|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-685 |
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: 1192.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFlrynfDVTKGKIFIEWMKGATTNICYNVLDRNVHekKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 125 WEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERIL 204
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 205 DSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAelgmgdstsqsppikrscpdvqISWNQG 284
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE----------------------VPMTEG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 285 IDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITG 364
Cdd:cd05966 208 RDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 365 HSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 444
Cdd:cd05966 288 HSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 445 EAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPG 524
Cdd:cd05966 368 EAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 525 IMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd05966 448 MARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 605 PVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVA 684
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLA 607
|
.
gi 8923896 685 D 685
Cdd:cd05966 608 D 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-692 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1117.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 31 PPPEVSRSAHVpSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPcpgpflrYNFDVTKGKIFIEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 111 NVHEKklGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIV 190
Cdd:PRK00174 76 HLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 191 FAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQekgfPVRCCIVVKHLGraelgmGDstsqsppi 270
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG------GD-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 271 krscpdvqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAE 350
Cdd:PRK00174 216 --------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 351 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRA 430
Cdd:PRK00174 288 DVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 431 SLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEG 510
Cdd:PRK00174 368 SLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 511 EAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK00174 448 GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
650 660
....*....|....*....|..
gi 8923896 671 AQNDHDLGDMSTVADPSVISHL 692
Cdd:PRK00174 608 AEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
43-692 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1032.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 43 SLQRYRELHRRSVEEPREFWGDIAKE-FYWKTPcpgpflrynFDVTK---GKIFIEWMKGATTNICYNVLDRnvHEKKLG 118
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFKP---------FTKVLdwsFPPFYKWFVGGELNVSYNCVDR--HLEARP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:TIGR02188 72 DKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfpVRCCIVVKHLGraelgmgdstsqsppikrscpDVQ 278
Cdd:TIGR02188 152 LADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG---------------------NPV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 ISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTAD 358
Cdd:TIGR02188 208 VPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 359 IGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTV 438
Cdd:TIGR02188 288 VGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 439 GEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNES-GEELEGEAEGYLV 517
Cdd:TIGR02188 368 GEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 518 FKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:TIGR02188 448 IKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 598 AVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD- 676
Cdd:TIGR02188 528 AVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEi 607
|
650
....*....|....*.
gi 8923896 677 LGDMSTVADPSVISHL 692
Cdd:TIGR02188 608 LGDTSTLEDPSVVEEL 623
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-692 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 898.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 31 PPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTP-CPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 110 RNVhEKKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSI 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 190 VFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHlgraelgmgdstsqSPP 269
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYEN--------------QLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 270 IKRscpdVQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA 349
Cdd:PLN02654 241 MKR----EDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 350 EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSR 429
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 430 ASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELE 509
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 510 GEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02654 477 GECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
650 660
....*....|....*....|....
gi 8923896 670 IAQNDHD-LGDMSTVADPSVISHL 692
Cdd:PLN02654 637 IASRQLDeLGDTSTLADPGVVDQL 660
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
94-692 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 874.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 94 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPEL 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 174 VVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEkgfpVRCCIVVKHL 253
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 254 GrAELGMGDstsqsppikrscpdvqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGY 333
Cdd:COG0365 154 G-ADVPMEG-----------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 334 MLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAI 413
Cdd:COG0365 210 LVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 414 RLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPF 493
Cdd:COG0365 290 RALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 494 FGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLN 573
Cdd:COG0365 366 PGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:COG0365 446 VSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDE 525
|
570 580 590
....*....|....*....|....*....|....*....
gi 8923896 654 LPKTRSGKIMRRVLRKIAQNDhDLGDMSTVADPSVISHL 692
Cdd:COG0365 526 LPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-663 |
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: 712.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCPGpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKklGDKVAFYWE 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 127 GNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDS 206
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 207 SCSLLITTDAFYRGEKLVNLKELADEALQKcqeKGFPVRCCIVVKHLGraelgmgdstsqsppikrscpdVQISWNQGID 286
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLKRTG----------------------SDIDWQEGRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 287 LWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHS 366
Cdd:cd17634 211 LWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 367 YVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 WLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIM 526
Cdd:cd17634 371 YEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 527 RTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd17634 451 RTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 607 KGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:cd17634 531 KGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-692 |
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: 604.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 47 YRELHRRSVEEPREFWGDIAKEFYWKTP-------CPGPFLRynfdvtkgkifieWMKGATTNICYNVLDRNVhEKKLGD 119
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPpekildnSNPPFTR-------------WFVGGRLNTCYNALDRHV-EAGRGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 120 KVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL 199
Cdd:cd05967 67 QIALIYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 200 CERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCciVVKHLGRAELGMGDStsqsppikrscpdvqi 279
Cdd:cd05967 147 ASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHV--LVLNRPQVPADLTKP---------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 280 swnqGIDLWWHELMQEAGdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI 359
Cdd:cd05967 207 ----GRDLDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 360 GWITGHSYVTYGPLANGATSVLFEGIPT-YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF--GDEPVTKHSRASLQVLG 436
Cdd:cd05967 282 GWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAILNESGEELEGEAEG 514
Cdd:cd05967 362 LAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 515 YLVFKQPW-PGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:cd05967 439 NIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:cd05967 519 VAECAVVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
650 660
....*....|....*....|
gi 8923896 673 NDhDLGDMSTVADPSVISHL 692
Cdd:cd05967 599 GE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
45-689 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 574.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPcPGPFLRYNfdvtkGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 125 WEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERIL 204
Cdd:PRK10524 74 AVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 205 DSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCCIVVKHLGRAElgmgdstsqsppikrscpdvqisWNQG 284
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLAPMA-----------------------RVAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 285 IDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 363
Cdd:PRK10524 209 RDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 364 GHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK10524 289 GHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 444 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAILNESGEELEGEAEG-YLVFKQ 520
Cdd:PRK10524 369 EPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKgVLVIEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 521 PW-PGIMRTVYGNHERFETTYFKKF-PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK10524 446 PLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 599 VVGHPHPVKGECLYCFVTLCDGHTFS-----PKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQn 673
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAE- 604
|
650
....*....|....*.
gi 8923896 674 DHDLGDMSTVADPSVI 689
Cdd:PRK10524 605 GRDPGDLTTIEDPAAL 620
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-686 |
1.03e-179 |
|
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: 525.52 E-value: 1.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 44 LQRYRELHRRSVEEPREFWGDIAKEF-YWKTPCPGPFLrynfDVTKGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 123 FYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCER 202
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 203 ILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAELgmgdstsqsppikrscpdvqisWN 282
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------------------PA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 283 QGIDLWWHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAED-VFWCTaDIGW 361
Cdd:cd05968 213 KGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGW 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 362 ITGhSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:cd05968 290 MMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 442 INPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQP 521
Cdd:cd05968 369 WNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPEVGE-LVLLAP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05968 447 WPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 602 HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKiAQNDHDLGDMS 681
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLS 605
|
....*
gi 8923896 682 TVADP 686
Cdd:cd05968 606 SLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
93-685 |
1.54e-179 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 523.30 E-value: 1.54e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 93 IEWMKGATTNICYNVLDRNVHEKkLGDKVAFYWEGNEPGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPE 172
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 173 LVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELadealqkcqekgfpvrccivvKH 252
Cdd:PRK04319 111 LYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 253 LgraeLGMGDSTSQSPPIkrscpdvqiswnqgIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHtVGG 332
Cdd:PRK04319 170 V----LLVGEDVEEGPGT--------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH-VHN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 333 YMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVDKYKVTKFYTAPTA 412
Cdd:PRK04319 229 AMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 413 IRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPgATPMKPGSATFP 492
Cdd:PRK04319 306 IRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 493 FFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETtYFKkfPGYYVTGDGCQRDQDGYYWITGRIDDML 572
Cdd:PRK04319 382 LPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK04319 459 KTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKD 538
|
570 580 590
....*....|....*....|....*....|...
gi 8923896 653 GLPKTRSGKIMRRVLrKIAQNDHDLGDMSTVAD 685
Cdd:PRK04319 539 KLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-671 |
8.65e-139 |
|
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: 414.21 E-value: 8.65e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 216
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 FYRgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppiKRscpdvqiswnqgidlwwhelmqea 296
Cdd:cd05969 82 LYE---------------------------------------------------RT------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 297 gdecepewcDAEDPLFILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05969 87 ---------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 377 ATSVLFEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGA 456
Cdd:cd05969 157 VTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 457 qrcPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERF 536
Cdd:cd05969 234 ---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 537 ETtYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05969 310 KN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 617 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05969 387 LKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-575 |
5.73e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 333.90 E-value: 5.73e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 108 LDRNVheKKLGDKVAFywegnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALH 187
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 188 SIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkelaDEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQS 267
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 268 PPIkrscpdvqiswnqgidlwwhelmqeagDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVgGYMLYVATTFKYV--- 344
Cdd:pfam00501 142 ADV---------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrpr 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 345 -FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP 423
Cdd:pfam00501 194 gFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 424 VTKHSraSLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSATFPFFGVAPAILN 502
Cdd:pfam00501 273 RALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVD 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 503 ESGEELEGEAEG-YLVFKQpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS 575
Cdd:pfam00501 348 DETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
137-669 |
1.78e-107 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 333.15 E-value: 1.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLIttda 216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 fyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelmqea 296
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 297 gdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGgYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05972 78 --------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLG 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 377 ATSVLFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGA 456
Cdd:cd05972 149 ATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATGL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 457 qrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERF 536
Cdd:cd05972 224 ---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKT 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 537 ETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05972 299 EASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 8923896 617 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05972 376 LTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-670 |
3.80e-87 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 286.09 E-value: 3.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 40 HVPSLQRYRELHRRSVEEPREFWGDIAKefYWKTPCPGPflrYNFDVTKGKIF--IEWMKGATTNICYNVLDRNVHEkkl 117
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 118 gDKVAFYweGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd05943 84 -DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 198 SLCERILDSSCSLLITTDAFYRGEKLVNLKEladealqKCQE--KGFPVRCCIVVKHlgraelgmgdSTSQSPPIKRSCP 275
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDVRE-------KVAElvKGLPSLLAVVVVP----------YTVAAGQPDLSKI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 276 DVQISWNQGidlwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWC 355
Cdd:cd05943 224 AKALTLEDF-------LATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 356 TADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL 435
Cdd:cd05943 297 YTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 436 GTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSATFPFFGVAPAILNESGEEL 508
Cdd:cd05943 375 LSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLGMAVEAFDEEGKPV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 509 EGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:cd05943 446 WGEKGE-LVCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIY 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 586 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRR 665
Cdd:cd05943 524 RVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEV 603
|
....*
gi 8923896 666 VLRKI 670
Cdd:cd05943 604 AVKKI 608
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
309-663 |
1.65e-84 |
|
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: 269.93 E-value: 1.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 388
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 389 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQT 468
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 469 ETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNHErfETTYFKKFPGYY 548
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWNNP--EATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 549 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPklt 628
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 8923896 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
107-675 |
5.35e-82 |
|
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: 267.45 E-value: 5.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 107 VLDRNVheKKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 187 HSIVFAGFSSESLcERIL-DSSCSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdsts 265
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 266 qsppikrscpdvqiswnqgidlwwhelmqeagdecepewcdaedpLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVF 345
Cdd:COG0318 103 ---------------------------------------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAAL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 346 DFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVT 425
Cdd:COG0318 137 GLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLR--HPEFA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 426 KHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESG 505
Cdd:COG0318 211 RYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 506 EELEGEAEGYLVFKQPWpgIMRTVYGNHERFEttyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:COG0318 288 RELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDR 438
|
570
....*....|.
gi 8923896 665 RVLRKIAQNDH 675
Cdd:COG0318 439 RALRERYAAGA 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-669 |
7.03e-82 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 272.77 E-value: 7.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 57 EPREFWGDIAKEF-YWKTpcpgpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQ 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFYRGEKLVNLKELADEALQKCQEKgfPVRcciVVKHLgraelgMGDSTSQS--------PPIKRScpdvqISWNQGIDL 287
Cdd:PTZ00237 173 YGILNDEIITFTPNLKEAIELSTFK--PSN---VITLF------RNDITSESdlkkietiPTIPNT-----LSWYDEIKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 288 WwHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSY 367
Cdd:PTZ00237 237 I-KENNQSPFYEYVP--VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 368 VtYGPLANGATSVLFEGIPTYPDV--NRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSR---ASLQVLGTVGEPI 442
Cdd:PTZ00237 314 L-YGSLSLGNTFVMFEGGIIKNKHieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 443 NPEAWLWYHRVVGAqRCPIVdtFWQTETGghMLTPLPGATPMKPGSAT-FPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:PTZ00237 393 EESIPEYIENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFKLP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WP-GIMRTVYGNHERFETTyFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:PTZ00237 468 MPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 601 GHPHPVKGECLYCFVTLCDGHTFSP----KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PTZ00237 547 GIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-669 |
6.55e-81 |
|
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: 264.00 E-value: 6.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERiLDSSCSLLITTD 215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFYRgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwHELmqe 295
Cdd:cd05973 80 AANR----------------------------------------------------------------------HKL--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 agdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05973 87 -----------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLAL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 376 GATSVLFEGIPTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:cd05973 155 GHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 456 AqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfKQPWPGIMRTVYGNHER 535
Cdd:cd05973 231 V---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELGPGEPGRLAIDIAN 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 536 FETTYFKKFP---------GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd05973 295 SPLMWFRGYQlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPE 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 607 KGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05973 375 RTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-667 |
5.94e-78 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 262.42 E-value: 5.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 29 WSPPPEVSRSAHVPSLQR------------YRELHRRSVEEPREFWGDIAkEFY---WKTPCPgpflrynfDVTKGKIFI 93
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYT--------VVLAGRRMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 94 --EWMKGATTNICYNVLdRNvhekKLGDKVAFYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIP 171
Cdd:PRK03584 77 gaRWFPGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 172 ELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVN----LKELADealqkcqekGFP-VRC 246
Cdd:PRK03584 151 ETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRA---------ALPsLEH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 247 CIVVKHLGRAELGmgdstsqsPPIKRSCPdvqiswnqgidlwWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKPKG 325
Cdd:PRK03584 222 VVVVPYLGPAAAA--------AALPGALL-------------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPKC 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 326 VVHTVGGYMLYVATTFKYVFDFHAED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVT 404
Cdd:PRK03584 281 IVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 405 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGATP 483
Cdd:PRK03584 358 VFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 484 MKP---GSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMrTVY----GNHERFETTYFKKFPGYYVTGDGCQR 556
Cdd:PRK03584 432 LLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDTFPGVWRHGDWIEI 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 557 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIR 636
Cdd:PRK03584 509 TEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIR 588
|
650 660 670
....*....|....*....|....*....|....*
gi 8923896 637 EKIGPIATPDYIQNAPGLPKTRSGKIM----RRVL 667
Cdd:PRK03584 589 TNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-672 |
2.42e-67 |
|
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: 233.62 E-value: 2.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 39 AHVPSLQRYRELHRRSVEEPREFWGDIAKEFywKTPCPGPFLRYnFDVTKGkIFIEWMKGATTNICYNVLdrnvhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWegNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:TIGR01217 100 EPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAFYRGEKlvnlKELADEALQKCQeKGFP-VRCCIVVKHLgraelgmGDSTSQSPPIKRScpdv 277
Cdd:TIGR01217 178 VLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYL-------GPRETEAPKIDGA---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 278 qiswnqgidLWWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCT 356
Cdd:TIGR01217 242 ---------LDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 357 ADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLG 436
Cdd:TIGR01217 313 TTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGATPMKP---GSATFPFFGVAPAILNESGEELEGEA 512
Cdd:TIGR01217 391 STGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGEV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 513 EGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:TIGR01217 465 GE-LVCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:TIGR01217 543 RLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKR 622
|
...
gi 8923896 670 IAQ 672
Cdd:TIGR01217 623 VLQ 625
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
131-668 |
5.27e-65 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 221.92 E-value: 5.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwh 290
Cdd:cd05971 82 LVT----------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 elmqeagDEcepewcdAEDPLFILYTSGSTGKPKGVVHT-------VGGYMLYvattfkyvFDF--HAEDVFWCTADIGW 361
Cdd:cd05971 85 -------DG-------SDDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpRDGDLYWTPADWAW 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 362 ItghsyvtyGPLANGATSVLFEGIP------TYPDVNRLWSIVDKYKVTKFYTAPTAIRLlMKFGDEPVtKHSRASLQVL 435
Cdd:cd05971 143 I--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGEQL-KHAQVKLRAI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 436 GTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGY 515
Cdd:cd05971 213 ATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 516 LVFKQPWPGIMRTVYGNHERFEttyfKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05971 289 IAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAV 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 595 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05971 365 LMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-669 |
9.00e-64 |
|
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: 220.80 E-value: 9.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 102 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAM 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 178 LACARIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladeaLQKCQEKgfpvrcCIVVkhlgrae 257
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVT------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 258 lgmGDSTSQS-PPIKRSCPDVQI-------SWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT 329
Cdd:cd05928 121 ---SDELAPEvDSVASECPSLKTkllvsekSRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 330 VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDVNRLWSIVDKYKVTKFYTA 409
Cdd:cd05928 196 HSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 410 PTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPLPGATPMKPGS- 488
Cdd:cd05928 274 PTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSm 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 489 -ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHERFETTYFKKFpgyYVTGDGCQRDQDGYYWITG 566
Cdd:cd05928 346 gKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC-DGHTFSP-KLTEELKKQIREKIGPIAT 644
Cdd:cd05928 423 RADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQFLSHDPeQLTKELQQHVKSVTAPYKY 502
|
570 580
....*....|....*....|....*
gi 8923896 645 PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05928 503 PRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
105-668 |
2.37e-62 |
|
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: 216.47 E-value: 2.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 105 YN---VLDRNVhEKKLGDKVAFYwegnepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 182 RIGALhSIVFAGFSSESLCERIL-DSSCSLLITTDAFYrgeklvnlkELADEALqkcqEKGFPVRCCIVVKHLGRAELGM 260
Cdd:cd05959 76 RAGIV-PVPVNTLLTPDDYAYYLeDSRARVVVVSGELA---------PVLAAAL----TKSEHTLVVLIVSGGAGPEAGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 261 gdstsqsppikrscpdvqiswnqgidLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATT 340
Cdd:cd05959 142 --------------------------LLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAEL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 341 F-KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKf 419
Cdd:cd05959 195 YaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFFGVPTLYAAMLA- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 420 gDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPA 499
Cdd:cd05959 271 -APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 500 ILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTyfkkFPGYYV-TGDGCQRDQDGYYWITGRIDDMLNVSGHL 578
Cdd:cd05959 345 LRDEDGGDVADGEPGELYVRGPSSATM--YWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIW 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 579 LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:cd05959 419 VSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTA 498
|
570
....*....|
gi 8923896 659 SGKIMRRVLR 668
Cdd:cd05959 499 TGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-674 |
8.62e-59 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 207.73 E-value: 8.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 102 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 182 RIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRGEKlVNLKeladeALQKCQEKGFPVRCcivvkHLGRAELGmg 261
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYRIES-ADIK-----MIVAIAEDNIPEEI-----EKAAPECP-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 262 dstsqSPPIKRSC-PDVQISWnqgIDLWwHELMQEAGDECEPEWCDA---EDPLFILYTSGSTGKPKGVVHtVGGYMLYV 337
Cdd:cd05970 144 -----SKPKLVWVgDPVPEGW---IDFR-KLIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKMVEH-DFTYPLGH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 338 ATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLM 417
Cdd:cd05970 214 IVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTTFCAPPTIYRFLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 418 KfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPmKPGSATFPFFGVA 497
Cdd:cd05970 292 R---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAPGYE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 498 PAILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLN 573
Cdd:cd05970 364 IDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:cd05970 440 SSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDE 519
|
570 580
....*....|....*....|.
gi 8923896 654 LPKTRSGKImRRVlrKIAQND 674
Cdd:cd05970 520 LPKTISGKI-RRV--EIRERD 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-668 |
1.96e-55 |
|
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: 195.76 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 215
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 afyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelmqe 295
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 agdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI--GWITGHSyvTYGPL 373
Cdd:cd05919 89 ----------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 374 ANGATSVLFegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPInPEAwLWYhRV 453
Cdd:cd05919 157 AVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGEAL-PRG-LGE-RW 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 454 VGAQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtvYGNh 533
Cdd:cd05919 229 MEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVG---YWN- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 534 eRFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 613
Cdd:cd05919 303 -NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 614 FVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05919 382 FVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-668 |
6.63e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 196.56 E-value: 6.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 105 YNVLDRNVheKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDGRR------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 185 A-LHSIVFagFSSESLCERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEalqkcqekgfpVRCCIVVKHLGRAELGmg 261
Cdd:PRK06187 81 AvLHPINI--RLKPEEIAYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------VRTVIVEGDGPAAPLA-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 262 dstsqsppikrscPDVQIswnqgidlwWHELMQEAGDEcePEWCDAE--DPLFILYTSGSTGKPKGVV--------HTVG 331
Cdd:PRK06187 143 -------------PEVGE---------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKGVVlshrnlflHSLA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 332 GymlyvattfKYVFDFHAEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegIPTYPDVNRLWSIVDK 400
Cdd:PRK06187 199 V---------CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV----IPRRFDPENLLDLIET 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 401 YKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGG--HMLTPL 478
Cdd:PRK06187 254 ERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGMTETSPvvSVLPPE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 479 PGATPM--KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFETTYFKkfpGYYVTGDGC 554
Cdd:PRK06187 329 DQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETIDG---GWLHTGDVG 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 555 QRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQ 634
Cdd:PRK06187 404 YIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK---ELRAF 480
|
570 580 590
....*....|....*....|....*....|....
gi 8923896 635 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK06187 481 LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
118-664 |
2.33e-54 |
|
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: 192.83 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 118 GDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 198 SLCERILDSSCSLLIttdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdv 277
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 278 qiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 357
Cdd:cd17631 98 ------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 358 DIGWITGHSYVTYGPLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGT 437
Cdd:cd17631 147 PLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 438 VGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd17631 221 GGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 518 FKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:cd17631 297 VRGP--HVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 598 AVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17631 372 AVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-668 |
3.01e-51 |
|
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: 185.07 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 105 YNVLDRNVheKKLGDKVAFYWegnePGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIF----MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 185 AlhsIVfagfsseslcerildsscsllITTDAFYRGEklvnlkELAdEALQKCQEKGfpvrccIVVkhlgraelgmgdst 264
Cdd:cd05936 74 A---VV---------------------VPLNPLYTPR------ELE-HILNDSGAKA------LIV-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 265 sqsppikrscpdvqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYV 344
Cdd:cd05936 103 ---------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 345 FDFH-AEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPDVNRLWSIVDKYKVTKFYTAPTAIRLL 416
Cdd:cd05936 162 EDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEIRKHRVTIFPGVPTMYIAL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 417 MKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETG--GHmLTPLPGatPMKPGSATFPFF 494
Cdd:cd05936 231 LNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG--PRKPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 GVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTyFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNV 574
Cdd:cd05936 303 GTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGYWNRPEETAEA-FVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIIV 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAGYKVPRQVEFRDEL 454
|
570
....*....|....
gi 8923896 655 PKTRSGKIMRRVLR 668
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-669 |
9.29e-51 |
|
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: 184.44 E-value: 9.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 130 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCS 209
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 LLITTDAFYRGEKLVNLKELADEALqkcqEKGFPVRCCIVVkhlgraelGMGDSTSQSPPIKrscpdvqiswnqgidlww 289
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAIL----ELALDVGVLIRA--------PSAESLSNLLADK------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 helmQEAGDECEPewcDAEDPLFILYTSGSTGKPKGV--VHT-VGGYMLYVATTFKYVFD---------FHaedvfwcta 357
Cdd:cd05926 138 ----KNAKSEGVP---LPDDLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvmplFH--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 358 digwITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTkFYTA-PTAIRLLMKFgDEPVTKHSRASLQVLG 436
Cdd:cd05926 202 ----VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHM-LTPLPgATPMKPGSATFPFfGVAPAILNESGEELEGEAEGY 515
Cdd:cd05926 272 SCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 516 LVFKQPwpGIMRTVYGNHE-RFEttYFKKFpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05926 347 ICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 595 AEAAVVGHPHPVKGECLYCFVTLCDGHtfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05926 422 LEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
307-668 |
6.61e-48 |
|
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: 6.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 307 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 386
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 387 TYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFW 466
Cdd:cd05958 174 ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 467 QTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVY-GNHERFETTYFKKfp 545
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 8923896 626 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-668 |
6.62e-48 |
|
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: 174.40 E-value: 6.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 134 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsscslLIT 213
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 TDAFYRGEKLvnlKELADEAlqkcqekgfpvRCCIVVKhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelm 293
Cdd:cd05934 58 INTALRGDEL---AYIIDHS-----------GAQLVVV------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 qeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:cd05934 82 ---------------DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 PLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgTVGEPINPEAWLWYH 451
Cdd:cd05934 144 ALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 452 RVVGaqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVY 530
Cdd:cd05934 216 ERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYY 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 531 GNHErfETTyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05934 291 NMPE--ATA--EAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 610 CLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05934 367 EVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-671 |
1.56e-47 |
|
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: 173.91 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsIVFAGfsseslcerildsscSLLITTD 215
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA---VVIPA---------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 afyrgeklvnlkELADEAlqkcqEKGFPVRCCIVvkhlgraelgmgDSTSqsppikrscpdvqiswnqgidlwwhelmqe 295
Cdd:cd05974 63 ------------DLRDRV-----DRGGAVYAAVD------------ENTH------------------------------ 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 agdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFkYVFDFHAEDVFWCTADIGWiTGHSYVT-YGPLA 374
Cdd:cd05974 84 -----------ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWN 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 375 NGATSVLFegipTYP--DVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHR 452
Cdd:cd05974 151 AGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 453 VVGAQRCPIVDTFWQTETgghmlTPLPGATP---MKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRT 528
Cdd:cd05974 220 VRRAWGLTIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 529 VYGNHERfetTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 608
Cdd:cd05974 294 YAGDPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 609 ECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 671
Cdd:cd05974 371 SVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-669 |
5.44e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 174.35 E-value: 5.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCeRILDSSCSLLITTDAfyrgeklvNLKELADEALQKCQEKGFPVRCcivvkhlgraelgmgdSTSQSPPikrscPDVQ 278
Cdd:PRK08316 100 LA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL----------------VLGGREA-----PGGW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 ISWNQgidlwwhelMQEAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----VGGYMLYVATTfkyvfDFHAEDVF 353
Cdd:PRK08316 150 LDFAD---------WAEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG-----DMSADDIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 354 WCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTA-IRLLmkfgdepvtKH- 427
Cdd:PRK08316 216 LHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISLL---------RHp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 428 --SRASLQVL--GTVGEPINPEAWLwyHRVvgAQRCPIVdTFW----QTETGghmltPL-----PGATPMKPGSATFPFF 494
Cdd:PRK08316 279 dfDTRDLSSLrkGYYGASIMPVEVL--KEL--RERLPGL-RFYncygQTEIA-----PLatvlgPEEHLRRPGSAGRPVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 GVAPAILNESGEELEgeaegylvfkqpwPGIMRTVYGNHERFETTYFKKfP---------GYYVTGDGCQRDQDGYYWIT 565
Cdd:PRK08316 349 NVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHSGDLGVMDEEGYITVV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 566 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATP 645
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|....
gi 8923896 646 DYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK08316 492 KRVIFVDELPRNPSGKILKRELRE 515
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
102-669 |
1.13e-45 |
|
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: 170.40 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 102 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 182 RIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKcqekgFPVRCCIVVkhLGRAELGmg 261
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGK-----SPHLEHRVV--VGRPEAG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 262 dstsqsppikrscpDVQISwnqgidlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTF 341
Cdd:TIGR02262 139 --------------EVQLA----------ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 342 KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKFYTAPTAIRLLMkfGD 421
Cdd:TIGR02262 195 RNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQPTIFYGVPTLYAAML--AD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 422 EPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAIL 501
Cdd:TIGR02262 270 PNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 502 NESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:TIGR02262 345 GDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 582 AEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfspKLTEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:TIGR02262 420 FEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTA 493
|
570
....*....|.
gi 8923896 659 SGKIMRRVLRK 669
Cdd:TIGR02262 494 TGKIQRFKLRE 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-663 |
2.93e-44 |
|
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: 165.85 E-value: 2.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTDAFYrgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSqsppikrscpdvqisWNQGIDLWWHE 291
Cdd:cd05911 87 FTDPDGL-------------EKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLS---------------PTLGEEDEDLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 LMQEAGDEcepewcdaeDPLFILYTSGSTGKPKGVV--HTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITG-HSYV 368
Cdd:cd05911 139 PPLKDGKD---------DTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGlFTTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TYgpLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAwl 448
Cdd:cd05911 209 AS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVILSGGAPLSKEL-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 wYHRV-VGAQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEaegylvfKQP---W-- 522
Cdd:cd05911 279 -QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP-------NEPgeiCvr 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 523 -PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05911 349 gPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIG 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 602 HPHPVKGECLYCFVTLCDGhtfsPKLTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSGKIM 663
Cdd:cd05911 427 IPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASGKIL 486
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
29-669 |
1.07e-39 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 156.01 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 29 WSPPPEVSRSAHVPSLQRYR-----------------ELHRRSVEEPREFWGDIAKEF--YWKTPcPGPFLRYNFDVTKG 89
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDELslVFSVP-PRCILDTSDESNPG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 90 KifiEWMKGATTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYM 167
Cdd:PLN03052 166 G---QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 168 PMIPELVVAMLAcarigalhsIVFAG---------FSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEAlqkcq 238
Cdd:PLN03052 241 PMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA----- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 239 ekgfpvrccivvkhlgraelgmgdstsQSP-----PIKRSCPDVQIswnQGIDLWWHELMQEA-----GDECEPEWCDAE 308
Cdd:PLN03052 307 ---------------------------KAPkaivlPADGKSVRVKL---REGDMSWDDFLARAnglrrPDEYKAVEQPVE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVF-WCTaDIGWITGHsYVTYGPLANGATSVLFEGIPT 387
Cdd:PLN03052 357 AFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 388 YPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGdePVTKHSRASLQVLGTVGEPINPEAWLWYhrVVGAQRCPIVDTFWQ 467
Cdd:PLN03052 434 GRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MSRAGYKPIIEYCGG 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 468 TETGGHMLTplpgATPMKPGS-ATF--PFFGVAPAILNESGeelegeaegylvfkQPWP----------------GIMRT 528
Cdd:PLN03052 507 TELGGGFVT----GSLLQPQAfAAFstPAMGCKLFILDDSG--------------NPYPddapctgelalfplmfGASST 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 529 VY-GNHERfetTYFKKFPGYYVT-----GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHEAVAEAA 598
Cdd:PLN03052 569 LLnADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DESVLETA 642
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923896 599 VVGHPHPVKG-ECLYCFVTLCDGHTFSPKLtEELKK----QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN03052 643 AIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
132-667 |
1.71e-39 |
|
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: 151.14 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERIL----DSS 207
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 208 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidl 287
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 288 wwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWItGHSY 367
Cdd:cd05930 91 ------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSVW 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 368 VTYGPLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVtkhsRASLQVLGTVGEPINPE 445
Cdd:cd05930 151 EIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSLRLVLVGGEALPPD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 446 AW-LWYHRVVGAQ--------RCPIVDTFWQTETGGHMLTPLPGATPMkPGSATFpffgvapaILNESGeelegeaegyl 516
Cdd:cd05930 224 LVrRWRELLPGARlvnlygptEATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLDENL----------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 517 vfkQPWP------------GIMRTVYGNHE----RFETTYFkkFPG--YYVTGD-GCQRDqDG--YYwiTGRIDDMLNVS 575
Cdd:cd05930 284 ---RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGDlVRWLP-DGnlEF--LGRIDDQVKIR 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:cd05930 356 GYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYMVPSAFVVLDALP 432
|
570
....*....|..
gi 8923896 656 KTRSGKIMRRVL 667
Cdd:cd05930 433 LTPNGKVDRKAL 444
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-669 |
3.82e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 151.60 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAfYWEGNEpgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagf 194
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 sseslcerildsscslLITtdafyrgeklVNLKELADEALQKCQEKGfpVRCCIVVKHLgraeLGMGDSTSQSPP---IK 271
Cdd:PRK07656 82 ----------------VVP----------LNTRYTADEAAYILARGD--AKALFVLGLF----LGVDYSATTRLPaleHV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 272 RSCPDVQISWNQGIDLWWHELMQEA-GDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGG-YMLY--VATTFKYVFD- 346
Cdd:PRK07656 130 VICETEEDDPHTEKMKTFTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAadWAEYLGLTEGd 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 347 --------FHaedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMK 418
Cdd:PRK07656 209 rylaanpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 419 FGDEpvTKHSRASLQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDT-FWQTETGGHM-LTPLPGATPMKPGSATFPFFGV 496
Cdd:PRK07656 272 HPDR--SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 497 APAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 576
Cdd:PRK07656 347 ENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 577 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspkLTEE-LKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK07656 423 FNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE----LTEEeLIAYCREHLAKYKVPRSIEFLDELP 498
|
570
....*....|....
gi 8923896 656 KTRSGKIMRRVLRK 669
Cdd:PRK07656 499 KNATGKVLKRALRE 512
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
136-687 |
2.61e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 150.88 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAcariGALHSIVFA---GFSSESLCErildsscsLLI 212
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 213 TTDAfyrgEKLVNLKELAD-EALQKCQEKgfpVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQIswnqGIDLWWHE 291
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGtDIWQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHA----RILDFDAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 LMQEAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVT- 369
Cdd:PRK07529 196 LARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNA-LLVTg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 370 YGPLANGAtSVLFEGIPTYPD---VNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:PRK07529 274 LAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 WLWYHRVVGAqrcPIVDTFWQTE-TGGHMLTPLPGatPMKPGSA--TFPFFGVAPAILNESGEELEGEAEG---YLVFKQ 520
Cdd:PRK07529 350 FRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLRDCAVDevgVLCIAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 521 P--WPGIMRTVYGNHERFEttyfkkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK07529 425 PnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 599 VVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREkigPIATPDYIQNAPGLPKTRSGKI---------MRRVLR 668
Cdd:PRK07529 498 AVGRPDAHAGELPVAYVQLKPGASATEaELLAFARDHIAE---RAAVPKHVRILDALPKTAVGKIfkpalrrdaIRRVLR 574
|
570 580
....*....|....*....|
gi 8923896 669 K-IAQNDHDLGDMSTVADPS 687
Cdd:PRK07529 575 AaLRDAGVEAEVVDVVEDGR 594
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
135-672 |
9.08e-38 |
|
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: 147.98 E-value: 9.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHsiVFAGFS---SE--SLCERildSSCS 209
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrrAEisHFAEQ---SEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 LLITTDAfYRGeklVNLKELADEALQKCQEkgfpVRCCIVVkhlgraelgmGDstsqsppikrscPDVQISWNqgidlww 289
Cdd:COG1021 125 AYIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV----------GD------------AGEFTSLD------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 hELMQEAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGwitgHSY-- 367
Cdd:COG1021 168 -ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPAA----HNFpl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 368 ---VTYGPLANGATSVLfegIPTyPDVNRLWSIVDKYKVTkfYTA--PTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPI 442
Cdd:COG1021 241 sspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDLSSLRVLQVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 443 NPEA----------WLW-----------Y-------HRVVGAQRCP--------IVDtfwqtETGghmlTPLPgatpmkP 486
Cdd:COG1021 313 SPELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG----NPVP------P 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 487 GSAtfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnherfettYFKKfP----------GYYVTGDGCQR 556
Cdd:COG1021 378 GEV-----GE-------------------LLTRGPY-----TIRG--------YYRA-PehnaraftpdGFYRTGDLVRR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 557 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcDGHTFSPKlteELKKQ 634
Cdd:COG1021 420 TPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-RGEPLTLA---ELRRF 493
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 8923896 635 IREKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:COG1021 494 LRER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
167-668 |
2.02e-35 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 140.72 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 167 MPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALqkcqekgfPVRC 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAA--------PAKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 247 cIVVKHLGRaelgmgdstSQSPPIKrscPDVQiSWNQ--GIDLWWHelmQEAGDECEPEWCDAEDPLFILYTSGSTGKPK 324
Cdd:PLN03051 73 -IVLPAAGE---------PVAVPLR---EQDL-SWCDflGVAAAQG---SVGGNEYSPVYAPVESVTNILFSSGTTGEPK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 325 GVVHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVNRLwsiVDKYKVT 404
Cdd:PLN03051 136 AIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQDAGVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 405 KFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcPIVDTFWQTETGGHML--TPLpgaT 482
Cdd:PLN03051 211 VLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLL---Q 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 483 PMKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHERfetTYFKKFPGYYVTGDGCQRDQD 559
Cdd:PLN03051 287 PQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKGMPLRRHGD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 560 -------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPVKG-ECLYCFVTLCD-GHTFSPKLTE 629
Cdd:PLN03051 364 imkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLVIFLVLGEeKKGFDQARPE 443
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 8923896 630 ELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PLN03051 444 ALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-667 |
3.63e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 140.48 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 101 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVL-RKQGIQKGDRVAIYMPMIPELVVAMLA 179
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 180 CARIGALHSIVFAGFSSESLCERILDSSCSLLITTDafyrgeklvnlkELADEALQKCQEKGfpVRCCIVVKhlgraelg 259
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS------------ELAPKVAPAVGNLR--LRHVIVAQ-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 260 MGDSTSQSPPIK-----RSCPDVQISWNQGIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYM 334
Cdd:PRK08314 139 YSDYLPAEPEIAvpawlRAEPPLQALAPGGVVAW--KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 335 LYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPT-AI 413
Cdd:PRK08314 217 ANAVGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERYRVTHWTNIPTmVV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 414 RLLMKFGdepVTKHSRASLQVLGTVGEPInPEAWlwyhrvvgAQR------CPIVDTFWQTETGGHMLTPLPGATpmKPG 487
Cdd:PRK08314 292 DFLASPG---LAERDLSSLRYIGGGGAAM-PEAV--------AERlkeltgLDYVEGYGLTETMAQTHSNPPDRP--KLQ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 488 SATFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTVYGNHERFETTyFKKFPG--YYVTGDGCQRDQDGYYW 563
Cdd:PRK08314 358 CLGIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 564 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlTEELKKQIREKIGPIA 643
Cdd:PRK08314 434 ITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYK 512
|
570 580
....*....|....*....|....
gi 8923896 644 TPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08314 513 YPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
132-667 |
7.36e-35 |
|
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: 138.21 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhe 291
Cdd:cd17643 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 lmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYM-LYVATTfkYVFDFHAEDVfwctadigWITGHSYV-- 368
Cdd:cd17643 91 --------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 -----TYGPLANGATSVlfegIPTYpDVNR----LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvG 439
Cdd:cd17643 147 fsvweIWGALLHGGRLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--G 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 440 EPINPeAWL--WYHRVvGAQRCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSATFPFFGVAPAILNESGEELEGE 511
Cdd:cd17643 220 EALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGVV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 512 AEGYLVFKQPWPGIMRTVYGNHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:cd17643 297 GELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMR 664
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADI---AELRALLKELL-----PDYMVPAryvplDALPLTVNGKLDR 447
|
...
gi 8923896 665 RVL 667
Cdd:cd17643 448 AAL 450
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
136-667 |
1.98e-32 |
|
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: 131.97 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AfyrgeklvNLKELADEALQkcqekgfpvrccIVVkhLGRAE---LGMGDSTSQSPPIkrSCPDVQISwnqgidlwwhel 292
Cdd:cd05904 113 E--------LAEKLASLALP------------VVL--LDSAEfdsLSFSDLLFEADEA--EPPVVVIK------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 mqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYmlyVATTFKYVFDF----HAEDVFWCTADIGWITGHSYV 368
Cdd:cd05904 157 --------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLPMFHIYGLSSF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAwl 448
Cdd:cd05904 220 ALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKEL-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 wYHRVvgAQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSATFPFFGVAPAILNESGEELegeaegyLVFKQP- 521
Cdd:cd05904 292 -IEAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES-------LPPNQTg 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 --W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 596
Cdd:cd05904 360 elWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 597 AAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGP------IATPDYIqnapglPKTRSGKIMRRVL 667
Cdd:cd05904 438 AAVIPYPDEEAGEVPMAFVVRKPGSSLTED---EIMDFVAKQVAPykkvrkVAFVDAI------PKSPSGKILRKEL 505
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-671 |
2.97e-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: 125.67 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 315 YTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 390
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 391 VNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE- 469
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 470 TGGHMLTPlPGaTPMKPGSA--TFPFFGVAPAILNESGEELEGEAEGylvfkQPWPGIM--RTVYGNH---ERFETTYFK 542
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVglRLPYARVRIKVLDGVGRLLRDCAPD-----EVGEICVagPGVFGGYlytEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 543 kfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 622
Cdd:cd05944 232 --DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 8923896 623 FSP-KLTEELKKQIREKigpIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05944 310 VEEeELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-672 |
8.00e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 127.85 E-value: 8.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK06178 48 QRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCqekgfPVRCCIVVkhlGRAELGMGDSTSQSPPIKRSCPDVQ 278
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---------PVVEQVRAET-----SLRHVIVT---SLADVLPAEPTLPLPDSLRAPRLAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 ISWnqgIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTFKYVFDFHAED-VFWCTA 357
Cdd:PRK06178 185 AGA---IDLL--PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAAAYAVAVVGGEDsVFLSFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 358 DIGWITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTK-FYTAPTAIRLLmkfgDEP-VTKHSRASLQVL 435
Cdd:PRK06178 259 PEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM----DHPrFAEYDLSSLRQV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 436 GTVG--EPINPEAWLWYHRVVGaqrCPIVDTFW-QTET------------GGHMLT--------PLPGA----TPMKPGs 488
Cdd:PRK06178 331 RVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefkiCDFETG- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 489 ATFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGY 561
Cdd:PRK06178 407 ELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEALRD--GWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 562 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGP 641
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCRENMAV 534
|
570 580 590
....*....|....*....|....*....|..
gi 8923896 642 IATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PRK06178 535 YKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-668 |
1.45e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 126.64 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM----LACARIGALHSIVfagf 194
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqLAGLRRTALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 SSESLCERILDSSCSLLITTDAFYRgeklvnlkELADEALQKCQEkgfpvrccivVKHLgraeLGMGDStsqsppikrsc 274
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPV----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 275 pdvqiswNQGIDLWwhelmqEAGDECEPE----WCDAEDPLFILYTSGSTGKPKGVVHTVGGYmlyvaTTFkyvfdfhae 350
Cdd:PRK06188 144 -------PDGVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSI-----ATM--------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 351 dVFWCTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDe 422
Cdd:PRK06188 197 -AQIQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLRAIEEQRITATFLVPTMIYALLDHPD- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 423 pVTKHSRASLQVLGTVGEPINP----EAwlwyHRVVGaqrcPI-VDTFWQTETGgHMLTPLP-----GATPMKPGSATFP 492
Cdd:PRK06188 275 -LRTRDLSSLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 493 FFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETT--YFKKfpGYYVTGDGCQRDQDGYYWITGRIDD 570
Cdd:PRK06188 345 TPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVAREDEDGFYYIVDRKKD 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQN 650
Cdd:PRK06188 418 MIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDF 494
|
570
....*....|....*...
gi 8923896 651 APGLPKTRSGKIMRRVLR 668
Cdd:PRK06188 495 VDSLPLTALGKPDKKALR 512
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-669 |
3.07e-30 |
|
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: 125.28 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFYRgeklvnlkeLADEALQKCqekgfpvrccivvkHLGRAELGMGDSTSQSPPIKRSCPdvqISWNQgidlwwhelMQE 295
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGDPAHASEGHPGEEP---ASWPK---------LLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT----VGGymlyvATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:TIGR03098 151 LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLShrnlVAG-----AQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 pLANGATSVLFEgiptYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTVGEPInPEAWLWYH 451
Cdd:TIGR03098 226 -FYVGATVVLHD----YLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGGAM-PRATLSRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 452 RvvgaQRCPIVDTFWQ---TETGGHMLTPlPGATPMKPGS--ATFPFFGVapAILNESGEELEGEAEGYLVFKQP----- 521
Cdd:TIGR03098 297 R----SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEEGELVHRGAlvamg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 -WPGIMRTVygnhERFE-TTYFK---KFPGYYV-TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:TIGR03098 370 yWNDPEKTA----ERFRpLPPFPgelHLPELAVwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVA 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 596 EAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:TIGR03098 446 EAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-667 |
4.75e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.53 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFYrgEKLVNLkeladEALQKCQEkgfpvrccIVVKHLgrAELGMGDSTSQSPPI--KRSCPDVQISWNQGIDLWwhELM 293
Cdd:PRK06710 130 LVF--PRVTNV-----QSATKIEH--------VIVTRI--ADFLPFPKNLLYPFVqkKQSNLVVKVSESETIHLW--NSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 QEAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD-FHAEDVFWCTADIGWITGHSYVTYG 371
Cdd:PRK06710 191 EKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 PLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTK-HSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PRK06710 271 SIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 HRVVGAQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGI 525
Cdd:PRK06710 344 ETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEIgEIVVKGP--QI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 526 MRTVYGNHErfETTYFKKfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:PRK06710 414 MKGYWNKPE--ETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923896 606 VKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
131-668 |
5.10e-30 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 124.38 E-value: 5.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSL 210
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAFYRGEklvnlkeLADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqGIDLWWH 290
Cdd:cd17651 95 LVLTHPALAGE-------LAVEL--------------------------------------------------VAVTLLD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ELMQEAGDECEPEW-CDAEDPLFILYTSGSTGKPKGVV------------HTVGGYMLYVATTFKYV---FDFHAEDVFw 354
Cdd:cd17651 118 QPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFAglgFDVSVQEIF- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 355 ctadigwitghsyvtyGPLANGATSVLfegIPTY--PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHsrASL 432
Cdd:cd17651 197 ----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL--AAL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 433 QVLGTVGEPINPEAWL--WYHRVVGAQrcpIVDTFWQTET---GGHMLTPLPGATPMKPGSATfPFFGVAPAILNEsgee 507
Cdd:cd17651 256 RYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PIDNTRVYVLDA---- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 508 legeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDM 571
Cdd:cd17651 328 ----------ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREKIGPIATPDYIQNA 651
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLL 474
|
570
....*....|....*..
gi 8923896 652 PGLPKTRSGKIMRRVLR 668
Cdd:cd17651 475 DALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
137-599 |
5.18e-30 |
|
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: 123.14 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLITT 214
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 DAFyrgeklvnlkeladealqkCQEKGFPVRCCIVVkhLGRAELGMGDSTSQSPPIKRSCPDvqiswnqgidlwwhelmq 294
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 eagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVfwctadigWITGHSYV------ 368
Cdd:TIGR01733 121 --------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasve 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 -TYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTkhSRASLQVLGTVGEPINPEAW 447
Cdd:TIGR01733 178 eIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRLVILGGEALTPALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 448 LWYHRVVGAQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP- 523
Cdd:TIGR01733 253 DRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL--------------RPVPv 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 -----------GIMRtvyGNHERFETT--YFKKFPGY-------YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:TIGR01733 317 gvvgelyiggpGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
490
....*....|....*.
gi 8923896 584 VESALVEHEAVAEAAV 599
Cdd:TIGR01733 394 IEAALLRHPGVREAVV 409
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-669 |
6.73e-30 |
|
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: 124.28 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 118 GDKVAFYWEGnePGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LHSI---VFAg 193
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 194 fsseslcERILdsscslLITTDAfyrGEKLVnlkeLADEALQKCQEKGFPVrcCIVVKHLgraeLGMGDSTSQSPPIkrs 273
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAPR--LPTVEHV----VVMTDDAAMPEPA--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 274 cPDVQISWnqgidlwWHELMQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMlyvattfKYVF 345
Cdd:cd12119 138 -GVGVLAY-------EELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAALL-------TDGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 346 DFHAEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvnrLWSIVDKYKVTKFYTAPTAIR 414
Cdd:cd12119 202 GLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFAAGVPTVWQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 415 LLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGAQRCP----------IVDTF--W-QTETG--GHMLTPLP 479
Cdd:cd12119 267 GLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSplGTVARPPS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 480 GATPMKPG-------SATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHErfeTTYFKKFPGYYVT 550
Cdd:cd12119 328 EHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKNDE---ESEALTEDGWLRT 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 551 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEE 630
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA---EE 479
|
570 580 590
....*....|....*....|....*....|....*....
gi 8923896 631 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd12119 480 LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
115-669 |
1.74e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 123.23 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFYWegnepGETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGf 194
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 sseslcerildsscsllittdafyrgeklVNLKELADEALQKCQEKGfpvrccivvkhlGRAELGMGDSTSQSPPIKRSC 274
Cdd:PRK07470 87 -----------------------------TNFRQTPDEVAYLAEASG------------ARAMICHADFPEHAAAVRAAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 275 PDvqISWNQGIDLWWHELMQEA------GDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTfkyvfdfH 348
Cdd:PRK07470 126 PD--LTHVVAIGGARAGLDYEAlvarhlGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAFVITN-------H 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 349 AEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVNRLWSIVDKYKVTKFYTAPTAI 413
Cdd:PRK07470 196 LADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNLFTVPTIL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 414 RLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMlTPLPGA------TPM-KP 486
Cdd:PRK07470 266 KMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdaedGPDaRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 487 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCQRDQDGYYWI 564
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavFAGYYNNPEANAKAFRDGWFR-------TGDLGHLDARGFLYI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 565 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIAT 644
Cdd:PRK07470 413 TGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGKVARYKL 489
|
570 580
....*....|....*....|....*
gi 8923896 645 PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07470 490 PKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-670 |
2.13e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 122.38 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAG--FSS 196
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 197 ESLCERILDSSCSLLITTDAFyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrsCPD 276
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF--------------------------------------------------------EAK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 277 VQIswnqGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWC 355
Cdd:PRK03640 113 LIP----GISVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 356 TADIGWITGHSYVTygplangaTSVLFeGIPTY-------PDVNRLwsIVDKyKVTKFYTAPTAI-RLLMKFGDEPVTKH 427
Cdd:PRK03640 188 AVPIFHISGLSILM--------RSVIY-GMRVVlvekfdaEKINKL--LQTG-GVTIISVVSTMLqRLLERLGEGTYPSS 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 428 SRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 502
Cdd:PRK03640 256 FRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEK 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 503 ESGEELEGEAEGYLVfKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK03640 323 DGVVVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIY 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 581 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK03640 395 PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKRFYFVEELPRNASG 469
|
570
....*....|
gi 8923896 661 KIMRRVLRKI 670
Cdd:PRK03640 470 KLLRHELKQL 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-668 |
5.68e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.07 E-value: 5.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 216
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 FYRGE-KLVNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelmqE 295
Cdd:PRK09088 104 VAAGRtDVEDLAAFIASA-------------------------------------------------------------D 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTAD----IGWITGHSYVtyg 371
Cdd:PRK09088 123 ALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRPV--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 pLANGATSVLFEGIPTYPDVNRLWSIvdKYKVTKFYTAPtaiRLLMKFGDEPVTKHSR-ASLQVLGTVGEPiNPE----A 446
Cdd:PRK09088 199 -LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFTGGAP-HAAedilG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 WLwyhrvvgAQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WP 523
Cdd:PRK09088 272 WL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnlSP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 GIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 603
Cdd:PRK09088 345 GYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMA 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 604 HPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK09088 419 DAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
119-674 |
5.88e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 122.08 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAFyRG---EKLVNlkELADE--ALQKcqekgfpvrccIVVkhlgraeLGMGDSTSqsppikrs 273
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGfdhAAMAR--RLRPElpALRH-----------VVV-------VGGDGADS-------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 274 cpdvqiswnqgidlwWHELMqeagdeCEPEWCDAEDPLFIL--------------YTSGSTGKPKGVVHT----VGGYML 335
Cdd:PRK13295 170 ---------------FEALL------ITPAWEQEPDAPAILarlrpgpddvtqliYTSGTTGEPKGVMHTantlMANIVP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 336 YVATtfkyvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVNRLWSIVDKYKVTkFYTAPTAirL 415
Cdd:PRK13295 229 YAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP--F 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 416 LMKFGDepVTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPMKpGS 488
Cdd:PRK13295 297 LTDLTR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDER-AS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 489 AT--FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITG 566
Cdd:PRK13295 366 TTdgCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PKLTEELKKQireKIGPIATP 645
Cdd:PRK13295 440 RSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQYIP 516
|
570 580
....*....|....*....|....*....
gi 8923896 646 DYIQNAPGLPKTRSGKIMRRVLRKIAQND 674
Cdd:PRK13295 517 ERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-667 |
9.00e-29 |
|
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: 120.04 E-value: 9.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LcERILD-SSCSLLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdv 277
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 278 qiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTA 357
Cdd:cd05945 98 -------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQA 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 358 ---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvnrlwsivdkykVTKFYTAPTAIRLL 416
Cdd:cd05945 146 pfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------ITVWVSTPSFAAMC 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 417 MkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRvvgAQRCPIVDTFWQTET----GGHMLTPLPGATpMKPGSAT 490
Cdd:cd05945 203 L--LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQR---FPDARIYNTYGPTEAtvavTYIEVTPEVLDG-YDRLPIG 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHERFettyFKKFPGY--YVTGDGCQRDQDGYYWITG 566
Cdd:cd05945 276 YAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDLVRLEADGLLFYRG 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFspKLTEELKKQIREKIGPIATPD 646
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA--GLTKAIKAELAERLPPYMIPR 428
|
570 580
....*....|....*....|.
gi 8923896 647 YIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05945 429 RFVYLDELPLNANGKIDRKAL 449
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
583-661 |
1.24e-28 |
|
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: 109.17 E-value: 1.24e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 583 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
135-667 |
1.65e-28 |
|
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: 119.12 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 214
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 dafyrgeklvnlKELADEALqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelmq 294
Cdd:cd05935 81 ------------SELDDLAL------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 eagdecepewcdaedplfILYTSGSTGKPKGVVHTvGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05935 89 ------------------IPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVY 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 375 NGATSVLFegipTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPInPEAWLwyHRVV 454
Cdd:cd05935 150 VGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPM-PPAVA--EKLL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 455 GAQRCPIVDTFWQTETgghmLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGIMRTvYG 531
Cdd:cd05935 221 KLTGLRFVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVgEIVVRGP--QIFKG-YW 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 532 NHERFETTYFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05935 294 NRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGE 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 610 CLYCFVTLCDGhtFSPKLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05935 374 EVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
137-669 |
2.63e-28 |
|
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: 118.25 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsSCSLLittdA 216
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV--------------------TNPIL----P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 FYRGEKLVNLkeladeaLQKCQEKGFpvrccIVVKHLGRAE-LGMGDSTSQsppikrscpdvqiswnqgidlwwhelmqe 295
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVF-----VVPERFRQFDpAAMPDAVAL----------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 agdecepewcdaedplfILYTSGSTGKPKGVVHTVGGYMlyvATTFKYV--FDFHAEDVFWCTADIGWITGHSYVTYGPL 373
Cdd:cd05903 98 -----------------LLFTSGTTGEPKGVMHSHNTLS---ASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 374 ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMK---FGDEPVtkhsrASLQVLGTVGEPINP----EA 446
Cdd:cd05903 158 LLGAPVVLQDIW----DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRslarRA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 WlwyhRVVGAQRCPIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgim 526
Cdd:cd05903 229 A----ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP----- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 527 RTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd05903 297 SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDER 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923896 607 KGECLYCFVTLCDGHTFS-PKLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05903 377 LGERACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
135-667 |
4.95e-28 |
|
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: 118.16 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 213
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 TDAfyrgeklvnlkeLADealqkcqekgfPVRCCIVVKHLGRAELGMGDSTSQSPPikrscpdvqiswnqgidlwwhelm 293
Cdd:cd12116 91 DDA------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPV------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 qeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGY------------------MLYVATtfkYVFDFHAEDVFWc 355
Cdd:cd12116 124 ------------SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT---YAFDISLLELLL- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 356 tadigwitghsyvtygPLANGATSVLFEGIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkhsRASLQVL 435
Cdd:cd12116 188 ----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTAL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 436 -GtvGEPINPEawlwyhrvVGAQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSATFPffgVAPAILNESGeeleg 510
Cdd:cd12116 246 cG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IGRPLANTQV----- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 511 eaegYLV--FKQPWP-GIMRTVY--------GNHERFETTyFKKF-------PG--YYVTGDGCQRDQDGYYWITGRIDD 570
Cdd:cd12116 303 ----YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADG 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQN 650
Cdd:cd12116 378 QVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVR 453
|
570
....*....|....*..
gi 8923896 651 APGLPKTRSGKIMRRVL 667
Cdd:cd12116 454 LDALPLTANGKLDRKAL 470
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-668 |
6.10e-28 |
|
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: 117.54 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 145 VCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSeslcerildsscsLLITTDAFYRGeklv 224
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNP-------------TLKESVLRYLV---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 225 nlkelADEALqkcqekgfpvrccivvkHLGRAELGMGDSTSQSPPIKRScPDVQISwnqgIDLWWHELMQEAGDECEPEw 304
Cdd:cd05922 66 -----ADAGG-----------------RIVLADAGAADRLRDALPASPD-PGTVLD----ADGIRAARASAPAHEVSHE- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 305 cdaeDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLF 382
Cdd:cd05922 118 ----DLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 383 EGipTYPDVNrLWSIVDKYKVTKFYTAPTAIRLL--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWLWYHR--VVGAQr 458
Cdd:cd05922 190 ND--GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 459 cpIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHERFET 538
Cdd:cd05922 260 --VYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 539 TYfKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLC 618
Cdd:cd05922 335 KE-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAP 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 8923896 619 DGHTFSPklteeLKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05922 413 DKIDPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-668 |
1.25e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.48 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 116 KLGDKVAFYWEgNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFS 195
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 196 SESlCERILDSS-CSLLITTDAFYRgeklvnlkelADEALQkcQEKGFPVRCCIVVKHLGRAELGMGDSTSQsppikrsc 274
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFYP----------MYRQIQ--QEDATPLRHICLTRVALPADDGVSSFTQL-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 275 pdvqiswnqgidlwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----VGGYmlY----VATTFKYVF 345
Cdd:PRK08008 157 -----------------KAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--YsawqCALRDDDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 346 -----DFHAEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfg 420
Cdd:PRK08008 218 ltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMV-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 421 dEPVTKHSRASL--QVLGTVgePINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGATPMKPgSATFPFFGVAP 498
Cdd:PRK08008 279 -QPPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 499 AILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 577
Cdd:PRK08008 352 EIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK08008 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKVPSYLEIRKDLPRN 506
|
570
....*....|.
gi 8923896 658 RSGKIMRRVLR 668
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-669 |
6.40e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 115.87 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 107 VLDRNVHEkkLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA- 185
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 186 --LHSIVFAGFSSESLCE----RIL---DSSCSLLITTDAFYRGEKL--VNLKElADEALQKcqekgFPVRCCIVVKHLG 254
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFEdhgaRVAivwDKVAPTVERLRRTTPLETIvsVNMIA-AMPLLQR-----LALRLPIPALRKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 255 RAELgmgdsTSQSPPIkrscpdvqISWNQGIDlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYM 334
Cdd:PRK05605 183 RAAL-----TGPAPGT--------VPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 335 LYVATTFKYVFD--------------FHAEDVFWCtadigwitghsyVTYGPLAnGATSVLFegiPTyPDVNRLWSIVDK 400
Cdd:PRK05605 246 ANAAQGKAWVPGlgdgpervlaalpmFHAYGLTLC------------LTLAVSI-GGELVLL---PA-PDIDLILDAMKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 401 YKVTKFYTAPTAIRLLMKFGDEP-VTKHS-RASLQvlgtvgepinpeawlwyhrvvGAQRCPiVDTF--WQTETGGHM-- 474
Cdd:PRK05605 309 HPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS---------------------GAMALP-VSTVelWEKLTGGLLve 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 475 ---LT---PLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVYGNHERFETTYFK 542
Cdd:PRK05605 367 gygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFKGYWNRPEETAKS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 543 KFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 622
Cdd:PRK05605 442 FLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 8923896 623 FSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05605 522 LDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
313-669 |
7.03e-27 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 113.60 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 313 ILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVN 392
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 393 RLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQ 467
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 468 TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTVYGNHER----FETTYFKk 543
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNRPDAteesFENGWFK- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 544 fpgyyvTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtf 623
Cdd:cd05912 297 ------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS------ 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 8923896 624 SPKLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05912 365 ERPISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-668 |
8.33e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 111.71 E-value: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 112 VHEKKLGDKVAFYWegnePGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVF 191
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 192 AGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCQEkgfpVRCCIVVKHLGRAElGMGDStsqsPPIK 271
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPG----VRHRLVLDGDGELE-GFVGY----AEAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 272 RSCPDVQISwnqgidlwwhelmqeagDECEPewcdaeDPLfiLYTSGSTGKPKGVV----HTVGGYMLYVATTFKYVFDF 347
Cdd:PRK13391 143 AGLPATPIA-----------------DESLG------TDM--LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 348 HAEDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFG 420
Cdd:PRK13391 198 RSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMFSRMLKLP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 421 DEPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgaqrCPIVDTFWQTETGGhmltplpGATPM-------KPG 487
Cdd:PRK13391 266 EEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-------GFTACdseewlaHPG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 488 SATFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTVYGNHER-FEttYFK----------KFPGYYVTGDGCQ 555
Cdd:PRK13391 329 TVGRAMFGD-LHILDDDG--------------AELPpGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGY 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 556 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQI 635
Cdd:PRK13391 392 VDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFC 471
|
570 580 590
....*....|....*....|....*....|...
gi 8923896 636 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13391 472 RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-667 |
1.48e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 110.75 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGF 194
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 SSESLCERIL----DSSCSLLITtdafyrgeklvnLKELADEAlqkcqekgfPVRCCIVVkhlgraeLGMGDSTSQSPPI 270
Cdd:cd12117 78 DPELPAERLAfmlaDAGAKVLLT------------DRSLAGRA---------GGLEVAVV-------IDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 271 KRSCpdvqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVfDFHAE 350
Cdd:cd12117 130 AVPV-------------------------------SPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 351 DVFWCTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK-FYTAPTaIRLLMKFGDEpvtkhSR 429
Cdd:cd12117 177 DRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQLADEDPE-----CF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 430 ASLQVLGTVGEPINPEawlWYHRVVgaQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGSatfPFFGVAPAIL 501
Cdd:cd12117 249 AGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---PIANTRVYVL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 502 NesgeelegeaegylVFKQPWP------------GIMRTvYGNH-----ERFETTYFkkFPG--YYVTGDGCQRDQDGYY 562
Cdd:cd12117 321 D--------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYRTGDLARWLPDGRL 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 563 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSPkltEELKKQIREKIGPI 642
Cdd:cd12117 384 EFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDA---AELRAFLRERLPAY 458
|
570 580
....*....|....*....|....*
gi 8923896 643 ATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12117 459 MVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
118-667 |
1.55e-25 |
|
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: 110.83 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 118 GDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 198 SLCERILDSSCSLLITT-DAFYRGEKLVNLKELADEALqkcqeKGFPVrccivvkhlgraelgmgdstsqSPPIKRSCPD 276
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL-----AAPPA----------------------TPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 277 vqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK----------- 342
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDEYPlgpgdrvlqkt 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 343 -YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFE----GIPTYpdvnrLWSIVDKYKVTKFYTAPTAIRLlm 417
Cdd:cd17646 187 pLSFDVSVWELFW-----------------PLVAGARLVVARpgghRDPAY-----LAALIREHGVTTCHFVPSMLRV-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 418 kFGDEPvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET----------GGHMLTPLPGATPMkPG 487
Cdd:cd17646 243 -FLAEP-AAGSCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV-PN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 488 SATFpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPGYYVTGD 552
Cdd:cd17646 317 TRLY----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLgrpaltaERFVPDPFGPGSRMYRTGD 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 553 GCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsPKLTEELK 632
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAA--GPDTAALR 453
|
570 580 590
....*....|....*....|....*....|....*
gi 8923896 633 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17646 454 AHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-669 |
2.15e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.02 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAfyrgekLVNLKELADEALqkcqekgfPVRCCIVVkhlgraelgMGDSTsqsppikrscpdvq 278
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIV--------PLLSTVVV---------AGGSS-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 iswnQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvggYMLYVATTFKYVFDFHA---EDVFWC 355
Cdd:PRK07786 149 ----DDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLRTNGAdinSDVGFV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 356 TADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSR 429
Cdd:PRK07786 222 GVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC---AEQQARPRD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 430 ASLQVLGTVGEPiNPEAWL--WYHRVVGAQrcpIVDTFWQTEtgghmLTPLpgaTPM--------KPGSATFPFFGVAPA 499
Cdd:PRK07786 290 LALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKLGSVGKVIPTVAAR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 500 ILNESGEELEGEAEGYLVFKQPwpGIMRTVYGN----HERFETtyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK07786 358 VVDENMNDVPVGEVGEIVYRAP--TLMSGYWNNpeatAEAFAG-------GWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLT-EELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDAL 505
|
570
....*....|....*
gi 8923896 655 PKTRSGKIMRRVLRK 669
Cdd:PRK07786 506 PRNPAGKVLKTELRE 520
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
131-601 |
2.21e-25 |
|
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: 109.99 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESlCERIL-DSSCS 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlww 289
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 helmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGHSYVT 369
Cdd:cd05907 87 ------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 370 YGPLANGATSVLFEGIPTYPD------------VNRLWSIVdkYKVTKFYTAPTAIRLLMKFgdepvtkHSRASLQVLGT 437
Cdd:cd05907 148 YVPLLAGARIYFASSAETLLDdlsevrptvflaVPRVWEKV--YAAIKVKAVPGLKRKLFDL-------AVGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 438 VGEPINPEAWLWYHrvvgAQRCPIVDTFWQTETGG-HMLTPLPGATPMKPGSATFPF-FGVAPA--ILNESgeelegeae 513
Cdd:cd05907 219 GGAPLPAELLHFFR----ALGIPVYEGYGLTETSAvVTLNPPGDNRIGTVGKPLPGVeVRIADDgeILVRG--------- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 514 gylvfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML-NVSGHLLSTAEVESALVEHE 592
Cdd:cd05907 286 ---------PNVMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASP 354
|
....*....
gi 8923896 593 AVAEAAVVG 601
Cdd:cd05907 355 LISQAVVIG 363
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
130-667 |
2.32e-25 |
|
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: 110.29 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 130 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERI-LDSSC 208
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 209 SLLITTDAF-YRGEKLVNLKELAdealqkcqekgfpvrccivvkhLGrAELGMGDSTSQSPPIkrscpdvqiswnqgidl 287
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLA----------------------LS-DLVGLGEPESAGPLI----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 288 wwhelmqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITG 364
Cdd:cd05923 143 -------------EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 365 HSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPInP 444
Cdd:cd05923 208 FFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATM-P 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 445 EAWLwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsatfpFFG---VAPaILNESGEELEGEAEGYLVFKQ 520
Cdd:cd05923 281 DAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEALANGEEGELIVAA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 521 P----WPGIMRtvygnheRFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 596
Cdd:cd05923 353 AadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTE 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 597 AAVVGHPHPVKGECLYCFVTLCDGhtfspKLTEELKKQ--IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05923 426 VVVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
308-668 |
3.33e-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: 109.38 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 308 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPT 387
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 388 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPINPE-AWLWyhrvvGAQRCPIVDTFW 466
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRW-----LKAPVRLFNAYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 467 QTETgghMLTPL--PGATPMKPGSATFP----FFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETTY 540
Cdd:cd17649 245 PTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVGVTGELYIGGE--GLAR---GYLGRPELTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 541 fKKF-------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECL 611
Cdd:cd17649 317 -ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 612 YCFVTLCDGHTfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd17649 395 VAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
309-669 |
3.44e-25 |
|
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: 109.30 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 388
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 389 PDVNRLWSIVDKYKVTKFYTAPTA-IRLL--MKFGDEPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhRVVGAQR 458
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyYEAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 459 cpIVDTFWQTETGGHMLTPLPGatPMKPGSATFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFE 537
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP--SVFKEYWNKPEATK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 538 ttyfKKFP--GYYVTGDGCQRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 614
Cdd:cd05941 314 ----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 615 VTLCDGHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05941 390 VVLRAGAA--ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
137-671 |
9.21e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 109.09 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 216
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 FYRGEKLVNLKELADEAlqkcqekgfpvrccivvkhlgrAELGMGDSTSQSPPIKRSCPDVQISWNQGIdLWWHELmQEA 296
Cdd:PRK12583 127 FKTSDYHAMLQELLPGL----------------------AEGQPGALACERLPELRGVVSLAPAPPPGF-LAWHEL-QAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 297 GDECEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTV--GGYMLYVAttfkyvFDFHAEDVFWCTADIGWITG 364
Cdd:PRK12583 183 GETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHDRLCVPVPLYHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 365 HSYVTYGPLANGATsVLFEGIPTYPDVNrlWSIVDKYKVTKFYTAPTairLLMKFGDEPvtKHSRASLQVLGT---VGEP 441
Cdd:PRK12583 257 MVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--QRGNFDLSSLRTgimAGAP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 442 INPEAwlwYHRVVGAQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSATF----PFFGVApaILNESGEELEGEAEGY 515
Cdd:PRK12583 329 CPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVDPDGATVPRGEIGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 516 LVFKqpwpG--IMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK12583 402 LCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8923896 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK12583 476 VADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
289-668 |
1.03e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 108.96 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 289 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgyMLYV---ATTFKYvfDFHAEDVFWCTADIGwitgH 365
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 366 S---YVTYGP-LANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQV-LGT 437
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 438 VGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSATFPFFGVApaILNESGEelegeaegy 515
Cdd:PRK13388 274 EASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA--IYNPETL--------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 516 lvfkQPWPgimRTVYGNH-----------ERFETTYFKKFPGYYV---------------TGDGCQRDQDGYYWITGRID 569
Cdd:PRK13388 331 ----TECA---VARFDAHgallnadeaigELVNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 570 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPIATPDYI 648
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYV 481
|
410 420
....*....|....*....|
gi 8923896 649 QNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13388 482 RIAADLPSTATNKVLKRELI 501
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-668 |
2.33e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 107.30 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAfyrgeklvnLKELADEALQKCQekgfpvrccivvkhLGRAELGMGDSTsqsPPIKRSCPDvqiswnqgidlwwh 290
Cdd:PRK08276 87 LIVSAA---------LADTAAELAAELP--------------AGVPLLLVVAGP---VPGFRSYEE-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ELMQEAGDECEPEWCDAEdplfILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHAEDVFWCTADIGwi 362
Cdd:PRK08276 127 ALAAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGPDSVYLSPAPLY-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 363 tgHSYVT-YG--PLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVG 439
Cdd:PRK08276 198 --HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 440 EPINPE------AWlWyhrvvGaqrcPIVD-TFWQTETGGHMLtplpgATP----MKPGSATFPFFGVApAILNESGEEL 508
Cdd:PRK08276 272 APCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSedwlAHPGSVGKAVLGEV-RILDEDGNEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 509 EGEAEGYLVFKQPWPGImrTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLnVSGHL-LSTAEVESA 587
Cdd:PRK08276 336 PPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVnIYPQEIENL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 588 LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08276 411 LVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
.
gi 8923896 668 R 668
Cdd:PRK08276 491 R 491
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-667 |
2.34e-24 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 106.63 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhe 291
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 lmqeagdecepewcDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTF------------KYVFDFHAEDVFwct 356
Cdd:cd12115 103 --------------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSICFDLSVFELF--- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 357 adigwitghsyvtyGPLANGATSVLFEGIPTYPDVNRLwsivdkYKVTKFYTAPTAIRLLMKFGDEPvtkhsrASLQVLG 436
Cdd:cd12115 166 --------------GPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP------ASVRVVN 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TVGEPINPEAWLWYHRVVGAQRC-----PIVDTFWQTetgGHMLTPLPGATPmkpgSATFPFFGVAPAILNEsgeelege 511
Cdd:cd12115 220 LAGEPLPRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYVLDR-------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 512 aegylvFKQPWP------------GIMRTVYGN----HERFETTYFkkFPG--YYVTGDGCQRDQDGYYWITGRIDDMLN 573
Cdd:cd12115 285 ------ALQPVPlgvpgelyiggaGVARGYLGRpgltAERFLPDPF--GPGarLYRTGDLVRWRPDGLLEFLGRADNQVK 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:cd12115 357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433
|
570
....*....|....
gi 8923896 654 LPKTRSGKIMRRVL 667
Cdd:cd12115 434 LPLTPNGKIDRSAL 447
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
288-669 |
3.61e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.07 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 288 WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG-----GYMLyvATTFkyvfDFHAEDVFWCTADI--- 359
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 360 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKF--------YTAPTAIR-------LL 416
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPERpddadnpLR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 417 MKFGDEpvtkhsraslqvlgtvGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTEtGGHMLTPLPGaTPmkPGSATFPFF 494
Cdd:PRK07867 271 IVYGNE----------------GAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 GVA-----------PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHErfeTTYFKKFPGYYVTGDGCQRDQDGYYW 563
Cdd:PRK07867 323 GVAivdpdtgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAY 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 564 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPI 642
Cdd:PRK07867 399 FAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPK 476
|
410 420
....*....|....*....|....*..
gi 8923896 643 ATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-672 |
4.88e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 106.75 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAFyRGEKLVN-LKELADEALQkcqekgfPVRCCIVVkhlgraelgmgDSTSQSPPikrscPDVQISWNQGIDLWW 289
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATP-----APAPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 HELMQEAGDECEPewcdaEDPLFILY-TSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 368
Cdd:PRK06164 167 PAPPAAAGERAAD-----PDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TyGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkHSRASLQVLGTVGepINPeAWL 448
Cdd:PRK06164 241 L-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFGFAS--FAP-ALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 WYHRVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEgylvf 518
Cdd:PRK06164 310 ELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRA----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 519 kqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK06164 385 ----PSLMRGYLDNPD--ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 599 VVGHPHPVKGEClYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG---KIMRRVLRKIAQ 672
Cdd:PRK06164 459 VVGATRDGKTVP-VAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ 531
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-605 |
6.47e-24 |
|
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: 108.02 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsivfA------GFSSESLcERIL- 204
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 205 DSSCSLLITTDAFyrgeklvnLKELADEALQkcqekgfpvrcCIVVKHLGRAElgmgdsTSQSPPIKRSCPDvqiswnqg 284
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLALDALALAA------EPATNPPVPVTPD-------- 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 285 idlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK------------YVFDFHA 349
Cdd:COG1020 618 ------------------------DLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRRYGlgpgdrvlqfasLSFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 350 EDVFWctadigwitghsyvtygPLANGATSVLF--EGIptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVtkh 427
Cdd:COG1020 674 WEIFG-----------------ALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLRALLDAAPEAL--- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 428 srASLQVLGTVGEPINPEAWLWYHRVVGAQR---------CPIVDTFWQTETGGHMLTPLP-GaTPMkPGSATFpffgva 497
Cdd:COG1020 731 --PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiG-RPI-ANTRVY------ 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 498 paILNEsgeelegeaegylvFKQPWP-GIM-------------------RTVygnhERFETTYFkKFPG--YYVTGDGCQ 555
Cdd:COG1020 801 --VLDA--------------HLQPVPvGVPgelyiggaglargylnrpeLTA----ERFVADPF-GFPGarLYRTGDLAR 859
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 8923896 556 RDQDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:COG1020 860 WLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
107-602 |
1.19e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 105.95 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 107 VLDRNVheKKLGDKVAFYWEGNepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 187 HSIVFAGfSSESLCERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--ALQKcqekgfpvrccIVVkhlgraelgMgds 263
Cdd:COG1022 92 TVPIYPT-SSAEEVAYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV---------L--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 264 tsqSPPIKRSCPDVqiswnqgidLWWHELMQEAGDECEPEW-------CDAEDPLFILYTSGSTGKPKGVVHTVGGyMLY 336
Cdd:COG1022 144 ---DPRGLRDDPRL---------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 337 VATTFKYVFDFHAEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGIPTYPD------------VNRLW-SIV 398
Cdd:COG1022 211 NARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkptfmlaVPRVWeKVY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 399 DKYkVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQvlgtvGEPINPEAWLWY---HRVVGAQrcpivdtfWQTETGGHML 475
Cdd:COG1022 285 AGI-QAKAEEAGGLKRKLFRWALAVGRRYARARLA-----GKSPSLLLRLKHalaDKLVFSK--------LREALGGRLR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 476 TPLPGATPMKPgsATFPFF---GV------------APAILNESGEelegeaegylvFK-----QPWPG----------- 524
Cdd:COG1022 351 FAVSGGAALGP--ELARFFralGIpvlegygltetsPVITVNRPGD-----------NRigtvgPPLPGvevkiaedgei 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 525 ------IMRTVYGNHErfETTyfKKFP--GYYVTGD-GcQRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAV 594
Cdd:COG1022 418 lvrgpnVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLI 492
|
....*...
gi 8923896 595 AEAAVVGH 602
Cdd:COG1022 493 EQAVVVGD 500
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
133-669 |
2.47e-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: 103.92 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 133 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSLLI 212
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI-AFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 213 TTDAFYRGEKLVNlkeladealqkcqekgfpvrccivvkhlgraelgMGDSTsqsppikrscpdvqiswnqgidlwwhEL 292
Cdd:cd12118 106 FVDREFEYEDLLA----------------------------------EGDPD--------------------------FE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 MQEAGDECepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLyVATTFKYVFDFHAEDVFWCTADI----GWItghsyV 368
Cdd:cd12118 126 WIPPADEW--------DPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC-----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TYGPLANGATSVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWL 448
Cdd:cd12118 192 PWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPAAVL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 WYHRVVGAQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSATFPffGVAPAILNESGEELEGEAEGYLVFKQ------P 521
Cdd:cd12118 265 AKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmkpvP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WPG------------IMRTVYGNHERFETTyFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:cd12118 334 RDGktigeivfrgniVMKGYLKNPEATAEA-FRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRK 669
Cdd:cd12118 411 KHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
134-667 |
8.59e-23 |
|
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: 102.41 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 134 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsIVFAGFSseslcerildsscsllit 213
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 tdafYRGEKLVNLKELADEALqkcqekgfpvrcCIVvkhlgraelgmgdstsqsppikrscPDVqiswNQGIDlwWHELM 293
Cdd:cd05920 99 ----HRRSELSAFCAHAEAVA------------YIV-------------------------PDR----HAGFD--HRALA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 QEAGDECEpewcdaeDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGwitgHSYVTYGP- 372
Cdd:cd05920 132 RELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPLACPg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 373 ----LANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAwl 448
Cdd:cd05920 200 vlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPAL-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 wYHRVVGAQRCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSAtfpffgvapailnes 504
Cdd:cd05920 272 -ARRVPPVLGCTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEE--------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 505 geelegeaeGYLVFKQPWP--GIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd05920 336 ---------GELLTRGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 583 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSPKLTEELKKQIREKigPIAT---PDYIQNAPGLPKTRS 659
Cdd:cd05920 401 EVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPDRIEFVDSLPLTAV 474
|
....*...
gi 8923896 660 GKIMRRVL 667
Cdd:cd05920 475 GKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-670 |
1.80e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 101.48 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALhSIVFagfsseslcerildsscs 209
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 llittdafyrgeklvNLKELADEALQKCQEKGFPVRCCivVKHLGRAELGMGDSTSQSPPIKRSCPDvqiswnqgidlww 289
Cdd:PRK06839 84 ---------------NIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVISITSLK------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 hELMQEAGDECEPEwcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVT 369
Cdd:PRK06839 134 -EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 370 YGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTKFYTAPT---AIRLLMKFgdepvTKHSRASLQVLGTVGEPInPEA 446
Cdd:PRK06839 210 FPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVRWFYNGGAPC-PEE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 WLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIM 526
Cdd:PRK06839 280 LM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 527 RTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:PRK06839 355 KEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVK 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 607 KGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK06839 432 WGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
117-670 |
3.80e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 100.99 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 117 LGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 196
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 197 ESLcERILDSSCSLLITTDAFYRgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPD 276
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEAALL------------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 277 VQISwnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTvggymlyvattfkyvfdfHAEDVFW-- 354
Cdd:PRK06155 175 AAVQ--------------------------PGDTAAILYTSGTTGPSKGVCCP------------------HAQFYWWgr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 355 -CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfg 420
Cdd:PRK06155 211 nSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLS-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 421 dEPVTKHSRAS-LQVLGTVGEPINpeawlwYHRVVGAqRC--PIVDTFWQTETGGHMLTPLPGAtpmKPGSATFPFFGVA 497
Cdd:PRK06155 285 -QPARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 498 PAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNH-----ERFETTYFKkfpgyyvTGDGCQRDQDGYYWITGRIDDML 572
Cdd:PRK06155 354 ARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMpektvEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK06155 427 RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVA 503
|
570
....*....|....*...
gi 8923896 653 GLPKTRSGKIMRRVLRKI 670
Cdd:PRK06155 504 ALPKTENGKVQKFVLREQ 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-667 |
7.53e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAFyrGEKLvnlkeladealqkcqekgfPVRCCIVVKHLGRAELGMgDSTSQSPPIKRSCPdvqiswnqgidlwwh 290
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRPAAWL-EGYSEENPGTELNP--------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 elmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHT------------------VGGYMLYVaTTFKyvFDFHAEDV 352
Cdd:PRK12316 655 -----------------ENLAYVIYTSGSTGKPKGAGNRhralsnrlcwmqqayglgVGDTVLQK-TPFS--FDVSVWEF 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 353 FWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkhSRAS 431
Cdd:PRK12316 715 FW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTS 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 432 LQVLGTVGEPINPEAWLwyhRVVG-AQRCPIVDTFWQTETGghmlTPLPGATPMKPGSATF----PFFGVAPAILNESGe 506
Cdd:PRK12316 772 LRRIVCSGEALPADAQE---QVFAkLPQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPIANLACYILDANL- 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 507 elegeaegylvfkQPWP------------GIMRTVYG----NHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDD 570
Cdd:PRK12316 844 -------------EPVPvgvlgelylagrGLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDH 910
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQN 650
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAASLPEYMVPAQWLA 983
|
570
....*....|....*..
gi 8923896 651 APGLPKTRSGKIMRRVL 667
Cdd:PRK12316 984 LERLPLTPNGKLDRKAL 1000
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
132-670 |
9.83e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 96.53 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTDAFyrgeklvnlkelaDEALQKCQEKgfpvrccivvkhLGRAeLGMGDSTSQSPPIKRSCPDVQiswnqgidlwwhE 291
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPPD------------LGRL-RAWGGNPDDDEPSGSTDETLD------------D 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 LMQEAGDECEPEWcdAEDPLFILYTSGSTGKPKGVVH-------TVGGYMLYVAttfkyvfdFHAEDVFWCTADIGWITG 364
Cdd:PRK07788 193 LIAGSSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGETTLLPAPMFHATG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 365 HSYVTYGpLANGATSVL---FEGIPTYPDVnrlwsivDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:PRK07788 263 WAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 442 INPEAWLWYHRVVGaqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSATFPFFGVAPAILNESGeelegeaegyl 516
Cdd:PRK07788 335 LSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENG----------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 517 vfkQPWPG--IMRTVYGNHERFETtYF-----KKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PRK07788 395 ---NEVPRgvVGRIFVGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07788 471 GHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
.
gi 8923896 670 I 670
Cdd:PRK07788 548 M 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
136-668 |
1.49e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 95.98 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFyrgeklvnlKELADEALQKCqekgfpvrccivvkhlgraelgmgdstsqsPPIKRScpdvqISWNQGIDLWWHELMQE 295
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI-----VAWTDEDHDLTVEVLIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 AGDECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-VGGYMlyvatTFKYVFDfhaedvfwctaDIGWITGHSYVTYGPL- 373
Cdd:PRK13382 185 AHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD-----------RTPWRAEEPTVIVAPMf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 374 -ANGATSVLFEGIPTYPDVNR-------LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPE 445
Cdd:PRK13382 248 hAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 446 AWLWYHRVVGAQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSATFPFFGVAPAILNESgeelegeaegylvFKQP 521
Cdd:PRK13382 328 VVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD-------------FREV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WPGIMRTVY-GNHERFE-----TTyfKKF-PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:PRK13382 387 PTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 595 AEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13382 465 AEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
309-664 |
3.54e-20 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 92.08 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDvfwctadigwitghSYVTYGPLA-----NGATSVLF 382
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIeSFVCN--EDLFNISGED--------------AILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 383 EG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKhsrasLQVLGTVGEPINPEAwlwyHRVVGAQ- 457
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 458 -RCPIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHERF 536
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 537 ETTY----FKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLY 612
Cdd:cd17633 195 FSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IA 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 8923896 613 CFVTLCDGHTFsPKLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17633 274 VALYSGDKLTY-KQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
309-671 |
3.94e-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: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 388
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 389 PDVNRlwsivdkYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGAQRCPIVDTFWQT 468
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 469 ETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHERFETTYFKKfPGYY 548
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 549 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspklT 628
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 8923896 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
152-673 |
9.47e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 93.51 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 152 LRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgEKLVNLKelAD 231
Cdd:PLN02246 67 LHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV--DKLKGLA--ED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 232 EALQKCQEKGFPVRCcivvkhLGRAELGMGDSTsqsppikrSCPDVQISwnqgidlwwhelmqeagdecepewcdAEDPL 311
Cdd:PLN02246 143 DGVTVVTIDDPPEGC------LHFSELTQADEN--------ELPEVEIS--------------------------PDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 312 FILYTSGSTGKPKGVVHTVGGYMLYVAttfKYV------FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegI 385
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI---M 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 386 PTYpDVNRLWSIVDKYKVTkfyTAPTAIRLLMKFGDEP-VTKHSRASLQVLGTVGEPINPEawlwYHRVVGAqRCP---I 461
Cdd:PLN02246 257 PKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKE----LEDAFRA-KLPnavL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 462 VDTFWQTETGGHMLTPLPGA---TPMKPGSAtfpffgvAPAILNESGEELEGEAEGYLVFKQP------WPGIMRTVYGN 532
Cdd:PLN02246 328 GQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELKIVDPETGASLPRNQPgeicirGPQIMKGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 533 HERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 612
Cdd:PLN02246 401 PEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPV 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8923896 613 CFVTLCDGHTFSpklTEELK----KQI--REKIGPIATPDYIqnapglPKTRSGKIMRRVLR-KIAQN 673
Cdd:PLN02246 479 AFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI------PKAPSGKILRKDLRaKLAAG 537
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
313-668 |
1.02e-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: 92.83 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 313 ILYTSGSTGKPKGVVHTVGGYMLYVAT--TFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 390
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 391 VNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgaqrcPIVDTFW 466
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 467 Q-TETGGhmLTPLPGATPMK-PGSATFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY--GN-----HERFE 537
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGpgfeyTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 538 TTYFKKFPGYYVT-GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05929 341 KTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 8923896 617 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
524-668 |
1.67e-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: 90.41 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 603
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 604 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
132-665 |
1.95e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.26 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsIVFAgfsseslceriLDSScslL 211
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTDAFYRGEKLVNLKELADeALQKCQEKGFPVRCCIVVKHLGRAElGMGDSTSQSPPIKRSCPDVQISWNQGIdlwwhe 291
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGGDS-GPSGGTLSVHLDAATEPTPATSTPEGL------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 lmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGymlyVATTFKYV---FDFHAEDVfwCTADIGWITGHSYV 368
Cdd:PRK05852 175 ---------------RPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--TVAVMPLYHGHGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 T--YGPLANGATSVLfegiptyPDVNRL-----WSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:PRK05852 234 AalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 442 INPEAWLWYHRVVGAqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSATFPFFGVA--------PAILNes 504
Cdd:PRK05852 307 LTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgsdglplpAGAVG-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 505 geelegeaegylvfkQPW---PGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:PRK05852 382 ---------------EVWlrgTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 582 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK05852 444 ERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520
|
....
gi 8923896 662 IMRR 665
Cdd:PRK05852 521 LDRR 524
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
129-668 |
8.01e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.07 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 129 EPGEttQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSC 208
Cdd:PRK13390 20 ETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 209 SLLITTDAfyrgeklvnLKELADEAlqkcqekGFPVrccivvkhlgraelgmgdstsqsppikrscpDVQISWNQGIDLW 288
Cdd:PRK13390 98 RVLVASAA---------LDGLAAKV-------GADL-------------------------------PLRLSFGGEIDGF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 289 --WHELMQEAGDECEPEWCDAedplFILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHAEDVFWCTAD 358
Cdd:PRK13390 131 gsFEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 359 IGwitgHSyvtyGPL-------ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRAS 431
Cdd:PRK13390 204 IY----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 432 LQVLGTVGEPINPEA------WLWyhrvvgaqrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSATFPFFGVA------- 497
Cdd:PRK13390 272 LRAVIHAAAPCPVDVkhamidWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDLhicdddg 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 498 ---PAilnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTYFKK-----------FPGYYVTGDGCQRDQDGYYW 563
Cdd:PRK13390 341 nelPA------------------------GRIGTVYFERDRLPFRYLNDpektaaaqhpaHPFWTTVGDLGSVDEDGYLY 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 564 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIA 643
Cdd:PRK13390 397 LADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYK 476
|
570 580
....*....|....*....|....*
gi 8923896 644 TPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13390 477 APRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
137-669 |
9.29e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 90.19 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsSCSLLITtda 216
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV--------------------SVPLLPS--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 fYRGEKLVnlkeladEALQKCQEKGF--PVR------------CCIVVKHLGRA-----------ELGMGDSTSQSPPIK 271
Cdd:PRK06087 108 -WREAELV-------WVLNKCQAKMFfaPTLfkqtrpvdlilpLQNQLPQLQQIvgvdklapatsSLSLSQIIADYEPLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 272 RSCPdvqiswnqgidlwwhelmqeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAED 351
Cdd:PRK06087 180 TAIT-----------------------------THGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 352 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPtyPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraS 431
Cdd:PRK06087 230 VFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT--PD--ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--A 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 432 LQVLGTVGEPInPEawlwyhRVVgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGE 506
Cdd:PRK06087 304 LRFFLCGGTTI-PK------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 507 ELEGEAEGYLVFKQPwpGIMRTVYGNHERfeTTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 586
Cdd:PRK06087 375 TLPPGCEGEEASRGP--NVFMGYLDEPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVED 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK06087 451 ILLQHPKIHDACVVAMPDERLGERSCAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFL 529
|
...
gi 8923896 667 LRK 669
Cdd:PRK06087 530 LRK 532
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
113-668 |
1.94e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 89.17 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 113 HEKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFA 192
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 193 GFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKcqekgfpvrccivvkhlgraelgmgDSTSQSPPikr 272
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQA-------------------------DSRRLAQG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 273 scpdvqiswnqgidlwwhelmqeaGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTVGgymlyvattfkyvfdfhaeD 351
Cdd:PRK06145 137 ------------------------GLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------N 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 352 VFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLM 417
Cdd:PRK06145 174 LHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 418 KFGDEpvTKHSRASLQVLGTVGEPiNPEAWLW-YHRVVGAQRcpIVDTFWQTET-GGHMLTPlPGATPMKPGSATFPFFG 495
Cdd:PRK06145 254 TVPDR--DRFDLDSLAWCIGGGEK-TPESRIRdFTRVFTRAR--YIDAYGLTETcSGDTLME-AGREIEKIGSTGRALAH 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 496 VAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK06145 328 VEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDELP 479
|
570
....*....|...
gi 8923896 656 KTRSGKIMRRVLR 668
Cdd:PRK06145 480 RNPSGKVLKRVLR 492
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
132-673 |
2.47e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 88.68 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITtDAFYrgeklvnLKELADEalqKCqekgfPVrccivvkhlgraelgmgdstsqsppikrscpdvqISWNQgidlwWHE 291
Cdd:PRK07638 102 VT-ERYK-------LNDLPDE---EG-----RV----------------------------------IEIDE-----WKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 LMQEAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMlyvattfkYVFDFHAEDVFWCTADIGWITG---HSY 367
Cdd:PRK07638 127 MIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMKREDSVLIAGtlvHSL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 368 VTYGplangATSVLFEG-----IPTYPDVNRLWSIvDKYKVTKFYTAPTAIRLLMK---FGDEPVT------KHSRASLQ 433
Cdd:PRK07638 198 FLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKMKiissgaKWEAEAKE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 434 VLGTvgepINPEAWLWyhrvvgaqrcpivdTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeae 513
Cdd:PRK07638 272 KIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAG-------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 514 gylvfKQPWPGIMRTVYGNHERFETTY------FKKFP--GYYVTGD-GCQrDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:PRK07638 326 -----EEVQKGEIGTVYVKSPQFFMGYiiggvlARELNadGWMTVRDvGYE-DEEGFIYIVGREKNMILFGGINIFPEEI 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 585 ESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSpkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:PRK07638 400 ESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
....*....
gi 8923896 665 RVLRKIAQN 673
Cdd:PRK07638 473 MEAKSWIEN 481
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
115-667 |
2.73e-18 |
|
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: 88.54 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFYWEGNepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 194
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 SSESLcERIL-DSSCSLLITTDAFYRGEKlvnlkeladealqkcqekgfpvrccivvkHLGRAELgMGDSTSQSppikrs 273
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQSHLQPPIA-----------------------------FIGLIDL-LDEDTIYH------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 274 cpdvqiswnqgidlwwhelmqEAGDECEPEwCDAEDPLFILYTSGSTGKPKGV----------VHTVGGYM-----LYVA 338
Cdd:cd17655 125 ---------------------EESENLEPV-SKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWANKVIyqgehLRVA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 339 TTFKYVFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMK 418
Cdd:cd17655 183 LFASISFDASVTEIF-----------------ASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITIIDLTPAHLKLLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 419 FGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGAqrCPIVDTFWQTETG-GHMLTPLpgaTPMKPGSATFPffgV 496
Cdd:cd17655 245 ADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSVP---I 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 497 APAILNESGeelegeaegYLVFK--QPWP------------GIMRTvYGNHErfETTYfKKF------PG--YYVTGDGC 554
Cdd:cd17655 312 GKPLGNTRI---------YILDQygRPQPvgvagelyiggeGVARG-YLNRP--ELTA-EKFvddpfvPGerMYRTGDLA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 555 QRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdghTFSPKLT-EELKK 633
Cdd:cd17655 379 RWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI------VSEKELPvAQLRE 452
|
570 580 590
....*....|....*....|....*....|....
gi 8923896 634 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17655 453 FLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
306-667 |
3.23e-18 |
|
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: 87.91 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV-------HTVGGY------------MLYVATtfkYVFDFHAEDvfWCTAdigwitghs 366
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD--FARS--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 367 yvtygpLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 444
Cdd:cd17650 157 ------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 445 EAWLwYHRVvgAQRCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegyl 516
Cdd:cd17650 228 FKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL----------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 517 vfkQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:cd17650 289 ---QPQPvgvagelyiggaGVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 581 TAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdgHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA----ATLN---TAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
410
....*....|
gi 8923896 658 RSGKIMRRVL 667
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
306-671 |
6.91e-18 |
|
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: 87.39 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGI 385
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 386 PTYPdvNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepVTKHSRASLQVLGTVGEPINPEAW-LWYHRvvgaQRCPIVDT 464
Cdd:cd05909 223 PLDY--KKIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDTLRqEFQEK----FGIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 465 FWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHERFETTYFKkf 544
Cdd:cd05909 293 YGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEPELTSFAFGD-- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 545 pGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVGHPHPVKGECLYCFVTlcdGHTF 623
Cdd:cd05909 369 -GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTT---TTDT 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 8923896 624 SPkltEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05909 445 DP---SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
132-674 |
1.06e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.92 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LH---------SIVFagfsseslce 201
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 202 rILDSSCS-LLITTDAFyrgeklvnlKELADEALQKCQekgfpvRCCIVVKHLGRAELGMGDSTSqsppikrscpdvqis 280
Cdd:PRK08162 110 -MLRHGEAkVLIVDTEF---------AEVAREALALLP------GPKPLVIDVDDPEYPGGRFIG--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 281 wnqgiDLWWHELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTVGGYMLYVATTFKYVFDFHAE-----DVF 353
Cdd:PRK08162 159 -----ALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGMPKHPVylwtlPMF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 354 WCTadiGWitGHSY-VTygplANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgdepvtkHSRASL 432
Cdd:PRK08162 234 HCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI---------NAPAEW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 433 QvlgtvgEPINpeawlwyHRVVG--AQRCPIVDTFWQTETGGHMLTPLPGATPM---------KPGSATFPFF------- 494
Cdd:PRK08162 292 R------AGID-------HPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvcawQPEWDALPLDeraqlka 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 --GV------APAILNESGEELEgeaegylvfkqPWPG-----IMrtVYGN-------------HERFETtyfkkfpGYY 548
Cdd:PRK08162 359 rqGVryplqeGVTVLDPDTMQPV-----------PADGetigeIM--FRGNivmkgylknpkatEEAFAG-------GWF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 549 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPklt 628
Cdd:PRK08162 419 HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE--- 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 8923896 629 EELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 674
Cdd:PRK08162 496 EEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
546-668 |
1.98e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 86.26 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 625
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8923896 626 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
135-669 |
4.70e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 84.79 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCErildsscsllitt 214
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAY------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 dafyrgeklvnlkeladeALQKCQEKGFPVRCcivvKHLGRAElgmgDSTSQSPPIKRScPDVQISWNQgidlwWHELMQ 294
Cdd:cd05915 91 ------------------ILNHAEDKVLLFDP----NLLPLVE----AIRGELKTVQHF-VVMDEKAPE-----GYLAYE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 EAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHT-VGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVtYGP 372
Cdd:cd05915 139 EALGEEADpVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 373 LANGATSVLFEGIPTypDVNRLWSIVdKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPinPEAWL---- 448
Cdd:cd05915 218 TLVGAKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRSLIarfe 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 -WYHRVVGAQRCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05915 292 rMGVEVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05915 367 GPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 602 HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKqireKIGPIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05915 445 IPHPKWQERPLAVVVPRGEKPTPEELNEHLLK----AGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
135-667 |
5.16e-17 |
|
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: 84.24 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 213
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 TDafyrgeklvnlkeladEALQKCQekgfPVRCCIVVkhlgraeLGMGDSTSQSPPIKRSCPDvqiswnqgidlwwhelm 293
Cdd:cd12114 91 DG----------------PDAQLDV----AVFDVLIL-------DLDALAAPAPPPPVDVAPD----------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 qeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV--------------FDFHAEDVFwctad 358
Cdd:cd12114 127 ---------------DLAYVIFTSGSTGTPKGVMISHRAALNTILdINRRFAvgpddrvlalsslsFDLSVYDIF----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 359 igwitghsyvtyGPLANGATSVLfegiPTY---PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF-GDEPVTKHS-R---- 429
Cdd:cd12114 187 ------------GALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVlEAAQALLPSlRlvll 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 430 ----------ASLQVLGTVGEPIN----PEAWLW--YHRVVGA---------------QRCPIVDTfwqtetgghMLTPL 478
Cdd:cd12114 251 sgdwipldlpARLRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP---------RGRDC 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 479 PGatpmkpgsatfpffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFETTYFKKFPG--YYVTGD- 552
Cdd:cd12114 322 PD--------------WVPGEL---------------------WiggRGVALGYLGDPELTAARFVTHPDGerLYRTGDl 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 553 GCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTfsPKLTEELK 632
Cdd:cd12114 367 GRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGT--PIAPDALR 442
|
570 580 590
....*....|....*....|....*....|....*
gi 8923896 633 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12114 443 AFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-672 |
5.69e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 84.90 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTDAFYrgeklvnlkELADEALQ---KCQEKGFPVRCCIVVkhlgraelgmGDSTSQSPPIKRSCPDVQISWnqgidlw 288
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKilaEKKKSSFKPPLLIVI----------GDPTCDPKSLQYALGKGAIEY------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 289 whELMQEAGDecePE--WCDAED---PLFILYTSGSTGKPKGVV-HTVGGYMLyvATTFKYVFDFHAEDVFWCTADIGWI 362
Cdd:PLN02479 176 --EKFLETGD---PEfaWKPPADewqSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYLWTLPMFHC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 363 TGHSYvTYGPLANGATSVLFEGIPTypdvNRLWSIVDKYKVTKFYTAPTAIRLL------------------MKFGDEP- 423
Cdd:PLN02479 249 NGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhvMTAGAAPp 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 424 ---VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------RVVGAQRCPIVDTfwqtetgghmltpl 478
Cdd:PLN02479 324 psvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT-------------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 479 pgaTPMKPGSATFPFFGVAPAILNesgeelegeaegyLVFKqpwpGIMRTVYGNHERFETtyfkkfpGYYVTGDGCQRDQ 558
Cdd:PLN02479 390 ---KTMKPVPADGKTMGEIVMRGN-------------MVMK----GYLKNPKANEEAFAN-------GWFHSGDLGVKHP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 559 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS--PKLTEELKKQIR 636
Cdd:PLN02479 443 DGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALAEDIMKFCR 522
|
570 580 590
....*....|....*....|....*....|....*.
gi 8923896 637 EKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN02479 523 ERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
107-669 |
5.72e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.93 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 107 VLDRNVHekKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 187 HSIVFAGFSSESL--CERILDSscSLLITtdafyrGEKLVNLKELADEALQKcqekgfPVRCCIVVKHLGRAELGMGD-- 262
Cdd:PRK08279 114 VALLNTQQRGAVLahSLNLVDA--KHLIV------GEELVEAFEEARADLAR------PPRLWVAGGDTLDDPEGYEDla 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 263 --STSQSPPIKRSCPDVQiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtT 340
Cdd:PRK08279 180 aaAAGAPTTNPASRSGVT----------------------------AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-G 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 341 FKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYtaptAI---- 413
Cdd:PRK08279 231 FGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRATAFQ----YIgelc 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 414 RLLMkfgDEPVTKHSRA-SLQVLgtVGEPINPEAW--------------LW--------------YHRVVGaqRCP---- 460
Cdd:PRK08279 300 RYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFDGTVG--RVPlwla 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 461 ----IVDtfWQTETGghmlTPLPGA----TPMKPGSAtfpffGVAPAILNEsgeelegeaegylvfKQPWPG-------- 524
Cdd:PRK08279 373 hpyaIVK--YDVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD---------------RGPFDGytdpease 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 525 --IMRTVygnherfettyFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML-----NVsghllSTAEVESALVEHEAVAEA 597
Cdd:PRK08279 427 kkILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEEA 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 598 AVVGHPHP-VKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK08279 491 VVYGVEVPgTDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
7.69e-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: 7.69e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8923896 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCpgpflRYNFDVTKGkIFIEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
306-672 |
7.85e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 7.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV--HTvGGYMLYVATTFKY---VFDFH--AEDVFWCTadiGWItghsyVTYGPLANGAT 378
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWemgTCPVYlwTLPMFHCN---GWT-----FTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 379 SVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGAQr 458
Cdd:PLN03102 255 SVCMRHV-TAPEI---YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 459 cpIVDTFWQTETGGHML--------TPLPGATPMK-PGSATFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGI 525
Cdd:PLN03102 327 --VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 526 MRTvYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:PLN03102 403 MKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923896 606 VKGECLYCFVTLCDGHTFSPKLTEELK-------KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN03102 480 TWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
290-670 |
9.05e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 HELMQEAGDEC-EPEWC-----DAEDPLFILYTSGSTGKPKGVVHTVGG-----------YMLYVATT----FKYVFDFH 348
Cdd:PRK12467 3213 TALTLDRLDLNgYSENNpstrvMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGA 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 349 AEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDepvtKHS 428
Cdd:PRK12467 3293 QERFLW-----------------TLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG----GAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 429 RASLQVLGTVGEPINPEAWLWYHRVV---------GAQRCPIVDTFWQTETGGhmlTPLPGATPMKPGSAtfpffGVAPA 499
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIY 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 500 ILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYY 562
Cdd:PRK12467 3422 VLDGQL--------------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVI 3487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 563 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSPKLTEELKKQIREKIgpi 642
Cdd:PRK12467 3488 EYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL--- 3560
|
410 420 430
....*....|....*....|....*....|...
gi 8923896 643 atPDYIQNA-----PGLPKTRSGKIMRRVLRKI 670
Cdd:PRK12467 3561 --PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-670 |
1.06e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 83.74 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITt 214
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 dafyrgeklvnlkelADEALQKCQEKGFPVrccivvkhLGRAELGMGDSTSQSPPIkrscpdvqiswnqgidlwWHELMQ 294
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV--------IGVPENYDFDSKRIEFPK------------------FYELIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 EAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA----EDVFWCTADIGWITGHSYVTY 370
Cdd:PLN02574 185 EDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYGLSLFVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 371 GPLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PLN02574 265 GLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDF 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 hrvvgAQRCPIVDtFWQtetgGHMLTPLPGATPMKPGSATFPFFG----VAPAILNESGEELEGEAEGYLVFKQPW---P 523
Cdd:PLN02574 340 -----VQTLPHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSsvglLAPNMQAKVVDWSTGCLLPPGNCGELWiqgP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 603
Cdd:PLN02574 410 GVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVP 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923896 604 HPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PLN02574 488 DKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
308-664 |
1.64e-16 |
|
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: 81.54 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 308 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 387
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 388 YpdvNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHRVvgaqrcPI 461
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLT------NT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 462 VDTFWQTETGGHMLTPLpGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFETTYF 541
Cdd:cd17635 146 AQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 542 KkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgh 621
Cdd:cd17635 223 D---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA---- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 8923896 622 tfSPKLTEE----LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17635 296 --SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
135-673 |
1.74e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 83.12 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAGFS---SEsLCERILDSSCSLL 211
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFShqrSE-LNAYASQIEPALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTdafyRGEKLVNLKELADEALQKCQekgfpvRCCIVVKHlgraelgmGDSTSQSppikrscpdvqiswnqgIDLWwhe 291
Cdd:PRK10946 125 IAD----RQHALFSDDDFLNTLVAEHS------SLRVVLLL--------NDDGEHS-----------------LDDA--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 292 lMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTADigwiTGHSYVTYG 371
Cdd:PRK10946 167 -INHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP----AAHNYPMSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 PlanGATSVLFEG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP--- 444
Cdd:PRK10946 241 P---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSEtla 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 445 ------------------EAWLWYHR-------VVGAQRCPIV--DTFWQTETGGHmltPLPGATP---MKPGSATFPff 494
Cdd:PRK10946 318 rripaelgcqlqqvfgmaEGLVNYTRlddsderIFTTQGRPMSpdDEVWVADADGN---PLPQGEVgrlMTRGPYTFR-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 gvapailnesgeelegeaegylvfkqpwpGIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNV 574
Cdd:PRK10946 393 -----------------------------GYYKSPQHNASAFDAN------GFYCSGDLVSIDPDGYITVVGREKDQINR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtfSPKLTEELKKQIREK-IGPIATPDYIQNA 651
Cdd:PRK10946 438 GGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK-------EPLKAVQLRRFLREQgIAEFKLPDRVECV 510
|
570 580
....*....|....*....|..
gi 8923896 652 PGLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK10946 511 DSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-668 |
2.07e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 83.16 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 107 VLDRNVHEKKLGDKVAFYwegnepgETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 187 HSIVFAGFSSESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADEAlqkcqekgfpvrccivvkhlgrAELGMGDS 263
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA----------------------ARVAPGGY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 264 tsqsppikrscpdvqiswnqgidlwwhelmqeagdecEPEWCDAEdpLFILYTSGSTGKPKGVVHTVggymlyvATTFKY 343
Cdd:PRK06060 140 -------------------------------------EPMGGDAL--AYATYTSGTTGPPKAAIHRH-------ADPLTF 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 344 VFDFHAEDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVNRLWSIvdKYKVTKFYTAPTAIRLL 416
Cdd:PRK06060 174 VDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAILSA--RFGPSVLYGVPNFFARV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 417 MkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrCPIVDTFWQTETGGHMLTPlpGATPMKPGS--ATFPFF 494
Cdd:PRK06060 251 I----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTlgRVLPPY 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 495 GVAPAILNESGEELEGEAEGYLvfkqPWPGIMRTVYGNHERFETTyfkkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNV 574
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWV----RGPAIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:PRK06060 394 GGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRL 473
|
570
....*....|....
gi 8923896 655 PKTRSGKIMRRVLR 668
Cdd:PRK06060 474 PRTPNGKLVRGALR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-675 |
2.09e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITtdafyrgeklvnlkelaDEALQKCQEKGFPVRCcivvkhlgrAELGMGDSTSQSPPIKrscpdvq 278
Cdd:PRK12316 3146 LAYMLEDSGAQLLLS-----------------QSHLRLPLAQGVQVLD---------LDRGDENYAEANPAIR------- 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 iswnqgidlwwhelmqeagdecepewCDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV------ 344
Cdd:PRK12316 3193 --------------------------TMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVlqfttf 3246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 345 -FDFHAEDVFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgdEP 423
Cdd:PRK12316 3247 sFDVFVEELFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EE 3304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 424 VTKHSRASLQVLGTVGEPINPEAwlwYHRVVGAQrcPIVDTFWQTETgghmlTPLPGATPMKPGSATFPFFGVAPAILNE 503
Cdd:PRK12316 3305 EDAHRCTSLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRAC 3374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 504 SGEELEGEAEGYLVFKQPWPGIMRTVYGNH-------ERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 576
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLGGEGLARGYHnrpgltaERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRG 3454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 577 HLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIgpiatPDYIQNA----- 651
Cdd:PRK12316 3455 FRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllfl 3522
|
570 580
....*....|....*....|....*...
gi 8923896 652 PGLPKTRSGKIMRRVLRK----IAQNDH 675
Cdd:PRK12316 3523 ERMPLTPNGKLDRKALPRpdaaLLQQDY 3550
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
308-670 |
2.33e-16 |
|
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: 82.57 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 308 EDPLFILYTSGSTGKPKGVVHT--------------VGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITGhsyvtygpl 373
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 374 anGATSVLfegIPTYPDVNRLWSIVDkYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrv 453
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 454 VGAQ-----RCPIV-DTFWQTETGGHML-TPlpgATPMKPGSA--TFPFFGvAPAILNESGEELEGEAEGYLVFKQpwPG 524
Cdd:cd17642 317 VGEAvakrfKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVgkVVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 525 IMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd17642 391 IMKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 605 PVKGECLYCFVTLCDGHTFSPKLTEEL-------KKQIRekiGPIATPDYIqnapglPKTRSGKIMRRVLRKI 670
Cdd:cd17642 469 EDAGELPAAVVVLEAGKTMTEKEVMDYvasqvstAKRLR---GGVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
117-661 |
2.77e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 82.24 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 117 LGDKVAFYWeGNEpgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 196
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 197 ESLCERILDSSCSLLITTDAFyrGEKLVNLKEladeALQKcqekgfpVRCCIVVkhlgraelgmGDSTSQSPPikrscpd 276
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLL------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 277 vqiswNQGIDlwWHELMQEAGDECEPEWCDAEDpLFILYTSGSTGKPKGVVHT--------VGGYMLYVATTFKYVFDfH 348
Cdd:PRK07798 140 -----PGAVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRqedifrvlLGGRDFATGEPIEDEEE-L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 349 AEDVFWCTADIGWITG---H---SYVTYGPLANGATSVLfegiptYP----DVNRLWSIVDKYKVTkfytaptairLLMK 418
Cdd:PRK07798 211 AKRAAAGPGMRRFPAPplmHgagQWAAFAALFSGQTVVL------LPdvrfDADEVWRTIEREKVN----------VITI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 419 FGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWLWY--HRVvgaqrcpIVDTFWQTETG-GHMLTPLPGAT 482
Cdd:PRK07798 275 VGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALLELlpNVV-------LTDSIGSSETGfGGSGTVAKGAV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 483 PmkPGSATF---PFFGVAPAILNEsgeelegeaegyLVFKQPWPG-IMRT------VYGNHERFETTyFKKFPG--YYVT 550
Cdd:PRK07798 348 H--TGGPRFtigPRTVVLDEDGNP------------VEPGSGEIGwIARRghiplgYYKDPEKTAET-FPTIDGvrYAIP 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 551 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEE 630
Cdd:PRK07798 413 GDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AE 489
|
570 580 590
....*....|....*....|....*....|.
gi 8923896 631 LKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK07798 490 LRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-667 |
5.81e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 81.59 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 133 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVfagfsSESLCERILDSSCslli 212
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA-----DGNLPIAAIERFC---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 213 ttdafyrgeklvnlkELADEAlqkcqekgfpvrcCIVVKHlgraelGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHEL 292
Cdd:PRK05857 110 ---------------QITDPA-------------AALVAP------GSKMASSAVPEALHSIPVIAVDIAAVTRESEHSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 mQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVvhtvggymLYVATTFKYVFD-FHAEDVFWctadIGWITGHSyvTYG 371
Cdd:PRK05857 156 -DAASLAGNADQ-GSEDPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW----VTWVVGET--TYS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 372 PLAngATSV---------LFEG---IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL---MKFGDEPVtkhsrASLQVLG 436
Cdd:PRK05857 220 PLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANATV-----PSLRLVG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TVG-EPINPEAwlwyhRVVGAQRCPIVDTFWQTETGGHMLTpLP----GATPMKPGSATFPFFGV----APAILNESGEE 507
Cdd:PRK05857 293 YGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdvylAATDGIGPTAP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 508 LEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:PRK05857 367 GAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 588 LVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfspklTEELKKQI----REKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:PRK05857 444 AEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSG 518
|
....*..
gi 8923896 661 KIMRRVL 667
Cdd:PRK05857 519 KVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-669 |
1.48e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 AFYrgEKLVNLKELADEALQKcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgiDLWWHELMQE 295
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLDR-------------------------------------------------DAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 AgdecePEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYMLYVATTFKY---------------VFDFHAEDVFWctadi 359
Cdd:PRK12316 2138 A-----PAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyelspadcelqfmsfSFDGAHEQWFH----- 2207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 360 gwitghsyvtygPLANGATSVLFEGipTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTVG 439
Cdd:PRK12316 2208 ------------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDGRPPAVRVYCFGG 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 440 EPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSATFPFFGVAPA-----ILNESGEELEGEAE 513
Cdd:PRK12316 2271 EAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayILDADLNLLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 514 GYLVFKQPwpGIMRTVYG----NHERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK12316 2346 GELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARL 2423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 589 VEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK12316 2424 QAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAEDLL---AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP 2499
|
.
gi 8923896 669 K 669
Cdd:PRK12316 2500 K 2500
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-671 |
4.67e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 78.77 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFYWEGnepgetTQITYHQLLVQVCQF-SNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 193
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 194 FSSESLCERILDSSCSLLITTDAFYRGEKLVnlkeLADEALQKCQEK------GFPVRCCI--VVKHlgraelgmgdsts 265
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 266 qsppIKRSCPDVQISwnqGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVvhtvggyMLYVATTFKYVF 345
Cdd:PRK08751 173 ----VKKLVPEYRIN---GAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGA-------MLTHRNLVANMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 346 DFHAedvfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGiptypdVNRLWS-------IVDKYKVTKFyTAP 410
Cdd:PRK08751 239 QAHQ----WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGG------CNHLISnprdmpgFVKELKKTRF-TAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 411 TAIRLLM-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETgghmlTPLPGATPMK--- 485
Cdd:PRK08751 308 TGVNTLFnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTET-----SPAACINPLTlke 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 486 -PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWI 564
Cdd:PRK08751 380 yNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 565 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPKLT-EELKKQIREKIGPIA 643
Cdd:PRK08751 456 VDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANLTGYK 530
|
570 580
....*....|....*....|....*...
gi 8923896 644 TPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08751 531 QPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
131-606 |
6.78e-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: 77.89 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSScsl 210
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTI-RYVLEHS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 littdafyrGEKLVNLKELADEALQKCQEKGFPVRCcivvkhlgraelgmgdstSQSPPikrSCPDVQISWNQGIDLwwH 290
Cdd:cd05932 78 ---------ESKALFVGKLDDWKAMAPGVPEGLISI------------------SLPPP---SAANCQYQWDDLIAQ--H 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ELMQEAGDEcepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMlYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05932 126 PPLEERPTR------FPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 371 GPLANGATSVLFEGIPTYPD------------VNRLWS-----IVDKYKVTKfytaptaIRLLMK--FGDEPVTKHSRAS 431
Cdd:cd05932 199 GSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWTkfqqgVQDKIPQQK-------LNLLLKipVVNSLVKRKVLKG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 432 L-----QVLGTVGEPINPEAWLWYHRVvgaqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSATFPFFGVAPAIlnesge 506
Cdd:cd05932 272 LgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI------ 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 507 elegEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS-GHLLSTAEVE 585
Cdd:cd05932 340 ----SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIE 411
|
490 500
....*....|....*....|...
gi 8923896 586 SALVEHEAVAEAAVVGH--PHPV 606
Cdd:cd05932 412 NKLAEHDRVEMVCVIGSglPAPL 434
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
309-664 |
8.30e-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: 76.15 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 309 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 388
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 389 pDVNRLWSIVDKYKVTKFYT-APTAIRLLMKFGDEPVtkhSRASLQVLGTVGEPINPEAWlwyHRVVGAqrcpivdTFW- 466
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 467 ---QTETGGhMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWpgimrtvyGNHERFE 537
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYW--------NLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 538 TTyFKKfpGYYVTGDGCQRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 615
Cdd:cd17637 211 YT-FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 8923896 616 TLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17637 288 VLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-669 |
8.38e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.85 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 214
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 DAFYrgEKLVNLKELADEALQKCQE-KGFPvrccivvkhlgraelgmgdstSQSPPIKrscpdvqiswnqgidlwwhelm 293
Cdd:PRK12316 4656 SHLL--QRLPIPDGLASLALDRDEDwEGFP---------------------AHDPAVR---------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 qeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTfkyvfdfhaEDVFWCTADIGWITGHSYV----- 368
Cdd:PRK12316 4691 -----------LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgsh 4750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 --TYGPLANGAtSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGtvGEPINPEA 446
Cdd:PRK12316 4751 egLYHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 447 W-LWY--------HRVVGAQRCPIVDTFWQTETGghmltPLPGATPMKPGSatfPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:PRK12316 4826 YdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 518 FKQpwPGIMRtvyGNH-------ERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK12316 4898 LGG--EGVAR---GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 589 VEHEAVAEAAVVGHPHPVkGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTR 658
Cdd:PRK12316 4972 REHPAVREAVVIAQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERL-----PEYMVPAhlvflARMPLTP 5045
|
570
....*....|.
gi 8923896 659 SGKIMRRVLRK 669
Cdd:PRK12316 5046 NGKLDRKALPQ 5056
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
546-669 |
9.63e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.48 E-value: 9.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8923896 626 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-669 |
1.25e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 215
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 216 afyrgeklvnlkeladealQKCQEKGFPVrcCIVVKHLGRAELGmgDSTSQSPPIKrscPDVQIswnqgidlwwhelmqe 295
Cdd:PRK12467 616 -------------------QSHLLAQLPV--PAGLRSLCLDEPA--DLLCGYSGHN---PEVAL---------------- 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 296 agdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHsYVTYGPLAN 375
Cdd:PRK12467 654 ----------DPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALAS 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 376 GATsVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGtvGEpINPEAWLWYHRVVG 455
Cdd:PRK12467 722 GAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GE-ALQVDLLARVRALG 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 456 AQrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF--PFFGVAPAILNEsgeelegeaegYLvfkQPWP---------- 523
Cdd:PRK12467 796 PG-ARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDH-----------YL---NPVPvgvvgelyig 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 --GIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:PRK12467 861 gaGLARGYHRrpalTAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVR 939
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8923896 596 EAAVVGHPHPVKGECL-YCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK12467 940 EAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
546-668 |
1.41e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.98 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 625
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----P 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8923896 626 KLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07059 510 ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
115-668 |
3.64e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 75.96 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFywegNEPGETtqITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 193
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 194 FSSESLCERILDSSCSLLITtdafyrgekLVNLKELADEALQKCQekgfpvrccivVKHLGRAELGmgdstSQSPPIKRS 273
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 274 CPDVQISWNQGIDLWWH---------ELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---VGGYMLYVATTF 341
Cdd:PRK05677 164 LINAVVKHVKKMVPAYHlpqavkfndALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQCRALM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 342 K-------------------YVFDFHaedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVNRLWSIVDKYK 402
Cdd:PRK05677 244 GsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKELGKWK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 403 VTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETgghmlTPLPGAT 482
Cdd:PRK05677 301 FSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 483 PMK---PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQD 559
Cdd:PRK05677 371 PSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIALIQED 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 560 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKI 639
Cdd:PRK05677 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANL 523
|
570 580
....*....|....*....|....*....
gi 8923896 640 GPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK05677 524 TGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
141-668 |
3.70e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 75.51 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 141 LLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFyrg 220
Cdd:PRK12406 17 LAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 221 eklvnLKELADEALQKCQEKGFPvrccivvkhlgraelgmgdstsqSPPikrscpdvQISWNQGIDLwwHELMQEAGDEC 300
Cdd:PRK12406 94 -----LHGLASALPAGVTVLSVP-----------------------TPP--------EIAAAYRISP--ALLTPPAGAID 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 301 EPEWCDAEDPL---------FILYTSGSTGKPKGVVHTVG------GYMLYVATTFkyvfdfhaedvfwctadiGWITGH 365
Cdd:PRK12406 136 WEGWLAQQEPYdgppvpqpqSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRALIY------------------GLKPGI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 366 SYVTYGPLANGATSV-------LFEGIPTYP--DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQvlg 436
Cdd:PRK12406 198 RALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLR--- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 tvgepinpeawlwyHRVVGAQRCP--------------IVDTFWQTETGGhmltpLPGATP----MKPGSATFPFFGVAP 498
Cdd:PRK12406 275 --------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGA-----VTFATSedalSHPGTVGKAAPGAEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 499 AILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHL 578
Cdd:PRK12406 336 RFVDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVN 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 579 LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:PRK12406 412 IYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPRED 488
|
570
....*....|
gi 8923896 659 SGKIMRRVLR 668
Cdd:PRK12406 489 SGKIFKRRLR 498
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
546-664 |
3.79e-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: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsp 625
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT--- 291
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 8923896 626 kLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17638 292 -LTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
307-667 |
3.80e-14 |
|
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: 74.98 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 307 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIP 386
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 387 TYPDvNRLWSIVDKYKVTkFYTAPTAIRLLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyhrvvgAQRCPIVDTF 465
Cdd:cd17652 170 LLPG-EPLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------APGRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 466 WQTET--GGHMLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTvYG 531
Cdd:cd17652 235 GPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpgvpgelyiagaGLARG-YL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 532 NH-----ERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd17652 297 NRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDD 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 605 PVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17652 376 RPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
129-668 |
5.10e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 75.30 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 129 EPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVF----AGFSSESLCERIL 204
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 205 DSSCSLLITTDAfyrgeklvnlkelADEALQKcqekgfpvrccIVVKHLGRAELGMGDSTSQSPPikrscpdvqiswnqg 284
Cdd:PRK07514 98 DAEPALVVCDPA-------------NFAWLSK-----------IAAAAGAPHVETLDADGTGSLL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 285 idlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITG 364
Cdd:PRK07514 139 ------EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLIHALPIFHTHG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 365 HSYVTYGPLANGA------------------TSVLFEGIPTypdvnrlwsivdkykvtkFYTaptaiRLLmkfgDEP--- 423
Cdd:PRK07514 212 LFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT-----RLL----QEPrlt 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 424 --VTKHSRasLQVLGTVgePINPE---AWlwyhrvvgAQRC--PIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGV 496
Cdd:PRK07514 265 reAAAHMR--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 497 APAILNESGEELEGEAEGYL-------VFKQPW--PgimrtvygnherfETTY--FKKfPGYYVTGDGCQRDQDGYYWIT 565
Cdd:PRK07514 331 SLRVTDPETGAELPPGEIGMievkgpnVFKGYWrmP-------------EKTAeeFRA-DGFFITGDLGKIDERGYVHIV 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 566 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATP 645
Cdd:PRK07514 397 GRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAALKGRLARFKQP 473
|
570 580
....*....|....*....|...
gi 8923896 646 DYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07514 474 KRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
308-667 |
8.57e-14 |
|
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: 74.39 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 308 EDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAEDVF--WCTadigwitghsyvty 370
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIYvtLLS-------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 371 gplanGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:cd17644 172 -----GATLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQW 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 HRVVGaQRCPIVDTFWQTE----TGGHMLTPLPGATPMKPGSATfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GI 525
Cdd:cd17644 245 QKNVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPVPvGV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 526 MRTVY--------G-------NHERFETTYFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:cd17644 309 PGELHiggvglarGylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVL 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 589 VEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-669 |
1.43e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.86 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYwegnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSS-- 196
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPta 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 197 -ESLCERILDSSCSLLITTDAFYRGEklvnlkeladealqkcqekgfpvrccivVKHLGRAELGMGDStsqsppikrsCP 275
Cdd:PLN02330 115 lESEIKKQAEAAGAKLIVTNDTNYGK----------------------------VKGLGLPVIVLGEE----------KI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 276 DVQISWNQGIDLwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT--------------VGGYMLYVATTF 341
Cdd:PLN02330 157 EGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLThrnlvanlcsslfsVGPEMIGQVVTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 342 KYVFDFHaedvfwctadIGWITGHSYVTygpLANGATSVLfegiptypdVNR--LWSIVDKYKVTKFYTAPTAIRLLMKF 419
Cdd:PLN02330 232 GLIPFFH----------IYGITGICCAT---LRNKGKVVV---------MSRfeLRTFLNALITQEVSFAPIVPPIILNL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 420 GDEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGAQrcpIVDTFWQTETGGHMLT---PLPGATPMKPGSATFP 492
Cdd:PLN02330 290 VKNPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 493 FFGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWI 564
Cdd:PLN02330 367 LPNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 565 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtfSPKLT---EELKKQIREKIGP 641
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI------NPKAKeseEDILNFVAANVAH 509
|
570 580
....*....|....*....|....*...
gi 8923896 642 IATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02330 510 YKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
131-669 |
1.63e-13 |
|
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: 73.11 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSS-CS 209
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlww 289
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 290 helmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATT---------------FKYVFDFHAEDVFW 354
Cdd:cd17653 104 -----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDACIGEIFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 355 CtadigwitghsyvtygpLANGATSVLFEGIPTYPDVNRlwsivdkyKVTKFYTAPTAIRLLmkfgdepvtkhSRASLQV 434
Cdd:cd17653 167 T-----------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL-----------SPQDFPN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 435 LGTV---GEPINP---EAWlWYHRVV----GAQRCPIVDTFWQTETGghmlTPLPGATPMkPGSATFpffgvapaILNES 504
Cdd:cd17653 211 LKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY--------ILDAD 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 505 geelegeaegylvfKQPWP------------GIMRTVYGNHERfETTYFKKFPGY-----YVTGDGCQRDQDGYYWITGR 567
Cdd:cd17653 277 --------------LQPVPegvvgeicisgvQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGR 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 568 IDDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTlcdghtfsPKL--TEELKKQIREKIGPIAT 644
Cdd:cd17653 342 EDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT--------PETvdVDGLRSELAKHLPSYAV 408
|
570 580
....*....|....*....|....*
gi 8923896 645 PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd17653 409 PDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
546-671 |
4.80e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.16 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 625
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----P 515
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 8923896 626 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK12492 516 GLSvEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
546-668 |
2.89e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.25 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 624
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8923896 625 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
550-671 |
3.16e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.45 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 550 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltE 629
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 8923896 630 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-667 |
3.37e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.58 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLitt 214
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL--- 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 dafyrgeklvnlkeLADEALQkcqekgfpvrccivvkhlgrAELGMGDStsqsppikrscpdVQISWNQGIDLWWhelmq 294
Cdd:PRK12467 1676 --------------LTQSHLQ--------------------ARLPLPDG-------------LRSLVLDQEDDWL----- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 EAGDECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDVfwctadigWITGHSYV---- 368
Cdd:PRK12467 1704 EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAfdvs 1773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 ---TYGPLANGAtSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKHSraSLQVLGTVGEPINPE 445
Cdd:PRK12467 1774 vweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SLRRVVCGGEALEVE 1849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 446 AW-LWYHRVVGAQrcpIVDTFWQTETGGHML------------TPLPGATPMkPGSATFpffgVAPAILNEsgeelegea 512
Cdd:PRK12467 1850 ALrPWLERLPDTG---LFNLYGPTETAVDVThwtcrrkdlegrDSVPIGQPI-ANLSTY----ILDASLNP--------- 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 513 egylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSG 576
Cdd:PRK12467 1913 -------VP-IGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRG 1984
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 577 HLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA 651
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYMVPA 2058
|
570 580
....*....|....*....|.
gi 8923896 652 -----PGLPKTRSGKIMRRVL 667
Cdd:PRK12467 2059 hlvflARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
306-673 |
6.27e-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: 68.34 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKY-----VFDF--HAEDVfwCTADIgwitghsyvtYGPLAN 375
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 376 GATSVlfegIPTYPD-VNRLWSIVDKYKVTkfyTA---PTAIRLLmkfgdEPVTKhsrASLQVLGTVGEPINPEAW-LWY 450
Cdd:cd05918 172 GGCLC----IPSEEDrLNDLAGFINRLRVT---WAfltPSVARLL-----DPEDV---PSLRTLVLGGEALTQSDVdTWA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 HRV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsatfpffgVA 497
Cdd:cd05918 237 DRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI-----------LA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 498 PAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHERFettyfkkfpgyYVTGDGCQRDQDG--YYwiTGRIDDMLNVS 575
Cdd:cd05918 305 RGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQVKIR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSPKLTEELKKQIREKIGPIAT-------- 644
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRALVAelrsklrq 443
|
410 420 430
....*....|....*....|....*....|....*.
gi 8923896 645 --PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 673
Cdd:cd05918 444 rlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
291-669 |
9.20e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.29 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ELMQEAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVvhTVGGYMLYVATTFKYVFDFHAE-DVFWCTADIGWITGHSYV 368
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIVGYGEdDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 tygpLAN---GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL----GTVGEP 441
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 442 INPEAWLWYhrvvgaQRCPIVDTFWQTETGGHMltplpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSL-------TFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 ---------------------WPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PLN02860 371 phvelkigldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 581 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLT-----------EELKKQIREK-IGPIATPD-Y 647
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlF 528
|
410 420
....*....|....*....|..
gi 8923896 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02860 529 VQWRKPFPLTTTGKIRRDEVRR 550
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
134-667 |
1.31e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.15 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 134 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLI 212
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 213 TTDAFyrGEKLVNLKELadEALQKCQEkgfpvrccivvkhlgraelgmgDSTSQSPPIKRSCPDvqiswnqgidlwwhel 292
Cdd:PRK10252 561 TTADQ--LPRFADVPDL--TSLCYNAP----------------------LAPQGAAPLQLSQPH---------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 mqeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HT-VGGYMLYVATTFKyvfdFHAEDVFW----CTADIG----- 360
Cdd:PRK10252 599 ----------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqktpCSFDVSvweff 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 361 WitghsyvtygPLANGATSVLFEgiptyPDVNR----LWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLG 436
Cdd:PRK10252 659 W----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASLTPEGARQSCASLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 437 TV---GEPINPEAWLWYHRVVGAqrcPIVDTFWQTE---------TGGHMLTPLPGAtPMKPGsatFPFFGVAPAILNES 504
Cdd:PRK10252 721 QVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGS-SVPIG---YPVWNTGLRILDAR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 505 GeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKkfPG--YYVTGDGCQRDQDGYYWITG 566
Cdd:PRK10252 794 M--------------RPVPpGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA--PGerMYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 567 RIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLCDGhtfSPKLTEELKKQIREKIG 640
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSG---LPLDTSALQAQLRERLP 934
|
570 580
....*....|....*....|....*..
gi 8923896 641 PIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-667 |
3.19e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAFYRGeklvnLKELADEALQKCQEKGFPVRccivvkhlgraelgmgDSTSQSPPIKRSCPDVQIswnqgidlwwh 290
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 elmqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDvfwCTADIGWIT--GHSYV 368
Cdd:PRK05691 2337 ---------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASER 2391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TYGPLANGATSVL-FEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdePVTKHSRASLQVLGTVGEPINPEAW 447
Cdd:PRK05691 2392 LLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRMCITGGEALTGEHL 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 448 LWYHRVVGAQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSATFPFFGVAPA----ILNESGEELEGEAEGYLvfkqp 521
Cdd:PRK05691 2466 QRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALVPQGATGEL----- 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 522 WPGIMRTVYGNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK05691 2536 YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA 2615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPK--LTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRV 666
Cdd:PRK05691 2616 VREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQaaLREALKAHLKQQL-----PDYMVPAhlillDSLPLTANGKLDRRA 2690
|
.
gi 8923896 667 L 667
Cdd:PRK05691 2691 L 2691
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
545-675 |
3.43e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.79 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 545 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFs 624
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 8923896 625 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 675
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
132-667 |
4.82e-11 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 65.57 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERI----LDSS 207
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGG----AFVPIDPEYPEERRiyimLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 208 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppiKRSCPDvQISWNQGIDL 287
Cdd:cd17656 86 VRVVLT---------------------------------------------------------QRHLKS-KLSFNKSTIL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 288 W-WHELMQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFW---CTADIGWIT 363
Cdd:cd17656 108 LeDPSISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQfatCSFDVCYQE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 364 GHSYVTYGplanGATSVLFEgiPTYPDVNRLWSIVDKYKVTKFYTaPTAIrLLMKFGDEPVTKHSRASLQVLGTVGEPI- 442
Cdd:cd17656 187 IFSTLLSG----GTLYIIRE--ETKRDVEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREFINRFPTCVKHIITAGEQLv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 443 --NPeawlwYHRVVGAQRCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSATFPFfgvapaILNESgeelege 511
Cdd:cd17656 259 itNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ILDQE------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 512 aegylvfKQPWP-GIMRTVY--------GNHERFETTYFKKFPG-------YYVTGDGCQRDQDGYYWITGRIDDMLNVS 575
Cdd:cd17656 319 -------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQLPEYMIPSFFVPLDQLP 466
|
570
....*....|..
gi 8923896 656 KTRSGKIMRRVL 667
Cdd:cd17656 467 LTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
131-374 |
6.89e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 65.52 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITtdafyrGEKlvNLKELAD--EALQkcqekgfpvrcciVVKHLgraeLGMGDSTSQSPPIKRSCPDVQISWNQGIDlw 288
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDSSLSGSSNWTVSSFSEVE-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 289 whELMQEAgdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVfwctadigwitghsYV 368
Cdd:PLN02387 235 --KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YL 296
|
....*.
gi 8923896 369 TYGPLA 374
Cdd:PLN02387 297 AYLPLA 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-667 |
7.39e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.96 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGNepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK05691 1146 ERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 LCERILDSSCSLLITTDAFYrgEKLVNLKELADEALQKCQEKGFPVrccivvkhlgraelgmgdstsqSPPikrscpdvq 278
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIALDSLHLDSWPS----------------------QAP--------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 279 iswnqGIDLWWHELMqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYVFDfhAEDVFWCTA 357
Cdd:PRK05691 1267 -----GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNTHAALAERLQwMQATYALD--DSDVLMQKA 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 358 DIGWITGhSYVTYGPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRaSLQVLGT 437
Cdd:PRK05691 1322 PISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPLAAACT-SLRRLFS 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 438 VGEPINPE---------AWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLpgatpmkpGSatfPFFGVAPAILNESGEEL 508
Cdd:PRK05691 1396 GGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR---PLGNVLCRVLDAELNLL 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 509 EGEAEGYLVFKQpwPGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:PRK05691 1465 PPGVAGELCIGG--AGLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPE 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 583 EVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA-----PGLPKT 657
Cdd:PRK05691 1542 EIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAEL-----PEYMVPAqlirlDQMPLG 1612
|
570
....*....|
gi 8923896 658 RSGKIMRRVL 667
Cdd:PRK05691 1613 PSGKLDRRAL 1622
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
308-661 |
7.75e-11 |
|
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: 64.33 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 308 EDPLFILYTSGSTGKPKGVV---HTVGGYMLYVA--TTFKYVFDFHAEDVFWCTADIGW------ITGHSYVTYGPLANG 376
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGAdfGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 377 ATSVLFEGIPTYPDvnRLWSIVDKYKVTKF------YTAPTaIRLLMKFGDEPVTkhsraSLQVLGTVGEPINPEawlwy 450
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 hrvVGAQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSATFPFFGVAPAILNESgeelegeaegyLVFKQPWPG 524
Cdd:cd05924 150 ---VKQGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 525 IMRTV----------YGNHERFETTyFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:cd05924 213 GVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923896 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:cd05924 292 AVYDVLVVGRPDERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
132-382 |
8.09e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.38 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 212 ITTdafyrGEKLVNLkeladeaLQKCQEKGFPvRCCIVvkHLGraelgmgdstsqSPPIKRSCPDVQ-ISWNQGIDLWWH 290
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD------------SLPASVDTEGCRlVAWTDVVAKGHS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ELMQEAGDECEpewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaeDVFWCTADigwitGHSYVTY 370
Cdd:PTZ00216 251 AGSHHPLNIPE----NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLN-----DLIGPPEE-----DETYCSY 316
|
250
....*....|....*.
gi 8923896 371 GPLAN----GATSVLF 382
Cdd:PTZ00216 317 LPLAHimefGVTNIFL 332
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-669 |
8.54e-11 |
|
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: 64.75 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 133 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 212
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 213 TtdafyrgeklvNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdsTSQSPPikrSCPDVqiswnqgidlwwhel 292
Cdd:cd05939 81 F-----------NLLDPLLTQ------------------------------SSTEPP---SQDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 mqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIgWITGHSYVTYGP 372
Cdd:cd05939 102 -------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL-YHSAGGIMGVGQ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 373 -LANGATSVLFEGIptypDVNRLWSIVDKYKVTKF-YTAPTAIRLLMKFGDEPVTKHsraslQVLGTVGEPINPEAWlwy 450
Cdd:cd05939 167 aLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLAVGNGLRPQIW--- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 HRVVGAQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSATF-PFFG--VAPAIL---NESGEELEGEAEGYLVFKQPW-P 523
Cdd:cd05939 235 EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRDSDGLCIPCQPGeP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 GIM----------RTVYG------NHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:cd05939 311 GLLvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 588 LVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSPKLTEELKkqirekigPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd05939 391 LSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKL 462
|
....*..
gi 8923896 663 MRRVLRK 669
Cdd:cd05939 463 QKTDLQK 469
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
137-669 |
9.21e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 64.76 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLIT 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 TDafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelm 293
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 294 qeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGgyMLYV-ATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGP 372
Cdd:cd05937 87 --------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 373 LANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRaslqVLGTVGEPINPEAWLW 449
Cdd:cd05937 151 LMSGGTLALsrkFS-------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRVAWGNGLRPDIWER 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 450 YHRVVGAqrcPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsatfpfFGvAPAILNESGEELEGEAEGYLVFK------QPW 522
Cdd:cd05937 220 FRERFNV---PEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQVVLVKmdpetdDPI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 523 ---------------PG--IMRTVYGNHERFETTY--------------FKKFPGYYVTGDGCQRDQDGYYWITGRIDDM 571
Cdd:cd05937 284 rdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTF-SPKLTEELKKQIREKIGPIATPDY 647
Cdd:cd05937 364 FRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVpTEFTKSLLASLARKNLPSYAVPLF 441
|
570 580
....*....|....*....|..
gi 8923896 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05937 442 LRLTEEVATTDNHKQQKGVLRD 463
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-382 |
1.58e-10 |
|
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: 64.18 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 115 KKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 194
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 195 SSESLcERIL----DSSCSLLITTDAFyrgeklvnLKELADEALQKCQEKGFPVRCCivvkhlgraelgmgdstsqsppi 270
Cdd:cd05931 83 PGRHA-ERLAailaDAGPRVVLTTAAA--------LAAVRAFAASRPAAGTPRLLVV----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 271 krscpdvqiswnqgiDLwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAE 350
Cdd:cd05931 131 ---------------DL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPG 190
|
250 260 270
....*....|....*....|....*....|....*.
gi 8923896 351 D--VFW--CTADIGWITGhsyvTYGPLANGATSVLF 382
Cdd:cd05931 191 DvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLM 222
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-664 |
2.42e-10 |
|
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: 63.23 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwh 290
Cdd:cd05914 83 IFVSDE-------------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 elmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdFHAEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05914 89 -----------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 371 GPLANGATSVLFEGIPT-------------YPDVNRLWSIVDKYKVTKFYTAPTAI---RLLMKFGDEPVTKHSRASLQ- 433
Cdd:cd05914 151 LPLLNGAHVVFLDKIPSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHe 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 434 ---------VLGtvGEPINPEAwLWYHRVVGAqrcPIVDTFWQTETGghmltPLPGATP---MKPGSATFPFFGVAPAIl 501
Cdd:cd05914 231 afggnikefVIG--GAKINPDV-EEFLRTIGF---PYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRI- 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 502 nesGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDM-LNVSGHLLS 580
Cdd:cd05914 299 ---DSPDPATGEGEIIVRGP--NVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIY 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 581 TAEVESALVEHEAVAEAAVV---------GHPHP----VKGECLycfvtlcdghtfsPKLTEELKKQIREKIGpIATPDY 647
Cdd:cd05914 372 PEEIEAKINNMPFVLESLVVvqekklvalAYIDPdfldVKALKQ-------------RNIIDAIKWEVRDKVN-QKVPNY 437
|
570 580
....*....|....*....|....
gi 8923896 648 -------IQNAPgLPKTRSGKIMR 664
Cdd:cd05914 438 kkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
550-667 |
2.43e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 550 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSPkl 627
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDP-- 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 8923896 628 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
540-677 |
4.83e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.42 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 540 YFKK-----FPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 614
Cdd:PRK07008 398 YFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923896 615 VTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDL 677
Cdd:PRK07008 478 VVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR-DYVL 536
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
545-669 |
6.46e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.60 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 545 PGYYVTGDGCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtLCDGHTfS 624
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 8923896 625 PKLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07824 310 PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
306-667 |
8.86e-10 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 61.65 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVVHTVGGYM--------LY---------VATTFKYVFDFHAEDVFwctadIGWITGHSYV 368
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 tygplangatsVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 448
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 449 wYHRVVGAQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP---- 523
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvgav 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 524 --------GIMRTvYGNH-----ERFETTYFK--------KFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd17648 288 gelylggdGVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 583 EVESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfspkLTE-ELKKQIREKIGPIATPDYIQNAPGLPK 656
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
410
....*....|.
gi 8923896 657 TRSGKIMRRVL 667
Cdd:cd17648 442 TINGKLDVRAL 452
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
546-667 |
1.22e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.17 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSp 625
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD- 474
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 8923896 626 klTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK13383 475 --AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
546-669 |
2.84e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.18 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 8923896 626 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
306-672 |
3.29e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.32 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATtfkyVFDFHAEDVfwctadigwITG-----HSY----VTYGPL 373
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 374 ANGATSVlFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLgtvgepinpeawlwyhrV 453
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------V 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 454 VGAQRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSATFPFFGVAPAILNESGe 506
Cdd:PRK08633 905 AGAEKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET- 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 507 elegeaegYLVFKQPWPG--------IMRTVYGNHERF-ETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 577
Cdd:PRK08633 979 --------FEELPPGEDGliliggpqVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGE 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 578 LLSTAEVESALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSPKLTEELKKQIRE-KIGPIATPDYIQNAP 652
Cdd:PRK08633 1051 MVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVE 1122
|
410 420
....*....|....*....|
gi 8923896 653 GLPKTRSGKIMRRVLRKIAQ 672
Cdd:PRK08633 1123 ALPLLGSGKLDLKGLKELAL 1142
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-669 |
3.24e-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: 56.59 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSivfagfsseslcerildsscslLITT 214
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA----------------------LINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 215 DAfyRGEKLVNlkeladeALQKCQEKGFPVrccivvkhlgraelgmgdstsqsppikrscpdvqiswnqgidlwwhelmq 294
Cdd:cd05940 61 NL--RGESLAH-------CLNVSSAKHLVV-------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 295 eagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05940 82 --------------DAALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 375 NGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTK-HsraslQVLGTVGEPINPEAWLWYHRV 453
Cdd:cd05940 147 SGATLVIRKKF----SASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERkH-----KVRMIFGNGLRPDIWEEFKER 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 454 VGAQRcpiVDTFWQTETGGHMLTPLPGatpmKPGSAtfpffGVAPAILnesgeeleGEAEGYLVFK------QPW----- 522
Cdd:cd05940 218 FGVPR---IAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLL--------RKVAPLALVKydlesgEPIrdaeg 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 523 ---------PGIMRTVYGNHERFE-------------TTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:cd05940 278 rcikvprgePGLLISRINPLEPFDgytdpaatekkilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVS 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 581 TAEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05940 358 TTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGT 434
|
570
....*....|
gi 8923896 660 GKIMRRVLRK 669
Cdd:cd05940 435 FKQQKVDLRN 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
548-667 |
8.08e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 548 YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSPKL 627
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 8923896 628 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
131-673 |
2.90e-07 |
|
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: 53.83 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERIldsscsl 210
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARL------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 littdafyrgEKLVNLKELADEALqkcqekgfpvrccIVVKHLGRAELGMGDSTSQSPPIKRScpDVQISWNQGIDLWWH 290
Cdd:cd05906 108 ----------RKLRHIWQLLGSPV-------------VLTDAELVAEFAGLETLSGLPGIRVL--SIEELLDTAADHDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 ElmqeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVF--WCTADigWITGHSYV 368
Cdd:cd05906 163 Q-------------SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 369 TYGPLANGATSVlfeGIPT---YPDVNRLWSIVDKYKVTkfYT-APT-AIRLLMKFGDEPVTKH-SRASLQVLGTVGEPI 442
Cdd:cd05906 227 HLRAVYLGCQQV---HVPTeeiLADPLRWLDLIDRYRVT--ITwAPNfAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 443 NP---EAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGvapailnesgeelegeaegylvfk 519
Cdd:cd05906 302 VAktiRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLG------------------------ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 520 QPWPGI-MRTVYGNHE--------RFETTYFKKFPGYY---------VTGDGCQRDQD------GYYWITGRIDDMLNVS 575
Cdd:cd05906 358 RPIPGVsMRIVDDEGQllpegevgRLQVRGPVVTKGYYnnpeanaeaFTEDGWFRTGDlgfldnGNLTITGRTKDTIIVN 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 576 GHLLSTAEVESALVEHEAVAE--AAVVGHPHPVKGECLYCFVtlcdghtFSPKLTE-----ELKKQIR----EKIGpiAT 644
Cdd:cd05906 438 GVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIF-------FVPEYDLqdalsETLRAIRsvvsREVG--VS 508
|
570 580 590
....*....|....*....|....*....|...
gi 8923896 645 PDYI----QNApgLPKTRSGKIMRRVLRKIAQN 673
Cdd:cd05906 509 PAYLiplpKEE--IPKTSLGKIQRSKLKAAFEA 539
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
131-375 |
4.83e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 53.31 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILD-SSCS 209
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV-EFIINhAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 210 LlittdAFYRGEKLvnlkeladEALQKCQEKgfpvrcCivVKHLgRAELGMGDSTSQSppiKRSCPdvqiswNQGIDLW- 288
Cdd:PLN02861 152 I-----AFVQESKI--------SSILSCLPK------C--SSNL-KTIVSFGDVSSEQ---KEEAE------ELGVSCFs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 289 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaedvfwcTADIGWITGHSYV 368
Cdd:PLN02861 201 WEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYF 270
|
....*..
gi 8923896 369 TYGPLAN 375
Cdd:PLN02861 271 SYLPLAH 277
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
546-660 |
8.85e-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: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 546 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 8923896 626 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
301-447 |
9.27e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.21 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 301 EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgymlyvattfkyvfDFHA------EDVFWCTADIGWITGHSYVTYGPlA 374
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHG--------------MFEAqiealrEDYGIEPGEIDLPTFPLFALFGP-A 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 375 NGATSVLFEGIPTYP-DVN--RLWSIVDKYKVTKFYTAPTAIrllmkfgdEPVTKHSRASLQVLGTV------GEPINPE 445
Cdd:PRK09274 232 LGMTSVIPDMDPTRPaTVDpaKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLrrvisaGAPVPIA 303
|
..
gi 8923896 446 AW 447
Cdd:PRK09274 304 VI 305
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
131-382 |
1.37e-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: 51.45 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 211 LITTdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrSCPDvqiswnqgidlwwh 290
Cdd:cd17639 81 IFTD----------------------------------------------------------GKPD-------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 291 elmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDvfwctadigwitgHSYVTY 370
Cdd:cd17639 89 ------------------DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAY 137
|
250
....*....|....*.
gi 8923896 371 GPLAN----GATSVLF 382
Cdd:cd17639 138 LPLAHifelAAENVCL 153
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
587-696 |
3.63e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 49.76 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSPKLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90 100 110
....*....|....*....|....*....|..
gi 8923896 667 LRKIAQNDHDLGD--MSTVADPSVISHLFSHR 696
Cdd:PRK09188 322 LRLIAMNQIDELDdlLREPEIRGLVEAIAAHR 353
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
307-632 |
3.68e-06 |
|
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: 50.15 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 307 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 386
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 387 TYP---DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVgAQRCPIVD 463
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKML-SDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 464 TFWQTET------GGHMLTPLPGATPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLVfkQPW---------PGI 525
Cdd:cd05910 232 PYGATEAlpvssiGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGeigeitvtgPTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 526 MRTVYGnheRFETTYFKKFPG-----YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:cd05910 309 TPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
330 340 350
....*....|....*....|....*....|..
gi 8923896 601 GHPHPVKGECLYCFVTLCDGHTFSPKLTEELK 632
Cdd:cd05910 386 GVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
306-667 |
1.63e-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: 47.93 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV---HTvggyMLYVATTFKYVFDFHAEDVFWCTADIGWiTGHSYVTYGPLANGAT-SVL 381
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMiehHN----LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAAlHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 382 FEGIPTypDVNRLWSIVDKYKVTKFYTaPTAIRllmkfgdEPVTKHSRASLQVLGTVGEPINpeawlwyhrVVGAQRCPI 461
Cdd:cd17645 177 PSERRL--DLDALNDYFNQEGITISFL-PTGAA-------EQFMQLDNQSLRVLLTGGDKLK---------KIERKGYKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 462 VDTFWQTETgghmlTPLPGATPMKPGSATFPFfGVAPA-----ILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERF 536
Cdd:cd17645 238 VNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEALQLQPIGVAGELCIAGE--GLAR---GYLNRP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 537 ETTYfKKF------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 608
Cdd:cd17645 307 ELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8923896 609 ECLYCFVTlcdghtfSPKLT--EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17645 386 KYLVAYVT-------APEEIphEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
137-337 |
2.92e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.50 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARigalHSIVfagfsseslcerildssCSLLITTDA 216
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAA----HSLI-----------------CVPLYDTLG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 217 FYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGraelGMGDSTSQSPPIKRSCPDVQI---SWNQgidlWWHELM 293
Cdd:PLN02430 137 PGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLK----AIVSFTSVTEEESDKASQIGVktySWID----FLHMGK 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 8923896 294 QEAGDECEPEwcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 337
Cdd:PLN02430 209 ENPSETNPPK---PLDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
301-669 |
4.60e-05 |
|
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: 46.71 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 301 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTVGGYMLYVATTfkyvFDFHAEDVF--W--CTADIGWITGHsyvtYGP 372
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 373 LANGATSVLfegIPTYPDVNR--LW-SIVDKYKVTKFYTAPTAIRLLMK-FGDEPVTKHSRASLQVLGTVGEPINPE--- 445
Cdd:cd05908 170 LIAGMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYElch 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 446 AWLWYHRVVGAQRCPIVDTFWQTETGghmltplPGATPMKPGSATFPFF--------GV-APAILNESGEELEGEAEGY- 515
Cdd:cd05908 247 EFLDHMSKYGLKRNAILPVYGLAEAS-------VGASLPKAQSPFKTITlgrrhvthGEpEPEVDKKDSECLTFVEVGKp 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 516 LVFKQpwpgiMRTVYGNHERFETTYFKKF--------PGYY---------VTGDGCQR--DQ----DGYYWITGRIDDML 572
Cdd:cd05908 320 IDETD-----IRICDEDNKILPDGYIGHIqirgknvtPGYYnnpeatakvFTDDGWLKtgDLgfirNGRLVITGREKDII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 573 NVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG-------PI 642
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwqinevlPI 474
|
410 420
....*....|....*....|....*..
gi 8923896 643 ATpdyiqnapgLPKTRSGKIMRRVLRK 669
Cdd:cd05908 475 RR---------IPKTTSGKVKRYELAQ 492
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
108-326 |
5.31e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 46.66 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 108 LDRNVHEkkLGDKVAFYW---EGNEPGETTQITYHQLLVQVCQFSNVLrKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 185 ALHSIVFA----GfSSESLCERILDSSCSLLITTDAfyrgeklvnLKELADEALQKcqekgfpvrccivVKHLGRAELGM 260
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA---------AAEAVEGFLRN-------------LPRLRRPRVIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923896 261 GDSTsqsppikrscPDvqiswnqgidlwwhelmqEAGDECEPEWCDAEDPLFILYTSGSTGKPKGV 326
Cdd:PRK12476 174 IDAI----------PD------------------SAGESFVPVELDTDDVSHLQYTSGSTRPPVGV 211
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
545-673 |
5.32e-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: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 545 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 624
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 8923896 625 PKLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-326 |
6.64e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.04 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGalHSIVFAGFSSES 198
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 199 lcERILD----SSCSLLITTDAFyrGEKLVNLKELADEALQkcqekgfpvrccivvkhlgraelgmgDSTSQSPPIKRSc 274
Cdd:PRK04813 89 --ERIEMiievAKPSLIIATEEL--PLEILGIPVITLDELK--------------------------DIFATGNPYDFD- 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 8923896 275 pdvqiSWNQGidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGV 326
Cdd:PRK04813 138 -----HAVKG-----------------------DDNYYIIFTSGTTGKPKGV 161
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
136-374 |
1.32e-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: 45.28 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 136 ITYHQLLVQVCQFSNVLRKQGI--QKGDRVAIYMPMIPELVVAMLACARIGalhsivfagfsseslcerildsscsllIT 213
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYS---------------------------LV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 214 TDAFYrgeklvnlKELADEAlqkcqekgfpvrCCIVVKHlgrAELGMgdstsqsppikrscpdvqISWNQGIDLW-WHEL 292
Cdd:cd05927 59 TVPLY--------DTLGPEA------------IEYILNH---AEISI------------------VFCDAGVKVYsLEEF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 293 MQE-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFwctaDIgwitghsYVTYG 371
Cdd:cd05927 98 EKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPT----DV-------YISYL 166
|
...
gi 8923896 372 PLA 374
Cdd:cd05927 167 PLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
306-388 |
3.46e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 383
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 8923896 384 GIPTY 388
Cdd:PRK06814 860 GVKVF 864
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
306-602 |
1.41e-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: 41.58 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 306 DAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 382
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 383 EGIPTYPD------------VNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepvtkhsrasLQVLGTVGEPINpeawlwy 450
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGIS------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 451 hrvvGAQRCPI-VDTFWQ------------TETGghmltplPGATPMKP-----GSATFPFFGVAPAILNESGEELEGEA 512
Cdd:cd17640 221 ----GGGALPPhVDTFFEaigievlngyglTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGNVVLPPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923896 513 EGYLVFKQPwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEH 591
Cdd:cd17640 290 EKGIVWVRG-PQVMKGYYKNPE--ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRS 366
|
330
....*....|.
gi 8923896 592 EAVAEAAVVGH 602
Cdd:cd17640 367 PFIEQIMVVGQ 377
|
|
| |
