHSIVFAGFSSESLCErilDSSCSLLITTDafyrgeKLVN-LKELADEAlqkcqekgfPVRCCIV 262
Cdd:PRK05605 96 IVAFYAVLRLGAvvvEHNPLYTAHELEHPFE---DHGARVAIVWD------KVAPtVERLRRTT---------PLETIVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 263 VkhlgraelgmgDSTSQSPPIKRscpdVQGKL---KEKSKRVQPQISWNQGIDlwWHELMQEA----GDECEPEWCDAED 335
Cdd:PRK05605 158 V-----------NMIAAMPLLQR----LALRLpipALRKARAALTGPAPGTVP--WETLVDAAiggdGSDVSHPRPTPDD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 336 PLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD--------------FHAEDVFWCtadigwitghsyVTYGPLAn 401
Cdd:PRK05605 221 VALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGlgdgpervlaalpmFHAYGLTLC------------LTLAVSI- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 402 GATSVLFegiPTyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP-VTKHS-RASLQvlgtvgepinpeawlwyhrv 479
Cdd:PRK05605 288 GGELVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS-------------------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 480 vGAQRCPiVDTF--WQTETGGHM-----LT---PLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LL 543
Cdd:PRK05605 344 -GAMALP-VSTVelWEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 544 LRTEtswlEVFKqpwpgimrtvyGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 623
Cdd:PRK05605 422 VRGP----QVFK-----------GYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 624 LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
..
gi 2462580884 704 RK 705
Cdd:PRK05605 564 RE 565
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
144-704 |
1.05e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 108.62 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESlCERILDSS-CS 222
Cdd:PRK08008 33 GVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE-SAWILQNSqAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAFYRgeklvnlkelADEALQkcQEKGFPVRCCIVvkhlgraelgmgdstsqsppikrscpdvqgkLKEKSKRVQ 302
Cdd:PRK08008 112 LLVTSAQFYP----------MYRQIQ--QEDATPLRHICL-------------------------------TRVALPADD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQISWNQgidlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----VGGYmlY----VATTFKYVF-- 371
Cdd:PRK08008 149 GVSSFTQ-------LKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--YsawqCALRDDDVYlt 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 372 ---DFHAEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdE 448
Cdd:PRK08008 220 vmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMV---Q 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 449 PVTKHSRASL--QVLGTVgePINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGATPMKPgSATFPFFGVAPAI 526
Cdd:PRK08008 280 PPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 527 LNESGEElegeaegylLLRTETSWLEVFKQPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDD 606
Cdd:PRK08008 354 RDDHNRP---------LPAGEIGEICIKGVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQN 686
Cdd:PRK08008 423 MIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKVPSYLEI 499
|
570
....*....|....*...
gi 2462580884 687 APGLPKTRSGKIMRRVLR 704
Cdd:PRK08008 500 RKDLPRNCSGKIIKKNLK 517
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
143-704 |
5.66e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 106.31 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 143 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCS 222
Cdd:PRK13391 19 ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAFYrgeklvnlkELADEALQKCQEkgfpVRCCIVVkhlgraelgmgDSTSQSPPIKRscpdvqgklkekskrvq 302
Cdd:PRK13391 99 ALITSAAKL---------DVARALLKQCPG----VRHRLVL-----------DGDGELEGFVG----------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqgidlwwhelMQEAGDECePEWCDAEDPL--FILYTSGSTGKPKGVV----HTVGGYMLYVATTFKYVFDFHAE 376
Cdd:PRK13391 138 ----------------YAEAVAGL-PATPIADESLgtDMLYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 377 DVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP 449
Cdd:PRK13391 201 MVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 VTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgaqrCPIVDTFWQTETGGhmltplpGATPM-------KPGSAT 516
Cdd:PRK13391 269 RDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-------GFTACdseewlaHPGTVG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 517 FPFFGVaPAILNESGEELEGEAEGYLLLRTETSWlEVFKQPwpgiMRTVYGNHERfettyfkkfPGYYVTGDGCQRDQDG 596
Cdd:PRK13391 332 RAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPF-EYLNDP----AKTAEARHPD---------GTWSTVGDIGYVDEDG 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 597 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG 676
Cdd:PRK13391 397 YLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLS 476
|
570 580
....*....|....*....|....*...
gi 2462580884 677 PIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK13391 477 RQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
144-637 |
6.64e-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: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESlCERIL-DSSCS 222
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvq 302
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCT 382
Cdd:cd05907 87 -------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSF 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 383 ADIGWITGHSYVTYGPLANGATSVLFEGI-----------PTY-PDVNRLWSIVdkYKVTKFYTAPTAIRLLMKFgdepv 450
Cdd:cd05907 135 LPLAHVFERRAGLYVPLLAGARIYFASSAetllddlsevrPTVfLAVPRVWEKV--YAAIKVKAVPGLKRKLFDL----- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 451 tkHSRASLQVLGTVGEPINPEAWLWYHrvvgAQRCPIVDTFWQTETGG-HMLTPLPGATPMKPGSatfPFFGVAPAILNE 529
Cdd:cd05907 208 --AVGGRLRFAASGGAPLPAELLHFFR----ALGIPVYEGYGLTETSAvVTLNPPGDNRIGTVGK---PLPGVEVRIADD 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 530 SGeelegeaegyLLLRTetswlevfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML- 608
Cdd:cd05907 279 GE----------ILVRG------------PNVMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIi 334
|
490 500
....*....|....*....|....*....
gi 2462580884 609 NVSGHLLSTAEVESALVEHEAVAEAAVVG 637
Cdd:cd05907 335 TSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
143-703 |
1.40e-23 |
|
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: 104.90 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 143 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERI-LDSSC 221
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 222 SLLITTDAF-YRGEKLVNLKELAdealqkcqekgfpvrccivvkhLGrAELGMGDSTSQSPPIkrscpdvqgklkekskr 300
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLA----------------------LS-DLVGLGEPESAGPLI----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 301 vqpqiswnqgidlwwhelmqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKYVFDFHaeD 377
Cdd:cd05923 143 --------------------------EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--N 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRAS 457
Cdd:cd05923 195 VVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 458 LQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsatfpFFG---VAPaILNESGEE 533
Cdd:cd05923 269 LRHVTFAGATM-PDAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 534 LEGEAEGYLLLRTETSWlevfkqPWPGIMRtvygnheRFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 613
Cdd:cd05923 340 LANGEEGELIVAAAADA------AFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGE 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 614 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfspKLTEELKKQ--IREKIGPIATPDYIQNAPGLP 691
Cdd:cd05923 407 NIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELP 481
|
570
....*....|..
gi 2462580884 692 KTRSGKIMRRVL 703
Cdd:cd05923 482 KNAMNKVLRRQL 493
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
317-705 |
5.91e-23 |
|
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: 103.15 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 317 ELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMLyVATTFKYVFDFHAEDVFWCTADI----GWItgh 391
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 392 syVTYGPLANGATSVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPE 471
Cdd:cd12118 191 --FPWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 472 AWLWYHRVVGAQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSATFPffGVAPAILNESGEELEGEAEGYLLLRTETSw 550
Cdd:cd12118 262 AVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPETM- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 551 LEVfkqPWPG------------IMRTVYGNHERFETTyFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 618
Cdd:cd12118 330 KPV---PRDGktigeivfrgniVMKGYLKNPEATAEA-FRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSV 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 619 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKI 698
Cdd:cd12118 404 EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
....*..
gi 2462580884 699 MRRVLRK 705
Cdd:cd12118 480 QKFVLRD 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
314-705 |
7.02e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 103.22 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 314 WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG-----GYMLyvATTFkyvfDFHAEDVFWCTADI--- 385
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 386 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKF--------YTAPTAIR-------LL 442
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPERpddadnpLR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 443 MKFGDEpvtkhsraslqvlgtvGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTEtGGHMLTPLPGaTPmkPGSATFPFF 520
Cdd:PRK07867 271 IVYGNE----------------GAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 521 GVApaILNESGEELEGEAEGYLLLRTETSWL--EVFKQPWPGIMRTVYGNHErfeTTYFKKFPGYYVTGDGCQRDQDGYY 598
Cdd:PRK07867 323 GVA--IVDPDTGTECPPAEDADGRLLNADEAigELVNTAGPGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 599 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGP 677
Cdd:PRK07867 398 YFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGP 475
|
410 420
....*....|....*....|....*...
gi 2462580884 678 IATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK07867 476 KQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
145-703 |
8.10e-23 |
|
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: 102.66 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERIL----DSS 220
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPLDPELPAERLAfmlaDAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 221 CSLLITtdafyrgeklvnLKELADEAlqkcqekgfPVRCCIVVkhlgraeLGMGDSTSQSPPIKRSCpdvqgklkekskr 300
Cdd:cd12117 95 AKVLLT------------DRSLAGRA---------GGLEVAVV-------IDEALDAGPAGNPAVPV------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 301 vqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVfDFHAEDVFW 380
Cdd:cd12117 134 -------------------------------SPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 CTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK-FYTAPTaIRLLMKFGDEpvtkhSRASLQ 459
Cdd:cd12117 181 QTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQLADEDPE-----CFAGLR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 460 VLGTVGEPINPEawlWYHRVVgaQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGSatfPFFGVAPAILNesg 531
Cdd:cd12117 253 ELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---PIANTRVYVLD--- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 532 eelegeaegylllrtetswleVFKQPWP------------GIMRTvYGNH-----ERFETTYFkkFPG--YYVTGDGCQR 592
Cdd:cd12117 322 ---------------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYRTGDLARW 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 593 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSPkltEELKKQIR 672
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDA---AELRAFLR 452
|
570 580 590
....*....|....*....|....*....|.
gi 2462580884 673 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
145-703 |
1.86e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 100.85 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpq 304
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 iswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTF------------KY 369
Cdd:cd12115 103 ---------------------------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 370 VFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGIPTYPDVNRLwsivdkYKVTKFYTAPTAIRLLMKFGDEP 449
Cdd:cd12115 156 CFDLSVFELF-----------------GPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 vtkhsrASLQVLGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghmlTPLPGATPMKPGSATFPFFGVApailne 529
Cdd:cd12115 213 ------ASVRVVNLAGEPLPRDLVQRLYARLQVER--VVNLYGPSED-----TTYSTVAPVPPGASGEVSIGRP------ 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 530 sgeelegeaegylLLRTETSWLEVFKQPWP------------GIMRTVYGN----HERFETTYFkkFPG--YYVTGDGCQ 591
Cdd:cd12115 274 -------------LANTQAYVLDRALQPVPlgvpgelyiggaGVARGYLGRpgltAERFLPDPF--GPGarLYRTGDLVR 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 592 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQI 671
Cdd:cd12115 339 WRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHL 415
|
570 580 590
....*....|....*....|....*....|..
gi 2462580884 672 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd12115 416 GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
150-707 |
1.93e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.16 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 229
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 230 FYRGEKLVNLKELADEalqkcqekgfpvrccivVKHLGRAELgmgdstsqsppikrSCPdvqgKLKEKSKRVQPQISWNQ 309
Cdd:PRK12583 127 FKTSDYHAMLQELLPG-----------------LAEGQPGAL--------------ACE----RLPELRGVVSLAPAPPP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 310 GIdLWWHELmQEAGDECEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTV--GGYMLYVAttfkyvFDFHAED 377
Cdd:PRK12583 172 GF-LAWHEL-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYPDVNrlWSIVDKYKVTKFYTAPTairLLMKFGDEPvtKHSRAS 457
Cdd:PRK12583 244 RLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--QRGNFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 458 LQVLGT---VGEPINPEAwlwYHRVVGAQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSATF----PFFGVApaILN 528
Cdd:PRK12583 316 LSSLRTgimAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 529 ESGEELEGEAEGYLLLRTETswlevfkqpwpgIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDML 608
Cdd:PRK12583 389 PDGATVPRGEIGELCTRGYS------------VMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 609 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAP 688
Cdd:PRK12583 455 IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVD 531
|
570
....*....|....*....
gi 2462580884 689 GLPKTRSGKIMRRVLRKIA 707
Cdd:PRK12583 532 EFPMTVTGKVQKFRMREIS 550
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
144-703 |
2.74e-22 |
|
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: 100.81 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITT-DAFYRGEKLVNLKELADEALqkcqeKGFPVrccivvkhlgraelgmgdstsqSPPIKRSCPDvqgklkekskrvq 302
Cdd:cd17646 99 VLTTaDLAARLPAGGDVALLGDEAL-----AAPPA----------------------TPPLVPPRPD------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK----------- 368
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDEYPlgpgdrvlqkt 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 369 -YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFE----GIPTYpdvnrLWSIVDKYKVTKFYTAPTAIRLlm 443
Cdd:cd17646 187 pLSFDVSVWELFW-----------------PLVAGARLVVARpgghRDPAY-----LAALIREHGVTTCHFVPSMLRV-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 444 kFGDEPvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET----------GGHMLTPLPGATPMkPG 513
Cdd:cd17646 243 -FLAEP-AAGSCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV-PN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 514 SATfpffgvapailnesgeelegeaegYLL---LRtetswlevfKQPwPGIMRTVY--------GNH-------ERFETT 575
Cdd:cd17646 317 TRL------------------------YVLddaLR---------PVP-VGVPGELYlggvqlarGYLgrpaltaERFVPD 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 576 YFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 655
Cdd:cd17646 363 PFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAA 442
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2462580884 656 GHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd17646 443 GAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
144-708 |
4.21e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 100.97 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAFyRGEKLVN-LKELADEALQkcqekgfPVRCCIVVkhlgraelgmgDSTSQSPPIKRSCpdvqgklkekskrvq 302
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATPAPAPG--------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiSWNQGIDLWWHELMQEAGDECEPEwcdaeDPLFILYT-SGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWC 381
Cdd:PRK06164 157 ---ARVQLFALPDPAPPAAAGERAADP-----DAGALLFTtSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 382 TADIGWITGHSYVTyGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkHSRASLQVL 461
Cdd:PRK06164 228 ALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 462 GTVGepINPeAWLWYHRVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGS---ATFPFFGVapailn 528
Cdd:PRK06164 300 GFAS--FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEArvrARDPQDGA------ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 529 esgeelegeaegyLLLRTETSWLEVFKqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML 608
Cdd:PRK06164 371 -------------LLPDGESGEIEIRA---PSLMRGYLDNPD--ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 609 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEClYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAP 688
Cdd:PRK06164 433 RLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVE 508
|
570 580
....*....|....*....|...
gi 2462580884 689 GLPKTRSG---KIMRRVLRKIAQ 708
Cdd:PRK06164 509 AFPVTESAngaKIQKHRLREMAQ 531
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
144-704 |
8.18e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 99.59 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAfyrgeklvnLKELADEALQKCQekgfpvrccivvkhLGRAELGMGDSTsqsPPIKRSCPDvqgklkekskrvqp 303
Cdd:PRK08276 87 LIVSAA---------LADTAAELAAELP--------------AGVPLLLVVAGP---VPGFRSYEE-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqgidlwwhELMQEAGDECEPEWCDAEdplfILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHA 375
Cdd:PRK08276 127 -------------ALAAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 376 EDVFWCTADIGwitgHSYVT-YG--PLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTK 452
Cdd:PRK08276 187 DSVYLSPAPLY----HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 453 HSRASLQVLGTVGEPINPE------AWlWyhrvvGaqrcPIVD-TFWQTETGGHMLtplpgATPM----KPGSATFPFFG 521
Cdd:PRK08276 259 YDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSEdwlaHPGSVGKAVLG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 522 VApAILNESGEElegeaegyllLRTETSWLEVFKQPWPGImrTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWIT 601
Cdd:PRK08276 324 EV-RILDEDGNE----------LPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLT 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 602 GRIDDMLnVSGHL-LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIAT 680
Cdd:PRK08276 389 DRKSDMI-ISGGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKC 467
|
570 580
....*....|....*....|....
gi 2462580884 681 PDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK08276 468 PRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
144-705 |
1.20e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.47 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTqiTYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK07786 40 GNTT--TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAfyrgekLVNLKELADEALqkcqekgfPVRCCIVVkhlgraelgMGDSTsqsppikrscpdvqgklkekskrvqp 303
Cdd:PRK07786 118 VVTEAA------LAPVATAVRDIV--------PLLSTVVV---------AGGSS-------------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvggYMLYVATTFKYVFDFHA---EDVFW 380
Cdd:PRK07786 149 -----DDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLRTNGAdinSDVGF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 CTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHS 454
Cdd:PRK07786 221 VGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC---AEQQARPR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 455 RASLQVLGTVGEPiNPEAWL--WYHRVVGAQrcpIVDTFWQTEtgghmLTPLpgaTPM--------KPGSATFPFFGVAP 524
Cdd:PRK07786 289 DLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKLGSVGKVIPTVAA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 525 AILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGN----HERFETtyfkkfpGYYVTGDGCQRDQDGYYWI 600
Cdd:PRK07786 357 RVVDENMNDVPVGEVGEIVYRA------------PTLMSGYWNNpeatAEAFAG-------GWFHSGDLVRQDEEGYVWV 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 601 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLT-EELKKQIREKIGPIA 679
Cdd:PRK07786 418 VDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYK 494
|
570 580
....*....|....*....|....*.
gi 2462580884 680 TPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK07786 495 HPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
145-641 |
1.35e-21 |
|
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: 100.70 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsivfA------GFSSESLcERIL- 217
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 218 DSSCSLLITTDAFyrgeklvnLKELADEALQkcqekgfpvrcCIVVKHLGRAElgmgdsTSQSPPIKRSCPDvqgklkek 297
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLALDALALAA------EPATNPPVPVTPD-------- 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 298 skrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK------ 368
Cdd:COG1020 618 -------------------------------------DLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRRYGlgpgdr 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 369 ------YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF--EGIptyPDVNRLWSIVDKYKVTKFYTAPTAIR 440
Cdd:COG1020 661 vlqfasLSFDASVWEIFG-----------------ALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 441 LLMKFGDEPVtkhsrASLQVLGTVGEPINPEAWLWYHRVVGAQR---------CPIVDTFWQTETGGHMLTPLP-GaTPM 510
Cdd:COG1020 721 ALLDAAPEAL-----PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiG-RPI 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 511 kPGSATFpffgvapaILNesgeelegeaegylllrtetSWLevfkQPWP-GIM-------------------RTVygnhE 570
Cdd:COG1020 795 -ANTRVY--------VLD--------------------AHL----QPVPvGVPgelyiggaglargylnrpeLTA----E 837
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 571 RFETTYFkKFPG--YYVTGDGCQRDQDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 641
Cdd:COG1020 838 RFVADPF-GFPGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
107-638 |
4.33e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 97.86 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 107 VLDRNVheKKLGDKVAFYWstsgnssyrytcregNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPEL 186
Cdd:COG1022 16 LLRRRA--ARFPDRVALRE---------------KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 187 VVAMLACARIGALHSIVFAGfSSESLCERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--ALQKcqekgfpvrccIVV 263
Cdd:COG1022 79 VIADLAILAAGAVTVPIYPT-SSAEEVAYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 264 khlgraelgmgdstsqsppikrscpdvqgkLKEKSKRVQPQIswnqgidLWWHELMQEAGDECEPEW-------CDAEDP 336
Cdd:COG1022 143 ------------------------------LDPRGLRDDPRL-------LSLDELLALGREVADPAElearraaVKPDDL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 337 LFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGI 411
Cdd:COG1022 186 ATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 412 PTYPD------------VNRLW-SIVDKYkVTKFYTAPTAIRLL----MKFGdepvTKHSRASLQvlgtvGEPINPEAWL 474
Cdd:COG1022 259 DTLAEdlrevkptfmlaVPRVWeKVYAGI-QAKAEEAGGLKRKLfrwaLAVG----RRYARARLA-----GKSPSLLLRL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 475 WY---HRVVGAQrcpivdtfWQTETGGHMLTPLPGATPMKPgsATFPFF---GVaPaILNesgeelegeaeGYLLlrTET 548
Cdd:COG1022 329 KHalaDKLVFSK--------LREALGGRLRFAVSGGAALGP--ELARFFralGI-P-VLE-----------GYGL--TET 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 549 S------WLEVFK-----QPWPG-----------------IMRTVYGNHErfETTyfKKFP--GYYVTGD-GcQRDQDGY 597
Cdd:COG1022 384 SpvitvnRPGDNRigtvgPPLPGvevkiaedgeilvrgpnVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-ELDEDGF 458
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2462580884 598 YWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGH 638
Cdd:COG1022 459 LRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-706 |
7.01e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 96.85 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALhSIVFagfsseslcerildsscs 222
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 llittdafyrgeklvNLKELADEALQKCQEKGFPVRCCivvkhlgraelgmgdstsqSPPIKRSCPDVQGKLKekskrVQ 302
Cdd:PRK06839 84 ---------------NIRLTENELIFQLKDSGTTVLFV-------------------EKTFQNMALSMQKVSY-----VQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQIsWNQGIDlwwhELMQEAGDECEPEwcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCT 382
Cdd:PRK06839 125 RVI-SITSLK----EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 383 ADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTKFYTAPT---AIRLLMKFgdepvTKHSRASLQ 459
Cdd:PRK06839 197 LPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 460 VLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 539
Cdd:PRK06839 268 WFYNGGAPC-PEELM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 540 GYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 619
Cdd:PRK06839 344 GELLIRG------------PNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 620 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 699
Cdd:PRK06839 409 VEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQ 485
|
....*..
gi 2462580884 700 RRVLRKI 706
Cdd:PRK06839 486 KAQLVNQ 492
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
147-703 |
8.63e-21 |
|
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: 96.24 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsIVFAGFSseslcerildsscsllit 226
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 tdafYRGEKLVNLKELADEALqkcqekgfpvrcCIVvkhlgraelgmgdstsqsppikrscPDVQGklkekskRVQPQis 306
Cdd:cd05920 99 ----HRRSELSAFCAHAEAVA------------YIV-------------------------PDRHA-------GFDHR-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 307 wnqgidlwwhELMQEAGDECEpewcdaeDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIG 386
Cdd:cd05920 129 ----------ALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 387 witgHSYVTYGP-----LANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVL 461
Cdd:cd05920 191 ----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 462 GTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSAtf 517
Cdd:cd05920 261 QVGGARLSPAL---ARRVPPVLGCTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEE-- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 518 pffgvapailnesgeelegeaeGYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGY 597
Cdd:cd05920 336 ----------------------GELLTRG------------PYTIRGYYRAPEHNARAFTPD--GFYRTGDLVRRTPDGY 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 598 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSPKLTEELKKQIREKigP 677
Cdd:cd05920 380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--G 453
|
570 580
....*....|....*....|....*....
gi 2462580884 678 IAT---PDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd05920 454 LAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
146-706 |
2.51e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 95.21 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 146 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSLLI 225
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL-EHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TTDAFYRgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQgklkekskrVQPQi 305
Cdd:PRK06155 123 VVEAALL------------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAA---------VQPG- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 swnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTvggymlyvattfkyvfdfHAEDVFW---CT 382
Cdd:PRK06155 181 -----------------------------DTAAILYTSGTTGPSKGVCCP------------------HAQFYWWgrnSA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 383 ADIGWITGHSYVTYGPL-------------ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEP 449
Cdd:PRK06155 214 EDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLS---QP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 VTKHSRAS-LQVLGTVGEPINpeawlwYHRVVGAqRC--PIVDTFWQTETGGHMLTPLPGAtpmKPGSATFPFFGVAPAI 526
Cdd:PRK06155 287 ARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEARV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 527 LNESGEELEGEAEGYLLLRTETswlevfkqpwPGIMRTVYGNH-----ERFETTYFKkfpgyyvTGDGCQRDQDGYYWIT 601
Cdd:PRK06155 357 VDEHDQELPDGEPGELLLRADE----------PFAFATGYFGMpektvEAWRNLWFH-------TGDRVVRDADGWFRFV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 602 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATP 681
Cdd:PRK06155 420 DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVP 496
|
570 580
....*....|....*....|....*
gi 2462580884 682 DYIQNAPGLPKTRSGKIMRRVLRKI 706
Cdd:PRK06155 497 RYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
335-707 |
3.69e-20 |
|
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: 92.01 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 414
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 415 PDVNRlwsivdkYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGAQRCPIVDTFWQT 494
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 495 ETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGeelegeaegyLLLRTETSWLEVFKQPWPGimrtvygnhERFEt 574
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGE----------IWVGGASLAMGYLRGQLVP---------EFNE- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 575 tyfkkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC 654
Cdd:cd17630 204 ------DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 655 DGHTfspklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:cd17630 278 GPAD-----PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
560-704 |
1.39e-19 |
|
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: 90.80 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 560 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 639
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462580884 640 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-703 |
5.21e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.71 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAFyrGEKLvnlkeladealqkcqekgfPVRCCIVVKHLGRAELGMgDSTSQSPPIKRSCPdvqgklkekskrvqp 303
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRPAAWL-EGYSEENPGTELNP--------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHT------------------VGGYMLYVaT 365
Cdd:PRK12316 655 ------------------------------ENLAYVIYTSGSTGKPKGAGNRhralsnrlcwmqqayglgVGDTVLQK-T 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 366 TFKyvFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMK 444
Cdd:PRK12316 704 PFS--FDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 445 FGDEPvtkhSRASLQVLGTVGEPINPEAWLwyhRVVG-AQRCPIVDTFWQTETGghmlTPLPGATPMKPGSATF----PF 519
Cdd:PRK12316 763 DEDVA----SCTSLRRIVCSGEALPADAQE---QVFAkLPQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPI 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 520 FGVAPAILNESGEELEGEAEGYLLLRTEtswlevfkqpwpGIMRTVYG----NHERFETTYFKKFPGYYVTGDGCQRDQD 595
Cdd:PRK12316 832 ANLACYILDANLEPVPVGVLGELYLAGR------------GLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRAD 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 596 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKI 675
Cdd:PRK12316 900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAASL 972
|
570 580
....*....|....*....|....*...
gi 2462580884 676 GPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK12316 973 PEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
339-704 |
7.27e-19 |
|
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: 90.13 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 339 ILYTSGSTGKPKGVVHTVGGYMLYVAT--TFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 416
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 417 VNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgaqrcPIVDTFW 492
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 Q-TETGGhmLTPLPGATPMK-PGSATFPFFGVApAILNesgeelegeaegylllrtetswlEVFKQPWPGIMRTVY--GN 568
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILD-----------------------EDGNEVPPGEIGEVYfaNG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 569 -----HERFETTYFKKFPGYYVT-GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 642
Cdd:cd05929 331 pgfeyTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEE 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462580884 643 KGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:cd05929 411 LGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
335-700 |
7.57e-19 |
|
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: 88.23 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDvfwctadigwitghSYVTYGPLA-----NGATSVLF 408
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIeSFVCN--EDLFNISGED--------------AILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 409 EG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKhsrasLQVLGTVGEPINPEAwlwyHRVVGAQ- 483
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 484 -RCPIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylllrtetswlevfkqpwpGIM 562
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG----------------------------GEI 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 563 RTVYGNHERFETTY----FKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGH 638
Cdd:cd17633 185 GKIFVKSEMVFSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 639 PHPVKGEcLYCFVTLCDGHTFsPKLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMR 700
Cdd:cd17633 265 PDARFGE-IAVALYSGDKLTY-KQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
145-706 |
8.50e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 90.37 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITTDAFyrgeklvnlkelaDEALQKCQEKgfpvrccivvkhLGRAeLGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQ 304
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPPD------------LGRL-RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 ISWNQGIdlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVH-------TVGGYMLYVAttfkyvfdFHAED 377
Cdd:PRK07788 205 PPKPGGI---------------------------VILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWCTADIGWITGHSYVTYGpLANGATSVL---FEGIPTYPDVnrlwsivDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 454
Cdd:PRK07788 250 TTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 455 RASLQVLGTVGEPINPEAWLWYHRVVGaqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSATFPFFGVAPAILNe 529
Cdd:PRK07788 322 TSSLKIIFVSGSALSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILD- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 530 sgeelegeaegylllrtetswlEVFKQPWPGIMRTVY-GNHERFETtYF-----KKFPGYYVTGDGCQRDQDGYYWITGR 603
Cdd:PRK07788 392 ----------------------ENGNEVPRGVVGRIFvGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 604 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDY 683
Cdd:PRK07788 449 DDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAIKDYVRDNLARYKVPRD 525
|
570 580
....*....|....*....|...
gi 2462580884 684 IQNAPGLPKTRSGKIMRRVLRKI 706
Cdd:PRK07788 526 VVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-705 |
1.48e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.81 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 114 EKKLGDkvafYWSTSGNSSYRYTCREGNEpgeTTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAC 193
Cdd:PRK06087 22 DASLAD----YWQQTARAMPDKIAVVDNH---GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 194 ARIGALhsivfagfsseslcerildsSCSLLITtdafYRGEKLVnlkeladEALQKCQEKGFpvrCCIVVKHLGRAElgm 273
Cdd:PRK06087 95 LKVGAV--------------------SVPLLPS----WREAELV-------WVLNKCQAKMF---FAPTLFKQTRPV--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 274 gdstSQSPPIKRSCPDVQG-KLKEKSKRVQPQISWNQGIDLwwHELMQEagdecePEWCDAEDPLFILYTSGSTGKPKGV 352
Cdd:PRK06087 138 ----DLILPLQNQLPQLQQiVGVDKLAPATSSLSLSQIIAD--YEPLTT------AITTHGDELAAVLFTSGTEGLPKGV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 353 VHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPtyPDvnRLWSIVDKYKVTKF 432
Cdd:PRK06087 206 MLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT--PD--ACLALLEQQRCTCM 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 433 YTAPTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPInPEawlwyhRVVgaQRC-----PIVDTFWQTETGGHMLTPLPGA 507
Cdd:PRK06087 281 LGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI-PK------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 508 TPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERfeTTYFKKFPGYYVTG 587
Cdd:PRK06087 350 LSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRG------------PNVFMGYLDEPEL--TARALDEEGWYYSG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 588 DGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcDGHTFSPKLTEEL 667
Cdd:PRK06087 416 DLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL-KAPHHSLTLEEVV 494
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462580884 668 KKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK06087 495 AFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
149-704 |
8.82e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 87.12 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 228
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AFyrgeklvnlKELADEALQKCqekgfpvrccivvkhlgraelgmgdstsqsPPIKRScpdvqgklkekskrvqpqISWN 308
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI------------------VAWT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 QGIDLWWHELMQEAGDECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-VGGYMlyvatTFKYVFDfhaedvfwctaDIGW 387
Cdd:PRK13382 172 DEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD-----------RTPW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 388 ITGHSYVTYGPL--ANGATSVLFEGIPTYPDVNR-------LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASL 458
Cdd:PRK13382 235 RAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 459 QVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSATFPFFGVAPAILNesgeel 534
Cdd:PRK13382 315 RFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILD------ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 535 egeaegylllrtetswlEVFKQPWPGIMRTVY-GNHERFE-----TTyfKKF-PGYYVTGDGCQRDQDGYYWITGRIDDM 607
Cdd:PRK13382 381 -----------------QDFREVPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 608 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNA 687
Cdd:PRK13382 442 IVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVL 518
|
570
....*....|....*..
gi 2462580884 688 PGLPKTRSGKIMRRVLR 704
Cdd:PRK13382 519 DELPRGATGKILRRELQ 535
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
194-704 |
8.95e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 86.99 E-value: 8.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 194 ARIGALHSIVFAGFSSESLCERILDSSCSLL--ITTDAFYR-GEKLVNLKELADEAL---QKCQEKGFPVRCciVVKHLG 267
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALarVLYDAGLRtGDVVALLSDNSPEALvvlWAALRSGLYITA--INHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 268 RAELG--MGDSTSQsppIKRSCPDVQGKLKEKSKRVQPQISWNQGIDLW--WHELMQEAGDECEPEWCDAedplFILYTS 343
Cdd:PRK13390 85 APEADyiVGDSGAR---VLVASAALDGLAAKVGADLPLRLSFGGEIDGFgsFEAALAGAGPRLTEQPCGA----VMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 344 GSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHAEDVFWCTADIGwitgHSyvtyGPL-------ANGATSVLF 408
Cdd:PRK13390 158 GTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 409 EGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEA------WLWyhrvvga 482
Cdd:PRK13390 227 KRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVkhamidWLG------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 483 qrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGeaegylllRTETSWLEVFKQPWpgi 561
Cdd:PRK13390 296 ---PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDLHICDDDGNELPAG--------RIGTVYFERDRLPF--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 562 mrTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 641
Cdd:PRK13390 361 --RYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 642 VKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK13390 439 EMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
145-701 |
1.18e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.86 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsIVFAgfsseslceriLDSScslL 224
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITTDAFYRGEKLVNLKELADeALQKCQEKGFPVRCCIVVKHLGRaelgmgdSTSQSPPIKRSCPDVQGKLkekskrvQPQ 304
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGG-------DSGPSGGTLSVHLDAATEP-------TPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 ISWNQGIdlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGymlyVATTFKYV---FDFHAEDVfwC 381
Cdd:PRK05852 168 TSTPEGL---------------------RPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 382 TADIGWITGHSYVT--YGPLANGATSVLfegiptyPDVNRL-----WSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 454
Cdd:PRK05852 221 VAVMPLYHGHGLIAalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 455 RASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSATFPFFGVA-- 523
Cdd:PRK05852 294 PAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgs 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 524 ------PAilnesgeelegeaegylllRTETSWLEvfkqpWPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGY 597
Cdd:PRK05852 371 dglplpAG-------------------AVGEVWLR-----GTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGD 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 598 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGP 677
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRERLAA 500
|
570 580
....*....|....*....|....
gi 2462580884 678 IATPDYIQNAPGLPKTRSGKIMRR 701
Cdd:PRK05852 501 FEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
145-710 |
1.45e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.54 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LH---------SIVFagfsseslce 214
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 215 rILDSSCS-LLITTDAFyrgeklvnlKELADEALQKCqekgfPVRCCIVVkhlgraelgmgdstsqsppikrscpDVQGK 293
Cdd:PRK08162 110 -MLRHGEAkVLIVDTEF---------AEVAREALALL-----PGPKPLVI-------------------------DVDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 294 LKEKSKRVQpqiswnqgiDLWWHELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTVGGYMLYVATTFKYVF 371
Cdd:PRK08162 150 EYPGGRFIG---------ALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 372 DFHAE-----DVFWCTadiGWitGHSY-VTygplANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMkf 445
Cdd:PRK08162 221 PKHPVylwtlPMFHCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 446 gdepvtkHSRASLQvlgtvgEPINpeawlwyHRVVG--AQRCPIVDTFWQTETGGHMLTPLPGATPM---------KPGS 514
Cdd:PRK08162 286 -------NAPAEWR------AGID-------HPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvcawQPEW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 515 ATFPFfgVAPAILNESGEELEGEAEGYLLLRTETSwLEVfkqPWPG-----IMrtVYGN-------------HERFETty 576
Cdd:PRK08162 346 DALPL--DERAQLKARQGVRYPLQEGVTVLDPDTM-QPV---PADGetigeIM--FRGNivmkgylknpkatEEAFAG-- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 577 fkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDG 656
Cdd:PRK08162 416 -----GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2462580884 657 HTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 710
Cdd:PRK08162 491 ASATE---EEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
582-704 |
2.18e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 86.26 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 661
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580884 662 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
165-709 |
2.24e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 85.80 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 165 LRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgEKLVNLKelad 244
Cdd:PLN02246 67 LHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV--DKLKGLA---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 245 ealqkcQEKGFPVRCCivvkhlgraelgmgdstsQSPPikRSCpdvqgklkekskrvqpqiswnqgidLWWHELMQEAGD 324
Cdd:PLN02246 141 ------EDDGVTVVTI------------------DDPP--EGC-------------------------LHFSELTQADEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 325 ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAttfKYV------FDFHAEDVFWCTADIGWITGHSYVTYGP 398
Cdd:PLN02246 170 ELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 399 LANGATSVLfegIPTYpDVNRLWSIVDKYKVTkfyTAPTAIRLLMKFGDEP-VTKHSRASLQVLGTVGEPINPEawlwYH 477
Cdd:PLN02246 247 LRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKE----LE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 478 RVVGAqRCP---IVDTFWQTETGGHMLTPLPGA---TPMKPGS-ATFpffgVAPAILNesgeelegeaegylLLRTETSW 550
Cdd:PLN02246 316 DAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGScGTV----VRNAELK--------------IVDPETGA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 551 LEVFKQPW------PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 624
Cdd:PLN02246 377 SLPRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 625 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELK----KQI--REKIGPIATPDYIqnapglPKTRSGKI 698
Cdd:PLN02246 455 ISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI------PKAPSGKI 525
|
570
....*....|..
gi 2462580884 699 MRRVLR-KIAQN 709
Cdd:PLN02246 526 LRKDLRaKLAAG 537
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
148-704 |
4.38e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.94 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGfsseslcerildsscsllitt 227
Cdd:PRK06145 27 EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA----VFLP--------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 dafyrgeklVNLKELADEALQKCQEKGfpvrccivvkhlgrAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVqpqisw 307
Cdd:PRK06145 82 ---------INYRLAADEVAYILGDAG--------------AKLLLVDEEFDAIVALETPKIVIDAAAQADSRR------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqgidlwwhelMQEAGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTVGgymlyvattfkyvfdfhaeDVFWCTAD-- 384
Cdd:PRK06145 133 -----------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhv 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 --IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTK 452
Cdd:PRK06145 183 iaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDR--DR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 453 HSRASLQVLGTVGEPiNPEAWLW-YHRVVGAQRcpIVDTFWQTET-GGHMLTPlPGATPMKPGSATFPFFGVAPAILNES 530
Cdd:PRK06145 261 FDLDSLAWCIGGGEK-TPESRIRdFTRVFTRAR--YIDAYGLTETcSGDTLME-AGREIEKIGSTGRALAHVEIRIADGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 531 GEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNV 610
Cdd:PRK06145 337 GRWLPPNMKGEICMRG------------PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIIS 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 611 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGL 690
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDEL 478
|
570
....*....|....
gi 2462580884 691 PKTRSGKIMRRVLR 704
Cdd:PRK06145 479 PRNPSGKVLKRVLR 492
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
332-703 |
5.24e-17 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 84.44 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVV-------HTVGGY------------MLYVATtfkYVFDFHAEDvfWCTAdigwitghs 392
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD--FARS--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 393 yvtygpLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 470
Cdd:cd17650 157 ------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 471 EAWLwYHRVvgAQRCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSatfPFFGVAPAILNEsgeelegeaegyl 542
Cdd:cd17650 228 FKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDE------------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 543 llRTETSWLEVFKQPWPGIMRTVYGNHERFETTYfKKF------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHL 614
Cdd:cd17650 287 --RLQPQPVGVAGELYIGGAGVARGYLNRPELTA-ERFvenpfaPGerMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 615 LSTAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdgHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLP 691
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA----ATLN---TAELRAFLAKELPSYMIPSYYVQLDALP 435
|
410
....*....|..
gi 2462580884 692 KTRSGKIMRRVL 703
Cdd:cd17650 436 LTPNGKVDRRAL 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
332-707 |
6.28e-17 |
|
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: 84.31 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGI 411
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 412 PTYPdvNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepVTKHSRASLQVLGTVGEPINPEAW-LWYHRvvgaQRCPIVDT 490
Cdd:cd05909 223 PLDY--KKIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDTLRqEFQEK----FGIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 491 FWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTEtswlevfkqpwPGIMRTVYGNHE 570
Cdd:cd05909 293 YGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-----------PNVMLGYLNEPE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 571 RFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVGHPHPVKGECLYC 649
Cdd:cd05909 361 LTSFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVL 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 650 FVTlcdGHTFSPkltEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:cd05909 438 LTT---TTDTDP---SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
7.27e-17 |
|
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: 74.82 E-value: 7.27e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCpgpflRYNFDVTKGkIFIEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
332-708 |
8.39e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVV--HTvGGYMLYVATTFKY---VFDFH--AEDVFWCTadiGWItghsyVTYGPLANGAT 404
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWemgTCPVYlwTLPMFHCN---GWT-----FTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 405 SVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGAQr 484
Cdd:PLN03102 255 SVCMRHV-TAPEI---YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 485 cpIVDTFWQTETGGHML--------TPLPGATPMKPGSATfpffGVApaILNESGEELEGEAEGYLLLRTETSWLEVFKQ 556
Cdd:PLN03102 327 --VMHAYGLTEATGPVLfcewqdewNRLPENQQMELKARQ----GVS--ILGLADVDVKNKETQESVPRDGKTMGEIVIK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 557 PwPGIMRTvYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 636
Cdd:PLN03102 399 G-SSIMKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVV 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 637 GHPHPVKGECLYCFVTLCDGHTFSPKLTEELK-------KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 708
Cdd:PLN03102 475 AMPHPTWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
318-711 |
9.46e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.39 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 318 LMQEAGDECEPEW-----CDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAED 377
Cdd:PRK12316 3175 LDLDRGDENYAEAnpairTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVlqfttfsFDVFVEE 3254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgdEPVTKHSRAS 457
Cdd:PRK12316 3255 LFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTS 3312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 458 LQVLGTVGEPINPEAwlwYHRVVGAQrcPIVDTFWQTETGGHMLT-----PLPGATPMKPgsatfPFFGVAPAILNESGE 532
Cdd:PRK12316 3313 LKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEATITVTHwqcveEGKDAVPIGR-----PIANRACYILDGSLE 3382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 533 ELEGEAEGYLLLRTETSWLEVFKQPWPgimrtvygNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 612
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLARGYHNRPGL--------TAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRG 3454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 613 HLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIgpiatPDYIQNA----- 687
Cdd:PRK12316 3455 FRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllfl 3522
|
410 420
....*....|....*....|....*...
gi 2462580884 688 PGLPKTRSGKIMRRVLRK----IAQNDH 711
Cdd:PRK12316 3523 ERMPLTPNGKLDRKALPRpdaaLLQQDY 3550
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
145-703 |
4.56e-16 |
|
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: 81.61 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSL 223
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI-QYILeDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkeksKRVQP 303
Cdd:cd17655 98 LLTQ-----------------------------------------------------------------------SHLQP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 QISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGV----------VHTVGGYM-----LYVATTFK 368
Cdd:cd17655 107 PIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWANKVIyqgehLRVALFAS 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 369 YVFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE 448
Cdd:cd17655 187 ISFDASVTEIF-----------------ASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 449 PvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGAqrCPIVDTFWQTETG-GHMLTPLpgaTPMKPGSATFPffgVAPAI 526
Cdd:cd17655 249 E-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSVP---IGKPL 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 527 LNESGeelegeaegYLLlrtetswlEVFKQPWP------------GIMRTvYGNHErfETTYfKKF------PG--YYVT 586
Cdd:cd17655 316 GNTRI---------YIL--------DQYGRPQPvgvagelyiggeGVARG-YLNRP--ELTA-EKFvddpfvPGerMYRT 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 587 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdghTFSPKLT-E 665
Cdd:cd17655 375 GDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI------VSEKELPvA 448
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462580884 666 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd17655 449 QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
303-709 |
5.03e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 81.36 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQISWNQgidlwWHELMQEAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMlyvattfkYVFDFHAEDVFWC 381
Cdd:PRK07638 117 RVIEIDE-----WKRMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 382 TADIGWITG---HSYVTYGplangATSVLFEG-----IPTYPDVNRLWSIvDKYKVTKFYTAPTAIRLLMK---FGDEPV 450
Cdd:PRK07638 183 REDSVLIAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 451 T------KHSRASLQVLGTvgepINPEAWLWyhrvvgaqrcpivdTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAP 524
Cdd:PRK07638 257 KiissgaKWEAEAKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 525 AILNesgeelegeaegylllrtetswlEVFKQPWPGIMRTVYGNHERFETTY------FKKFP--GYYVTGD-GCQrDQD 595
Cdd:PRK07638 319 RICN-----------------------EAGEEVQKGEIGTVYVKSPQFFMGYiiggvlARELNadGWMTVRDvGYE-DEE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 596 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSpkltEELKKQIREKI 675
Cdd:PRK07638 375 GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRL 447
|
410 420 430
....*....|....*....|....*....|....
gi 2462580884 676 GPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 709
Cdd:PRK07638 448 SSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
316-706 |
8.17e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 8.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 316 HELMQEAGDEC-EPEWC-----DAEDPLFILYTSGSTGKPKGVVHTVGG-----------YMLYVATT----FKYVFDFH 374
Cdd:PRK12467 3213 TALTLDRLDLNgYSENNpstrvMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGA 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 375 AEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDepvtKHS 454
Cdd:PRK12467 3293 QERFLW-----------------TLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG----GAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 455 RASLQVLGTVGEPINPEAWLWYHRVV---------GAQRCPIVDTFWQTETGGhmlTPLPGATPMKPGSAtfpffGVAPA 525
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIY 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 526 ILNESGEELEGEAEGYLLLRTEtswlevfkqpwpGIMRtvyGNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGY 597
Cdd:PRK12467 3422 VLDGQLNPVPVGVAGELYIGGV------------GLAR---GYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGV 3486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 598 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSPKLTEELKKQIREKIgp 677
Cdd:PRK12467 3487 IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL-- 3560
|
410 420 430
....*....|....*....|....*....|....
gi 2462580884 678 iatPDYIQNA-----PGLPKTRSGKIMRRVLRKI 706
Cdd:PRK12467 3561 ---PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
334-706 |
1.38e-15 |
|
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: 80.26 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVVHT--------------VGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITGhsyvtygpl 399
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 400 anGATSVLfegIPTYPDVNRLWSIVDkYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrv 479
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 480 VGAQ-----RCPIV-DTFWQTETGGHML-TPlpgATPMKPGSA--TFPFFGVAPAILNESGeelegeaegyLLLRTETSW 550
Cdd:cd17642 317 VGEAvakrfKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVgkVVPFFYAKVVDLDTGK----------TLGPNERGE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 551 LeVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 630
Cdd:cd17642 384 L-CVKGP--MIMKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKI 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 631 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEEL-------KKQIRekiGPIATPDYIqnapglPKTRSGKIMRRVL 703
Cdd:cd17642 459 FDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYvasqvstAKRLR---GGVKFVDEV------PKGLTGKIDRRKI 529
|
...
gi 2462580884 704 RKI 706
Cdd:cd17642 530 REI 532
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
145-708 |
1.47e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 80.27 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITTDAFYrgeklvnlkELADEALQ---KCQEKGFPVRCCIVVkhlgraelgmGDSTSQSPPIKRSCPDVQGKLKEKSKRV 301
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKilaEKKKSSFKPPLLIVI----------GDPTCDPKSLQYALGKGAIEYEKFLETG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 302 QPQISWNQGIDLWwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV-HTVGGYMLyvATTFKYVFDFHAEDVFW 380
Cdd:PLN02479 183 DPEFAWKPPADEW--------------------QSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 CTADIGWITGHSYvTYGPLANGATSVLFEGIPTypdvNRLWSIVDKYKVTKFYTAPTAIRLL------------------ 442
Cdd:PLN02479 241 WTLPMFHCNGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 443 MKFGDEP----VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------RVVGAQRCPIVDTfwqtet 496
Cdd:PLN02479 316 MTAGAAPppsvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT------ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 497 gghmltplpgaTPMKPGSATFPFFGvapailnesgeelegeaegYLLLRTETswleVFKqpwpGIMRTVYGNHERFETty 576
Cdd:PLN02479 390 -----------KTMKPVPADGKTMG-------------------EIVMRGNM----VMK----GYLKNPKANEEAFAN-- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 577 fkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDG 656
Cdd:PLN02479 430 -----GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPG 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2462580884 657 HTFS--PKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 708
Cdd:PLN02479 505 VDKSdeAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
582-709 |
1.97e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.65 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtf 659
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK------- 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 660 SPKLTEELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 709
Cdd:PRK10946 482 EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
148-703 |
2.58e-15 |
|
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: 79.24 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 226
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 TDafyrgeklvnlkeladEALQKCQekgfPVRCCIVVkhlgraeLGMGDSTSQSPPikrscpdvqgklkekSKRVQPQis 306
Cdd:cd12114 91 DG----------------PDAQLDV----AVFDVLIL-------DLDALAAPAPPP---------------PVDVAPD-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 307 wnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV--------------F 371
Cdd:cd12114 127 ----------------------------DLAYVIFTSGSTGTPKGVMISHRAALNTILdINRRFAvgpddrvlalsslsF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 372 DFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegiPTY---PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF-GD 447
Cdd:cd12114 179 DLSVYDIF-----------------GALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVlEA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 448 EPVTKHS-R--------------ASLQVLGTVGEPIN----PEAWLW--YHRVVGA---------------QRCPIVDTf 491
Cdd:cd12114 238 AQALLPSlRlvllsgdwipldlpARLRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 492 wqtetgghMLTPLPgatPMKPGSATFPFFGVAPAILNESgeelegeaegyllLRTETSWLEVfkqpwpgimrtvyGNHER 571
Cdd:cd12114 317 --------RGRDCP---DWVPGELWIGGRGVALGYLGDP-------------ELTAARFVTH-------------PDGER 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 572 FettyfkkfpgyYVTGD-GCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCF 650
Cdd:cd12114 360 L-----------YRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAF 426
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 651 VTLCDGHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd12114 427 VVPDNDGT--PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
335-700 |
2.89e-15 |
|
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: 77.70 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 335 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 414
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 415 pDVNRLWSIVDKYKVTKFYT-APTAIRLLMKFGDEPVtkhSRASLQVLGTVGEPINPEAWlwyHRVVGAqrcpivdTFW- 492
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 493 ---QTETGGhMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTETswleVFKQPWpgimrtvyGNH 569
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL----VFQGYW--------NLP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 570 ERFETTyFKKfpGYYVTGDGCQRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL 647
Cdd:cd17637 207 ELTAYT-FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 648 YCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 700
Cdd:cd17637 284 KAVCVLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
138-704 |
4.07e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.31 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 138 REGNEPGETTQ--------ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 209
Cdd:PRK06060 12 EQASEAGWYDRpafyaadvVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 210 ESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrs 286
Cdd:PRK06060 92 DDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA---------------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 287 cpdvqgklkeksKRVQPQiswnqgidlwwhelmqeagdECEPEWCDAEdpLFILYTSGSTGKPKGVVHTVggymlyvATT 366
Cdd:PRK06060 132 ------------ARVAPG--------------------GYEPMGGDAL--AYATYTSGTTGPPKAAIHRH-------ADP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 367 FKYVFDFHAEDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVNRLWSIvdKYKVTKFYTAPTAI 439
Cdd:PRK06060 171 LTFVDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAILSA--RFGPSVLYGVPNFF 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 440 RLLMkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrCPIVDTFWQTETGGHMLTPlpGATPMKPGS--ATF 517
Cdd:PRK06060 248 ARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTlgRVL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 518 PFFG---VAPailneSGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTyfkkfPGYYVTGDGCQRDQ 594
Cdd:PRK06060 320 PPYEirvVAP-----DGTTAGPGVEGDLWVRG------------PAIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDS 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 595 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREK 674
Cdd:PRK06060 378 DGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNR 457
|
570 580 590
....*....|....*....|....*....|
gi 2462580884 675 IGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK06060 458 LSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
149-706 |
5.95e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 78.35 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITt 227
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 dafyrgeklvnlkelADEALQKCQEKGFPVrccivvkhlgraeLGMGDStsqsppikrscpdvqGKLKEKSKRVQPqisw 307
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV-------------IGVPEN---------------YDFDSKRIEFPK---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqgidlwWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA----EDVFWCTA 383
Cdd:PLN02574 179 -------FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 384 DIGWITGHSYVTYGPLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGT 463
Cdd:PLN02574 252 PMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPINPEAWLWYhrvvgAQRCPIVDtFWQtetgGHMLTPLPGATPMKPGSATFPFFGvAPAILNESGEELEGEAEGYLL 543
Cdd:PLN02574 327 GAAPLSGKFIQDF-----VQTLPHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYS-SVGLLAPNMQAKVVDWSTGCL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 544 LRTETS---WLEvfkqpWPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 620
Cdd:PLN02574 396 LPPGNCgelWIQ-----GPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 621 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 700
Cdd:PLN02574 469 EAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
....*.
gi 2462580884 701 RVLRKI 706
Cdd:PLN02574 546 RELKRS 551
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
148-705 |
7.12e-15 |
|
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: 77.86 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCErildsscsllitt 227
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAY------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 dafyrgeklvnlkeladeALQKCQEKGFPVRCCIVvkHLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQisw 307
Cdd:cd05915 91 ------------------ILNHAEDKVLLFDPNLL--PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADP--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqgidlwwhelmqEAGDECepewcdaeDPLFILYTSGSTGKPKGVVHT-VGGYMLYVATTFKYVFDFHAEDVFWCTADIG 386
Cdd:cd05915 148 -------------VRVPER--------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 387 WITGHSYVtYGPLANGATSVLFEGIPTypDVNRLWSIVdKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGE 466
Cdd:cd05915 207 HVNAWCLP-YAATLVGAKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 467 PinPEAWL-----WYHRVVGAQRCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSATFPFFGVAPAILNESGEELE 535
Cdd:cd05915 282 A--PRSLIarferMGVEVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 536 G--EAEGYLLLRTETswlevfkqpwpgIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 613
Cdd:cd05915 355 KdgKALGEVQLKGPW------------ITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 614 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKqireKIGPIAT-PDYIQNAPGLPK 692
Cdd:cd05915 421 WISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLK----AGFAKWQlPDAYVFAEEIPR 496
|
570
....*....|...
gi 2462580884 693 TRSGKIMRRVLRK 705
Cdd:cd05915 497 TSAGKFLKRALRE 509
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
582-705 |
8.81e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.87 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 661
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580884 662 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
315-642 |
9.51e-15 |
|
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: 77.51 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 315 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMlYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 394
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 395 TYGPLANGATSVLFEGIPTYPD------------VNRLWS-----IVDKYKVTKfytaptaIRLLMK--FGDEPVTKHSR 455
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWTkfqqgVQDKIPQQK-------LNLLLKipVVNSLVKRKVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 456 ASL-----QVLGTVGEPINPEAWLWYHRVvgaqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSATFPFFGVAPAIlnes 530
Cdd:cd05932 270 KGLgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 531 geelegEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNV 610
Cdd:cd05932 340 ------SEDGEILVRS------------PALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKT 399
|
330 340 350
....*....|....*....|....*....|....*
gi 2462580884 611 S-GHLLSTAEVESALVEHEAVAEAAVVGH--PHPV 642
Cdd:cd05932 400 SkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
148-697 |
1.10e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 77.62 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 227
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 DAFyrGEKLVNLKEladeALQKcqekgfpVRCCIVVkhlgraelgmGDSTSQSPPikrscpdvqgklkekskrvqpqisw 307
Cdd:PRK07798 108 REF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLL------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 NQGIDlwWHELMQEAGDECEPEWCDAEDpLFILYTSGSTGKPKGVVHT--------VGGYMLYVATTFKYVFDfHAEDVF 379
Cdd:PRK07798 140 PGAVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRqedifrvlLGGRDFATGEPIEDEEE-LAKRAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 380 WCTADIGWITG---H---SYVTYGPLANGATSVLfegiptYP----DVNRLWSIVDKYKVTkfytaptairLLMKFGD-- 447
Cdd:PRK07798 216 AGPGMRRFPAPplmHgagQWAAFAALFSGQTVVL------LPdvrfDADEVWRTIEREKVN----------VITIVGDam 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 448 -EPVTKHSRA-------SLQVLGTVGEPINP---EAWLWY--HRVvgaqrcpIVDTFWQTETGGHMLtplpGATPMKPGS 514
Cdd:PRK07798 280 aRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALLELlpNVV-------LTDSIGSSETGFGGS----GTVAKGAVH 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 515 ATFPFFGVAPAILnesgeelegeaegylLLRTETSWLEvfkqpwPG------IMRT------VYGNHERFETTyFKKFPG 582
Cdd:PRK07798 349 TGGPRFTIGPRTV---------------VLDEDGNPVE------PGsgeigwIARRghiplgYYKDPEKTAET-FPTIDG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 583 --YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS 660
Cdd:PRK07798 407 vrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPD 486
|
570 580 590
....*....|....*....|....*....|....*..
gi 2462580884 661 PkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 697
Cdd:PRK07798 487 L---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
582-704 |
1.53e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.98 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 661
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----P 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580884 662 KLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK07059 510 ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
332-705 |
2.16e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTfkyvfdfhaEDVFWCTADIGWITGHSYV-------TYGPLANGAt 404
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYHPLINGA- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 405 SVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGtvGEPINPEAW-LWY------- 476
Cdd:PRK12316 4762 SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQASYdLAWralkpvy 4837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 477 -HRVVGAQRCPIVDTFWQTETGghmltPLPGATPMKPGSatfPFFGVAPAILNESGEELEGEAEGYLLLRTETSWLEVFK 555
Cdd:PRK12316 4838 lFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLE 4909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 556 QPwpgiMRTVygnhERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 633
Cdd:PRK12316 4910 RP----ALTA----ERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 634 AVVGHPHPVkGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 703
Cdd:PRK12316 4981 VVIAQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERL-----PEYMVPAhlvflARMPLTPNGKLDRKAL 5054
|
..
gi 2462580884 704 RK 705
Cdd:PRK12316 5055 PQ 5056
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
149-705 |
3.91e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.92 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 228
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 229 AFYrgEKLVNLKELADEALQKcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 308
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLDR----------------------------------------------------------- 2127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 309 qgiDLWWHELMQEAgdecePEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYMLYVATTFKY---------------VFD 372
Cdd:PRK12316 2128 ---DAEWADYPDTA-----PAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyelspadcelqfmsfSFD 2199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 373 FHAEDVFWctadigwitghsyvtygPLANGATSVLFEGipTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTK 452
Cdd:PRK12316 2200 GAHEQWFH-----------------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERD 2257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 453 HSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSATFPFFGVAPA-----I 526
Cdd:PRK12316 2258 GRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayI 2332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 527 LNESGEELEGEAEGYLLLRTEtswlevfkqpwpGIMRTVYG----NHERFETTYFKKFPG-YYVTGDGCQRDQDGYYWIT 601
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGE------------GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYL 2400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 602 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATP 681
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAEDLL---AELRAWLAARLPAYMVP 2476
|
570 580
....*....|....*....|....
gi 2462580884 682 DYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
582-700 |
4.08e-14 |
|
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: 74.07 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsp 661
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT--- 291
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462580884 662 kLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 700
Cdd:cd17638 292 -LTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
142-704 |
4.23e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 75.30 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 142 EPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVF----AGFSSESLCERIL 217
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 218 DSSCSLLITTDAfyrgeklvnlkelADEALQKcqekgfpvrccIVVKHLGRAELGMGDstsqsppikrscpDVQGKLKEk 297
Cdd:PRK07514 98 DAEPALVVCDPA-------------NFAWLSK-----------IAAAAGAPHVETLDA-------------DGTGSLLE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 298 skrvqpqiswnqgidlwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAED 377
Cdd:PRK07514 140 --------------------AAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 VFWCTADIGWITGHSYVTYGPLANGA------------------TSVLFEGIPTypdvnrlwsivdkykvtkFYTaptai 439
Cdd:PRK07514 199 VLIHALPIFHTHGLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 440 RLLmkfgDEP-----VTKHSRasLQVLGTVgePINPE---AWlwyhrvvgAQRC--PIVDTFWQTETGghMLTPLPGATP 509
Cdd:PRK07514 256 RLL----QEPrltreAAAHMR--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 510 MKPGSATFPFFGVAPAILNESGEELegeaegylLLRTETSWLE-----VFKQPW--PgimrtvygnherfETTY--FKKf 580
Cdd:PRK07514 318 RRAGTVGFPLPGVSLRVTDPETGAE--------LPPGEIGMIEvkgpnVFKGYWrmP-------------EKTAeeFRA- 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 581 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS 660
Cdd:PRK07514 376 DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD 455
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2462580884 661 PkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK07514 456 E---AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
145-705 |
4.42e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 75.68 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERILDSscS 222
Cdd:PRK08279 59 EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLahSLNLVDA--K 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITtdafyrGEKLVNLKELADEALQKcqekgfPVRCCIVVKHLGRAELGMGD----STSQSPPIKRSCPDVQgklkeks 298
Cdd:PRK08279 137 HLIV------GEELVEAFEEARADLAR------PPRLWVAGGDTLDDPEGYEDlaaaAAGAPTTNPASRSGVT------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 299 krvqpqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtTFKYVFDFHAEDV 378
Cdd:PRK08279 198 ----------------------------------AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 379 FWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYtaptAI----RLLMkfgDEPVT 451
Cdd:PRK08279 243 LYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRATAFQ----YIgelcRYLL---NQPPK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 452 KHSRA-SLQVLgtVGEPINPEAW--------------LW--------------YHRVVGaqRCP--------IVDtfWQT 494
Cdd:PRK08279 309 PTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFDGTVG--RVPlwlahpyaIVK--YDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 495 ETGghmlTPLPGA----TPMKPG---------SATFPFFGVA-PAilnesgeelegeaegylllRTETSwlevfkqpwpg 560
Cdd:PRK08279 383 DTG----EPVRDAdgrcIKVKPGevglligriTDRGPFDGYTdPE-------------------ASEKK----------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 561 IMRTVygnherfettyFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML-----NVsghllSTAEVESALVEHEAVAEAAV 635
Cdd:PRK08279 429 ILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEEAVV 492
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 636 VGHPHP-VKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK08279 493 YGVEVPgTDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
334-700 |
8.20e-14 |
|
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: 73.45 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 413
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 414 YpdvNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHRVvgaqrcPI 487
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLT------NT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 488 VDTFWQTETGGHMLTPLpGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLllrtetswleVFKQPWpgIMRTVYG 567
Cdd:cd17635 146 AQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTI----------WIKSPA--NMLGYWN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 568 NHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL 647
Cdd:cd17635 213 NPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462580884 648 YCFVTLcdghtfSPKLTEE----LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 700
Cdd:cd17635 290 GLAVVA------SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
334-703 |
1.04e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 74.01 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAEDVF--WCTadigwitghsyvty 396
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIYvtLLS-------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 397 gplanGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWY 476
Cdd:cd17644 172 -----GATLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQW 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 477 HRVVGaQRCPIVDTFWQTE----TGGHMLTPLPGATPMKPGsatfpffgVAPAILNesgeelegeaegylllrTETSWLE 552
Cdd:cd17644 245 QKNVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSVP--------IGRPIAN-----------------TQVYILD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 553 VFKQPWP-GIMRTVY--------G-------NHERFETTYFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHL 614
Cdd:cd17644 299 ENLQPVPvGVPGELHiggvglarGylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFR 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 615 LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTR 694
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTP 455
|
....*....
gi 2462580884 695 SGKIMRRVL 703
Cdd:cd17644 456 NGKIDRRAL 464
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
303-704 |
1.39e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 PQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPL---------FILYTSGSTGKPKGVVHTVG------GYMLYVATTF 367
Cdd:PRK12406 114 PEIAAAYRISP--ALLTPPAGAIDWEGWLAQQEPYdgppvpqpqSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRALIY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 368 kyvfdfhaedvfwctadiGWITGHSYVTYGPLANGATSV-------LFEGIPTYP--DVNRLWSIVDKYKVTKFYTAPTA 438
Cdd:PRK12406 192 ------------------GLKPGIRALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTM 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 439 IRLLMKFGDEPVTKHSRASLQvlgtvgepinpeawlwyHRVVGAQRCP--------------IVDTFWQTETGGhmltpL 504
Cdd:PRK12406 254 FIRLLKLPEEVRAKYDVSSLR-----------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGA-----V 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 505 PGATP----MKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKKf 580
Cdd:PRK12406 312 TFATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI------------AGNPDFTYHNKPEKRAEIDRG- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 581 pGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS 660
Cdd:PRK12406 379 -GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462580884 661 PkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK12406 458 E---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
333-703 |
1.41e-13 |
|
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: 73.44 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIP 412
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 TYPDvNRLWSIVDKYKVTkFYTAPTAIRLLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyhrvvgAQRCPIVDTF 491
Cdd:cd17652 170 LLPG-EPLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------APGRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 492 WQTET--GGHMLTPLPGATPMKPGSatfPFFGVAPAILNesgeelegeaegylllrtetSWLevfkQPWP---------- 559
Cdd:cd17652 235 GPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLD--------------------ARL----RPVPpgvpgelyia 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 560 --GIMRTvYGNH-----ERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 630
Cdd:cd17652 288 gaGLARG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGV 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 631 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd17652 366 AEAVVVVRDDRPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
324-705 |
2.40e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.43 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 324 DECEPEWCD--------AEDP---LFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHs 392
Cdd:PRK12467 635 DEPADLLCGysghnpevALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 393 YVTYGPLANGATsVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGtvGEpINPEA 472
Cdd:PRK12467 713 TELFGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GE-ALQVD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 473 WLWYHRVVGAQrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEGYLLLRTEtsw 550
Cdd:PRK12467 787 LLARVRALGPG-ARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDHYLNPVPVGVVGELYIGGA--- 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 551 levfkqpwpGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 624
Cdd:PRK12467 863 ---------GLARGYHRrpalTAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARL 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 625 VEHEAVAEAAVVGHPHPVKGECL-YCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK12467 933 LAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
..
gi 2462580884 704 RK 705
Cdd:PRK12467 1013 PK 1014
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
149-704 |
2.59e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 73.26 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 149 ITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITt 227
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 dafyrgekLVNLKELADEALQKCQekgfpvrccivVKHLGRAELGmgdstSQSPPIKRSCpdVQGKLKEKSKRVqPQISW 307
Cdd:PRK05677 129 --------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRLL--INAVVKHVKKMV-PAYHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 NQGIDLWwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---VGGYMLYVATTFK---------------- 368
Cdd:PRK05677 182 PQAVKFN-DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQCRALMGsnlnegceiliaplpl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 369 ---YVFDFHaedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKf 445
Cdd:PRK05677 261 yhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCN- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 446 gDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETgghmlTPLPGATPMK---PGSATFPFFGV 522
Cdd:PRK05677 317 -NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPST 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 523 APAILNESGEElegeaegylLLRTETSWLEVfkqPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITG 602
Cdd:PRK05677 388 LCKVIDDDGNE---------LPLGEVGELCV---KGPQVMKGYWQRPE--ATDEILDSDGWLKTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 603 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPD 682
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTGYKVPK 530
|
570 580
....*....|....*....|..
gi 2462580884 683 YIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK05677 531 AVEFRDELPTTNVGKILRRELR 552
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
146-703 |
2.64e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.12 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 146 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVfagfsSESLCERILDSSCslli 225
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA-----DGNLPIAAIERFC---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 ttdafyrgeklvnlkELADEAlqkcqekgfpvrCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQI 305
Cdd:PRK05857 110 ---------------QITDPA------------AALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 SWNQGidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVvhtvggymLYVATTFKYVFD-FHAEDVFWctad 384
Cdd:PRK05857 163 NADQG----------------------SEDPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 385 IGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL---MKFGDEP 449
Cdd:PRK05857 209 VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 VtkhsrASLQVLGTVG-EPINPEAwlwyhRVVGAQRCPIVDTFWQTETGGHMLTpLP----GATPMKPGSATFPFFGV-- 522
Cdd:PRK05857 285 V-----PSLRLVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdv 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 523 --APAILNESGEELEGEAEGYlllrtETSWLEVfkqpwPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWI 600
Cdd:PRK05857 354 ylAATDGIGPTAPGAGPSASF-----GTLWIKS-----PANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYI 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 601 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfspklTEELKKQI----RE 673
Cdd:PRK05857 421 KGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRR 495
|
570 580 590
....*....|....*....|....*....|
gi 2462580884 674 KIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK05857 496 ESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
582-707 |
5.21e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.16 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 661
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----P 515
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462580884 662 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:PRK12492 516 GLSvEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
332-709 |
1.78e-12 |
|
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: 70.26 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKY-----VFDF--HAEDVfwCTADIgwitghsyvtYGPLAN 401
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 402 GATSVlfegIPTYPD-VNRLWSIVDKYKVTkfyTA---PTAIRLLmkfgdEPVTKhsrASLQVLGTVGEPINPEAW-LWY 476
Cdd:cd05918 172 GGCLC----IPSEEDrLNDLAGFINRLRVT---WAfltPSVARLL-----DPEDV---PSLRTLVLGGEALTQSDVdTWA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 477 HRV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsatfpffgVA 523
Cdd:cd05918 237 DRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI-----------LA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 524 PailnesgeelegeaeGYLLLRTETSwlEVFKQPWPGIMRTVYGNHERFettyfkkfpgyYVTGDGCQRDQDG--YYwiT 601
Cdd:cd05918 305 R---------------GYLNDPEKTA--AAFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--V 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 602 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSPKLTEELKKQIREKIGPI 678
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRAL 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462580884 679 AT----------PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 709
Cdd:cd05918 434 VAelrsklrqrlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
582-704 |
2.36e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.63 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 660
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580884 661 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 704
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
586-707 |
2.91e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.84 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 586 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltE 665
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462580884 666 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
147-707 |
3.98e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 69.52 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQF-SNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 225
Cdd:PRK08751 49 KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TTDAFYRGEKLVnlkeLADEALQKCQEK------GFPVRCCI--VVKHlgraelgmgdstsqsppIKRSCPDVqgklkek 297
Cdd:PRK08751 129 VIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY-----------------VKKLVPEY------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 298 skRVQPQISWNQGIDLWWHELMqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVvhtvggyMLYVATTFKYVFDFHAed 377
Cdd:PRK08751 181 --RINGAIRFREALALGRKHSM-------PTLQIEPDDIAFLQYTGGTTGVAKGA-------MLTHRNLVANMQQAHQ-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 378 vfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGiptypdVNRLWS-------IVDKYKVTKFyTAPTAIRLL 442
Cdd:PRK08751 243 --WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGG------CNHLISnprdmpgFVKELKKTRF-TAFTGVNTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 443 M-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETgghmlTPLPGATPMK----PGSAT 516
Cdd:PRK08751 314 FnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTET-----SPAACINPLTlkeyNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 517 FPFFGVAPAILNESGEELEGEAEGYLLLRTetswlevfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDG 596
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVLAIGEIGELCIKG------------PQVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 597 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPKLT-EELKKQIREKI 675
Cdd:PRK08751 452 FVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANL 526
|
570 580 590
....*....|....*....|....*....|..
gi 2462580884 676 GPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 707
Cdd:PRK08751 527 TGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
581-711 |
3.70e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.79 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 581 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFs 660
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 661 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 711
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
317-705 |
5.16e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 65.98 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 317 ELMQEAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVvhTVGGYMLYVATTFKYVFDFHAE-DVFWCTADIGWITGHSYV 394
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIVGYGEdDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 395 tygpLAN---GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL----GTVGEP 467
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 468 INPEAWLWYhrvvgaQRCPIVDTFWQTETGGHM-LTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLR- 545
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSLtFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKi 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 546 --TETSWLEVFKQPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 623
Cdd:PLN02860 378 glDESSRVGRILTRGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 624 LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLT-----------EELKKQIREK-IGPIATPD-YIQNAPGL 690
Cdd:PLN02860 456 LSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlFVQWRKPF 535
|
410
....*....|....*
gi 2462580884 691 PKTRSGKIMRRVLRK 705
Cdd:PLN02860 536 PLTTTGKIRRDEVRR 550
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
144-705 |
5.31e-11 |
|
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: 65.41 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSS-CS 222
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvq 302
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATT---------------F 367
Cdd:cd17653 104 ------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 368 KYVFDFHAEDVFWCtadigwitghsyvtygpLANGATSVLFEGIPTYPDVNRlwsivdkyKVTKFYTAPTAIRLLmkfgd 447
Cdd:cd17653 154 SIAFDACIGEIFST-----------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL----- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 448 epvtkhSRASLQVLGTV---GEPINP---EAWlWYHRVV----GAQRCPIVDTFWQTETGghmlTPLPGATPMkPGSATF 517
Cdd:cd17653 204 ------SPQDFPNLKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 518 pffgvapaILNESgeelegeaegyLLLRTETSWLEVFKQPwPGIMRTVYGNHERfETTYFKKFPGY-----YVTGDGCQR 592
Cdd:cd17653 272 --------ILDAD-----------LQPVPEGVVGEICISG-VQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRW 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 593 DQDGYYWITGRIDDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTlcdghtfsPKL--TEELKK 669
Cdd:cd17653 331 TEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT--------PETvdVDGLRS 397
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462580884 670 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd17653 398 ELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-705 |
8.05e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.39 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 119 DKVAFYWSTSGNSsyrytcregnepgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA 198
Cdd:PLN02330 43 DKVAFVEAVTGKA-----------------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 199 lhsiVFAGFSS---ESLCERILDSSCSLLITTDAFYRGEklvnlkeladealqkcqekgfpvrccivVKHLGRAELGMGD 275
Cdd:PLN02330 106 ----VFSGANPtalESEIKKQAEAAGAKLIVTNDTNYGK----------------------------VKGLGLPVIVLGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 276 StsqsppikrscpdvqgklkekskRVQPQISWNQGIDLwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT 355
Cdd:PLN02330 154 E-----------------------KIEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 356 --------------VGGYMLYVATTFKYVFDFHaedvfwctadIGWITGHSYVTygpLANGATSVLfegiptypdVNR-- 419
Cdd:PLN02330 206 hrnlvanlcsslfsVGPEMIGQVVTLGLIPFFH----------IYGITGICCAT---LRNKGKVVV---------MSRfe 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 420 LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGAQrcpIVDTFWQTE 495
Cdd:PLN02330 264 LRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 496 TGGHMLT---PLPGATPMKPGSATFPFFGVAPAILNESGEELegeaegylLLRTETSWLEVFKQpwpGIMRTVYGNHERF 572
Cdd:PLN02330 341 HSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRS--------LPKNTPGELCVRSQ---CVMQGYYNNKEET 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 573 ETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 652
Cdd:PLN02330 410 DRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 653 LcdghtfSPKLT---EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PLN02330 488 I------NPKAKeseEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
321-703 |
2.26e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.41 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 321 EAGDECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDVfwctadigWITGHSYV---- 394
Cdd:PRK12467 1704 EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAfdvs 1773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 395 ---TYGPLANGAtSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKHSraSLQVLGTVGEPINPE 471
Cdd:PRK12467 1774 vweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SLRRVVCGGEALEVE 1849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 472 AW-LWYHRVVGAQrcpIVDTFWQTETGGHMLT-PLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEGYLLLRTE 547
Cdd:PRK12467 1850 ALrPWLERLPDTG---LFNLYGPTETAVDVTHwTCRRKDLEGRDSVPIgqPIANLSTYILDASLNPVPIGVAGELYLGGV 1926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 548 tswlevfkqpwpGIMRtvyGNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 619
Cdd:PRK12467 1927 ------------GLAR---GYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 1991
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 620 VESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA-----PG 689
Cdd:PRK12467 1992 IEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYMVPAhlvflAR 2065
|
410
....*....|....
gi 2462580884 690 LPKTRSGKIMRRVL 703
Cdd:PRK12467 2066 MPLTPNGKLDRKAL 2079
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
586-703 |
2.48e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 586 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSPkl 663
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDP-- 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462580884 664 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
145-408 |
2.65e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.84 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 225 ITTdafyrGEKLVNLkeladeaLQKCQEKGFPvRCCIVvkHLGraelgmgdstsqsppikrSCPDvqgKLKEKSKRVqpq 304
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD------------------SLPA---SVDTEGCRL--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 305 ISWNQGIDLWWHELMQEAGDECEpewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaeDVFWCTAD 384
Cdd:PTZ00216 239 VAWTDVVAKGHSAGSHHPLNIPE----NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLN-----DLIGPPEE 309
|
250 260
....*....|....*....|....*...
gi 2462580884 385 igwitGHSYVTYGPLAN----GATSVLF 408
Cdd:PTZ00216 310 -----DETYCSYLPLAHimefGVTNIFL 332
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
150-705 |
2.81e-10 |
|
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: 63.22 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLIT 226
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 227 TDafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqis 306
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 307 wnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGgyMLYV-ATTFKYVFDFHAEDVFWCTADI 385
Cdd:cd05937 87 ---------------------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPL 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 386 GWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRaslqVLG 462
Cdd:cd05937 138 YHGTAAFLGACNCLMSGGTLALsrkFS-------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRV 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 463 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsatfpfFGvAPAILNESGEELEGEAEGY 541
Cdd:cd05937 207 AWGNGLRPDIWERFRERFNV---PEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQV 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 542 LLLRTETSWLEVFKQPWPG-------------IMRTVYGNHERFETTY--------------FKKFPGYYVTGDGCQRDQ 594
Cdd:cd05937 271 VLVKMDPETDDPIRDPKTGfcvrapvgepgemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDA 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 595 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTF-SPKLTEELKKQ 670
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVpTEFTKSLLASL 428
|
570 580 590
....*....|....*....|....*....|....*
gi 2462580884 671 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
576-713 |
4.46e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 576 YFKK-----FPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 650
Cdd:PRK07008 398 YFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462580884 651 VTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDL 713
Cdd:PRK07008 478 VVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR-DYVL 536
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
334-697 |
6.64e-10 |
|
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: 61.63 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 334 EDPLFILYTSGSTGKPKGVV---HTVGGYMLYVA--TTFKYVFDFHAEDVFWCTADIGW------ITGHSYVTYGPLANG 402
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGAdfGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 403 ATSVLFEGIPTYPDvnRLWSIVDKYKVTKF------YTAPTaIRLLMKFGDEPVTkhsraSLQVLGTVGEPINPEawlwy 476
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 477 hrvVGAQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSATFPFFGvapailnesgeelegeaEGYLLLRTETSW 550
Cdd:cd05924 150 ---VKQGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRAN-----------------PDTVVLDDDGRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 551 LEvfkqPWPGIMRTV----------YGNHERFETTyFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 618
Cdd:cd05924 207 VP----PGSGGVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPE 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580884 619 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 697
Cdd:cd05924 282 EVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
581-705 |
6.93e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.60 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 581 PGYYVTGDGCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtLCDGHTfS 660
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462580884 661 PKLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK07824 310 PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
147-703 |
1.02e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 62.37 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 147 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLI 225
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TTDAFyrgeklvnlkeladealqkcQEKgFPvrccivvkhlgraelGMGDSTSQSPPIKRSCPDVQGKLkekskRVQPQi 305
Cdd:PRK10252 561 TTADQ--------------------LPR-FA---------------DVPDLTSLCYNAPLAPQGAAPLQ-----LSQPH- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 swnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HT-VGGYMLYVATTFKyvfdFHAEDVFW-- 380
Cdd:PRK10252 599 -----------------------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqk 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 381 --CTADIG-----WitghsyvtygPLANGATSVLFEgiptyPDVNR----LWSIVDKYKVTKFYTAPTairLLMKFGDEP 449
Cdd:PRK10252 646 tpCSFDVSvweffW----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 450 VTKHSRASLQVLGTV---GEPINPEAWLWYHRVVGAqrcPIVDTFWQTE---------TGGHMLTPLPGAtPMKPGsatF 517
Cdd:PRK10252 708 TPEGARQSCASLRQVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGS-SVPIG---Y 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 518 PFFGVAPAILNEsgeelegeaegylLLRtetswlevfKQPwPGIMRTVY--------GNH-------ERFETTYFKkfPG 582
Cdd:PRK10252 781 PVWNTGLRILDA-------------RMR---------PVP-PGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA--PG 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 583 --YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLC 654
Cdd:PRK10252 836 erMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQ 915
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2462580884 655 DGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK10252 916 SG---LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
332-708 |
1.06e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATtfkyVFDFHAEDVfwctadigwITG-----HSY----VTYGPL 399
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 400 ANGATSVlFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLgtvgepinpeawlwyhrV 479
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------V 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 480 VGAQRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSATFPFFGVAPAILNESGe 532
Cdd:PRK08633 905 AGAEKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET- 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 533 elegeaegYLLLRTETSWLEVFKQPwpGIMRTVYGNHERF-ETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVS 611
Cdd:PRK08633 979 --------FEELPPGEDGLILIGGP--QVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 612 GHLLSTAEVESALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSPKLTEELKKQIRE-KIGPIATPDYIQN 686
Cdd:PRK08633 1049 GEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFK 1120
|
410 420
....*....|....*....|..
gi 2462580884 687 APGLPKTRSGKIMRRVLRKIAQ 708
Cdd:PRK08633 1121 VEALPLLGSGKLDLKGLKELAL 1142
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
144-400 |
1.28e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.67 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITtdafyrGEKlvNLKELAD--EALQkcqekgfpvrcciVVKHLgraeLGMGDSTSQSPPikrSCPDVQGKLKEKSKRV 301
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDS---SLSGSSNWTVSSFSEV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 302 QpqiswnqgidlwwhELMQEAgdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVfwc 381
Cdd:PLN02387 234 E--------------KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--- 294
|
250
....*....|....*....
gi 2462580884 382 tadigwitghsYVTYGPLA 400
Cdd:PLN02387 295 -----------YLAYLPLA 302
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
332-700 |
1.30e-09 |
|
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: 60.92 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGI 411
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 412 PT-------------YPDVNRLWSIVDKYKVTKFYTAPTAI---RLLMKFGDEPVTKHSRASLQ----------VLGtvG 465
Cdd:cd05914 166 PSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggnikefVIG--G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 466 EPINPEAwLWYHRVVGAqrcPIVDTFWQTETGghmltPLPGATP---MKPGSATFPFFGVAPAIlnesGEELEGEAEGYL 542
Cdd:cd05914 244 AKINPDV-EEFLRTIGF---PYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRI----DSPDPATGEGEI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 543 LLRTetswlevfkqpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDM-LNVSGHLLSTAEVE 621
Cdd:cd05914 311 IVRG------------PNVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 622 SALVEHEAVAEAAVV---------GHPHP----VKGECLycfvtlcdghtfsPKLTEELKKQIREKIGpIATPDY----- 683
Cdd:cd05914 377 AKINNMPFVLESLVVvqekklvalAYIDPdfldVKALKQ-------------RNIIDAIKWEVRDKVN-QKVPNYkkisk 442
|
410
....*....|....*....
gi 2462580884 684 --IQNAPgLPKTRSGKIMR 700
Cdd:cd05914 443 vkIVKEE-FEKTPKGKIKR 460
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
582-703 |
1.31e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.17 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSp 661
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD- 474
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462580884 662 klTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK13383 475 --AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
144-703 |
1.50e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 224 LITTDAFYRGeklvnLKELADEALQKCQEKGFPVRccivvkhlgraelgmgDSTSQSPPIKRSCPDVQGklkekskrvqp 303
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 304 qiswnqgidlwwhelmqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDvfwCTA 383
Cdd:PRK05691 2337 ----------------------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL 2378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 384 DIGWIT--GHSYVTYGPLANGATSVL-FEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdePVTKHSRASLQV 460
Cdd:PRK05691 2379 HFYSINfdAASERLLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRM 2452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 461 LGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSATFPFFGVAPA----ILNESGEel 534
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLA-- 2525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 535 egeaegyLLLRTETSWLEVfkqpwpGIMRTVYGNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDD 606
Cdd:PRK05691 2526 -------LVPQGATGELYV------GGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDH 2592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 607 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPK--LTEELKKQIREKIgpiatPDYI 684
Cdd:PRK05691 2593 QVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQaaLREALKAHLKQQL-----PDYM 2667
|
570 580
....*....|....*....|....
gi 2462580884 685 QNA-----PGLPKTRSGKIMRRVL 703
Cdd:PRK05691 2668 VPAhlillDSLPLTANGKLDRRAL 2691
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
146-705 |
1.63e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 60.90 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 146 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 225
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 226 TtdafyrgeklvNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdsTSQSPPikrSCPDVqgklkekskrvqpqi 305
Cdd:cd05939 81 F-----------NLLDPLLTQ------------------------------SSTEPP---SQDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 306 swnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADI 385
Cdd:cd05939 102 --------------------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 386 gWITGHSYVTYGP-LANGATSVLFEGIptypDVNRLWSIVDKYKVTKF-YTAPTAIRLLMKFGDEPVTKHsraslQVLGT 463
Cdd:cd05939 155 -YHSAGGIMGVGQaLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 464 VGEPINPEAWlwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSATFpffgvAPAILNESGEELegeaegylL 543
Cdd:cd05939 225 VGNGLRPQIW---EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGF-----NSRILPSVYPIR--------L 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 544 LRTETSWLEVFKQP----------WPGIM----------RTVYG------NHERFETTYFKKFPGYYVTGDGCQRDQDGY 597
Cdd:cd05939 285 IKVDEDTGELIRDSdglcipcqpgEPGLLvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 598 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSPKLTEELKkqir 672
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP---- 440
|
570 580 590
....*....|....*....|....*....|...
gi 2462580884 673 ekigPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:cd05939 441 ----PYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
582-705 |
2.79e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.18 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 661
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462580884 662 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 705
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
332-703 |
1.16e-08 |
|
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: 58.18 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGYM--------LY---------VATTFKYVFDFHAEDVFwctadIGWITGHSYV 394
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 395 tygplangatsVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 474
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 475 wYHRVVGAQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSATFPFFGVAPAILNESGEELEGEAEGYLLLRTEtswlev 553
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGD------ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 554 fkqpwpGIMRTvYGNH-----ERFETTYFK--------KFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 620
Cdd:cd17648 296 ------GVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 621 ESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfspkLTE-ELKKQIREKIGPIATPDYIQNAPGLPKTR 694
Cdd:cd17648 369 EAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
|
....*....
gi 2462580884 695 SGKIMRRVL 703
Cdd:cd17648 444 NGKLDVRAL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
145-703 |
1.58e-08 |
|
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: 57.87 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERI----LDSS 220
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGG----AFVPIDPEYPEERRiyimLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 221 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppiKRSCPDVQGKLKEKSKR 300
Cdd:cd17656 86 VRVVLT---------------------------------------------------------QRHLKSKLSFNKSTILL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 301 VQPQISwnqgidlwwHELMQEAGDECEpewcdAEDPLFILYTSGSTGKPKGVV--HTVggymlyVATTFKYVFDFHAEDV 378
Cdd:cd17656 109 EDPSIS---------QEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQleHKN------MVNLLHFEREKTNINF 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 379 FwctADIGWITGHSY-VTYGPLAngaTSVLFEG----IP--TYPDVNRLWSIVDKYKVTKFYTaPTAIrLLMKFGDEPVT 451
Cdd:cd17656 169 S---DKVLQFATCSFdVCYQEIF---STLLSGGtlyiIReeTKRDVEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREFI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 452 KHSRASLQVLGTVGEPI---NPeawlwYHRVVGAQRCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSATFPF 519
Cdd:cd17656 241 NRFPTCVKHIITAGEQLvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 520 fgvapaILNESgeelegeaegylllrtetswlevfKQPWP-GIMRTVY--------GNHERFETTYFKKFPG-------Y 583
Cdd:cd17656 314 ------ILDQE------------------------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerM 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 584 YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSpkl 663
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN--- 438
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2462580884 664 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd17656 439 ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
133-408 |
2.11e-08 |
|
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: 57.25 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 133 YRYTCREGnepGETTQITYHQLLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL 212
Cdd:cd05931 12 YTFLDDEG---GREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 213 cERIL----DSSCSLLITTDAFyrgeklvnLKELADEALQKCQEKGFPVRCCivvkhlgraelgmgdstsqsppikrscp 288
Cdd:cd05931 88 -ERLAailaDAGPRVVLTTAAA--------LAAVRAFAASRPAAGTPRLLVV---------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 289 dvqgklkekskrvqpqiswnqgiDLwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFK 368
Cdd:cd05931 131 -----------------------DL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462580884 369 yVFDFHAED--VFW--CTADIGWITGhsyvTYGPLANGATSVLF 408
Cdd:cd05931 184 -AYGLDPGDvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLM 222
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
148-231 |
4.07e-08 |
|
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: 56.21 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLI 225
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLahCLNV--SSAKHLV 80
|
....*.
gi 2462580884 226 TTDAFY 231
Cdd:cd05940 81 VDAALY 86
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
331-709 |
8.09e-08 |
|
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: 55.37 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 331 CDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVF--WCTADigWITGHSYVTYGPLANGATSVlf 408
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLGCQQV-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 409 eGIPT---YPDVNRLWSIVDKYKVTkfYT-APT-AIRLLMKFGDEPVTKH-SRASLQVLGTVGEPINP---EAWLWYHRV 479
Cdd:cd05906 239 -HVPTeeiLADPLRWLDLIDRYRVT--ITwAPNfAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAktiRRLLRLLEP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 480 VGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF-----PFFGVAPAILNESGEelegeaegyLLLRTETSWLEVf 554
Cdd:cd05906 316 YGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrPIPGVSMRIVDDEGQ---------LLPEGEVGRLQV- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 555 kqpwPGIMRTV--YGNHERFETTYFKKfpGYYVTGD-GCQRDqdGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 631
Cdd:cd05906 386 ----RGPVVTKgyYNNPEANAEAFTED--GWFRTGDlGFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 632 E--AAVVGHPHPVKGECLYCFVtlcdghtFSPKLTE-----ELKKQIR----EKIGpiATPDYI----QNApgLPKTRSG 696
Cdd:cd05906 458 PsfTAAFAVRDPGAETEELAIF-------FVPEYDLqdalsETLRAIRsvvsREVG--VSPAYLiplpKEE--IPKTSLG 526
|
410
....*....|...
gi 2462580884 697 KIMRRVLRKIAQN 709
Cdd:cd05906 527 KIQRSKLKAAFEA 539
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
584-703 |
8.55e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 584 YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSPKL 663
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462580884 664 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
333-668 |
1.05e-07 |
|
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: 55.16 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 333 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 412
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 413 TYP---DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVV--------- 480
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKMLsdeaeiltp 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 481 -GAQRC-PIvdtfwqTETGGHMLTPLPGATPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLLLRTETSWLEVFK 555
Cdd:cd05910 233 yGATEAlPV------SSIGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLELPRGEIGEITVTG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 556 qpwPGIMRTVYGnheRFETTYFKKFPG-----YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 630
Cdd:cd05910 306 ---PTVTPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462580884 631 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELK 668
Cdd:cd05910 380 RRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
148-703 |
1.88e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 148 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 227
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 228 DAFYrgEKLVNLKELADEALQKCQEKGFPVrccivvkhlgraelgmgdstsqSPPikrscpdvqgklkekskrvqpqisw 307
Cdd:PRK05691 1236 SHLL--ERLPQAEGVSAIALDSLHLDSWPS----------------------QAP------------------------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 308 nqGIDLWWHELMqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYVFDfhAEDVFWCTADIG 386
Cdd:PRK05691 1267 --GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNTHAALAERLQwMQATYALD--DSDVLMQKAPIS 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 387 WITGhSYVTYGPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRaSLQVLGTVGE 466
Cdd:PRK05691 1325 FDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPLAAACT-SLRRLFSGGE 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 467 PINPE---------AWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLpgatpmkpGSatfPFFGVAPAILNESGEELEGE 537
Cdd:PRK05691 1399 ALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR---PLGNVLCRVLDAELNLLPPG 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 538 AEGYLLLRTEtswlevfkqpwpGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVS 611
Cdd:PRK05691 1468 VAGELCIGGA------------GLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLDQQVKLR 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 612 GHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA---- 687
Cdd:PRK05691 1535 GFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAEL-----PEYMVPAqlir 1605
|
570
....*....|....*..
gi 2462580884 688 -PGLPKTRSGKIMRRVL 703
Cdd:PRK05691 1606 lDQMPLGPSGKLDRRAL 1622
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
582-696 |
8.35e-07 |
|
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: 51.53 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 661
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 2462580884 662 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 696
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
327-473 |
8.65e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.21 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 327 EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgymlyvattfkyvfDFHA------EDVFWCTADIGWITGHSYVTYGPlA 400
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHG--------------MFEAqiealrEDYGIEPGEIDLPTFPLFALFGP-A 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 401 NGATSVLFEGIPTYP-DVN--RLWSIVDKYKVTKFYTAPTAIrllmkfgdEPVTKHSRASLQVLGTV------GEPINPE 471
Cdd:PRK09274 232 LGMTSVIPDMDPTRPaTVDpaKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLrrvisaGAPVPIA 303
|
..
gi 2462580884 472 AW 473
Cdd:PRK09274 304 VI 305
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
144-401 |
1.47e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 51.77 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILD-SSCS 222
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV-EFIINhAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 223 LlittdAFYRGEKLvnlkeladEALQKCQEKgfpvrcCivVKHLgRAELGMGDSTSQsppikrscpdvqgkLKEKSKrvq 302
Cdd:PLN02861 152 I-----AFVQESKI--------SSILSCLPK------C--SSNL-KTIVSFGDVSSE--------------QKEEAE--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 303 pqiswNQGIDLW-WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaedvfwc 381
Cdd:PLN02861 193 -----ELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK---------- 257
|
250 260
....*....|....*....|
gi 2462580884 382 TADIGWITGHSYVTYGPLAN 401
Cdd:PLN02861 258 VTDRVATEEDSYFSYLPLAH 277
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
623-732 |
3.87e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 49.76 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 623 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSPKLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 702
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90 100 110
....*....|....*....|....*....|..
gi 2462580884 703 LRKIAQNDHDLGD--MSTVADPSVISHLFSHR 732
Cdd:PRK09188 322 LRLIAMNQIDELDdlLREPEIRGLVEAIAAHR 353
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
325-408 |
5.31e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.52 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 325 ECEPEWCD--AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDvfwctadigwitgHSYVTYGPLAN- 401
Cdd:cd17639 77 ECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAYLPLAHi 143
|
90
....*....|
gi 2462580884 402 ---GATSVLF 408
Cdd:cd17639 144 felAAENVCL 153
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
327-705 |
8.98e-06 |
|
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: 49.02 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 327 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTVGGYMLYVATTfkyvFDFHAEDVF--W--CTADIGWITGHsyvtYGP 398
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 399 LANGATSVLfegIPTYPDVNR--LW-SIVDKYKVTKFYTAPTAIRLLMK-FGDEPVTKHSRASLQVLGTVGEPINPE--- 471
Cdd:cd05908 170 LIAGMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYElch 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 472 AWLWYHRVVGAQRCPIVDTFWQTETGghmltplPGATPMKPGSATFPffgvaPAILNESGEELEGEAEgylLLRTET--- 548
Cdd:cd05908 247 EFLDHMSKYGLKRNAILPVYGLAEAS-------VGASLPKAQSPFKT-----ITLGRRHVTHGEPEPE---VDKKDSecl 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 549 SWLEVFKQPWPGIMRTVYGNHERFETTYFKKF--------PGYY---------VTGDGCQR--DQ----DGYYWITGRID 605
Cdd:cd05908 312 TFVEVGKPIDETDIRICDEDNKILPDGYIGHIqirgknvtPGYYnnpeatakvFTDDGWLKtgDLgfirNGRLVITGREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 606 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG------ 676
Cdd:cd05908 392 DIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwqinev 471
|
410 420 430
....*....|....*....|....*....|
gi 2462580884 677 -PIATpdyiqnapgLPKTRSGKIMRRVLRK 705
Cdd:cd05908 472 lPIRR---------IPKTTSGKVKRYELAQ 492
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
108-229 |
1.06e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 108 LDRNVHEkkLGDKVAfywstsgnssYRYTCREGNEPGETTQITYHQLLVQVCQFSNVLrKQGIQKGDRVAIYMPMIPELV 187
Cdd:PRK12476 40 IERNIAN--VGDTVA----------YRYLDHSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYV 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462580884 188 VAMLACARIGALHSIVFA----GfSSESLCERILDSSCSLLITTDA 229
Cdd:PRK12476 107 AGFFAAIKAGTIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA 151
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
570-703 |
2.00e-05 |
|
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: 47.55 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 570 ERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 649
Cdd:cd17645 311 EKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVA 390
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462580884 650 FVTlcdghtfSPKLT--EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 703
Cdd:cd17645 391 YVT-------APEEIphEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
144-226 |
4.03e-05 |
|
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: 46.82 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 144 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 223
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
...
gi 2462580884 224 LIT 226
Cdd:cd17639 81 IFT 83
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
581-709 |
5.69e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.63 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 581 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 660
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462580884 661 PKLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 709
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
310-400 |
1.66e-04 |
|
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: 44.90 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 310 GIDLW-WHELMQE-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFwctaDIgw 387
Cdd:cd05927 88 GVKVYsLEEFEKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPT----DV-- 161
|
90
....*....|...
gi 2462580884 388 itghsYVTYGPLA 400
Cdd:cd05927 162 -----YISYLPLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
332-414 |
3.70e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 409
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 2462580884 410 GIPTY 414
Cdd:PRK06814 860 GVKVF 864
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
150-363 |
5.95e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.27 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 150 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARigalHSIVfagfsseslcerildssCSLLITTDA 229
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAA----HSLI-----------------CVPLYDTLG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 230 FYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGraelGMGDSTSQSPPIKRSCPDVQGKLkekskrvqpqISWNQ 309
Cdd:PLN02430 137 PGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLK----AIVSFTSVTEEESDKASQIGVKT----------YSWID 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462580884 310 gidlWWHELMQEAGDECEPEwcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 363
Cdd:PLN02430 203 ----FLHMGKENPSETNPPK---PLDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
582-708 |
2.19e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.49 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 582 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfSP 661
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTT-------AS 1082
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462580884 662 KLT-EELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 708
Cdd:PRK06814 1083 DATrAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
332-424 |
3.08e-03 |
|
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: 40.81 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 332 DAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 408
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100
....*....|....*....|....*...
gi 2462580884 409 EGIPTYPD------------VNRLWSIV 424
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESL 187
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
145-226 |
6.68e-03 |
|
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: 39.46 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580884 145 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 224
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKIL 99
|
..
gi 2462580884 225 IT 226
Cdd:cd17645 100 LT 101
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
334-352 |
7.88e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.49 E-value: 7.88e-03
|
| |
