|
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: 1181.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 45 QRYRELHRRSVEEPREFWGNIAKEFYWKTACPGPFlqynfDVTKGKIFTEWMKGATTNICYNVLDRNVHekKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 125 WEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIL 204
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 205 DSSCCLLITTDAFYRGEKLVNLKELADESLEKCrekgFPVRCCIVVKHLGRaelgmndspsqsppvkrPCPdvqicWNEG 284
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGG-----------------EVP-----MTEG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 285 VDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITG 364
Cdd:cd05966 208 RDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 365 HSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINP 444
Cdd:cd05966 288 HSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 445 EAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPG 524
Cdd:cd05966 368 EAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 525 IMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd05966 448 MARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 605 PVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVA 684
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLA 607
|
.
gi 31980996 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: 1110.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 31 PPPEVRRSAHVpSLQRYRELHRRSVEEPREFWGNIAKEFYWKTacpgPFLQyNFDvtKGKIFTEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFK----PFDT-VLD--WNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 111 NVHEKklGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIV 190
Cdd:PRK00174 76 HLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 191 FAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCRekgfPVRCCIVVKHLGRAelgmndspsqsppv 270
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTGGD-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 271 krpcpdvqICWNEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPE 350
Cdd:PRK00174 216 --------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 351 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRA 430
Cdd:PRK00174 288 DVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 431 SLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEG 510
Cdd:PRK00174 368 SLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 511 EAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK00174 448 GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
650 660
....*....|....*....|..
gi 31980996 671 AQNDHDLGDTSTVADPSVINHL 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: 1033.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 43 SLQRYRELHRRSVEEPREFWGNIAKE-FYWKTacpgPF---LQYNFDVtkgkiFTEWMKGATTNICYNVLDRnvHEKKLG 118
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFK----PFtkvLDWSFPP-----FYKWFVGGELNVSYNCVDR--HLEARP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:TIGR02188 72 DKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKgfpVRCCIVVKHLGraelgmNDSPSqsppvkrpcpdvq 278
Cdd:TIGR02188 152 LADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG------NPVVP------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icWNEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTAD 358
Cdd:TIGR02188 210 --WVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 359 IGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTV 438
Cdd:TIGR02188 288 VGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNES-GEELEGEAEGYLV 517
Cdd:TIGR02188 368 GEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 518 FKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:TIGR02188 448 IKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 598 AVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD- 676
Cdd:TIGR02188 528 AVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEi 607
|
650
....*....|....*.
gi 31980996 677 LGDTSTVADPSVINHL 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: 899.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 31 PPPEVRRSAHVPSLQRYRELHRRSVEEPREFWGNIAKEFYWKTA-CPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 110 RNVhEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSI 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 190 VFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHlgraELGMNDSPSQspp 269
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYEN----QLAMKREDTK--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 270 vkrpcpdvqicWNEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP 349
Cdd:PLN02654 248 -----------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 350 EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSR 429
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 430 ASLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELE 509
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 510 GEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02654 477 GECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
650 660
....*....|....*....|....
gi 31980996 670 IAQNDHD-LGDTSTVADPSVINHL 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: 872.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 94 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 174 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREkgfpVRCCIVVKHL 253
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 254 GrAELGMNDspsqsppvkrpcpdvqicwnegvDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGY 333
Cdd:COG0365 154 G-ADVPMEG-----------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 334 MLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAI 413
Cdd:COG0365 210 LVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 414 RMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETGGHMLTPLPGaTPMKPGSASFPF 493
Cdd:COG0365 290 RALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 494 FGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:COG0365 366 PGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:COG0365 446 VSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDE 525
|
570 580 590
....*....|....*....|....*....|....*....
gi 31980996 654 LPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADPSVINHL 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: 709.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 47 YRELHRRSVEEPREFWGNIAKEFYWKTacPGPFLQyNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKklGDKVAFYWE 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWIT--PYQKVK-NTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 127 GNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDS 206
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 207 SCCLLITTDAFYRGEKLVNLKELADESLEKcreKGFPVRCCIVVKHLGraelgmndspsqsppvkrpcpdVQICWNEGVD 286
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLKRTG----------------------SDIDWQEGRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 287 LWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:cd17634 211 LWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 YVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 447 WLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIM 526
Cdd:cd17634 371 YEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 527 RTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd17634 451 RTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 607 KGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 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: 603.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 47 YRELHRRSVEEPREFWGNIAKEFYWKTacpgPFLQYnFDVTKGKiFTEWMKGATTNICYNVLDRNVhEKKLGDKVAFYWE 126
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFK----PPEKI-LDNSNPP-FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 127 GNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDS 206
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 207 SCCLLITTDAFYRGEKLVNLKELADESLEKCREKgfPVRCCIVVKHLGRAELGmndspsqsppvkRPcpdvqicwneGVD 286
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHVLVLNRPQVPADLT------------KP----------GRD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 287 LWWHELMQQAGdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:cd05967 210 LDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 YVTYGPLANGATSVLFEGIPT-YPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFgdDP----VTKHSRASLQVLGTVGEP 441
Cdd:cd05967 289 YIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKE--DPdgkyIKKYDLSSLRTLFLAGER 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 442 INPEAWLWYHRVVGSqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFK 519
Cdd:cd05967 367 LDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 520 QPW-PGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:cd05967 444 LPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 599 VVGHPHPVKGECLYCFVTLCDGHTFSP-TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDL 677
Cdd:cd05967 524 VVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE-DY 602
|
650
....*....|....*
gi 31980996 678 GDTSTVADPSVINHL 692
Cdd:cd05967 603 TIPSTIEDPSVLDEI 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: 569.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 45 QRYRELHRRSVEEPREFWGNIAKEFYWKTacpgPFLQYnFDVTKGKiFTEWMKGATTNICYNVLDRnvHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQT----PFTQV-LDYSNPP-FARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 125 WEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIL 204
Cdd:PRK10524 74 AVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 205 DSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKgfPVRCCIVVKHLGraelgmndspsqsppvkrPCPdvqicWNEG 284
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLA------------------PMA-----RVAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 285 VDLWWHELMQQAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWIT 363
Cdd:PRK10524 209 RDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 364 GHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK10524 289 GHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 444 PEAWLWYHRVVGSqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQ 520
Cdd:PRK10524 369 EPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKgVLVIEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 PW-PGIMRTVYGNHTRFETTYFKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK10524 446 PLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 599 VVGHPHPVKGECLYCFVTLCDGHTFS-----PTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQn 673
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAE- 604
|
650
....*....|....*.
gi 31980996 674 DHDLGDTSTVADPSVI 689
Cdd:PRK10524 605 GRDPGDLTTIEDPAAL 620
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
94-685 |
6.82e-180 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 524.46 E-value: 6.82e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 94 EWMKGATTNICYNVLDRNVHEKkLGDKVAFYWEGNEPGEttKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 173
Cdd:PRK04319 35 SWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 174 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRgeklvnlKELADE--SLEKCrekgfpvrccIVVK 251
Cdd:PRK04319 112 YFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDlpSLKHV----------LLVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 252 HLGRAELGMNDspsqsppvkrpcpdvqicwnegvdlwWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIG 331
Cdd:PRK04319 175 EDVEEGPGTLD--------------------------FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 332 GYMLYVATTfKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiptypDEGRL----W-SIVDKYKVTKF 406
Cdd:PRK04319 229 AMLQHYQTG-KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVI--------DGGRFsperWyRILEDYKVTVW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 407 YTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqrcPIVDTFWQTETGGHMLTPLPgATPMKP 486
Cdd:PRK04319 300 YTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 487 GSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETtYFKkfPGYYVTGDGCRRDQDGYYWITG 566
Cdd:PRK04319 376 GSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPD 646
Cdd:PRK04319 453 RVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPR 532
|
570 580 590
....*....|....*....|....*....|....*....
gi 31980996 647 YIQNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDTSTVAD 685
Cdd:PRK04319 533 EIEFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-686 |
2.15e-178 |
|
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: 522.05 E-value: 2.15e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 44 LQRYRELHRRSVEEPREFWGNIAKEF-YWKTACPGPFLqynfDVTKGKIFTEWMKGATTNICYNVLDRnvHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 123 FYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCER 202
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 203 ILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCrekgFPVRCCIVVKHLGRAELgmndspsqsppvkrpcpdvqicWN 282
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------------------PA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 283 EGVDLWWHELMQQAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPED-VFWCTaDIGW 361
Cdd:cd05968 213 KGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGW 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 ITGhSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEP 441
Cdd:cd05968 290 MMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 442 INPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAEGyLVFKQP 521
Cdd:cd05968 369 WNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPEVGE-LVLLAP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 WPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05968 447 WPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 602 HPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKiAQNDHDLGDTS 681
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLS 605
|
....*
gi 31980996 682 TVADP 686
Cdd:cd05968 606 SLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-671 |
4.39e-133 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 399.57 E-value: 4.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDA 216
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 FYRgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvKRpcpdvqicwnegvdlwwhelmqqa 296
Cdd:cd05969 82 LYE---------------------------------------------------RT------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 gdecepewcDAEDPLFILYTSGSTGKPKGVVHtIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05969 87 ---------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGiptYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGs 456
Cdd:cd05969 157 VTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 457 qrCPIVDTFWQTETGGHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRF 536
Cdd:cd05969 233 --VPIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 537 ETtYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05969 310 KN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 617 LCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05969 387 LKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-575 |
3.99e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 334.28 E-value: 3.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 108 LDRNVheKKLGDKVAFywegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALH 187
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 188 SIVFAGFSAESLCERILDSSCCLLITTDAFYrgeklvnlkelaDESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQS 267
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 268 PPVkrpcpdvqicwnegvdlwwhelmqqagDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIgGYMLYVATTFKYV--- 344
Cdd:pfam00501 142 ADV---------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrpr 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 345 -FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDP 423
Cdd:pfam00501 194 gFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 424 VTKHSraSLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSASFPFFGVAPAILN 502
Cdd:pfam00501 273 RALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVD 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980996 503 ESGEELEGEAEG-YLVFKQpwPGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 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 |
1.03e-105 |
|
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: 328.53 E-value: 1.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSsccllittda 216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 fyrgeklvNLKeladeslekcrekgfpvrcCIVvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelmqqa 296
Cdd:cd05972 72 --------GAK-------------------AIV----------------------------------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 gdecepewCDAEDPLFILYTSGSTGKPKGVVHTIGgYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05972 78 --------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLG 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGIPTYPDegRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGS 456
Cdd:cd05972 149 ATVFVYEGPRFDAE--RILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATGL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 457 qrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRF 536
Cdd:cd05972 224 ---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKT 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 537 ETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05972 299 EASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 31980996 617 LCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05972 376 LTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-670 |
7.60e-89 |
|
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: 290.71 E-value: 7.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 40 HVPSLQRYRELHRRSVEEPREFWGNIAKefYWKTACPGPflqYNFDVTKGKIF--TEWMKGATTNICYNVLDRNVHEkkl 117
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 118 gDKVAFYweGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 197
Cdd:cd05943 84 -DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 198 SLCERILDSSCCLLITTDAFYRGEKLVNLkeladesLEKCRE--KGFPVRCCIVVkhlgraelgmndspsqsppVKRPCP 275
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDV-------REKVAElvKGLPSLLAVVV-------------------VPYTVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 276 DVQICWNEGVDLWWHELMQQAGDECEPEWC--DAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVF 353
Cdd:cd05943 215 AGQPDLSKIAKALTLEDFLATGAAGELEFEplPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 354 WCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQ 433
Cdd:cd05943 295 FYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 434 VLGTVGEPINPEAWLWYHRVVGSqrcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSASFPFFGVAPAILNESGE 506
Cdd:cd05943 373 TILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLGMAVEAFDEEGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 507 ELEGEAEGyLVFKQPWPGImrTVY----GNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd05943 444 PVWGEKGE-LVCTKPFPSM--PVGfwndPDGSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 583 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd05943 521 EIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
....*...
gi 31980996 663 MRRVLRKI 670
Cdd:cd05943 601 VEVAVKKI 608
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
309-663 |
4.06e-87 |
|
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: 276.86 E-value: 4.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 388
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 389 PDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFgdDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQT 468
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKA--PESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 469 ETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNhtRFETTYFKKFPGYY 548
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWN--NPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 549 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtlt 628
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 31980996 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 |
9.44e-83 |
|
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: 269.37 E-value: 9.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 107 VLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 187 HSIVFAGFSAESLcERIL-DSSCCLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndsps 265
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 266 qsppvkrpcpdvqicwnegvdlwwhelmqqagdecepewcdaedpLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVF 345
Cdd:COG0318 103 ---------------------------------------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAAL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 346 DFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvt 425
Cdd:COG0318 137 GLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFA-- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 426 KHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESG 505
Cdd:COG0318 211 RYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 506 EELEGEAEGYLVFKQPWpgIMRTVYGNHTRFEttyfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:COG0318 288 RELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDR 438
|
570
....*....|.
gi 31980996 665 RVLRKIAQNDH 675
Cdd:COG0318 439 RALRERYAAGA 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-669 |
1.20e-79 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 266.61 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 57 EPREFWGNIAKEF-YWKTacpgpflQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTK 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYRGEKLV----NLKELADESLEKCREkgfpvrcciVVKHLgraelgMNDSPSQSPPVK-RPCPDVQICWNegvdlWWH 290
Cdd:PTZ00237 173 YGILNDEIItftpNLKEAIELSTFKPSN---------VITLF------RNDITSESDLKKiETIPTIPNTLS-----WYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEP--EWCDAED--PLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:PTZ00237 233 EIKKIKENNQSPfyEYVPVESshPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 YVtYGPLANGATSVLFEGIPTYPD--EGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSR---ASLQVLGTVGEP 441
Cdd:PTZ00237 313 FL-YGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGGEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 442 INPEAWLWYHRVVGSqRCPIVdtFWQTETGghMLTPLPGATPMKPGSAS-FPFFGVAPAILNESGEELEGEAEGYLVFKQ 520
Cdd:PTZ00237 392 IEESIPEYIENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 PWP-GIMRTVYGNHTRFETTyFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 599
Cdd:PTZ00237 467 PMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980996 600 VGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIRE----KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PTZ00237 546 IGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEINNiitqDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-691 |
1.47e-79 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 266.66 E-value: 1.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 29 WSPPPEVRRSAHVPSLQR------------YRELHRRSVEEPREFWGNIAKEFYWKTACPGPFLQYNfdvtKGKIFTEWM 96
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLAG----RRMPGARWF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 97 KGATTNICYNVLdRNvhekKLGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVA 176
Cdd:PRK03584 82 PGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 177 MLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVN----LKELADE--SLEKCrekgfpvrccIVV 250
Cdd:PRK03584 156 MLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRAAlpSLEHV----------VVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 251 KHLGraelgmndspsqSPPVKRPCPDVQIcwnegvdlwWHELMQQAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHT 329
Cdd:PRK03584 226 PYLG------------PAAAAAALPGALL---------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPKCIVHG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 330 IGGYMLYVATTFKYVFDFHPED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYT 408
Cdd:PRK03584 285 HGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 409 APTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqrcpivDTFWQTETGG-HMLTPLPGATPMKP- 486
Cdd:PRK03584 362 SAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNPLLPv 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 487 --GSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMrTVY----GNHTRFETTYFKKFPGYYVTGDGCRRDQDG 560
Cdd:PRK03584 436 yrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHG 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 561 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIG 640
Cdd:PRK03584 513 GVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLS 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 641 PIATPDYIQNAPGLPKTRSGKIM----RRVLR----KIAQNdhdlgdTSTVADPSVINH 691
Cdd:PRK03584 593 PRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHgrpvKKAVN------RDALANPEALDW 645
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-669 |
1.59e-79 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 260.53 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERiLDSSCCLLITTD 215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYRgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwHELmqq 295
Cdd:cd05973 80 AANR----------------------------------------------------------------------HKL--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATtFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05973 87 -----------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLAL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 376 GATSVLFEGIPTYPDegrLWSIVDKYKVTKFYTAPTAIRMLMKFGDdPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:cd05973 155 GHPTILLEGGFSVES---TWRVIERLGVTNLAGSPTAYRLLMAAGA-EVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 SqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfKQPWPGIMRTV------ 529
Cdd:cd05973 231 V---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELGPGEPGRLaidian 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 530 -----YGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd05973 295 splmwFRGYQLPDTPAIDG--GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 605 PVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05973 373 PERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
131-668 |
2.06e-67 |
|
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: 228.09 E-value: 2.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITtdafyrgeklvnlkelaDESlekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwh 290
Cdd:cd05971 82 LVT-----------------DGS--------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 elmqqagdecepewcdaEDPLFILYTSGSTGKPKGVVHT-------IGGYMLYvattfkyvFDFHP--EDVFWCTADIGW 361
Cdd:cd05971 88 -----------------DDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLFPrdGDLYWTPADWAW 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 ItghsyvtyGPLANGATSVLFEGIP------TYPDEGRLWSIVDKYKVTKFYTAPTAIRMlMKFGDDPVtKHSRASLQVL 435
Cdd:cd05971 143 I--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGEQL-KHAQVKLRAI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 436 GTVGEPINPEAWLWYHRVVGSqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGY 515
Cdd:cd05971 213 ATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 516 LVFKQPWPGIMRTVYGNHTRFEttyfKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05971 289 IAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAV 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980996 595 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05971 365 LMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-672 |
4.10e-66 |
|
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: 230.15 E-value: 4.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 39 AHVPSLQRYRELHRRSVEEPREFWGNIAKEFywKTACPGPFLQYnFDVTKGkIFTEWMKGATTNICYNVLdrnvhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWegNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:TIGR01217 100 EPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFYRGEKlvnlKELADESLEKCReKGFP-VRCCIVVKHLGraelgmnDSPSQSPPVkrpcpdv 277
Cdd:TIGR01217 178 VLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYLG-------PRETEAPKI------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 278 qicwnEGvDLWWHELMQQAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCT 356
Cdd:TIGR01217 239 -----DG-ALDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 357 ADIGWITGHSYVTygPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLG 436
Cdd:TIGR01217 313 TTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 437 TVGEPINPEAWLWYHRVVGSqrcpivDTFWQTETGG-HMLTPLPGATPMKP---GSASFPFFGVAPAILNESGEELEGEA 512
Cdd:TIGR01217 391 STGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGEV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 513 EGyLVFKQPWPGiMRTVYGNH---TRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:TIGR01217 465 GE-LVCTNPMPS-MPIRFWNDpdgSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:TIGR01217 543 RLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKR 622
|
...
gi 31980996 670 IAQ 672
Cdd:TIGR01217 623 VLQ 625
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-669 |
6.10e-61 |
|
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: 213.10 E-value: 6.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 102 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAM 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 178 LACARLGAlhsivfagfsaeslcerILDSSCCLLITTDAFYRgeklvnlkeladesLEKCREKgfpvrcCIVVKHLGRAE 257
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVTSDELAPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 258 LgmnDSpsqsppVKRPCPDVQ---ICWNEGVDLW--WHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGG 332
Cdd:cd05928 128 V---DS------VASECPSLKtklLVSEKSRDGWlnFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 333 YMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDEGRLWSIVDKYKVTKFYTAPTA 412
Cdd:cd05928 199 LGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAPTV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 413 IRMLMKfgdDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQrcpIVDTFWQTETGghMLTPLPGATPMKPGS--AS 490
Cdd:cd05928 277 YRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSmgKA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHTRFETTYFKKFpgyYVTGDGCRRDQDGYYWITGRID 569
Cdd:cd05928 349 SPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRAD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 570 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC-DGHTFSP-TLTEELKKQIREKIGPIATPDY 647
Cdd:cd05928 426 DVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQFLSHDPeQLTKELQQHVKSVTAPYKYPRK 505
|
570 580
....*....|....*....|..
gi 31980996 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05928 506 VEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
105-668 |
1.34e-60 |
|
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: 211.84 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 105 YN---VLDRNVhEKKLGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 182 RLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYrgeklvnlkELADESLEKcrekgfpvrccivVKHLGRAELGMN 261
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA---------PVLAAALTK-------------SEHTLVVLIVSG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 262 DSPSQSPpvkrpcpdvqicwnegvDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTF 341
Cdd:cd05959 134 GAGPEAG-----------------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 342 -KYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDegRLWSIVDKYKVTKFYTAPTAIRMLMKfg 420
Cdd:cd05959 196 aRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFFGVPTLYAAMLA-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 421 DDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAI 500
Cdd:cd05959 271 APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVEL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 501 LNESGEELEGEAEGYLVFKQPWPGIMrtvYGNhtRFETTYfKKFPGYYV-TGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:cd05959 346 RDEDGGDVADGEPGELYVRGPSSATM---YWN--NRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTAT 499
|
....*....
gi 31980996 660 GKIMRRVLR 668
Cdd:cd05959 500 GKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-668 |
2.89e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 205.81 E-value: 2.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 105 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 185 A-LHSI-VFagFSAESLcerildssccLLITTDAfyrGEKLVnlkeLADESLEKCREKGFP----VRCCIVVKHLGRAEL 258
Cdd:PRK06187 81 AvLHPInIR--LKPEEI----------AYILNDA---EDRVV----LVDSEFVPLLAAILPqlptVRTVIVEGDGPAAPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 259 GmndspsqsPPVKRpcpdvqicwnegvdlwWHELMQQAGDEcePEWCDAE--DPLFILYTSGSTGKPKGVVHT---IGGY 333
Cdd:PRK06187 142 A--------PEVGE----------------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKGVVLShrnLFLH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 334 MLYVATtfkyVFDFHPEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegiptYPDE---GRLWSIVD 399
Cdd:PRK06187 196 SLAVCA----WLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV-------IPRRfdpENLLDLIE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 400 KYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETGG--HMLTP 477
Cdd:PRK06187 253 TERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGMTETSPvvSVLPP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 478 LPGATPM--KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHTRFETTYFKkfpGYYVTGDG 553
Cdd:PRK06187 328 EDQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETIDG---GWLHTGDV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 554 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKK 633
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRA 479
|
570 580 590
....*....|....*....|....*....|....*
gi 31980996 634 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK06187 480 FLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-674 |
2.78e-56 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 200.80 E-value: 2.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 102 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 182 RLGAlhsivfagfsaeslcerILDSSCCLLITTDAFYRGEKlvnlkelADESLEKC-REKGFPVRCcivvkHLGRAELGm 260
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYRIES-------ADIKMIVAiAEDNIPEEI-----EKAAPECP- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 261 ndSPSQSPPVKRPCPDVQICWNEgvdlwwhELMQQAGDECEPEWCDA---EDPLFILYTSGSTGKPKGVVHTIGgYMLYV 337
Cdd:cd05970 144 --SKPKLVWVGDPVPEGWIDFRK-------LIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKMVEHDFT-YPLGH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 338 ATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDegRLWSIVDKYKVTKFYTAPTAIRMLM 417
Cdd:cd05970 214 IVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTTFCAPPTIYRFLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 418 KfgdDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQrcpIVDTFWQTETGGHMLTpLPGATPmKPGSASFPFFGVA 497
Cdd:cd05970 292 R---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAPGYE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 498 PAILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:cd05970 364 IDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:cd05970 440 SSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDE 519
|
570 580
....*....|....*....|.
gi 31980996 654 LPKTRSGKImRRVlrKIAQND 674
Cdd:cd05970 520 LPKTISGKI-RRV--EIRERD 537
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-668 |
4.99e-56 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 198.17 E-value: 4.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 105 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 185 AlhsIVFagfsaeslcerildssccllittdafyrgekLVNLKELADEslekcrekgfpvrccivVKHLgraelgMNDSP 264
Cdd:cd05936 74 A---VVV-------------------------------PLNPLYTPRE-----------------LEHI------LNDSG 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 265 SQsppvkrpcpdVQICwnegvDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYV 344
Cdd:cd05936 97 AK----------ALIV-----AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 345 FDFH-PEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTYPDEGRLWSIvDKYKVTKFYTAPTAIRML 416
Cdd:cd05936 162 EDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPRFRPIGVLKEI-RKHRVTIFPGVPTMYIAL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 417 MKFGDDpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETG--GHmLTPLPGatPMKPGSASFPFF 494
Cdd:cd05936 231 LNAPEF--KKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG--PRKPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 495 GVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:cd05936 303 GTEVKIVDDDGEELPPGEVGELWVRGP--QVMK---GYWNRPEETaeAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAP 652
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAGYKVPRQVEFRD 452
|
570
....*....|....*.
gi 31980996 653 GLPKTRSGKIMRRVLR 668
Cdd:cd05936 453 ELPKSAVGKILRRELR 468
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
118-664 |
2.18e-55 |
|
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: 195.52 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 118 GDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 197
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 198 SLCErILDSSccllittdafyrGEKLVnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdv 277
Cdd:cd17631 83 EVAY-ILADS------------GAKVL----------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 278 qicwnegvdlwwhelmqqagdecepewcdAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTA 357
Cdd:cd17631 97 -----------------------------FDDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 358 DIGWITGHSYVTYGPLANGATSVLFEGiptyPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSraSLQVLGT 437
Cdd:cd17631 147 PLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 438 VGEPInPEAWLwyhRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd17631 221 GGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 518 FKQPwpGIMRtvyGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:cd17631 297 VRGP--HVMA---GYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 598 AVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17631 372 AVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-668 |
2.11e-53 |
|
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: 189.98 E-value: 2.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITtd 215
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 afyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelmqq 295
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADI--GWITGHSyvTYGPL 373
Cdd:cd05919 89 ----------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 374 ANGATSVLFegiPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvtKHSRASLQVLGTVGEPInPEAwLWYhRV 453
Cdd:cd05919 157 AVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGEAL-PRG-LGE-RW 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 454 VGSQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtvYGNh 533
Cdd:cd05919 229 MEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVG---YWN- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 534 tRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 613
Cdd:cd05919 303 -NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 614 FVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05919 382 FVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-669 |
1.92e-50 |
|
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: 183.28 E-value: 1.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 130 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCC 209
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLITTDAFYRGEKLVNLKELADESLEKcrekGFPVRCCIVVKHLGRAELGMNDSPSQSPPvKRPCPDvqicwnegvdlww 289
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAILEL----ALDVGVLIRAPSAESLSNLLADKKNAKSE-GVPLPD------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 helmqqagdecepewcdaeDPLFILYTSGSTGKPKGV--VHT-IGGYMLYVATTFKYVFD---------FHpedvfwcta 357
Cdd:cd05926 150 -------------------DLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvmplFH--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 358 digwITGHSYVTYGPLANGATSVlfegIPTYPDEGRLWSIVDKYKVTkFYTA-PTAIRMLMKFgDDPVTKHSRASLQVLG 436
Cdd:cd05926 202 ----VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 437 TVGEPINPEAwlwYHRVVGSQRCPIVDTFWQTETGGHM-LTPLPgATPMKPGSASFPFfGVAPAILNESGEELEGEAEGY 515
Cdd:cd05926 272 SCSASLPPAV---LEALEATFGAPVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 516 LVFKQPwpGIMRTVYGNHT-RFEttYFKKFpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05926 347 ICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 595 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05926 422 LEAVAFGVPDEKYGEEVAAAVVLREGASVTE---EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
307-668 |
1.29e-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: 176.90 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 307 AEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 386
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 387 TYPDEgrLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqrcPIVDTFW 466
Cdd:cd05958 174 ATPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 467 QTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVY-GNHTRFETTYFKKfp 545
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 31980996 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 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 |
5.70e-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: 174.79 E-value: 5.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildsscclLIT 213
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 214 TDAFYRGEKLvnlKELADESlekcrekgfpvRCCIVVKhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelm 293
Cdd:cd05934 58 INTALRGDEL---AYIIDHS-----------GAQLVVV------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 qqagdecepewcdaeDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYG 371
Cdd:cd05934 82 ---------------DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 372 PLANGATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLqvlgTVGEPINPEAWLWYH 451
Cdd:cd05934 144 ALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 452 RVVGsqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSASFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVY 530
Cdd:cd05934 216 ERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYY 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 531 GNhtrfETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05934 291 NM----PEATAEAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 610 CLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 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 |
6.86e-48 |
|
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: 174.68 E-value: 6.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIldssccllittd 215
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 afyrgeklvnlkeladeslekcrEKGFPVRCCIVvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelmqq 295
Cdd:cd05974 69 -----------------------DRGGAVYAAVD---------------------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFkYVFDFHPEDVFWCTADIGWiTGHSYVT-YGPLA 374
Cdd:cd05974 80 -------ENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWN 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 375 NGATSVLFegipTYP--DEGRLWSIVDKYKVTKFYTAPTAIRMLMKfgdDPVTKHSRASLQVLGTvGEPINPEAwlwYHR 452
Cdd:cd05974 151 AGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 453 VVGSQRCPIVDTFWQTETgghmlTPLPGATP---MKPGSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRT 528
Cdd:cd05974 220 VRRAWGLTIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 529 VYGNHTRfetTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 608
Cdd:cd05974 294 YAGDPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980996 609 ECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 671
Cdd:cd05974 371 SVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-669 |
1.53e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 175.89 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFYrgeklvnlkELADESLEKCREKGFPVRCcivVKHLGRAELGMNDspsqsppvkrpcpdvq 278
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALA---------PTAEAALALLPVDTLILSL---VLGGREAPGGWLD---------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icwnegVDLWwhelmQQAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----IGGYMLYVATTfkyvfDFHPEDVF 353
Cdd:PRK08316 152 ------FADW-----AEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG-----DMSADDIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 354 WCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDEGRLWSIVDKYKVTKFYTAPTA-IRMLmkfgddpvtKH- 427
Cdd:PRK08316 216 LHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISLL---------RHp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 428 --SRASLQVL--GTVGEPINPEAWLWYHRvvgsQRCPIVdTFW----QTETGghmltPL-----PGATPMKPGSASFPFF 494
Cdd:PRK08316 279 dfDTRDLSSLrkGYYGASIMPVEVLKELR----ERLPGL-RFYncygQTEIA-----PLatvlgPEEHLRRPGSAGRPVL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 495 GVAPAILNESGEELEgeaegylvfkqpwPGIMRTVYGNHTRFETTYFKKfP---------GYYVTGDGCRRDQDGYYWIT 565
Cdd:PRK08316 349 NVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHSGDLGVMDEEGYITVV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 566 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATP 645
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|....
gi 31980996 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 |
6.81e-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: 168.09 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 102 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 182 RLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYrgeklvnlkeladeslekcrekgfPVRccivvkhlgRAELGMN 261
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL------------------------PVI---------KAALGKS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 262 DSPSQSPPVKRP-CPDVQICwnegvdlwwhELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATT 340
Cdd:TIGR02262 124 PHLEHRVVVGRPeAGEVQLA----------ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 341 FKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDegRLWSIVDKYKVTKFYTAPTAIRMLMkfG 420
Cdd:TIGR02262 194 ARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQPTIFYGVPTLYAAML--A 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 421 DDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQrcpIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAI 500
Cdd:TIGR02262 269 DPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 501 LNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:TIGR02262 344 VGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVS 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 581 TAEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfspTLTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:TIGR02262 419 PFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKT 492
|
570
....*....|..
gi 31980996 658 RSGKIMRRVLRK 669
Cdd:TIGR02262 493 ATGKIQRFKLRE 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-663 |
9.52e-45 |
|
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: 167.39 E-value: 9.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITTDAFYrgEKLvnlkeladesLEKCREKGFPVRccIVVkhlgraelgMNDSPsqsPPVKRPCPDVQicWNEGVDLWWHE 291
Cdd:cd05911 87 FTDPDGL--EKV----------KEAAKELGPKDK--IIV---------LDDKP---DGVLSIEDLLS--PTLGEEDEDLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 292 LMQQAGDecepewcdaEDPLFILYTSGSTGKPKGVV--HTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITG-HSYV 368
Cdd:cd05911 139 PPLKDGK---------DDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGlFTTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYgpLANGATSVLFEGiptyPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKfgdDP-VTKHSRASLQVLGTVGEPINPEAw 447
Cdd:cd05911 209 AS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK---SPlLDKYDLSSLRVILSGGAPLSKEL- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 448 lwYHRV-VGSQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEaegylvfKQP---W- 522
Cdd:cd05911 279 --QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP-------NEPgeiCv 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 --PGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:cd05911 348 rgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 601 GHPHPVKGECLYCFVTLCDGhtfsPTLTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSGKIM 663
Cdd:cd05911 426 GIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASGKIL 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
136-687 |
8.69e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 161.28 E-value: 8.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLAcarlGALHSIVFA---GFSAESLCErildssccLLI 212
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 213 TTDAfyrgEKLVNLKELAD----ESLEKCREKGFPVRCCIVVkHLGRAElgmndSPSQSPPVKRPCPDVQIcwneGVDLW 288
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGtdiwQKVAEVLAALPELRTVVEV-DLARYL-----PGPKRLAVPLIRRKAHA----RILDF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 WHELMQQAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGhSY 367
Cdd:PRK07529 193 DAELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNA-LL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 368 VT-YGPLANGAtSVLFEGIPTYPDEG---RLWSIVDKYKVTKFYTAPTAIRMLMKFgddPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK07529 271 VTgLAPLARGA-HVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALLQV---PVDGHDISSLRYALCGAAPLP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 444 PEAWLWYHRVVGsqrCPIVDTFWQTE-TGGHMLTPLPGatPMKPGSASFPFFGVAPAILNESGEELEGEAEGY-----LV 517
Cdd:PRK07529 347 VEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYQRVRVVILDDAGRYLRDCAVdevgvLC 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 518 FKQPwpgimrTVYGNHTRFETTYFKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 596
Cdd:PRK07529 422 IAGP------NVFSGYLEAAHNKGLWLeDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 597 AAVVGHPHPVKGECLYCFVTLCDGHTFSPT-LTEELKKQIREkigPIATPDYIQNAPGLPKTRSGKI---------MRRV 666
Cdd:PRK07529 496 AAAVGRPDAHAGELPVAYVQLKPGASATEAeLLAFARDHIAE---RAAVPKHVRILDALPKTAVGKIfkpalrrdaIRRV 572
|
570 580
....*....|....*....|..
gi 31980996 667 LRK-IAQNDHDLGDTSTVADPS 687
Cdd:PRK07529 573 LRAaLRDAGVEAEVVDVVEDGR 594
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
132-667 |
1.38e-40 |
|
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: 154.61 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVF----AGFSAESLcERILDSS 207
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYvpldPSYPAERL-AYILEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 208 CC-LLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvd 286
Cdd:cd05930 84 GAkLVLT------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 287 lwwhelmqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATtFKYVFDFHPEDVFWCTADIGWItGHS 366
Cdd:cd05930 91 -------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSV 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 YVTYGPLANGATSVLfegIP--TYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVtkhsRASLQVLGTVGEPINP 444
Cdd:cd05930 150 WEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSLRLVLVGGEALPP 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 445 EAWLWYHRVVGSQR---------CPIVDTFWQTETGGHMLTPLP-GAtpmkpgsasfPFFGVAPAILNESGeelegeaeg 514
Cdd:cd05930 223 DLVRRWRELLPGARlvnlygpteATVDATYYRVPPDDEEDGRVPiGR----------PIPNTRVYVLDENL--------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 515 ylvfkQPWP------------GIMRTVYGNH--T--RFETTYFkkFPG--YYVTGDGCRRDQDG--YYwiTGRIDDMLNV 574
Cdd:cd05930 284 -----RPVPpgvpgelyiggaGLARGYLNRPelTaeRFVPNPF--GPGerMYRTGDLVRWLPDGnlEF--LGRIDDQVKI 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd05930 355 RGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYMVPSAFVVLDAL 431
|
570
....*....|...
gi 31980996 655 PKTRSGKIMRRVL 667
Cdd:cd05930 432 PLTPNGKVDRKAL 444
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-669 |
1.29e-38 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 152.93 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 28 GWSPPPEVRRSAHVPSLQRYR-----------------ELHRRSVEEPREFWGNIAKE----FYWKTACpgpFLQYNFDV 86
Cdd:PLN03052 86 AWFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDElslvFSVPPRC---ILDTSDES 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 87 TKGKiftEWMKGATTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVA 164
Cdd:PLN03052 163 NPGG---QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 165 IYMPMILELVVAMLAcarlgalhsIVFAG---------FSAESLCERILDSSCCLLITTDAFYRGEKLVNLKEladesle 235
Cdd:PLN03052 238 IDMPMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYS------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 236 kcrekgfpvRcciVVKhlgraelgmndspSQSP-----PVKRPCPDVQIcwNEGvDLWWHELMQQA-----GDECEPEWC 305
Cdd:PLN03052 302 ---------R---VVE-------------AKAPkaivlPADGKSVRVKL--REG-DMSWDDFLARAnglrrPDEYKAVEQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVF-WCTaDIGWITGHsYVTYGPLANGATSVLFEG 384
Cdd:PLN03052 354 PVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 385 IPTYPDEGRLwsiVDKYKVTKFYTAPTAIRMLMKFGddPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQrcPIVDT 464
Cdd:PLN03052 431 SPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEY 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 465 FWQTETGGHMLTplpgATPMKP---GSASFPFFGVAPAILNESGeelegeaegylvfkQPWP---------GIMRTVYGN 532
Cdd:PLN03052 504 CGGTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFILDDSG--------------NPYPddapctgelALFPLMFGA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 533 HTRF-----ETTYFKKFPGYYVT-----GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHEAVAEAA 598
Cdd:PLN03052 566 SSTLlnadhYKVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DESVLETA 642
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 599 VVGHPHPVKG-ECLYCFVTLCDGHTFSPTLtEELKK----QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN03052 643 AIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-669 |
3.79e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 148.90 E-value: 3.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAfYWEGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 SAESLCERILDSSCCLLITTDAFyrgeklVNLKELADESLEkcrekgfpvrcciVVKHLGRAELGmndSPSQSPPVKRPC 274
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF------LGVDYSATTRLP-------------ALEHVVICETE---EDDPHTEKMKTF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 PDVqicwnegvdlwwheLMQQAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTIGG-YMLY--VATTFKYVFD----- 346
Cdd:PRK07656 148 TDF--------------LAAGDPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAadWAEYLGLTEGdryla 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 347 ----FHpedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDd 422
Cdd:PRK07656 213 anpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPD- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 423 pVTKHSRASLQVLGTVGEPInPEAWLwyHRVVGSQRCPIVDT-FWQTETGGHM-LTPLPGATPMKPGSASFPFFGVAPAI 500
Cdd:PRK07656 275 -RSAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 501 LNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK07656 351 VNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVY 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 581 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsPTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PRK07656 427 PAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNAT 502
|
570
....*....|
gi 31980996 660 GKIMRRVLRK 669
Cdd:PRK07656 503 GKVLKRALRE 512
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-667 |
4.73e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 148.95 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 101 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVL-RKQGIQKGDRVAIYMPMILELVVAMLA 179
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 180 CARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFY-RGEKLVNLKELAdeslekcrekgfpvrcCIVVKHLGRAel 258
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELApKVAPAVGNLRLR----------------HVIVAQYSDY-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 259 gMNDSPSQSPPVK-RPCPDVQICWNEGVDLWwhELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYV 337
Cdd:PRK08314 143 -LPAEPEIAVPAWlRAEPPLQALAPGGVVAW--KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 338 ATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYPDE--GRLwsiVDKYKVTKFYTAPTairM 415
Cdd:PRK08314 220 VGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRWDREaaARL---IERYRVTHWTNIPT---M 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 416 LMKFGDDP-VTKHSRASLQVLGTVGEPInPEAwlwyhrvVGS---QRC--PIVDTFWQTETGGHMLTPLPGATpmKPGSA 489
Cdd:PRK08314 290 VVDFLASPgLAERDLSSLRYIGGGGAAM-PEA-------VAErlkELTglDYVEGYGLTETMAQTHSNPPDRP--KLQCL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 490 SFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTVYGNHTRFETTyFKKFPG--YYVTGDGCRRDQDGYYWIT 565
Cdd:PRK08314 360 GIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFFIT 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 566 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTlTEELKKQIREKIGPIATP 645
Cdd:PRK08314 436 DRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYP 514
|
570 580
....*....|....*....|..
gi 31980996 646 DYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08314 515 RIVEFVDSLPKSGSGKILWRQL 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
167-668 |
2.52e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 146.11 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 167 MPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVnlkELADESLEKCREKgfpvrc 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRAL---PLYSKVVEAAPAK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 247 CIVVKHLGRaelgmndspsqsppvkrpcpDVQICWNEGvDLWWHELMQQA-------GDECEPEWCDAEDPLFILYTSGS 319
Cdd:PLN03051 72 AIVLPAAGE--------------------PVAVPLREQ-DLSWCDFLGVAaaqgsvgGNEYSPVYAPVESVTNILFSSGT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 320 TGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIPTYPDEGRLwsiVD 399
Cdd:PLN03051 131 TGEPKAIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFGKF---VQ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 400 KYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQRcPIVDTFWQTETGGHML--TP 477
Cdd:PLN03051 206 DAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 478 LpgaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHtrfETTYFKKFPGYYVTGDGC 554
Cdd:PLN03051 285 L---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADH---DKVYYKGMPMYGSKGMPL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 555 RRDQD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPVKG-ECLYCFVTLCD-GHTFS 624
Cdd:PLN03051 359 RRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLVIFLVLGEeKKGFD 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 31980996 625 PTLTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PLN03051 439 QARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
136-672 |
1.72e-36 |
|
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: 144.13 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHsiVFAGFS-----AESLCERIlDSSccL 210
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrraeISHFAEQS-EAV--A 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAfYRGeklVNLKELADESLEKCREkgfpVRCCIVVkhlGRAElgmndspsqsppvkrpcpdvqicwnEGVDLwwH 290
Cdd:COG1021 126 YIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV---GDAG-------------------------EFTSL--D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGwitgHSY--- 367
Cdd:COG1021 168 ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPAA----HNFpls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 368 --VTYGPLANGATSVLFEGipTYPDEgrLWSIVDKYKVTkfYTA--PTAIRMLMKFGDDpvTKHSRASLQVLGTVGEPIN 443
Cdd:COG1021 242 spGVLGVLYAGGTVVLAPD--PSPDT--AFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDLSSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 444 PEA----------WLW-----------Y-------HRVVGSQRCP--------IVDtfwqtETGghmlTPLPgatpmkPG 487
Cdd:COG1021 314 PELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG----NPVP------PG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 488 SAsfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnhtrfettYFKKfP----------GYYVTGDGCRRD 557
Cdd:COG1021 379 EV-----GE-------------------LLTRGPY-----TIRG--------YYRA-PehnaraftpdGFYRTGDLVRRT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 558 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcDGHTFSPtltEELKKQI 635
Cdd:COG1021 421 PDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-RGEPLTL---AELRRFL 494
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 31980996 636 REKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:COG1021 495 RER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
132-667 |
4.67e-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: 138.59 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhe 291
Cdd:cd17643 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 292 lmqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYM-LYVATTfkYVFDFHPEDVfwctadigWITGHSYV-- 368
Cdd:cd17643 91 --------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 -----TYGPLANGATSVlfegIPTY-----PDEgrLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGtv 438
Cdd:cd17643 147 fsvweIWGALLHGGRLV----VVPYevarsPED--FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG-- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPeAWL--WYHRVvGSQRCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSASFPFFGVAPAILNESGEELEG 510
Cdd:cd17643 219 GEALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 511 EAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:cd17643 296 VGELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAAL 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 589 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIM 663
Cdd:cd17643 375 ATHPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELL-----PDYMVPAryvplDALPLTVNGKLD 446
|
....
gi 31980996 664 RRVL 667
Cdd:cd17643 447 RAAL 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-671 |
4.00e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 133.76 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 315 YTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPDEG- 392
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNPGl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 393 --RLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvtkhSRASLQVLGTVGEPINPEAwlwYHRVVGSQRCPIVDTFWQTE- 469
Cdd:cd05944 86 fdNFWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 470 TGGHMLTPlPGaTPMKPGSAS--FPFFGVAPAILNESGEELEGEAEGylvfkQPWPGIM--RTVYGNHTRFETTYFKKF- 544
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVGlrLPYARVRIKVLDGVGRLLRDCAPD-----EVGEICVagPGVFGGYLYTEGNKNAFVa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 545 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS 624
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 31980996 625 PT-LTEELKKQIREKigpIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05944 312 EEeLLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
136-667 |
9.25e-34 |
|
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: 135.83 E-value: 9.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYrgeklvnlkeladeslEKCREKGFPVRCC-IVVKHLGRAELGMNDSPSQSPPVkrpcpdVQIcwnegvdlwwhelmq 294
Cdd:cd05904 113 ELA----------------EKLASLALPVVLLdSAEFDSLSFSDLLFEADEAEPPV------VVI--------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 295 qagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYmlyVATTFKYVFDF----HPEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05904 156 -----------KQDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 371 GPLANGATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKfgDDPVTKHSRASLQVLGTVGEPINPEAwlwY 450
Cdd:cd05904 222 GLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKEL---I 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 451 HRVvgSQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSASFPFFGVAPAILNESGEELegeaegyLVFKQP--- 521
Cdd:cd05904 293 EAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES-------LPPNQTgel 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 W---PGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:cd05904 362 WirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAA 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 599 VVGHPHPVKGECLYCFVTLCDGhtfsPTLTE-ELKKQIREKIGP------IATPDYIqnapglPKTRSGKIMRRVL 667
Cdd:cd05904 440 VIPYPDEEAGEVPMAFVVRKPG----SSLTEdEIMDFVAKQVAPykkvrkVAFVDAI------PKSPSGKILRKEL 505
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
137-599 |
2.32e-33 |
|
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: 132.77 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCCLLITT 214
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 DAFyrgeklvnlkeladesLEKCREKGFPVRCCivvkhLGRAELGMNDSPSQSPPVKRPCPDvqicwnegvdlwwhelmq 294
Cdd:TIGR01733 80 SAL----------------ASRLAGLVLPVILL-----DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 295 qagdecepewcdaeDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVfwctadigWITGHSYV------ 368
Cdd:TIGR01733 121 --------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasve 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 -TYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLmkfgdDPVTKHSRASLQVLGTVGEPINPEAW 447
Cdd:TIGR01733 178 eIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL-----AAALPPALASLRLVILGGEALTPALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 448 LWYHRVVGSQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfkQPWP- 523
Cdd:TIGR01733 253 DRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL--------------RPVPv 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 524 -----------GIMRtvyGNHTRFETT--YFKKFPGY-------YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:TIGR01733 317 gvvgelyiggpGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
490
....*....|....*.
gi 31980996 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 |
5.20e-32 |
|
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: 130.83 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 118 GDKVAFYWEGnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LHSI---VFAg 193
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 194 fsaeslcERILdsscclLITTDAfyrGEKLVnlkeLADESLEKCREKGFPVrcCIVVKHLGRAELGmNDSPSQSPPvkrp 273
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAPR--LPTVEHVVVMTDD-AAMPEPAGV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 274 cpdvqicwneGVDLWWHELMQQAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTIGGYMlyvattfKYVF 345
Cdd:cd12119 140 ----------GVLAYEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAALL-------TDGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 346 DFHPEDVF-----------WCTADIGWITGHSYVTYGPlangatsvlfegiptYPDEGRLWSIVDKYKVTKFYTAPTAIR 414
Cdd:cd12119 202 GLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGP---------------YLDPASLAELIEREGVTFAAGVPTVWQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 415 MLMKFGDDpvTKHSRASLQVLgtvgepinpeawlwyhrVVGSQRCP----------IVDTF--W-QTETG--GHMLTPLP 479
Cdd:cd12119 267 GLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSplGTVARPPS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 480 GATP----------MKPGsasFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHtrfETTYFKKFPGY 547
Cdd:cd12119 328 EHSNlsedeqlalrAKQG---RPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKND---EESEALTEDGW 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 548 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtl 627
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA-- 477
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 31980996 628 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd12119 478 -EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
115-669 |
5.64e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 130.93 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWegnepGETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGF 194
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 S---------AESlcerildSSCCLLITTDAFyrgeklvnlkelaDESLEKCREKGFPVRCCIVvkhLGRAELGmndsps 265
Cdd:PRK07470 90 RqtpdevaylAEA-------SGARAMICHADF-------------PEHAAAVRAASPDLTHVVA---IGGARAG------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 266 qsppvkrpcPDVQicwnegvdlwwHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTfkyvf 345
Cdd:PRK07470 141 ---------LDYE-----------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAFVITN----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 346 dfHPEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLFEGIPTYPDEgrLWSIVDKYKVTKFYTAPT 411
Cdd:PRK07470 195 --HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 412 AIRMLMkfgDDP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQrcpIVDTFWQTETGGHMlTPLPGA------TPM 484
Cdd:PRK07470 264 ILKMLV---EHPaVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdaedGPD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 485 -KPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTVYGNHTRFETTYFKkfpgyyvTGDGCRRDQDGY 561
Cdd:PRK07470 337 aRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavFAGYYNNPEANAKAFRDGWFR-------TGDLGHLDARGF 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 562 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGP 641
Cdd:PRK07470 410 LYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGKVAR 486
|
570 580
....*....|....*....|....*...
gi 31980996 642 IATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07470 487 YKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-668 |
7.27e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.49 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG----ALHSIVfagf 194
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrtALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 SAESLCERILDSSCCLLITTDAFYRgeklvnlkELADESLEKCREkgfpvrccivVKHLgraeLGMNDSPsqsppvkrpc 274
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPVP---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 pdvqicwnEGVDLWwhELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFKYvfdfhPED 351
Cdd:PRK06188 145 --------DGVDLL--AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGThrsIATMAQIQLAEWEW-----PAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 352 V-FWCTADIGWITGHSYVtygP-LANGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSr 429
Cdd:PRK06188 210 PrFLMCTPLSHAGGAFFL---PtLLRGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLS- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 430 aSLQVLGTVGEPINP----EAwlwyHRVVGsqrcPI-VDTFWQTETGgHMLTPLP-----GATPMKPGSASFPFFGVAPA 499
Cdd:PRK06188 282 -SLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 500 ILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:PRK06188 352 LLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGF 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK06188 425 NVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLT 501
|
570
....*....|.
gi 31980996 658 RSGKIMRRVLR 668
Cdd:PRK06188 502 ALGKPDKKALR 512
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
137-669 |
4.20e-31 |
|
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: 126.73 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildssCCLLIttdA 216
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---------------------TNPIL---P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 FYRGEKLVNLkeladesLEKCREKGFpvrccIVVKHLGRaelgmnDSPSQSPpvkrpcpdvqicwnegvdlwwhelmqqa 296
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVF-----VVPERFRQ------FDPAAMP---------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 gdecepewcdaEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05903 93 -----------DAVALLLFTSGTTGEPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMK---FGDDPVtkhsrASLQVLGTVGEPINP----EAWlw 449
Cdd:cd05903 161 APVVLQDIW----DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRslarRAA-- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 450 yhRVVGSQRCPIvdtFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimRTV 529
Cdd:cd05903 230 --ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP-----SVF 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 530 YGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05903 300 LGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980996 610 CLYCFVTLCDGHTFS-PTLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05903 380 RACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-669 |
2.07e-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: 126.05 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AfyrgekLVNLKELADESlekcrekgfpvrcCIVVKHLGRAelgmnDSPSQSPPvKRPCPDVqICWNEgvdlwwhelMQQ 295
Cdd:TIGR03098 106 E------RLDLLHPALPG-------------CHDLRTLIIV-----GDPAHASE-GHPGEEP-ASWPK---------LLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGHSYVTYGpLAN 375
Cdd:TIGR03098 151 LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYL-ENRPDDRLLAVLPLSFDYGFNQLTTA-FYV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 376 GATSVLFEgiptYPDEGRLWSIVDKYKVTKFYTAPTairMLMKFGDDPVTKHSRASLQVLGTVGEPInPEAWLWYHRvvg 455
Cdd:TIGR03098 229 GATVVLHD----YLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSGGAM-PRATLSRLR--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 sQRCPIVDTFWQ---TETGGHMLTPlPGATPMKPGS--ASFPFFGVapAILNESGEELEGEAEGYLVFKQPwpgIMRTVY 530
Cdd:TIGR03098 298 -SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEEGELVHRGA---LVAMGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 531 GNHTRFETTYFKKFPGYYV----------TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:TIGR03098 371 WNDPEKTAERFRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 601 GHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:TIGR03098 451 GVPDPTLGQAIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-667 |
2.31e-30 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 124.67 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LcERILDSSCCLLITTDafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvq 278
Cdd:cd05945 80 I-REILDAAKPALLIAD--------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icwnegvdlwwhelmqqaGDecepewcdaeDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTA- 357
Cdd:cd05945 96 ------------------GD----------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAp 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 358 --------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdegrlwsivdkykVTKFYTAPTAIRMLM 417
Cdd:cd05945 147 fsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------ITVWVSTPSFAAMCL 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 418 kfGDDPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRVvgsQRCPIVDTFWQTET----GGHMLTPLPGATpMKPGSASF 491
Cdd:cd05945 204 --LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQRF---PDARIYNTYGPTEAtvavTYIEVTPEVLDG-YDRLPIGY 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 492 PFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHTRFettyFKKFPGY--YVTGDGCRRDQDGYYWITGR 567
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDLVRLEADGLLFYRGR 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 568 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLteELKKQIREKIGPIATPDY 647
Cdd:cd05945 352 LDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTK--AIKAELAERLPPYMIPRR 429
|
570 580
....*....|....*....|
gi 31980996 648 IQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05945 430 FVYLDELPLNANGKIDRKAL 449
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-668 |
3.18e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.92 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDA 216
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 fyrgeklvnlkeLADeslekcrekgfpvrccivvkhlGRAElgmndspsqsppvkrpcpdvqicwneGVDLwwhELMQQA 296
Cdd:PRK09088 104 ------------VAA----------------------GRTD--------------------------VEDL---AAFIAS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 GDECEP---EWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTAD----IGWITGHSYVt 369
Cdd:PRK09088 121 ADALEPadtPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRPV- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 370 ygpLANGATSVLFEGIPTYPDEGRLWSIvdKYKVTKFYTAPtaiRMLMKFGDDPVTKHSR-ASLQVLGTVGEPiNPE--- 445
Cdd:PRK09088 199 ---LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFTGGAP-HAAedi 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 446 -AWLwyhrvvgSQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP-- 521
Cdd:PRK09088 270 lGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnl 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 WPGIMRTVYGNHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:PRK09088 343 SPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 602 HPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK09088 417 MADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
131-668 |
4.32e-30 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 124.76 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCCL 210
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFYRGEklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqSPPVKRPcpdvqicwneGVDLWWH 290
Cdd:cd17651 95 LVLTHPALAGE---------------------------------------------LAVELVA----------VTLLDQP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTfKYVFDFHPEDVFWCTADIGWITGHSYVtY 370
Cdd:cd17651 120 GAAAGADAEPDPA-LDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQ-ARASSLGPGARTLQFAGLGFDVSVQEI-F 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 371 GPLANGATSVLFegiptyPDEGR-----LWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHsrASLQVLGTVGEPINPE 445
Cdd:cd17651 197 STLCAGATLVLP------PEEVRtdppaLAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL--AALRYLLTGGEQLVLT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 446 -------AWLWYHRVVgsqrcpivDTFWQTET---GGHMLTPLPGATPMKPgSASFPFFGVAPAILNEsgeelegeaegy 515
Cdd:cd17651 269 edlrefcAGLPGLRLH--------NHYGPTEThvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVLDA------------ 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 516 lvFKQPWP------------GIMRTVYGN----HTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:cd17651 328 --ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd17651 406 ELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPN 482
|
....*....
gi 31980996 660 GKIMRRVLR 668
Cdd:cd17651 483 GKLDRRALP 491
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-668 |
5.80e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 123.70 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 145 VCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAeslcerildssccLLITTDAFY----RG 220
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNP-------------TLKESVLRYlvadAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 221 EKLVnlkeLADESLEKcrekgfpvrccivvkhlgRAELGMNDSPSqsppvkrpcPDVQIcwneGVDLWWHELMQQAGDEC 300
Cdd:cd05922 70 GRIV----LADAGAAD------------------RLRDALPASPD---------PGTVL----DADGIRAARASAPAHEV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 301 EPEwcdaeDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGpLANGAT 378
Cdd:cd05922 115 SHE-----DLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGAT 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 379 SVLFEGipTYPDEGrLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVtkhSRASLQVLGTVGEPInPEAWLWYHR--VVGS 456
Cdd:cd05922 186 LVLTND--GVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPA---KLPSLRYLTQAGGRL-PQETIARLRelLPGA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 457 QrcpIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHTRF 536
Cdd:cd05922 259 Q---VYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 537 ETTYfKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVT 616
Cdd:cd05922 333 RRKE-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVT 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 31980996 617 LCDGHTFSPTLteelkKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05922 411 APDKIDPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-672 |
6.03e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 122.07 E-value: 6.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK06178 48 QRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFYrgeklvnlkeladESLEKCREkGFPVRCCIVVkhlGRAELgMNDSPSQSPPVKRPCPDVQ 278
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA-------------PVVEQVRA-ETSLRHVIVT---SLADV-LPAEPTLPLPDSLRAPRLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 IcwnEGvdlwWHELMQQAGDECEP---EWCDAEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPED-VFW 354
Cdd:PRK06178 184 A---AG----AIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAAAYAVAVVGGEDsVFL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 CTADIGWITGHSYVTYGPLANGATSVLFegipTYPDEGRLWSIVDKYKVTkfytaptaiRMLMKF-GDDPVTKHSRA--- 430
Cdd:PRK06178 256 SFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVT---------RTVMLVdNAVELMDHPRFaey 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 431 ---SLQVLGTVG--EPINPEAWLWYHRVVGSQrcpIVDTFW-QTET------------GGHMLT--------PLPGA--- 481
Cdd:PRK06178 323 dlsSLRQVRVVSfvKKLNPDYRQRWRALTGSV---LAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefk 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 482 -TPMKPGsASFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTVYGNHTRFETTYFKKfpGYYVTGDG 553
Cdd:PRK06178 400 iCDFETG-ELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEALRD--GWLHTGDI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 554 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKK 633
Cdd:PRK06178 450 GKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQA 526
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 31980996 634 QIREKIGPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PRK06178 527 WCRENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
137-667 |
1.03e-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: 120.09 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCCLLITTD 215
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AfyrgeklvnlkeLADeslekcrekgfPVRCCIVVKHLGRAELGMndSPSQSPPVKRPcpdvqicwnegvdlwwhelmqq 295
Cdd:cd12116 93 A------------LPD-----------RLPAGLPVLLLALAAAAA--APAAPRTPVSP---------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepewcdaEDPLFILYTSGSTGKPKGVVHTIGGY------------------MLYVATtfkYVFDFHPEDVFWcta 357
Cdd:cd12116 126 ------------DDLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT---YAFDISLLELLL--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 358 digwitghsyvtygPLANGATSVLFEGIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvtkhsRASLQVL-G 436
Cdd:cd12116 188 --------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 437 tvGEPINPEawlwyhrvVGSQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSASFPffgVAPAILNESGeelegea 512
Cdd:cd12116 248 --GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IGRPLANTQV------- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 513 egYLV--FKQPWP-GIMRTVY--------GNHTRFETTyFKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:cd12116 303 --YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:cd12116 380 KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVRLD 455
|
570
....*....|....*
gi 31980996 653 GLPKTRSGKIMRRVL 667
Cdd:cd12116 456 ALPLTANGKLDRKAL 470
|
|
| 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 31980996 583 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-670 |
1.55e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 119.68 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhSIVFAG--FSA 196
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 197 ESLCERILDSSCCLLITTDAFyrgeklvnlkelADESLEKCREKgfpvrccivvkhlgraelgmndspsqsppvkrpcpd 276
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF------------EAKLIPGISVK------------------------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 277 vqicwnegvdlwWHELMQQAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWC 355
Cdd:PRK03640 121 ------------FAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 356 TADIGWITGHSYVTygplangaTSVLFeGIPTYpdegrlwsIVDKY------------KVTKFYTAPTAI-RMLMKFGDD 422
Cdd:PRK03640 188 AVPIFHISGLSILM--------RSVIY-GMRVV--------LVEKFdaekinkllqtgGVTIISVVSTMLqRLLERLGEG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 423 PVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgsQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVA 497
Cdd:PRK03640 251 TYPSSFRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 498 PAILNESGEELEGEAEGYLVfKQP--WPGIMRTVYGNHTRFETTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK03640 318 LKIEKDGVVVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISG 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK03640 390 GENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKRFYFVEELP 464
|
570
....*....|....*
gi 31980996 656 KTRSGKIMRRVLRKI 670
Cdd:PRK03640 465 RNASGKLLRHELKQL 479
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
119-674 |
1.90e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 120.16 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFyRG---EKLVNlkELADE--SLEKcrekgfpvrccIVV----------KHLgrAELGMNDS 263
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGfdhAAMAR--RLRPElpALRH-----------VVVvggdgadsfeALL--ITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 264 PSQSPPVKRPCPDvqicwnegvdlwwhelmqqagdecepewcdAEDPLFILYTSGSTGKPKGVVHT----IGGYMLYVAT 339
Cdd:PRK13295 183 PDAPAILARLRPG------------------------------PDDVTQLIYTSGTTGEPKGVMHTantlMANIVPYAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 340 tfkyvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDEGRLWSIVDKYKVTkFYTAPTAirMLMKF 419
Cdd:PRK13295 233 -----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP--FLTDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 420 GDdpVTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGSQrcpIVDTFWQTETGGHMLTpLPGATPMKPG-SASF 491
Cdd:PRK13295 301 TR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDERAStTDGC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 492 PFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:PRK13295 371 PLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PTLTEELKKQireKIGPIATPDYIQN 650
Cdd:PRK13295 445 IIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQYIPERLVV 521
|
570 580
....*....|....*....|....
gi 31980996 651 APGLPKTRSGKIMRRVLRKIAQND 674
Cdd:PRK13295 522 RDALPRTPSGKIQKFRLREMLRGE 545
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-668 |
3.36e-28 |
|
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: 118.24 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:cd17649 2 DAVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkHLGRaelgmndspsqsppvkrpcpdvq 278
Cdd:cd17649 76 LRYMLEDSGAGLLLT--------------------------------------HHPR----------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icwnegvdlwwhelmQQAgdecepewcdaedplFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTAD 358
Cdd:cd17649 95 ---------------QLA---------------YVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFAS 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 359 IGWITGHSYVtYGPLANGAtSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpVTKHSRASLQVLGTV 438
Cdd:cd17649 144 FNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPE-AWLWyhrvvGSQRCPIVDTFWQTETgghMLTPL--PGATPMKPGSASFP----FFGVAPAILNESGEELEGE 511
Cdd:cd17649 221 GEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 512 AEGYLVFKQPwpGIMRtvyGNHTRFETTYfKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd17649 293 VTGELYIGGE--GLAR---GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 583 EVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
....*.
gi 31980996 663 MRRVLR 668
Cdd:cd17649 445 DRKALP 450
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-667 |
3.19e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 116.67 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYrgEKLVNLKELAD-ESLEKCREKGF-PVRCCIVVKHLGRaelgmndspsqsppvKRPCPDVQICWNEGVDLWwhELM 293
Cdd:PRK06710 130 LVF--PRVTNVQSATKiEHVIVTRIADFlPFPKNLLYPFVQK---------------KQSNLVVKVSESETIHLW--NSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 QQAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTIGGYMLYVATTFKYVFD-FHPEDVFWCTADIGWITGHSYVTYG 371
Cdd:PRK06710 191 EKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 372 PLANGATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgDDPVTK-HSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PRK06710 271 SIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 451 HRVVGSQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGI 525
Cdd:PRK06710 344 ETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEIgEIVVKGP--QI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 526 MRtvyGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:PRK06710 414 MK---GYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980996 606 VKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
136-667 |
4.07e-27 |
|
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: 114.88 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTd 215
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 afyrgeklvnlkeladeslekcrekgfpvrccivvkhlgrAELgmndspsqsppvkrpcpdvqicwnegvdlwwhelmqq 295
Cdd:cd05935 81 ----------------------------------------SEL------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepewcdaEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05935 84 ------------DDLALIPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYV 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 376 GATSVLFegipTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfGDDPVTKHSRASLQVLGTVGEPInPEAWLwyHRVVG 455
Cdd:cd05935 151 GGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPM-PPAVA--EKLLK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 SQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGIMRTvYGNHT 534
Cdd:cd05935 222 LTGLRFVEGYGLTETMSQTHTNPPLR--PKLQCLGIP*FGVDARVIDIETGRELPPNEVgEIVVRGP--QIFKG-YWNRP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 535 RFETTYFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 612
Cdd:cd05935 297 EETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVK 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 613 CFVTLCDGhtFSPTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05935 377 AFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
130-667 |
9.45e-27 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 114.53 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 130 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCC 209
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLITTDAfyrgeklvnlKELADESLEKcrekgfpVRCCIVVKHLGRAELGMNDSPSQSPPVKRPcpdvqicwnegvdlww 289
Cdd:cd05923 103 AAVIAVD----------AQVMDAIFQS-------GVRVLALSDLVGLGEPESAGPLIEDPPREP---------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 helmqqagdecepewcdaEDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATTFKYVFDFHpeDVFWCTADIGWITGHS 366
Cdd:cd05923 150 ------------------EQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIGFF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 YVTYGPLANGATSVLfegiPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSraSLQVLGTVGEPInPEA 446
Cdd:cd05923 210 AVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLS--SLRHVTFAGATM-PDA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 447 WLwyHRVVGSQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsasfpFFG---VAPaILNESGEELEGEAEGYLVFKQP- 521
Cdd:cd05923 283 VL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEALANGEEGELIVAAAa 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 ---WPGIMRtvygnhtRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:cd05923 355 daaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980996 599 VVGHPHPVKGECLYCFVTLCDGhtfspTLTEELKKQ--IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05923 428 VIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
118-667 |
1.12e-26 |
|
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: 114.29 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 118 GDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 197
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 198 SLCERILDSSCCLLITT-DAFYRGEKLVNLKELADESLekcrekgfpvrccivvkhlgraelgmnDSPSQSPPVKRPCPD 276
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 277 vqicwnegvdlwwhelmqqagdecepewcdaeDPLFILYTSGSTGKPKGVV---HTIGGYMLYvattFKYVFDFHPEDVF 353
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPKGVMvthAGIVNRLLW----MQDEYPLGPGDRV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 354 WCTADIG-----WitghsyVTYGPLANGATSVLFEgiP-TYPDEGRLWSIVDKYKVTKFYTAPTairMLMKFGDDPvTKH 427
Cdd:cd17646 183 LQKTPLSfdvsvW------ELFWPLVAGARLVVAR--PgGHRDPAYLAALIREHGVTTCHFVPS---MLRVFLAEP-AAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 428 SRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTET----------GGHMLTPLPGATPMkPGSASFpffgVA 497
Cdd:cd17646 251 SCASLRRVFCSGEALPPELAARFLALPG---AELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV-PNTRLY----VL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 498 PAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGY 561
Cdd:cd17646 323 DDALRP----------------VP-VGVPGELYlggvqlarGYLGRPALTA-ERFvpdpfgPGsrMYRTGDLARWRPDGA 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 562 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsPTLTEELKKQIREKIGP 641
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAA--GPDTAALRAHLAERLPE 462
|
570 580
....*....|....*....|....*.
gi 31980996 642 IATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17646 463 YMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-668 |
1.76e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 113.85 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFyrgekLVNLKELADESlekcrEKGFPVRccivvkhlgraelGMNDSPSqsppvkrpcpdvqicwnEGVDLWWH 290
Cdd:PRK08276 87 LIVSAAL-----ADTAAELAAEL-----PAGVPLL-------------LVVAGPV-----------------PGFRSYEE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEWCDAEdplfILYTSGSTGKPKGV--------VHTIGGYMLYVATTFkyvFDFHPEDVFWCTADIGwi 362
Cdd:PRK08276 127 ALAAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGPDSVYLSPAPLY-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 363 tgHSYVT-YG--PLANGATSVLFEGiptYPDEGRLwSIVDKYKVTKFYTAPTA-IRMLmKFGDDPVTKHSRASLQVLGTV 438
Cdd:PRK08276 198 --HTAPLrFGmsALALGGTVVVMEK---FDAEEAL-ALIERYRVTHSQLVPTMfVRML-KLPEEVRARYDVSSLRVAIHA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPE------AWlWyhrvvGsqrcPIVD-TFWQTETGGHMLtplpgATP----MKPGSASFPFFGVApAILNESGEE 507
Cdd:PRK08276 271 AAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSedwlAHPGSVGKAVLGEV-RILDEDGNE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 508 LEGEAEGYLVFKQPWPGImrTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLnVSGHL-LSTAEVES 586
Cdd:PRK08276 335 LPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVnIYPQEIEN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK08276 410 LLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRR 489
|
..
gi 31980996 667 LR 668
Cdd:PRK08276 490 LR 491
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
290-669 |
4.21e-26 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 111.28 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 HELMQQAgDECEPewcDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVT 369
Cdd:cd05912 63 NELAFQL-KDSDV---KLDDIATIMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 370 YGpLANGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLqvLGtvGEPInPEAWLw 449
Cdd:cd05912 138 RS-VIYGMTVYLVDKF----DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 450 yhrvvgsQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAegyLVFKQPwpG 524
Cdd:cd05912 207 -------EQCkekgiPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--N 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 525 IMRTVYG----NHTRFETTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:cd05912 275 VTKGYLNrpdaTEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVV 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 601 GHPHPVKGECLYCFVTLCdghtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05912 348 GIPDDKWGQVPVAFVVSE-----RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-667 |
5.11e-26 |
|
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: 112.29 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGF 194
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 SAESLCERILdsscclLITTDAfyrGEKLVnlkeLADESLEKcrekgfpvrcciVVKHLGRAELGMNDSPSQSPPVKRPC 274
Cdd:cd12117 78 DPELPAERLA------FMLADA---GAKVL----LTDRSLAG------------RAGGLEVAVVIDEALDAGPAGNPAVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 pdvqicwnegvdlwwhelmqqagdecepewCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVfDFHPEDVFW 354
Cdd:cd12117 133 ------------------------------VSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 CTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDEGRLWSIVDKYKVTK-FYTAP-------TAIRMLmkfgddpvtk 426
Cdd:cd12117 181 QTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAlfnqladEDPECF---------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 427 hsrASLQVLGTVGEPINPEawlWYHRVVgsQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGSasfPFFGVAP 498
Cdd:cd12117 249 ---AGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---PIANTRV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 499 AILNesgeelegeaegylVFKQPWP-GIMRTVY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGY 561
Cdd:cd12117 318 YVLD--------------EDGRPVPpGVPGELYvggdglalGYLNRPALTA-ERFvadpfgPGerLYRTGDLARWLPDGR 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 562 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdghTFSPTLT-EELKKQIREKIG 640
Cdd:cd12117 383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV------VAEGALDaAELRAFLRERLP 456
|
570 580
....*....|....*....|....*..
gi 31980996 641 PIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12117 457 AYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-668 |
9.55e-26 |
|
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: 113.80 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsivfA------GFSAESLcERIL- 204
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 205 DSSCCLLITTDAFyrgeklvnLKELADESLEkcrekgfpvrcCIVVkhlgrAELGMNDSPSQSPPVKRpcpdvqicwneg 284
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLAL-----DALALAAEPATNPPVPV------------ 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 285 vdlwwhelmqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVF-WCTA---DIG 360
Cdd:COG1020 615 ---------------------TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR-YGLGPGDRVlQFASlsfDAS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 361 witghsyVT--YGPLANGATSVLfegiptYPDEGR-----LWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVtkhsrASLQ 433
Cdd:COG1020 673 -------VWeiFGALLSGATLVL------APPEARrdpaaLAELLARHRVTVLNLTPSLLRALLDAAPEAL-----PSLR 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 434 VLGTVGEPINPEAWLWYHRVVGSQR---------CPIVDTFWQTETGGHMLTPLP-GAtpmkpgsasfPFFGVAPAILNE 503
Cdd:COG1020 735 LVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiGR----------PIANTRVYVLDA 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 504 sgeelegeaegylvFKQPWP-GimrtVYG-----------------NHT--RFETTYFkKFPG--YYVTGDGCRRDQDG- 560
Cdd:COG1020 805 --------------HLQPVPvG----VPGelyiggaglargylnrpELTaeRFVADPF-GFPGarLYRTGDLARWLPDGn 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 561 --YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREK 638
Cdd:COG1020 866 leF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG---AAAAAALLRLALALL 939
|
570 580 590
....*....|....*....|....*....|
gi 31980996 639 IGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:COG1020 940 LPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-668 |
1.03e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 111.71 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 112 VHEKKLGDKVAFYWegnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVF 191
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 192 AGFSAESLCERILDSSCCLLITTDAFYrgeklvnlkELADESLEKCrekgfP-VRCCIVVKHLGRAE--LGMNDSPSQSP 268
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQC-----PgVRHRLVLDGDGELEgfVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 269 PVkrPCPDVQicwnEGVDLwwhelmqqagdecepewcdaedplfiLYTSGSTGKPKGVV----HTIGGYMLYVATTFKYV 344
Cdd:PRK13391 147 AT--PIADES----LGTDM--------------------------LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 345 FDFHPEDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTA-IRML 416
Cdd:PRK13391 195 WGFRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMfSRML 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 417 mKFGDDPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgsqrCPIVDTFWQTETGGhmltplpGATPM------ 484
Cdd:PRK13391 263 -KLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-------GFTACdseewl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 485 -KPGSASFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTVYgnhtrFET-TYFKKF-------------PGYY 548
Cdd:PRK13391 325 aHPGTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIW-----FEGgRPFEYLndpaktaearhpdGTWS 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 549 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLT 628
Cdd:PRK13391 385 TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALA 464
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 31980996 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13391 465 AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-669 |
1.75e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.02 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAfyrgekLVNLKELADESLEKCRekgfpvrccIVVKHLGRAE---LGMNDSPSQSPPVKRPcp 275
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIVPLLS---------TVVVAGGSSDdsvLGYEDLLAEAGPAHAP-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 276 dvqicwnegVDLwwhelmqqagdecePEwcdaEDPLFILYTSGSTGKPKGVV--HT-IGGYMLYVATTFKYvfdFHPEDV 352
Cdd:PRK07786 169 ---------VDI--------------PN----DSPALIMYTSGTTGRPKGAVltHAnLTGQAMTCLRTNGA---DINSDV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 353 FWCTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgDDPVTK 426
Cdd:PRK07786 219 GFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC---AEQQAR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 427 HSRASLQVLGTVGEPiNPEAWL--WYHRVVGSQrcpIVDTFWQTEtgghmLTPLpgaTPM--------KPGSASFPFFGV 496
Cdd:PRK07786 287 PRDLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKLGSVGKVIPTV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 497 APAILNESGEELEGEAEGYLVFKQPwpgIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSG 576
Cdd:PRK07786 355 AARVVDENMNDVPVGEVGEIVYRAP---TLMSGYWNNPEATAEAFAG--GWFHSGDLVRQDEEGYVWVVDRKKDMIISGG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 577 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLT-EELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK07786 430 ENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALP 506
|
570
....*....|....
gi 31980996 656 KTRSGKIMRRVLRK 669
Cdd:PRK07786 507 RNPAGKVLKTELRE 520
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-667 |
1.77e-25 |
|
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: 110.10 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhe 291
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 292 lmqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGymlyvATTFkyvfdfhpedVFWCTADIG--WITGHSYVT 369
Cdd:cd12115 103 --------------DPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAF----------LQWAAAAFSaeELAGVLAST 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 370 -----------YGPLANGATSVLFEGIPTYPDEGRLwsivdkYKVTKFYTAPTAIRMLMKFGDDPvtkhsrASLQVLGTV 438
Cdd:cd12115 154 sicfdlsvfelFGPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP------ASVRVVNLA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPEAWLWYHRVVGSQRC-----PIVDTFWQTetgGHMLTPLPGATPmkpgSASFPFFGVAPAILNEsgeelegeae 513
Cdd:cd12115 222 GEPLPRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYVLDR---------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 514 gylvFKQPWP------------GIMRTVYGNHT----RFETTYFkkFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:cd12115 285 ----ALQPVPlgvpgelyiggaGVARGYLGRPGltaeRFLPDPF--GPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALP 435
|
570
....*....|..
gi 31980996 656 KTRSGKIMRRVL 667
Cdd:cd12115 436 LTPNGKIDRSAL 447
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
134-667 |
2.04e-25 |
|
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: 110.49 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSaeslcerildssccllit 213
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 214 tdafYRGEKLVNLKELADESLekcrekgfpvrcCIVvkhlgraelgmndspsqsppvkrpcPDVqicwNEGVDlwWHELM 293
Cdd:cd05920 99 ----HRRSELSAFCAHAEAVA------------YIV-------------------------PDR----HAGFD--HRALA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 QQAGDECEpewcdaeDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGwitgHSYVTYGP- 372
Cdd:cd05920 132 RELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPLACPg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 373 ----LANGATSVLfegiPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLM----KFGDDPvtkhsrASLQVLGTVGEPINP 444
Cdd:cd05920 200 vlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLdaaaSRRADL------SSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 445 EAWLWYHRVVGsqrCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSASfpffgvapai 500
Cdd:cd05920 270 ALARRVPPVLG---CTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEEG---------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 501 lnesgeelegeaegYLVFKQPWP--GIMRTVYGNHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHL 578
Cdd:cd05920 337 --------------ELLTRGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 579 LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSPTLTEELKKQIREKigPIAT---PDYIQNAPGLP 655
Cdd:cd05920 397 IAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPDRIEFVDSLP 470
|
570
....*....|..
gi 31980996 656 KTRSGKIMRRVL 667
Cdd:cd05920 471 LTAVGKIDKKAL 482
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-672 |
4.97e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.83 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFyRGEKLVN-LKELADESLEkcrekgfPVRCCIVVkhlgraelgmnDSPSQSPPVKRPCPDVQICwnegvdlww 289
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATPAPAPGARVQLF--------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 hELMQQAGDECEPEWCDAEDPLFILY-TSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYV 368
Cdd:PRK06164 163 -ALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TyGPLANGATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvtkHSRASLQVLGTVGepINPeAWL 448
Cdd:PRK06164 241 L-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFGFAS--FAP-ALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 449 WYHRVVGSQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEgylvf 518
Cdd:PRK06164 310 ELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRA----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 519 kqpwPGIMRTVYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 596
Cdd:PRK06164 385 ----PSLMRGYLDNpdATARALTD----DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAA 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 597 AAVVGHPHPVKGEClYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG---KIMRRVLRKIAQ 672
Cdd:PRK06164 457 AQVVGATRDGKTVP-VAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ 531
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
309-669 |
9.77e-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: 107.76 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 388
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 389 PDEGRLWsivdKYKVTKFYTAPTAIRMLMK---FGDDPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhRVVGSQR 458
Cdd:cd05941 169 EVAISRL----MPSITVFMGVPTIYTRLLQyyeAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 459 cpIVDTFWQTETGGHMLTPLPGatPMKPGSASFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpgimrTVYgnhtrfe 537
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP------SVF------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 538 TTYFKKfP----------GYYVTGDGCRRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd05941 303 KEYWNK-PeatkeeftddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980996 607 KGECLYCFVTLCDGhtfSPTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05941 382 WGERVVAVVVLRAG---AAALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-670 |
2.12e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 107.25 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGalhsivfagfsaeslcerildsscC 209
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVE------------------------C 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLITtdafyrgeklVNLKELADESLEKCREKGFPVRCCivVKHLGRAELGMNDSPSQSPPVkrpcpdvqicWNEGVDlww 289
Cdd:PRK06839 79 IAVP----------LNIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVI----------SITSLK--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 hELMQQAGDECEPEwcDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVT 369
Cdd:PRK06839 134 -EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 370 YGPLANGATSVlfegIPTYPDEGRLWSIVDKYKVTKFYTAPT---AIRMLMKFgddpvTKHSRASLQVLGTVGEPInPEA 446
Cdd:PRK06839 210 FPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVRWFYNGGAPC-PEE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 447 WLwyhRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIM 526
Cdd:PRK06839 280 LM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 527 RTVYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:PRK06839 355 KEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVK 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980996 607 KGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK06839 432 WGEIPIAFIVKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
107-602 |
2.21e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 108.26 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 107 VLDRNVheKKLGDKVAFYWEGNepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 187 HSIVFAGFSAESLcERIL-DSSCCLLITTDAfyrgEKLVNLKELADE--SLEKcrekgfpvrccIVVkhlgraelgMNds 263
Cdd:COG1022 92 TVPIYPTSSAEEV-AYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV---------LD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 264 psqsPPVKRPCPDVqicwnegvdLWWHELMQQAGDECEPEW-------CDAEDPLFILYTSGSTGKPKGVVHTIGGyMLY 336
Cdd:COG1022 145 ----PRGLRDDPRL---------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 337 VATTFKYVFDFHPEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGI-----------PTY----PdegRLW- 395
Cdd:COG1022 211 NARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPdtlaedlrevkPTFmlavP---RVWe 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 396 SIVDKYkVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQvlgtvGEPINPEAWLWY---HRVVGSQrcpivdtfWQTETGG 472
Cdd:COG1022 282 KVYAGI-QAKAEEAGGLKRKLFRWALAVGRRYARARLA-----GKSPSLLLRLKHalaDKLVFSK--------LREALGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 473 HMLTPLPGATPMKPGSASFpFFGV--------------APAILNESGEelegeaegylvFK-----QPWPG--------- 524
Cdd:COG1022 348 RLRFAVSGGAALGPELARF-FRALgipvlegygltetsPVITVNRPGD-----------NRigtvgPPLPGvevkiaedg 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 525 --------IMRtvyGnhtrfettYFKKfP----------GYYVTGD-GcRRDQDGYYWITGRIDDMLNVS-GHLLSTAEV 584
Cdd:COG1022 416 eilvrgpnVMK---G--------YYKN-PeataeafdadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAPQPI 482
|
570
....*....|....*...
gi 31980996 585 ESALVEHEAVAEAAVVGH 602
Cdd:COG1022 483 ENALKASPLIEQAVVVGD 500
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
135-671 |
3.98e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITT 214
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 DAFYRGEKLVNLKELADESLEKCREKGFPVRccivVKHL-GRAELGMNDSPSQsppvkrpcpdvqicwnegvdLWWHELm 293
Cdd:PRK12583 125 DAFKTSDYHAMLQELLPGLAEGQPGALACER----LPELrGVVSLAPAPPPGF--------------------LAWHEL- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 QQAGDECEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTI--GGYMLYVAttfkyvFDFHPEDVFWCTADIGW 361
Cdd:PRK12583 180 QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 ITGHSYVTYGPLANGATsVLFEGIPTYPDEgrLWSIVDKYKVTKFYTAPTairMLMKFGDDPvtKHSRASLQVLGT---V 438
Cdd:PRK12583 254 CFGMVLANLGCMTVGAC-LVYPNEAFDPLA--TLQAVEEERCTALYGVPT---MFIAELDHP--QRGNFDLSSLRTgimA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPEAwlwYHRVVGSQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSASF----PFFGVApaILNESGEELEGEA 512
Cdd:PRK12583 326 GAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVDPDGATVPRGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 513 EGYLVFKqpwpG--IMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK12583 399 IGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK12583 473 HPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
.
gi 31980996 671 A 671
Cdd:PRK12583 550 S 550
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
131-601 |
4.72e-24 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 105.76 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESlCERILDSSCCL 210
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwh 290
Cdd:cd05907 80 ALFVE--------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 elmqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05907 85 ---------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGLY 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 371 GPLANGATSVLFEGIPTYPDEGRlwsivdKYKVTKFYTAP---------------TAIRMLMkfgddpVTKHSRASLQVL 435
Cdd:cd05907 149 VPLLAGARIYFASSAETLLDDLS------EVRPTVFLAVPrvwekvyaaikvkavPGLKRKL------FDLAVGGRLRFA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 436 GTVGEPINPEAWLWYHRvVGsqrCPIVDTFWQTETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGeelegeaegy 515
Cdd:cd05907 217 ASGGAPLPAELLHFFRA-LG---IPVYEGYGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIADDGE---------- 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 516 LVFKQpwPGIMRTVYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDML-NVSGHLLSTAEVESALVEHE 592
Cdd:cd05907 281 ILVRG--PNVMLGYYKNpeATAEALDA----DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASP 354
|
....*....
gi 31980996 593 AVAEAAVVG 601
Cdd:cd05907 355 LISQAVVIG 363
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-668 |
8.09e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.92 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 116 KLGDKVAFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFS 195
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 196 AESlCERILDSS-CCLLITTDAFYrgeklvnlkELADESLekcREKGFPVRCCIVVKhlgraelgmndspSQSPPVkrpc 274
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFY---------PMYRQIQ---QEDATPLRHICLTR-------------VALPAD---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 pdvqicwnEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----IGGYmlY----VATTFKYVF 345
Cdd:PRK08008 148 --------DGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--YsawqCALRDDDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 346 -----DFHPEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYPDEgRLWSIVDKYKVTKFYTAPTAIRMLMKfg 420
Cdd:PRK08008 218 ltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KYSAR-AFWGQVCKYRATITECIPMMIRTLMV-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 421 dDPVTKHSRASL--QVLGTVgePINPEAWLWYHRVVGSQrcpIVDTFWQTETGGHMLTPLPGATPMKPgSASFPFFGVAP 498
Cdd:PRK08008 279 -QPPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 499 AILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:PRK08008 352 EIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK08008 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKVPSYLEIRKDLPRN 506
|
570
....*....|.
gi 31980996 658 RSGKIMRRVLR 668
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
291-669 |
1.06e-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: 105.07 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVVHTIGGYMLyVATTFKYVFDFHPEDVFWCTADI----GWItgh 365
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 366 syVTYGPLANGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgDDPVTKHSRASLQVLGTVGEPINPE 445
Cdd:cd12118 191 --FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLA---NAPPSDARPLPHRVHVMTAGAPPPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 446 AWLWYHRVVGSQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSASFPffGVAPAILNESGEELEGEAEGYLVFKQ---- 520
Cdd:cd12118 262 AVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmk 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 --PWPG------------IMRTVYGNHtrfETTYfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:cd12118 331 pvPRDGktigeivfrgniVMKGYLKNP---EATA-EAFRgGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 586 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRR 665
Cdd:cd12118 407 GVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKF 482
|
....
gi 31980996 666 VLRK 669
Cdd:cd12118 483 VLRD 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-669 |
1.50e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 105.47 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 107 VLDRNVHEkkLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA- 185
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFGAT------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 186 --LHSIVFAGFSAESLCErilDSSCCLLITTD-AFYRGEKLVnlkelADESLEKcrekgfpvrccIVVKHLGRAelgMnd 262
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFE---DHGARVAIVWDkVAPTVERLR-----RTTPLET-----------IVSVNMIAA---M-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 263 spsqsPPVKR-------------------PCPDVqicwnegvdLWWHELMQQA----GDECEPEWCDAEDPLFILYTSGS 319
Cdd:PRK05605 165 -----PLLQRlalrlpipalrkaraaltgPAPGT---------VPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 320 TGKPKGVVHTIGGYMLYVATTFKYVFDF--HPEDV------FwctadigwitgHSY-----VTYGPLAnGATSVLFegiP 386
Cdd:PRK05605 231 TGKPKGAQLTHRNLFANAAQGKAWVPGLgdGPERVlaalpmF-----------HAYgltlcLTLAVSI-GGELVLL---P 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 387 TyPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKfgddpVTKHSRASLQvlgTVGEPINpeawlwyhrvvGSQRCPiVDTF- 465
Cdd:PRK05605 296 A-PDIDLILDAMKKHPPTWLPGVPPLYEKIAE-----AAEERGVDLS---GVRNAFS-----------GAMALP-VSTVe 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 466 -WQTETGGHM-----LT---PLPGATPM----KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVY 530
Cdd:PRK05605 355 lWEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFK 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 531 GNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 610
Cdd:PRK05605 430 GYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 611 LYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05605 510 VVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
289-668 |
2.91e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 104.34 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 WHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGgyMLYV---ATTFKYvfDFHPEDVFWCTADIGwitgH 365
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 366 S---YVTYGP-LANGATSVLfegIPTYPDEGRLwSIVDKYKVTKFYTAPTAIRMLM---KFGDDPVTKHSRAslqvLGTV 438
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVAL---PAKFSASGFL-DDVRRYGATYFNYVGKPLAYILatpERPDDADNPLRVA----FGNE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 439 GEPINPEAWlwyhrvvgSQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSASFPFFGVApaILNESGEelegeaegyl 516
Cdd:PRK13388 275 ASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA--IYNPETL---------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 517 vfkQPWPgimRTVYGNHTRF-----------ETTYFKKFPGYYV---------------TGDGCRRDQDGYYWITGRIDD 570
Cdd:PRK13388 331 ---TECA---VARFDAHGALlnadeaigelvNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTAD 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-TLTEELKKQirEKIGPIATPDYIQ 649
Cdd:PRK13388 405 WMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYVR 482
|
410
....*....|....*....
gi 31980996 650 NAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13388 483 IAADLPSTATNKVLKRELI 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
288-669 |
4.08e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 103.61 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 288 WWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----IGGYMLyvATTFkyvfDFHPEDVFWCTADI--- 359
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCThrkvaSAGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 360 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDegrlwsiVDKYKVTKF--------YTAPTAIRmlmkfGDDP 423
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPD-------VRRYGATYAnyvgkplsYVLATPER-----PDDA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 424 VTkhsraSLQVL-GTVGEPINPEAwlwYHRVVGsqrCPIVDTFWQTEtGGHMLTPLPGaTPmkPGSASFPFFGVA----- 497
Cdd:PRK07867 266 DN-----PLRIVyGNEGAPGDIAR---FARRFG---CVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGVAivdpd 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 498 ------PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:PRK07867 331 tgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDP---EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDW 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPT-LTEELKKQirEKIGPIATPDYIQN 650
Cdd:PRK07867 407 MRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDaFAEFLAAQ--PDLGPKQWPSYVRV 484
|
410
....*....|....*....
gi 31980996 651 APGLPKTRSGKIMRRVLRK 669
Cdd:PRK07867 485 CAELPRTATFKVLKRQLSA 503
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
136-670 |
4.41e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 100.77 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCErildssCCLLITTD 215
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAE------VAAREGVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYRGEKLVNLKELADESLEKCRekgfpvrccivvkhlgraelGMNDSPSQSPPVKRPCPDVQicwnegvdlwwhELMQQ 295
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLR--------------------AWGGNPDDDEPSGSTDETLD------------DLIAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 AGDECEPEWcdAEDPLFILYTSGSTGKPKGVVH-------TIGGYMLYVAttfkyvfdFHPEDVFWCTADIGWITGHSYV 368
Cdd:PRK07788 197 SSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGETTLLPAPMFHATGWAHL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGpLANGATSVL---FEGIPTYPDegrlwsiVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPE 445
Cdd:PRK07788 267 TLA-MALGSTVVLrrrFDPEATLED-------IAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 446 AWLWYHRVVGsqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSASFPFFGVAPAILNESGeelegeaegylvfkQ 520
Cdd:PRK07788 339 LATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENG--------------N 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 PWPG--IMRTVYGNHTRFETtYF-----KKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK07788 396 EVPRgvVGRIFVGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPD 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK07788 475 VVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-667 |
2.17e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.42 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFyrGEKLvnlkeladeslekcrekgfPVRCCIVVKHLGRAELGMnDSPSQSPPVKRPCPdvqicwnegvdlwwh 290
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRPAAWL-EGYSEENPGTELNP--------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 elmqqagdecepewcdaEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFK------------YVFDFHPEDVFWc 355
Cdd:PRK12316 655 -----------------ENLAYVIYTSGSTGKPKGAGNRhraLSNRLCWMQQAYGlgvgdtvlqktpFSFDVSVWEFFW- 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 356 tadigwitghsyvtygPLANGATSVLF-EGIPTYPDegRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPvtkhSRASLQV 434
Cdd:PRK12316 717 ----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLRR 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 435 LGTVGEPINPEAWLwyhRVVGSQ-RCPIVDTFWQTETGghmlTPLPGATPMKPGSASF----PFFGVAPAILNESGeele 509
Cdd:PRK12316 775 IVCSGEALPADAQE---QVFAKLpQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPIANLACYILDANL---- 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 510 geaegylvfkQPWP-GIMRTVY--------GNHTRFETTYFKKFPGYYV-------TGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:PRK12316 844 ----------EPVPvGVLGELYlagrglarGYHGRPGLTAERFVPSPFVagermyrTGDLARYRADGVIEYAGRIDHQVK 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 574 VSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:PRK12316 914 LRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAASLPEYMVPAQWLALER 986
|
570
....*....|....
gi 31980996 654 LPKTRSGKIMRRVL 667
Cdd:PRK12316 987 LPLTPNGKLDRKAL 1000
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
117-670 |
2.64e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 98.29 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 117 LGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 196
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 197 ESLcERILDSSCCLLITTDAfyrgeKLVNLKELADESLekcrekgfpvrccivvkhLGRAELGMNDSPSQSppvkrpcpd 276
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEA-----ALLAALEAADPGD------------------LPLPAVWLLDAPASV--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 277 vqicwneGVDLWWHELMQQAGDECEPEwcdAE----DPLFILYTSGSTGKPKGVVHTiggymlyvattfkyvfdfHPEDV 352
Cdd:PRK06155 155 -------SVPAGWSTAPLPPLDAPAPA---AAvqpgDTAAILYTSGTTGPSKGVCCP------------------HAQFY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 353 FW---CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIPTypdeGRLWSIVDKYKVTKFYTAPTAIRML 416
Cdd:PRK06155 207 WWgrnSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRFSA----SGFWPAVRRHGATVTYLLGAMVSIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 417 MKfgdDPVTKHSRAS-LQV-LGTVGEPINPEAWlwyhrvvgSQRC--PIVDTFWQTETGGHMLTPLPGAtpmKPGSASFP 492
Cdd:PRK06155 283 LS---QPARESDRAHrVRVaLGPGVPAALHAAF--------RERFgvDLLDGYGSTETNFVIAVTHGSQ---RPGSMGRL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 493 FFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFpgYYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:PRK06155 349 APGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKTVEAWRNL--WFHTGDRVVRDADGWFRFVDRIKDAI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK06155 427 RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVA 503
|
570
....*....|....*...
gi 31980996 653 GLPKTRSGKIMRRVLRKI 670
Cdd:PRK06155 504 ALPKTENGKVQKFVLREQ 521
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
309-671 |
2.69e-21 |
|
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: 95.48 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 388
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 389 PDEGRlwsivdkYKVTKFYTAPTAIRMLMkfgDDPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGSQRCPIVDTFWQT 468
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 469 ETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHTRFETTYFKKfPGYY 548
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 549 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsptlT 628
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 31980996 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
134-671 |
4.10e-21 |
|
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: 97.40 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 134 TKITYRELLVQVCQFSNVLRKQGIQkGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSAEslcERILDSSCCL--- 210
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAG---LRELRACIKLagi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 --LITTDAFYRGEKLVNLKELADE----SLEKCREK-GFPVRCcivvkhlgRAELGMNDSPSqsppvkrpcpdvqicwne 283
Cdd:cd05909 80 ktVLTSKQFIEKLKLHHLFDVEYDarivYLEDLRAKiSKADKC--------KAFLAGKFPPK------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 284 gvdlWWHELMQQAGDecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDVFWCTADIGWIT 363
Cdd:cd05909 134 ----WLLRIFGVAPV-------QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 364 GHSYVTYGPLANGAtSVLFEGIPTYPDegRLWSIVDKYKVTKFYTAPTAIRMLMKFgddpVTKHSRASLQVLGTVGEPIN 443
Cdd:cd05909 202 GLTGCLWLPLLSGI-KVVFHPNPLDYK--KIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 444 PEAW-LWYHRvvgsQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPw 522
Cdd:cd05909 275 DTLRqEFQEK----FGIRILEGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 PGIMRTVYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVG 601
Cdd:cd05909 349 PNVMLGYLNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVS 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980996 602 HPHPVKGECLycfvTLCdghTFSPTLT-EELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05909 426 VPDGRKGEKI----VLL---TTTTDTDpSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
136-668 |
1.50e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 95.98 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFyrgeklvnlKELADESLEKCrekgfpvrccivvkhlgraelgmndspsqsppvkrPCPDVQICWNEGVDLWWHELMQQ 295
Cdd:PRK13382 149 EF---------SATVDRALADC-----------------------------------PQATRIVAWTDEDHDLTVEVLIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 AGDECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-IGGYMlyvatTFKYVFDFHPedvfwctadigWITGHSYVTYGPL- 373
Cdd:PRK13382 185 AHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP-----------WRAEEPTVIVAPMf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 374 -ANGATSVLFEG-----IPT---YPDEGRLwSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINP 444
Cdd:PRK13382 248 hAWGFSQLVLAAslactIVTrrrFDPEATL-DLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 445 EAWLWYHRVVGSQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSASFPFFGVAPAILNESgeelegeaegylvFKQ 520
Cdd:PRK13382 327 DVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD-------------FRE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 PWPGIMRTVY-GNHTRFE-----TTyfKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK13382 386 VPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13382 464 VAEAAVIGVDDEQYGQRLAAFVVLKPGASATP---ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
132-665 |
3.70e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.57 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsIVFAgfsaeslceriLDSSccll 211
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ittdafyrgeklvnlkeLAD-ESLEKCREKGfpvrccivvkhlGRAELGMNDSPSQSPPVKRPCPDVQICWNEGVDLWWH 290
Cdd:PRK05852 102 -----------------LPIaEQRVRSQAAG------------ARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEWCDA------EDPLFILYTSGSTGKPKGVVHTIGGymlyVATTFKYV---FDFHPEDVfwCTADIGW 361
Cdd:PRK05852 153 TLSVHLDAATEPTPATStpeglrPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--TVAVMPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 ITGHSYVT--YGPLANGATSVLfegiptyPDEGRL-----WSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQV 434
Cdd:PRK05852 227 YHGHGLIAalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 435 LGTVGEPINPEAWLWYHRVVGSqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSASFPFFGVA-------- 497
Cdd:PRK05852 300 IRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgsdglplp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 498 PAILNesgeelegeaegylvfkQPW---PGIMRTVYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:PRK05852 377 AGAVG-----------------EVWlrgTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcDGHTFSPTlTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:PRK05852 437 GGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPT-AEELVQFCRERLAAFEIPASFQEASGL 513
|
570
....*....|.
gi 31980996 655 PKTRSGKIMRR 665
Cdd:PRK05852 514 PHTAKGSLDRR 524
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
313-668 |
1.35e-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: 92.44 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 313 ILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP--EDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 390
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 391 EGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgsqrcPIVDTFW 466
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 467 Q-TETGGhmLTPLPGATPMK-PGSASFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY--GNHTRFETTYFK 542
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGPGFEYTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 543 KFP------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05929 341 KTAaarnegGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 31980996 617 LCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
137-669 |
2.56e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.12 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDA 216
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 FYRGEKLVNLKELADEslekcrekgfpvrccivVKHLGRAELGMNDSPSQSPPVKRpcpdvQICWNegvdlwwHELMQqa 296
Cdd:PRK06087 131 FKQTRPVDLILPLQNQ-----------------LPQLQQIVGVDKLAPATSSLSLS-----QIIAD-------YEPLT-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 gdecEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:PRK06087 180 ----TAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGIPtyPDEGrlWSIVDKYKVTKFYTA-PTAIRMLMKFGDDPVtkhSRASLQVLGTVGEPInPEawlwyhRVVg 455
Cdd:PRK06087 255 ARSVLLDIFT--PDAC--LALLEQQRCTCMLGAtPFIYDLLNLLEKQPA---DLSALRFFLCGGTTI-PK------KVA- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 sQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgiMRTVY 530
Cdd:PRK06087 320 -RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPN---VFMGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 531 GNHTRfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 610
Cdd:PRK06087 396 LDEPE-LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGER 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 611 LYCFVTLcDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06087 475 SCAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
136-667 |
3.14e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 91.18 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCCLLITt 214
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 dafyrgeklvnlkelaDESLEKCREKGFPVRccivvkhlgrAELGMNDSPSQSPPVKRPCPDvqicwnegvdlwwhelmq 294
Cdd:cd12114 91 ----------------DGPDAQLDVAVFDVL----------ILDLDALAAPAPPPPVDVAPD------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 295 qagdecepewcdaeDPLFILYTSGSTGKPKGVV--H-----TIGgymlyvATTFKYVFDfhPEDVFWCTA---------D 358
Cdd:cd12114 127 --------------DLAYVIFTSGSTGTPKGVMisHraalnTIL------DINRRFAVG--PDDRVLALSslsfdlsvyD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 359 IgwitghsyvtYGPLANGATSVLfegiptyPDEGRL-----W-SIVDKYKVTKFYTAPTAIRMLMKFGDDPvtkhsrasl 432
Cdd:cd12114 185 I----------FGALSAGATLVL-------PDEARRrdpahWaELIERHGVTLWNSVPALLEMLLDVLEAA--------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 433 qvlgtvgepinpeawlwyHRVVGSQRCPIV----------DTFWQTETGGHmLTPLPGAT------------PMKPGSAS 490
Cdd:cd12114 239 ------------------QALLPSLRLVLLsgdwipldlpARLRALAPDAR-LISLGGATeasiwsiyhpidEVPPDWRS 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 491 FPFfGVAPA-----ILNESgeelegeaegylvfKQPWP------------GIMRTVYGNHTRFETTYFKKFPG--YYVTG 551
Cdd:cd12114 300 IPY-GRPLAnqryrVLDPR--------------GRDCPdwvpgelwiggrGVALGYLGDPELTAARFVTHPDGerLYRTG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 552 D-GCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTfsPTLTEE 630
Cdd:cd12114 365 DlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGT--PIAPDA 440
|
570 580 590
....*....|....*....|....*....|....*..
gi 31980996 631 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12114 441 LRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
113-668 |
3.27e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.49 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 113 HEKKLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFA 192
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 193 GFSAESLCerildsscclLITTDAfyrGEKLVnlkeLADESLEKCREKGFPVrccIVVkhlgraelgmnDSPSQSppvkr 272
Cdd:PRK06145 85 RLAADEVA----------YILGDA---GAKLL----LVDEEFDAIVALETPK---IVI-----------DAAAQA----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 273 pcpDVQIcwnegvdlwwhelMQQAGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTIGgymlyvattfkyvfdfhpeD 351
Cdd:PRK06145 129 ---DSRR-------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------N 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 352 VFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG-----IPTYPDEGRLWSIvDKYKVTKFYTAPTAI-RM 415
Cdd:PRK06145 174 LHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlriHREFDPEAVLAAI-ERHRLTCAWMAPVMLsRV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 416 LMkfgddpVTKHSRASLQVLGTV--GEPINPEAWLwyhRVVGS--QRCPIVDTFWQTET-GGHMLTPlPGATPMKPGSAS 490
Cdd:PRK06145 253 LT------VPDRDRFDLDSLAWCigGGEKTPESRI---RDFTRvfTRARYIDAYGLTETcSGDTLME-AGREIEKIGSTG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDD 570
Cdd:PRK06145 323 RALAHVEIRIADGAGRWLPPNMKGEICMRGP-----KVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKD 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQN 650
Cdd:PRK06145 398 MIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKV 474
|
570
....*....|....*...
gi 31980996 651 APGLPKTRSGKIMRRVLR 668
Cdd:PRK06145 475 RDELPRNPSGKVLKRVLR 492
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
133-667 |
3.95e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 90.60 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLI 212
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 213 Ttdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhel 292
Cdd:cd17650 90 T------------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 293 mqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYM-LYVATTFKYVFDFHPE----------DVFwcTADIGW 361
Cdd:cd17650 91 -------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVrllqmasfsfDVF--AGDFAR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 itghsyvtygPLANGATSVLfegIP--TYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVG 439
Cdd:cd17650 156 ----------SLLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 440 EPINPEAWLwYHRVVGSQRcpIVDTFWQTET--------GGhmLTPLPGATPMKPGSasfPFFGVAPAILNESGeelege 511
Cdd:cd17650 223 CKAQDFKTL-AARFGQGMR--IINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL------ 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 512 aegylvfkQPWP-GIMRTVY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:cd17650 289 --------QPQPvGVAGELYiggagvarGYLNRPELTA-ERFvenpfaPGerMYRTGDLARWRADGNVELLGRVDHQVKI 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 575 SGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdghtfSPTLTEELKKQIREKIGPIATPDYIQNA 651
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA-------ATLNTAELRAFLAKELPSYMIPSYYVQL 431
|
570
....*....|....*.
gi 31980996 652 PGLPKTRSGKIMRRVL 667
Cdd:cd17650 432 DALPLTPNGKVDRRAL 447
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
132-673 |
8.81e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 89.84 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITtDAFYrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgMNDSPSQSPPVkrpcpdvqICWNEgvdlwWHE 291
Cdd:PRK07638 102 VT-ERYK-----------------------------------------LNDLPDEEGRV--------IEIDE-----WKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 292 LMQQAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTfkyVFDFH--PEDVFWctadigwITG---H 365
Cdd:PRK07638 127 MIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCN---VHDFHmkREDSVL-------IAGtlvH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 366 SYVTYGplangATSVLFEG-----IPTY-PDEGRLWsiVDKYKVTKFYTAPTAIRMLMK---FGDDPVT------KHSRA 430
Cdd:PRK07638 196 SLFLYG-----AISTLYVGqtvhlMRKFiPNQVLDK--LETENISVMYTVPTMLESLYKenrVIENKMKiissgaKWEAE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 431 SLQVLGTvgepINPEAWLWyhrvvgsqrcpivdTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeeleg 510
Cdd:PRK07638 269 AKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAG----- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 511 eaegylvfKQPWPGIMRTVYGNHTRFettyfkkFPGYYVTGDGCRR---------------DQDGYYWITGRIDDMLNVS 575
Cdd:PRK07638 326 --------EEVQKGEIGTVYVKSPQF-------FMGYIIGGVLARElnadgwmtvrdvgyeDEEGFIYIVGREKNMILFG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSptltEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK07638 391 GINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
570
....*....|....*...
gi 31980996 656 KTRSGKIMRRVLRKIAQN 673
Cdd:PRK07638 464 YTNSGKIARMEAKSWIEN 481
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
115-667 |
1.61e-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: 89.31 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 SAESLcERILDSSccllittdafyrGEKLVnlkeLADESLEKCRekgfpvrccivvKHLGRAELgMNDSPSQSppvkrpc 274
Cdd:cd17655 82 PEERI-QYILEDS------------GADIL----LTQSHLQPPI------------AFIGLIDL-LDEDTIYH------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 pdvqicwnegvdlwwhelmqQAGDECEPEwCDAEDPLFILYTSGSTGKPKGV----------VHTIGGYM-----LYVAT 339
Cdd:cd17655 125 --------------------EESENLEPV-SKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWANKVIyqgehLRVAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 340 TFKYVFDFHPEDVFwctadigwitghsyvtyGPLANGATSVLfegiptYPDEGR-----LWSIVDKYKVTKFYTAPTAIR 414
Cdd:cd17655 184 FASISFDASVTEIF-----------------ASLLSGNTLYI------VRKETVldgqaLTQYIRQNRITIIDLTPAHLK 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 415 MLmkfgdDPVTKHSRASLQVLGTVGEPINPE-AWLWYHRVVGSqrCPIVDTFWQTETG-GHMLTPLpgaTPMKPGSASFP 492
Cdd:cd17655 241 LL-----DAADDSEGLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSVP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 493 ffgVAPAILNESGeelegeaegYLVFK--QPWP-GIMRTVY--------GNHTRFETTYfKKF------PG--YYVTGDG 553
Cdd:cd17655 311 ---IGKPLGNTRI---------YILDQygRPQPvGVAGELYiggegvarGYLNRPELTA-EKFvddpfvPGerMYRTGDL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 554 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdghTFSPTLT-EELK 632
Cdd:cd17655 378 ARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI------VSEKELPvAQLR 451
|
570 580 590
....*....|....*....|....*....|....*
gi 31980996 633 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17655 452 EFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
309-664 |
4.31e-18 |
|
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: 85.92 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTiggYMLYVATtfkyvfdfhpedvFWCTADIGWITGHSYVTY-GPLA-----NGATSVLF 382
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRS---ERSWIES-------------FVCNEDLFNISGEDAILApGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 383 EG----IPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFgDDPVTKhsrasLQVLGTVGEPINPEAwlwyHRVV--GS 456
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLknIF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 457 QRCPIVDTFWQTETGghMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHTRF 536
Cdd:cd17633 135 PKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 537 ETTY----FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLY 612
Cdd:cd17633 195 FSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IA 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 31980996 613 CFVTLCDGHTFsPTLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17633 274 VALYSGDKLTY-KQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
546-668 |
5.30e-18 |
|
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: 86.18 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE 309
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31980996 626 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05917 310 ---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-684 |
6.14e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDafyrgeklvnlkeladeslekcrekgfpvrccivvkHLgraelgmndSPSQSPPVKRPCPDVQ 278
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQS------------------------------------HL---------RLPLAQGVQVLDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icwnegvdlwwhelMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVV--------HTIGGYMLYVATTFKYVFDFHPE 350
Cdd:PRK12316 3181 --------------DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVLQFTTF 3246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 351 DvfwctadigwITGHSYVTYGPLANGATSVLfEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgdDPVTKHSRA 430
Cdd:PRK12316 3247 S----------FDVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 431 SLQVLGTVGEPINPEAwlwYHRVVGSQrcPIVDTFWQTETgghmlTPLPGATPMKPGSASFPFFGVAPAILNESGEELEG 510
Cdd:PRK12316 3312 SLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSL 3381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 511 EAEGYLVFKQPWPGIMRTVYGNHTR-------FETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 584 VESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTR 658
Cdd:PRK12316 3462 IEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflERMPLTP 3529
|
570 580
....*....|....*....|....*.
gi 31980996 659 SGKIMRRVLRKIaqnDHDLGDTSTVA 684
Cdd:PRK12316 3530 NGKLDRKALPRP---DAALLQQDYVA 3552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
546-668 |
7.82e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 87.42 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 625
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31980996 626 TLT-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 ... |
298-669 |
1.03e-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: 86.72 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 298 DECepewcdaeDPLFILYTSGSTGKPKGVVHT-IGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVtYGPLANG 376
Cdd:cd05915 151 PER--------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGIPTypDEGRLWSIVdKYKVTKFYTAPTAIRMLMKfGDDPVTKHSRASLQVLGTVGEPinPEAWL-----WYH 451
Cdd:cd05915 222 AKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALAD-YLESTGHRLKTLRRLVVGGSAA--PRSLIarferMGV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 452 RVVGSQRCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGI 525
Cdd:cd05915 296 EVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 526 MRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:cd05915 371 TGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHP 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 606 VKGECLYCFVTLCDGHTFSptltEELKKQIREKIGPIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05915 449 KWQERPLAVVVPRGEKPTP----EELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
306-672 |
1.81e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.23 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVV--HTiGGYMLYVATTFKYVFDFHPedVFWCTADIGWITGHSYvTYGPLANGATSVLFE 383
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTF-TWGTAARGGTSVCMR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 384 GIpTYPDegrLWSIVDKYKVTKFYTAPTAIRMLMKfGDDPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGSQrcpIVD 463
Cdd:PLN03102 260 HV-TAPE---IYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ---VMH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 464 TFWQTETGGHML--------TPLPGATPMK-PGSASFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGIMRTvY 530
Cdd:PLN03102 330 AYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SIMKG-Y 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 531 GNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 610
Cdd:PLN03102 407 LKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 611 LYCFVTLCDGHT-----FSPTLTEE--LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN03102 485 PCAFVVLEKGETtkedrVDKLVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
137-667 |
3.25e-17 |
|
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: 84.61 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTda 216
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 217 fyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelmqqa 296
Cdd:cd17652 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 297 gdecepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLAnG 376
Cdd:cd17652 92 ----------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-G 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 377 ATSVLFEGIPTYPDEGrLWSIVDKYKVTkFYTAPTAIRMLMKFGDDPvtkhsraSLQVLGTVGEPINPE-AWLWyhrvvg 455
Cdd:cd17652 160 ATLVLAPAEELLPGEP-LADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------ 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 SQRCPIVDTFWQTET--GGHMLTPLPGATPMKPGSasfPFFGVAPAILNESGeelegeaegylvfkQPWP---------- 523
Cdd:cd17652 225 APGRRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpgvpgelyia 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 524 --GIMRtvyGNHTRFETTYfKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:cd17652 288 gaGLAR---GYLNRPGLTA-ERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17652 364 GVAEAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
131-673 |
5.00e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 84.65 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKI-TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCC 209
Cdd:PLN02246 45 GATGRVyTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLITTDAFYrgEKLVNLKEladeslekcrEKGFPVRCCivvkhlgraelgmnDSPsqsppvkrpcpdVQICwnegvdLWW 289
Cdd:PLN02246 125 LIITQSCYV--DKLKGLAE----------DDGVTVVTI--------------DDP------------PEGC------LHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 HELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAttfKYV------FDFHPEDVFWCTADIGWIT 363
Cdd:PLN02246 161 SELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 364 GHSYVTYGPLANGATSVLfegIPTYpDEGRLWSIVDKYKVTkfyTAPTAIRMLMKFGDDP-VTKHSRASLQVLGTVGEPI 442
Cdd:PLN02246 238 SLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 443 NPEawlwYHRVVGSqRCP---IVDTFWQTETGGHMLTPLPGA---TPMKPGSAsfpffgvAPAILNESGEELEGEAEGYL 516
Cdd:PLN02246 311 GKE----LEDAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELKIVDPETGASL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 517 VFKQPW------PGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PLN02246 379 PRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELK----KQI--REKIGPIATPDYIqnapglPKTRSGKIMR 664
Cdd:PLN02246 457 HPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI------PKAPSGKILR 527
|
570
....*....|
gi 31980996 665 RVLR-KIAQN 673
Cdd:PLN02246 528 KDLRaKLAAG 537
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-669 |
5.19e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITT 214
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 DAFYrgEKLVNLKELADESLEKCRE-KGFPvrccivvkhlgraelgmndspSQSPPVKrpcpdvqicwnegvdlwwhelm 293
Cdd:PRK12316 4656 SHLL--QRLPIPDGLASLALDRDEDwEGFP---------------------AHDPAVR---------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 qqagdecepewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPED-VFWCTA---DI---GWitghs 366
Cdd:PRK12316 4691 -----------LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER-YELTPDDrVLQFMSfsfDGsheGL----- 4753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 367 yvtYGPLANGAtSVLFEGiPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKfgdDPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:PRK12316 4754 ---YHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE---HAERDGEPPSLRVYCFGGEAVAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 447 W-LWY--------HRVVGSQRCPIVDTFWQTETGghmltPLPGATPMKPGSasfPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:PRK12316 4826 YdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 518 FKQPwpGIMRtvyGNH-------TRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK12316 4898 LGGE--GVAR---GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 589 VEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTFSPTLTE-ELKKQIREKIGPiATPDYIQNA-----PGLPKTRSGKI 662
Cdd:PRK12316 4972 REHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADEAQaELRDELKAALRE-RLPEYMVPAhlvflARMPLTPNGKL 5049
|
....*..
gi 31980996 663 MRRVLRK 669
Cdd:PRK12316 5050 DRKALPQ 5056
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
107-686 |
5.58e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.93 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 107 VLDRNVHekKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 187 HSIVFAGFSAESL--CERILDSSccLLITtdafyrGEKLVnlkeladESLEKCREkgfpvrccivvkHLGRAelgmndsp 264
Cdd:PRK08279 114 VALLNTQQRGAVLahSLNLVDAK--HLIV------GEELV-------EAFEEARA------------DLARP-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 265 sqsppvkrpcpdvQICWNEGVD-----LWWHELMQQAG--DECEPEWCD---AEDPLFILYTSGSTGKPKGVVHTIGGYM 334
Cdd:PRK08279 159 -------------PRLWVAGGDtlddpEGYEDLAAAAAgaPTTNPASRSgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 335 LYVAtTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEGiptypdeGRLWSIVDKYKVTKFYtapt 411
Cdd:PRK08279 226 KAMG-GFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFSA-------SRFWDDVRRYRATAFQ---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 412 AI----RMLMkfgDDPVTKHSRA-SLQVLgtVGEPINPEAW--------------LW--------------YHRVVGsqR 458
Cdd:PRK08279 294 YIgelcRYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFDGTVG--R 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 459 CP--------IVDtfWQTETGghmlTPLPGA----TPMKPGSAsfpffGVAPAILNEsgeelegeaegylvfKQPWPG-- 524
Cdd:PRK08279 367 VPlwlahpyaIVK--YDVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD---------------RGPFDGyt 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 525 --------IMRTVygnhtrfettyFKKFPGYYVTGDGCRRDQDGYYWITGRIDDML-----NVsghllSTAEVESALVEH 591
Cdd:PRK08279 421 dpeasekkILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGF 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 592 EAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSPTlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK08279 485 PGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKE 561
|
650
....*....|....*.
gi 31980996 671 AQNDHDLGDTSTVADP 686
Cdd:PRK08279 562 GFDPSKVDDPLYVLDP 577
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-668 |
7.06e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 84.70 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 107 VLDRNVHEKKLGDKVAFYwegnepgETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 187 HSIVFAGFSAESLCERILDSSCCLLITTDAF---YRGEKLVNLKELADESlekcrekgfpvrccivvkhlGRAElgmnds 263
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 264 PSQSPPVkrpcpdvqicwnegvdlwwhelmqqAGDECEpewcdaedplFILYTSGSTGKPKGVVHTIGGYMLYVATTFKY 343
Cdd:PRK06060 136 PGGYEPM-------------------------GGDALA----------YATYTSGTTGPPKAAIHRHADPLTFVDAMCRK 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 344 VFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfEGIPTYPDEGRLWSIvdKYKVTKFYTAPTAIRMLMkfgdDP 423
Cdd:PRK06060 181 ALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA--RFGPSVLYGVPNFFARVI----DS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 424 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqrCPIVDTFWQTETGGHMLTPlpGATPMKPGSAS--FPFFG---VAP 498
Cdd:PRK06060 254 CSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGrvLPPYEirvVAP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 499 AILNESgeelegeaegylvfkqpwPGIMRTVYGNHTRFETTYFKKfP-------GYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:PRK06060 330 DGTTAG------------------PGVEGDLWVRGPAIAKGYWNR-PdspvaneGWLDTRDRVCIDSDGWVTYRCRADDT 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNA 651
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVV 470
|
570
....*....|....*..
gi 31980996 652 PGLPKTRSGKIMRRVLR 668
Cdd:PRK06060 471 DRLPRTPNGKLVRGALR 487
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-671 |
8.68e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 84.16 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQF-SNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 194 FSAESLCERILDSSCCLLITTDAFYRGEKLVnlkeLADESLEKCREK------GFPVRCCI--VVKHlgraelgmndsps 265
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 266 qsppVKRPCPDVQIcwnEGVDLWWHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVvhtiggyMLyvatTFKYVF 345
Cdd:PRK08751 173 ----VKKLVPEYRI---NGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGA-------ML----THRNLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 346 DFHPEDVFWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGIPTYPDEGR-LWSIVDKYKVTKFyTAPTAIRML 416
Cdd:PRK08751 235 ANMQQAHQWLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGGCNHLISNPRdMPGFVKELKKTRF-TAFTGVNTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 417 M-KFGDDP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETgghmlTPLPGATPMK----PGSAS 490
Cdd:PRK08751 314 FnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG---LTLVEAYGLTET-----SPAACINPLTlkeyNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDD 570
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPTLT-EELKKQIREKIGPIATPDYIQ 649
Cdd:PRK08751 462 MILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANLTGYKQPRIIE 536
|
570 580
....*....|....*....|..
gi 31980996 650 NAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08751 537 FRKELPKTNVGKILRRELRDAA 558
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
290-670 |
8.83e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 HELMQQAGDEC-EPEWC-----DAEDPLFILYTSGSTGKPKGVVHTIGG-----------YMLYVATT----FKYVFDFH 348
Cdd:PRK12467 3213 TALTLDRLDLNgYSENNpstrvMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGA 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 349 PEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDEgrLWSIVDKYKVTKFYTAPTAIRMLMKFGDdpvtKHS 428
Cdd:PRK12467 3293 QERFLW-----------------TLICGGCLVVRDNDLWDPEE--LWQAIHAHRISIACFPPAYLQQFAEDAG----GAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 429 RASLQVLGTVGEPINPEAWLWYHRVV---------GSQRCPIVDTFWQTETGGhmlTPLPGATPMkpgsaSFPFFGVAPA 499
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPI-----GRPVAGRSIY 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 500 ILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYY 562
Cdd:PRK12467 3422 VLDGQL--------------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVI 3487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 563 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSPTLTEELKKQIREKIgpi 642
Cdd:PRK12467 3488 EYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL--- 3560
|
410 420 430
....*....|....*....|....*....|...
gi 31980996 643 atPDYIQNA-----PGLPKTRSGKIMRRVLRKI 670
Cdd:PRK12467 3561 --PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
308-664 |
8.84e-17 |
|
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: 82.31 E-value: 8.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 308 EDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 387
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 388 YPDegrLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpvTKHSRASLQVLGTVGE-PINPEA--WLWYHRVvgsqrcPIVDT 464
Cdd:cd17635 80 YKS---LFKILTTNAVTTTCLVPTLLSKLVSELKS--ANATVPSLRLIGYGGSrAIAADVrfIEATGLT------NTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 465 FWQTETGGHMLTPLpGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHTRFETTYFKkf 544
Cdd:cd17635 149 YGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLID-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 545 pGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtfS 624
Cdd:cd17635 224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA------S 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 31980996 625 PTLTEE----LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17635 297 AELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
129-668 |
1.72e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 82.75 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 129 EPGETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSC 208
Cdd:PRK13390 20 ETGEQ--VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 209 CLLITTDAfyrgeklvnLKELADESlekcrEKGFPVRCCIVVKHLGRAELGMNDSPSQSPPVKRPCPDVqicwnegvdlw 288
Cdd:PRK13390 98 RVLVASAA---------LDGLAAKV-----GADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPCGAV----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 whelmqqagdecepewcdaedplfILYTSGSTGKPKGV--------VHTIGGYMLYVATTFkyvFDFHPEDVFWCTADIG 360
Cdd:PRK13390 153 ------------------------MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 361 witgHSyvtyGPL-------ANGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQ 433
Cdd:PRK13390 206 ----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 434 VLGTVGEPINPEA------WLWyhrvvgsqrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSASFPFFGVApAILNESGE 506
Cdd:PRK13390 274 AVIHAAAPCPVDVkhamidWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDL-HICDDDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 507 ELEGEAEGYLVFKQPwpgimRTVYGNHTRFETTYFKKFPG---YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:PRK13390 342 ELPAGRIGTVYFERD-----RLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 584 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:PRK13390 417 TENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLV 496
|
....*
gi 31980996 664 RRVLR 668
Cdd:PRK13390 497 KGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-669 |
1.73e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYrgEKLVNLKELADESLEkcrekgfpvrccivvkhlgrAELGMNDSPSQSPPVKrpcpdvqicwnegvdlwwhelmqq 295
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLD--------------------RDAEWADYPDTAPAVQ------------------------ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 agdecepewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVtYGPLAN 375
Cdd:PRK12316 2143 ---------LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQW-FHPLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 376 GATSVLFEGipTYPDEGRLWSIVDKYKVTKFYTAPTairMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:PRK12316 2212 GARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 456 SQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSASFPFFGVAPA-----ILNESGEELEGEAEGYLVFKQPwpGIMRTV 529
Cdd:PRK12316 2287 PVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayILDADLNLLAPGMAGELYLGGE--GLARGY 2359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 530 YG----NHTRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:PRK12316 2360 LNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDG 2439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 605 PvKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK12316 2440 A-SGKQLVAYVVPDDAAEDLL---AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-670 |
2.21e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.97 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITt 214
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 dafyrgeklvnlkelADESLEKCREKGFPVrccivvkhLGRAELGMNDSPSQSPPVkrpcpdvqicwnegvdlwWHELMQ 294
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV--------IGVPENYDFDSKRIEFPK------------------FYELIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 295 QAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP----EDVFWCTADIGWITGHSYVTY 370
Cdd:PLN02574 185 EDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYGLSLFVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 371 GPLANGATSVLFEGIptypDEGRLWSIVDKYKVTKFYTAPTAIRMLMKfGDDPVTKHSRASLQVLGTVGEPInpeawlwY 450
Cdd:PLN02574 265 GLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPL-------S 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 451 HRVVGS--QRCPIVDtFWQtetgGHMLTPLPGATPMKPGSASFPFFG----VAPAILNESGEELEGEAEGYLVFKQPW-- 522
Cdd:PLN02574 333 GKFIQDfvQTLPHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSsvglLAPNMQAKVVDWSTGCLLPPGNCGELWiq 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 -PGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:PLN02574 408 gPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 602 HPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PLN02574 486 VPDKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
308-670 |
4.02e-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: 81.80 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 308 EDPLFILYTSGSTGKPKGVVHT--------------IGGYMLYVATTFKYVFDFHpeDVFWCTADIGWITGhsyvtygpl 373
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 374 anGATSVLfegIPTYPDEGRLWSIVDkYKVTKFYTAPTAIRMLMKfgDDPVTKHSRASLQVLGTVGEPINPEawlwyhrv 453
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 454 VGSQ-----RCPIV-DTFWQTETGGHML-TPlpgATPMKPGSAS--FPFFGvAPAILNESGEELEGEAEGYLVFKQpwPG 524
Cdd:cd17642 317 VGEAvakrfKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVGkvVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 525 IMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd17642 391 IMKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980996 605 PVKGECLYCFVTLCDGHtfspTLTEelkKQIREKIGPIATPDY-----IQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:cd17642 469 EDAGELPAAVVVLEAGK----TMTE---KEVMDYVASQVSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
546-674 |
4.39e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.92 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE 495
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31980996 626 tltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 674
Cdd:PRK08162 496 ---EEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
309-664 |
4.87e-16 |
|
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: 80.01 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 388
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 389 pDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgdDPVTKHSR--ASLQVLGTVGEPINPEAWlwyHRVVGSqrcpivdTFW 466
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSFPPILSNLL----DAAEKSGVdlSSLRHVLGLDAPETIQRF---EETTGA-------TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 467 ----QTETGGhMLTPLPGATpmKPGSASFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWPGIMRTvygNHTrf 536
Cdd:cd17637 141 slygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYWNLPELT---AYT-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 537 ettyFKKfpGYYVTGDGCRRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 614
Cdd:cd17637 213 ----FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 31980996 615 VTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17637 287 CVLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
136-668 |
6.62e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 81.22 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTD 215
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 AFYRGEKLV----NLKELADESL-EKCREKGFPVRccIVVKHLGRAelgmndSPSQSPPVKRPCPDVqicwnegvdlwwh 290
Cdd:PRK07059 129 NFATTVQQVlaktAVKHVVVASMgDLLGFKGHIVN--FVVRRVKKM------VPAWSLPGHVRFNDA------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 eLMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFKYVFDF--HPEDVFWCTA----DIGW 361
Cdd:PRK07059 188 -LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLhrnIVANVLQMEAWLQPAFEKkpRPDQLNFVCAlplyHIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 362 ITGHSYVTygpLANGATSVLfegIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLG--TVG 439
Cdd:PRK07059 267 LTVCGLLG---MRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGgmAVQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 440 EPInPEAWLwyhRVVGsqrCPIVDTFWQTETGGhMLTPLPGATPMKPGSASFPFFGVAPAILNESGEElegeaegyLVFK 519
Cdd:PRK07059 341 RPV-AERWL---EMTG---CPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGND--------LPLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 520 QPW------PGIMRtvyGNHTRFETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:PRK07059 405 EPGeicirgPQVMA---GYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 593 AVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07059 482 GVLEVAAVGVPDEHSGEAVKLFVVKKD-----PALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-669 |
8.05e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITtd 215
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 afyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndSPSQSPPVKRPCPDVQICWNEGVDLWWHelmqQ 295
Cdd:PRK12467 616 -----------------------------------------------QSHLLAQLPVPAGLRSLCLDEPADLLCG----Y 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 296 AGDECEPewcdAEDP---LFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHsYVTYGP 372
Cdd:PRK12467 645 SGHNPEV----ALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGA 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 373 LANGATsVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMkfgDDPVTKHSRASLQVLgtVGEPINPEAWLWYHR 452
Cdd:PRK12467 719 LASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALL---QASRVALPRPQRALV--CGGEALQVDLLARVR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 453 VVGSQrCPIVDTFWQTETGGHMLT-PLPGATpmKPGSASF---PFFGVAPAILNEsgeelegeaegYLvfkQPWP-GIMR 527
Cdd:PRK12467 793 ALGPG-ARLINHYGPTETTVGVSTyELSDEE--RDFGNVPigqPLANLGLYILDH-----------YL---NPVPvGVVG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 528 TVY--------GNHTR--FETTYFKKFPG------YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 591
Cdd:PRK12467 856 ELYiggaglarGYHRRpaLTAERFVPDPFgadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQ 935
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31980996 592 EAVAEAAVVGHPHPVKGECL-YCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK12467 936 PGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
9.52e-16 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 71.73 E-value: 9.52e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980996 47 YRELHRRSVEEPREFWGNIAKEFYWKTacpgPFlQYNFDVTKGkIFTEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFK----PF-DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
117-661 |
1.49e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.93 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 117 LGDKVAFYWeGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 196
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 197 ESLCERILDSSCCLLITTDAFyrGEKLVNLKEladeSLEKcrekgfpVRCCIVVkhlgraelgmNDSPSQSPPVkrpcpd 276
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLLP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 277 vqicwnEGVDlwWHELMQQAGDECEPEWCDAEDpLFILYTSGSTGKPKGVV---HTI-----GGYMLYVATTFKYVFDfH 348
Cdd:PRK07798 141 ------GAVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMwrqEDIfrvllGGRDFATGEPIEDEEE-L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 349 PEDVFWCTADIGWITG---H---SYVTYGPLANGATSVLFEGIPTYPDEgrLWSIVDKYKVTkfytaptaiRMLMkFGD- 421
Cdd:PRK07798 211 AKRAAAGPGMRRFPAPplmHgagQWAAFAALFSGQTVVLLPDVRFDADE--VWRTIEREKVN---------VITI-VGDa 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 422 ---------DPVTKHSRASLQVLGTVGEPINP---EAWLWY--HRVvgsqrcpIVDTFWQTETGGHMLtplpGATPMKPG 487
Cdd:PRK07798 279 marplldalEARGPYDLSSLFAIASGGALFSPsvkEALLELlpNVV-------LTDSIGSSETGFGGS----GTVAKGAV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 488 SASFPFFGVAP--AILNESGEElegeaegyLVFKQPWPGIMrtvyGNHTRFETTYFKK-------FP---G--YYVTGDG 553
Cdd:PRK07798 348 HTGGPRFTIGPrtVVLDEDGNP--------VEPGSGEIGWI----ARRGHIPLGYYKDpektaetFPtidGvrYAIPGDR 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 554 CRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKK 633
Cdd:PRK07798 416 ARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL---AELRA 492
|
570 580
....*....|....*....|....*...
gi 31980996 634 QIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK07798 493 HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
546-673 |
5.21e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 78.49 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtf 623
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK------- 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 31980996 624 SPTLTEELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK10946 482 EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
131-669 |
5.76e-15 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 77.73 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSS-CC 209
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlww 289
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 helmqqagdecepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATT---------------FKYVFDFhpedvfw 354
Cdd:cd17653 104 -----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDA------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 CTADIgwitghsyvtYGPLANGATSVLFEGIPTYPDEGRlwsivdkyKVTKFYTAPTAIRMLmkfgddpvtkhSRASLQV 434
Cdd:cd17653 160 CIGEI----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL-----------SPQDFPN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 435 LGTV---GEPINP---EAWlWYHRVV----GSQRCPIVDTFWQTETGghmlTPLPGATPMkPGSASFpffgvapaILNES 504
Cdd:cd17653 211 LKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY--------ILDAD 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 505 geelegeaegylvfKQPWP------------GIMRTVYGNH----TRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRI 568
Cdd:cd17653 277 --------------LQPVPegvvgeicisgvQVARGYLGNPaltaSKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 569 DDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTlcdghtfspTLT---EELKKQIREKIGPIAT 644
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT---------PETvdvDGLRSELAKHLPSYAV 408
|
570 580
....*....|....*....|....*
gi 31980996 645 PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd17653 409 PDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
129-668 |
8.15e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 129 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVF-----AGFSAEslceri 203
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplntAYTLAE------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 204 ldssccllitTDAFyrgekLVNlkelADESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQSPPvkrpcpdvqicwne 283
Cdd:PRK07514 92 ----------LDYF-----IGD----AEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLL-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 284 gvdlwwhELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWIT 363
Cdd:PRK07514 139 -------EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLIHALPIFHTH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 364 GHSYVTYGPLANGA------------------TSVLFEGIPTypdegrlwsivdkykvtkFYTaptaiRMLmkfgDDP-- 423
Cdd:PRK07514 211 GLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT-----RLL----QEPrl 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 424 ---VTKHSRasLQVLGTVgePINPE---AWlwyhrvvgSQRC--PIVDTFWQTETGghMLTPLPGATPMKPGSASFPFFG 495
Cdd:PRK07514 264 treAAAHMR--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGERRAGTVGFPLPG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 496 VAPAILNESGEELEGEAEGYL-------VFKQPW--PGimrtvygnHTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITG 566
Cdd:PRK07514 330 VSLRVTDPETGAELPPGEIGMievkgpnVFKGYWrmPE--------KTAEEFRA----DGFFITGDLGKIDERGYVHIVG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-TLTEELKKQI-REKIgpiat 644
Cdd:PRK07514 398 RGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEaAILAALKGRLaRFKQ----- 472
|
570 580
....*....|....*....|....
gi 31980996 645 PDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07514 473 PKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
546-669 |
1.01e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.48 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31980996 626 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
289-606 |
1.42e-14 |
|
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: 76.74 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 WHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMlYVATTFKYVFDFHPEDVFWCTADIGWITGHSYV 368
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGPLANGATSVLFEGIPTYPDEgrlwsiVDKYKVTKFYTAPtaiRMLMKFGDDPVTKHSRASLQ--------------- 433
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVED------VQRARPTLFFSVP---RLWTKFQQGVQDKIPQQKLNlllkipvvnslvkrk 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 434 -----------VLGTVGEPINPEAWLWYHRVvgsqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSASFPFFGVAPAIln 502
Cdd:cd05932 268 vlkglgldqcrLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 503 esgeelegEAEGYLVFKQPwpGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLST 581
Cdd:cd05932 340 --------SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAP 407
|
330 340
....*....|....*....|....*..
gi 31980996 582 AEVESALVEHEAVAEAAVVGH--PHPV 606
Cdd:cd05932 408 APIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-667 |
1.73e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITT 214
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 DAFyrgeklvnLKELadeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrPCPD-VQICWNEGVDLWWhelm 293
Cdd:PRK12467 1679 SHL--------QARL-------------------------------------------PLPDgLRSLVLDQEDDWL---- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 qQAGDECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTIGGYM-LYVATtfKYVFDFHPEDVfwctadigWITGHSYV--- 368
Cdd:PRK12467 1704 -EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAfdv 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 ----TYGPLANGAtSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFgdDPVTKHSRaSLQVLGTVGEPINP 444
Cdd:PRK12467 1773 svweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM--DEQVEHPL-SLRRVVCGGEALEV 1848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 445 EAW-LWYHRVVGSQrcpIVDTFWQTETGGHmLTPLPGATPMKPGSASFPFfGVAPAILNEsgeelegeaegYLVFKQ--P 521
Cdd:PRK12467 1849 EALrPWLERLPDTG---LFNLYGPTETAVD-VTHWTCRRKDLEGRDSVPI-GQPIANLST-----------YILDASlnP 1912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 WP-GIMRTVY--------GNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:PRK12467 1913 VPiGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 585 ESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSPTLTEELKKQIREKIgpiatPDYIQNA-----PGL 654
Cdd:PRK12467 1993 EARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYMVPAhlvflARM 2066
|
570
....*....|...
gi 31980996 655 PKTRSGKIMRRVL 667
Cdd:PRK12467 2067 PLTPNGKLDRKAL 2079
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
134-667 |
2.37e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.01 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCCLLI 212
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 213 TTDAFyrGEKLVNLKELADESLekcrekgfpvrccivvkhlgRAELgmndSPSQSPPVKRPCPDvqicwnegvdlwwhel 292
Cdd:PRK10252 561 TTADQ--LPRFADVPDLTSLCY--------------------NAPL----APQGAAPLQLSQPH---------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 293 mqqagdecepewcdaeDPLFILYTSGSTGKPKGVV--HT-IGGYMLYVATTFKyvfdFHPEDVFW----CTADIG----- 360
Cdd:PRK10252 599 ----------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqktpCSFDVSvweff 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 361 WitghsyvtygPLANGATSVLFEgiptyPDEGR----LWSIVDKYKVTKFYTAPTairMLMKFGDDPVTKHSRASLQVLG 436
Cdd:PRK10252 659 W----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASLTPEGARQSCASLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 437 TV---GEPINPEAWLWYHRVVGSqrcPIVDTFWQTE---------TGGHMLTPLPGAT-PMkpgsaSFPFFGVAPAILNE 503
Cdd:PRK10252 721 QVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGSSvPI-----GYPVWNTGLRILDA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 504 SGeelegeaegylvfkQPWP-GIMRTVY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITG 566
Cdd:PRK10252 793 RM--------------RPVPpGVAGDLYltgiqlaqGYLGRPDLTA-SRFiadpfaPGerMYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 567 RIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLCDGhtfSPTLTEELKKQIREKIG 640
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSG---LPLDTSALQAQLRERLP 934
|
570 580
....*....|....*....|....*..
gi 31980996 641 PIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
115-668 |
2.73e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 76.34 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFywegNEPGETtkITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 194 FSAESLCERILDSSCCLLITtdafyrgekLVNLKELADESLEKCREK-----------GFPVRCCI--VVKHLGRAelgm 260
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTGVKhvivtevadmlPPLKRLLInaVVKHVKKM---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 261 ndSPSQSPPVKRPCPDVqicwnegvdlwwheLMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYV 337
Cdd:PRK05677 176 --VPAYHLPQAVKFNDA--------------LAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 338 ATTFK-------------------YVFDFHpedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDEGRLWSIV 398
Cdd:PRK05677 240 RALMGsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 399 DKYKVTKFYTAPTAIRMLMKfgDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqrCPIVDTFWQTETgghmlTPL 478
Cdd:PRK05677 297 GKWKFSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 479 PGATPMK---PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHTrfETTYFKKFPGYYVTGDGCR 555
Cdd:PRK05677 367 VSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIAL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 556 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsPTLTEE-LKKQ 634
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG----ETLTKEqVMEH 518
|
570 580 590
....*....|....*....|....*....|....
gi 31980996 635 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK05677 519 MRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-669 |
3.51e-14 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 75.79 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYwegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAES 198
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILD----SSCCLLITTDAFYrgeklvnlkeladeslEKCREKGFPVrccIVvkhLGRAelgmndspsqsppvkrpC 274
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV---IV---LGEE-----------------K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 PDVQICWNEGVDLwwhelMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTiggYMLYVATTFKYVFDFHPEDVFW 354
Cdd:PLN02330 156 IEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLT---HRNLVANLCSSLFSVGPEMIGQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 CTAdIGWITG-HSYvtygplanGATSVLFegiPTYPDEGRLwSIVDKYKVTKFYTA------------PTAIRMLMKfgd 421
Cdd:PLN02330 228 VVT-LGLIPFfHIY--------GITGICC---ATLRNKGKV-VVMSRFELRTFLNAlitqevsfapivPPIILNLVK--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 422 DPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGSQrcpIVDTFWQTETGGHMLT---PLPGATPMKPGSASFPFF 494
Cdd:PLN02330 292 NPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 495 GVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITG 566
Cdd:PLN02330 369 NLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPD 646
Cdd:PLN02330 438 RIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES---EEDILNFVAANVAHYKKVR 514
|
570 580
....*....|....*....|...
gi 31980996 647 YIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02330 515 VVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
546-664 |
6.21e-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: 73.69 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHtfsp 625
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV---- 290
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 31980996 626 TLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17638 291 TLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
546-672 |
6.40e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.88 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS- 624
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSd 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31980996 625 -PTLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN02479 510 eAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-671 |
1.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 73.70 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFywegNEPGETtkITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK12492 35 KKFADRPAF----SNLGVT--LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 194 FSAESLCERILDSSCCLLITTDAFyrgEKLVNlKELADESLEKCRE----------KGFPVRccIVVKHlgraelgmnds 263
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIEYLIEakmgdllpaaKGWLVN--TVVDK----------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 264 psqsppVKRPCPDVQICWNEGVDlwwHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGY---MLYVATT 340
Cdd:PRK12492 172 ------VKKMVPAYHLPQAVPFK---QALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 341 F-KYVFDFHP-----EDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYP-DEGRLWSIVDKYKVTKFYTAPTAI 413
Cdd:PRK12492 243 LsQLGPDGQPlmkegQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLI----TNPrDIPGFIKELGKWRFSALLGLNTLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 414 RMLMkfgDDPVTKHSRAS-LQVLGTVGEPI---NPEAWlwyHRVVGsqrCPIVDTFWQTETgghmlTPLPGATPM----K 485
Cdd:PRK12492 319 VALM---DHPGFKDLDFSaLKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTET-----SPVASTNPYgelaR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 486 PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHTRFETTY-FKKFPGYYVTGDGCRRDQDGYYWI 564
Cdd:PRK12492 385 LGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMK---GYWQQPEATAeALDAEGWFKTGDIAVIDPDGFVRI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 565 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPTLT-EELKKQIREKIGPIA 643
Cdd:PRK12492 460 VDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----PGLSvEELKAYCKENFTGYK 534
|
570 580
....*....|....*....|....*...
gi 31980996 644 TPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK12492 535 VPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-668 |
1.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.58 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 140 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLIT-TDAFy 218
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 219 rgeklvnlkeladESLEKCREKGFPVRCCIVVKHLgRAELGMndspsqsPPVKRPCPDVQICWNEgvdlwWheLMQQAGD 298
Cdd:PRK12406 95 -------------HGLASALPAGVTVLSVPTPPEI-AAAYRI-------SPALLTPPAGAIDWEG-----W--LAQQEPY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 299 ECEPewcdAEDPLFILYTSGSTGKPKGVVHTIG------GYMLYVATtfkyVFDFHPEDVFWCTadigwitGHSYVT--- 369
Cdd:PRK12406 147 DGPP----VPQPQSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRAL----IYGLKPGIRALLT-------GPLYHSapn 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 370 -YGPLAN--GATSVL---FEgiptyPDEgrLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK12406 212 aYGLRAGrlGGVLVLqprFD-----PEE--LLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 444 PE------AWlWyhrvvgsqrCPIVDTFW-QTETGGhmltpLPGATP----MKPGSASFPFFGVAPAILNESGEELEGEA 512
Cdd:PRK12406 285 ADvkramiEW-W---------GPVIYEYYgSTESGA-----VTFATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 513 EGYLVFKQPwpGIMRTVYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:PRK12406 350 IGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK12406 426 GVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
308-667 |
5.64e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 71.70 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 308 EDPLFILYTSGSTGKPKGVV--------HTIGGYMLYVATTFKYV-------FDFHPEDVFwctadIGWITGHSYVTygp 372
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 373 langatsVLFEGIPTYPDegrLWSIVDKYKVTKFYTAPTAIRMLMKFGDdPVTKHSRASLQVLGTVGEPINPEAW-LW-- 449
Cdd:cd17644 178 -------RPEEMRSSLED---FVQYIQQWQLTVLSLPPAYWHLLVLELL-LSTIDLPSSLRLVIVGGEAVQPELVrQWqk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 450 -------YHRVVGSQRCPIVDTFW----------------------QTETGGHMLTPLPGATPmkpGSASFPFFGVAPAI 500
Cdd:cd17644 247 nvgnfiqLINVYGPTEATIAATVCrltqlternitsvpigrpiantQVYILDENLQPVPVGVP---GELHIGGVGLARGY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 501 LNEsgeelegeaegylvfkqpwPGIMRTVYGNHTrFETTYFKKFpgyYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:cd17644 324 LNR-------------------PELTAEKFISHP-FNSSESERL---YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 581 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17644 381 LGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNG 457
|
....*..
gi 31980996 661 KIMRRVL 667
Cdd:cd17644 458 KIDRRAL 464
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
125-673 |
6.15e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 71.42 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 125 WEGNepgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsivfagfsaeslceril 204
Cdd:cd05918 21 WDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 205 dsSCCLLittdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndSPSQspPVKRpcpdvqicwneg 284
Cdd:cd05918 75 --AFVPL---------------------------------------------------DPSH--PLQR------------ 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 285 vdlwWHELMQQAGdecePEW---CDAEDPLFILYTSGSTGKPKGVV--HtigGYMLYVATTFKYVFDFHPED-VFW---- 354
Cdd:cd05918 88 ----LQEILQDTG----AKVvltSSPSDAAYVIFTSGSTGKPKGVVieH---RALSTSALAHGRALGLTSESrVLQfasy 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 ----CTADIgwitghsyvtYGPLANGATSVlfegIPtyPDEGRLWSIVD---KYKVTkfyTA---PTAIRMLmkfgdDPV 424
Cdd:cd05918 157 tfdvSILEI----------FTTLAAGGCLC----IP--SEEDRLNDLAGfinRLRVT---WAfltPSVARLL-----DPE 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 425 TKhsrASLQVLGTVGEPINPEAW-LWYHRV------------VGSQRCPIVD-------------TFWQTETGGH-MLTP 477
Cdd:cd05918 213 DV---PSLRTLVLGGEALTQSDVdTWADRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 478 LpGAT-------PMkpgsasfpffgVAPAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHTRFettyfkkfpgyYVT 550
Cdd:cd05918 290 I-GAVgelliegPI-----------LARGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRT 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 551 GDGCRRDQDG--YYwiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSP 625
Cdd:cd05918 340 GDLVRYNPDGslEY--VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGS 416
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980996 626 TLTEELKKQIREKIGPIAT----------PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 673
Cdd:cd05918 417 GDGDSLFLEPSDEFRALVAelrsklrqrlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
546-668 |
1.78e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 70.02 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfs 624
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD----- 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31980996 625 PTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-667 |
1.78e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFYRGeklvnLKELADESLEKCREKGFPVRccivvkhlgraelgmnDSPSQSPPVKRPCPDvqicwnegvdlwwh 290
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQ-------------- 2333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 elmQQAgdecepewcdaedplFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDvfwCTADIGWIT--GHSYV 368
Cdd:PRK05691 2334 ---HQA---------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASER 2391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGPLANGATSVL-FEGiptYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFgddPVTKHSRASLQVLGTVGEPINPEAW 447
Cdd:PRK05691 2392 LLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRMCITGGEALTGEHL 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 448 LWYHRVVGSQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSASFPFFGVAPA----ILNESGEELEGEAEGYLvfkqp 521
Cdd:PRK05691 2466 QRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALVPQGATGEL----- 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 522 WPGIMRTVYGNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK05691 2536 YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA 2615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 594 VAEAAVVGHPHPvKGECLYCFV---TLCDGHTFSPTLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRR 665
Cdd:PRK05691 2616 VREAVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQL-----PDYMVPAhlillDSLPLTANGKLDRR 2689
|
..
gi 31980996 666 VL 667
Cdd:PRK05691 2690 AL 2691
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-667 |
1.93e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL---CErILDSSCC 209
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIerfCQ-ITDPAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 LLIttdafyRGEKLvnlkelADESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQSPpvkrpcpdvqicwNEGVDlww 289
Cdd:PRK05857 118 LVA------PGSKM------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-------------DQGSE--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 290 helmqqagdecepewcdaeDPLFILYTSGSTGKPKGVvhtiggymLYVATTFKYVFD-FHPEDVFWctadIGWITGHSyv 368
Cdd:PRK05857 170 -------------------DPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW----VTWVVGET-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGPLAngATSV---------LFEG---IPTYPDEGRLWSIVDKYKVTKFYTAPTAIRML---MKFGDDPVtkhsrASLQ 433
Cdd:PRK05857 217 TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANATV-----PSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 434 VLGTVG-EPINPEAwlwyhRVVGSQRCPIVDTFWQTETGGHMLTpLP----GATPMKPGSASFPFFGV----APAILNES 504
Cdd:PRK05857 290 LVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdvylAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 505 GEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:PRK05857 364 TAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfsptlTEELKKQI----REKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK05857 441 DRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRRESEPMARPSTIVIVTDIPRT 515
|
570
....*....|
gi 31980996 658 RSGKIMRRVL 667
Cdd:PRK05857 516 QSGKVMRASL 525
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
308-661 |
6.73e-12 |
|
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: 67.79 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 308 EDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATTFKYVF----DFHPEDVfwCTADIGW------ITGHSYVTYGPLA 374
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGADFGTGEFtpseDAHKAAA--AAAGTVMfpapplMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 375 NGATSVLFEGIPTYPDEgrLWSIVDKYKVTKFYTAPTAI-RMLMKFGDDPVTkHSRASLQVLGTVGEPINPEawlwyhrv 453
Cdd:cd05924 81 LGGQTVVLPDDRFDPEE--VWRTIEKHKVTSMTIVGDAMaRPLIDALRDAGP-YDLSSLFAISSGGALLSPE-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 454 VGSQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSASFPFFGVAPAILNESgeelegeaegyLVFKQPWPGIMR 527
Cdd:cd05924 150 VKQGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSGGVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 528 TV----------YGNHTRFETTyFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:cd05924 216 WIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVY 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 596 EAAVVGHPHPVKGECLYCFVTLCDGHtfSPTLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:cd05924 295 DVLVVGRPDERWGQEVVAVVQLREGA--GVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
550-671 |
8.58e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 68.30 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 550 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPtltE 629
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 31980996 630 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
132-382 |
1.42e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 67.69 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITTdafyrGEKLVNLkeladesLEKCREKGFPvRCCIVvkHLGRAELGMNDSpsqsppvkrpcpDVQ-ICWNEGVDLWWH 290
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLDSLPASVDTE------------GCRlVAWTDVVAKGHS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEpewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDF--HPEDvfwctadigwitGHSYV 368
Cdd:PTZ00216 251 AGSHHPLNIPE----NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLigPPEE------------DETYC 314
|
250
....*....|....*...
gi 31980996 369 TYGPLAN----GATSVLF 382
Cdd:PTZ00216 315 SYLPLAHimefGVTNIFL 332
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
291-669 |
2.25e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.75 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQQAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVvhTIGGYMLYVATTFKYVF-DFHPEDVFWCTADIGWITGHSYV 368
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 tygpLAN---GATSVLfegIPTYpDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVL----GTVGEP 441
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 442 INPEAWLWYhrvvgsQRCPIVDTFWQTETGGHM-LTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQ 520
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSLtFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 521 PWPGIMRT----VYGNHT--RF-----ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02860 378 GLDESSRVgrilTRGPHVmlGYwgqnsETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLT-----------EELKKQIREK-IGPIATPD-YIQNAPGLPK 656
Cdd:PLN02860 458 QHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlFVQWRKPFPL 537
|
410
....*....|...
gi 31980996 657 TRSGKIMRRVLRK 669
Cdd:PLN02860 538 TTTGKIRRDEVRR 550
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-382 |
6.20e-11 |
|
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: 65.34 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFA-- 192
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 193 -GFSAESLCERILDSSCCLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhlgRAELgmndspsqsPPVK 271
Cdd:cd05931 83 pGRHAERLAAILADAGPRVVLTTAAA-------------------------------------LAAV---------RAFA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 272 RPCPDVQICWNEGVDLwwheLMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPED 351
Cdd:cd05931 117 ASRPAAGTPRLLVVDL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGD 191
|
250 260 270
....*....|....*....|....*....|....*
gi 31980996 352 --VFW--CTADIGWITGhsyvTYGPLANGATSVLF 382
Cdd:cd05931 192 vvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLM 222
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
545-675 |
7.95e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.63 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 545 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfs 624
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP---- 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 31980996 625 PTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 675
Cdd:PRK07445 399 SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
545-669 |
9.46e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.91 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 545 PGYYVTGDGCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtLCDGHTfS 624
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 31980996 625 PTLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 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 |
1.55e-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: 63.96 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVVHTIGGYM--------LY---------VATTFKYVFDFHPEDVFwctadIGWITGHSYV 368
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGPlangatSVLFegiptypDEGRLWSIVDKYKVTKFYTAPTAIRMLmKFGddpvtkhSRASLQVLGTVGEPINPEAwl 448
Cdd:cd17648 167 VPPD------EMRF-------DPDRFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 449 wYHRVVGSQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSASFPFFGVAPAILNESGeelegeaegylvfkQPWP-GIM 526
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvGAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 527 RTVY--------GNHTRFETTYFK---------------KFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:cd17648 288 GELYlggdgvarGYLNRPELTAERflpnpfqteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 584 VESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfsptLTE-ELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17648 368 VEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
410
....*....|
gi 31980996 658 RSGKIMRRVL 667
Cdd:cd17648 443 INGKLDVRAL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
132-667 |
1.64e-10 |
|
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: 64.03 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLL 211
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 212 ITtdafyrgeklvnlkeladeslekCREkgfpvrccivvkhlgraelgMNDSPSQSPPVkrpcpdvqicwnegVDLWWHE 291
Cdd:cd17656 90 LT-----------------------QRH--------------------LKSKLSFNKST--------------ILLEDPS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 292 LMQQAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--HTiggymlYVATTFKYVFDFHPEDVFwctADIGWITGHSY-V 368
Cdd:cd17656 113 ISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKGVQleHK------NMVNLLHFEREKTNINFS---DKVLQFATCSFdV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 369 TYGPLAngaTSVLFEG----IP--TYPDEGRLWSIVDKYKVTKFYTAPTAIRMLmkFGDDPVTKHSRASLQVLGTVGEPI 442
Cdd:cd17656 183 CYQEIF---STLLSGGtlyiIReeTKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FSEREFINRFPTCVKHIITAGEQL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 443 ---NPeawlwYHRVVGSQRCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSASFPFfgvapaILNESgeeleg 510
Cdd:cd17656 258 vitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ILDQE------ 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 511 eaegylvfKQPWP-GIMRTVY--------GNHTRFETTYFKKFPG-------YYVTGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:cd17656 319 --------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQLPEYMIPSFFVPLDQL 465
|
570
....*....|...
gi 31980996 655 PKTRSGKIMRRVL 667
Cdd:cd17656 466 PLTPNGKVDRKAL 478
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
550-667 |
2.48e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 550 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSPtl 627
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDP-- 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 31980996 628 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
520-677 |
3.79e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 520 QPWPGImrtVYGN-HTR---FETTYFKK-----FPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK07008 377 LPWDGK---AFGDlQVRgpwVIDRYFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
....*..
gi 31980996 671 AQnDHDL 677
Cdd:PRK07008 531 FR-DYVL 536
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
306-664 |
4.39e-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: 62.46 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFdFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGI 385
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 386 PT-----------YPDEG--RLWSIVDKYKVTKFYTAPTAI---RMLMKFGDDPVTKHSRASLQ----------VLGtvG 439
Cdd:cd05914 166 PSakiialafaqvTPTLGvpVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggnikefVIG--G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 440 EPINPEAwLWYHRVVGsqrCPIVDTFWQTETGghmltPLPGATP---MKPGSASFPFFGVAPAILNESGEELEGEaegyL 516
Cdd:cd05914 244 AKINPDV-EEFLRTIG---FPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRIDSPDPATGEGE----I 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 517 VFKQpwPGIMRTVYGNHtrfETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05914 311 IVRG--PNVMKGYYKNP---EATAEAFDKdGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 595 AEAAVV---------GHPHP----VKGECLycfvtlcdghtfsPTLTEELKKQIREKIGpIATPDY-------IQNAPgL 654
Cdd:cd05914 386 LESLVVvqekklvalAYIDPdfldVKALKQ-------------RNIIDAIKWEVRDKVN-QKVPNYkkiskvkIVKEE-F 450
|
410
....*....|
gi 31980996 655 PKTRSGKIMR 664
Cdd:cd05914 451 EKTPKGKIKR 460
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-669 |
5.98e-10 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 62.06 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLI 212
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 213 TtdafyrgeklvNLKELADESLEKcrekgfpvrccivvkhlgraelgmndspsqSPPVkrpCPDVqicwnegvdlwwhel 292
Cdd:cd05939 81 F-----------NLLDPLLTQSST------------------------------EPPS---QDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 293 mqqagdecepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIgWITGHSYVTYGP 372
Cdd:cd05939 102 -------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL-YHSAGGIMGVGQ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 373 -LANGATSVLFEGIPTypdeGRLWSIVDKYKVTKF-YTAPTAIRMLMKFGDDPVTKHsraslQVLGTVGEPINPEAWlwy 450
Cdd:cd05939 167 aLLHGSTVVIRKKFSA----SNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLAVGNGLRPQIW--- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 451 HRVVGSQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSASF-PFFG--VAPAIL---NESGEELEGEAEGYLVFKQPW-P 523
Cdd:cd05939 235 EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRDSDGLCIPCQPGeP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 524 GIM--RTVYGNHTRFETTY--------------FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:cd05939 311 GLLvgKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 588 LVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSPTLTEELKkqirekigPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd05939 391 LSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKL 462
|
....*..
gi 31980996 663 MRRVLRK 669
Cdd:cd05939 463 QKTDLQK 469
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
131-374 |
7.28e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.44 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCL 210
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITtdafyrGEKlvNLKELAD--ESLEkcrekgfpvrcciVVKHLgraeLGMNDSPSQSPPVKRPCPDVQICWNEGVDlw 288
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDSSLSGSSNWTVSSFSEVE-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 whELMQQAgdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVfwctadigwitghsYV 368
Cdd:PLN02387 235 --KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YL 296
|
....*.
gi 31980996 369 TYGPLA 374
Cdd:PLN02387 297 AYLPLA 302
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
546-667 |
7.81e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.94 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgHTFSP 625
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVL---HPGSG 472
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 31980996 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
546-669 |
2.29e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.57 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 625
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31980996 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
137-669 |
1.00e-08 |
|
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: 58.21 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL--CERIldSSCCLLIT 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 214 TDafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelm 293
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 294 qqagdecepewcdaEDPLFILYTSGSTGKPKGVVHTIGgyMLYV-ATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGP 372
Cdd:cd05937 87 --------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 373 LANGATSVL---FEGiptypdeGRLWSIVDKYKVTKFYTAPTAIRMLMkfgDDPVTKHSRASlQVLGTVGEPINPEAWLW 449
Cdd:cd05937 151 LMSGGTLALsrkFSA-------SQFWKDVRDSGATIIQYVGELCRYLL---STPPSPYDRDH-KVRVAWGNGLRPDIWER 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 450 YHRVVGsqrCPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsasfpfFGvAPAILNESGEELEGEAEGYLVFK------QPW 522
Cdd:cd05937 220 FRERFN---VPEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQVVLVKmdpetdDPI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 ---------------PG--IMRTVYGNHTRFETTY--------------FKKFPGYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:cd05937 284 rdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTFSPTLT-EELKKQIREKIGPIATPDY 647
Cdd:cd05937 364 FRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVPTEFTkSLLASLARKNLPSYAVPLF 441
|
570 580
....*....|....*....|..
gi 31980996 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05937 442 LRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
306-672 |
1.01e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.78 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATtfkyVFDFHPEDVfwctadigwITG-----HSY----VTYGPL 373
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 374 ANGATSVlfegipTYPD--EGR-LWSIVDKYKVTKFYTAPTAIRMLMKfgDDPVTKHSRASLQVLGTVGEPINPEawlwy 450
Cdd:PRK08633 847 LEGIKVV------YHPDptDALgIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPE----- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 451 hrvvgsqrcpIVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSASFPFFGVAPAILNESG 505
Cdd:PRK08633 914 ----------VADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 506 eelegeaegYLVFKQPWPG--------IMRTVYGNHTRF-ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSG 576
Cdd:PRK08633 979 ---------FEELPPGEDGliliggpqVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGG 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 577 HLLSTAEVESALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSPTLTEELKKQIRE-KIGPIATPDYIQNA 651
Cdd:PRK08633 1050 EMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKV 1121
|
410 420
....*....|....*....|.
gi 31980996 652 PGLPKTRSGKIMRRVLRKIAQ 672
Cdd:PRK08633 1122 EALPLLGSGKLDLKGLKELAL 1142
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
548-667 |
1.33e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 548 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSPTL 627
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 31980996 628 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-667 |
3.20e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.49 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK05691 1146 ERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 199 LCERILDSSCCLLITTDAFYrgEKLVNLKELADESLEkcrekgfpvrccivvkhlgraELGMNDSPSQSPpvkrpcpdvq 278
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIALD---------------------SLHLDSWPSQAP---------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 279 icwneGVDLWWHELMqqagdecepewcdaedplFILYTSGSTGKPKGVVHT---IGGYMLYVATTfkYVFDfhPEDVFWC 355
Cdd:PRK05691 1267 -----GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNThaaLAERLQWMQAT--YALD--DSDVLMQ 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 356 TADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDEGRLWSIVDKYKVTKFYTAPTairMLMKFGDDPVTKHSRaSLQVL 435
Cdd:PRK05691 1320 KAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPLAAACT-SLRRL 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 436 GTVGEPINPE---------AWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLpgatpmkpgsaSFPFFGVAPAILNESGE 506
Cdd:PRK05691 1394 FSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELN 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 507 ELEGEAEGYLVFKQPwpGIMRTVYG----NHTRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK05691 1463 LLPPGVAGELCIGGA--GLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVE 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 581 TAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHTFSPtltEELKKQIREKIgpiatPDYIQNA-----PGLP 655
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAEL-----PEYMVPAqlirlDQMP 1610
|
570
....*....|..
gi 31980996 656 KTRSGKIMRRVL 667
Cdd:PRK05691 1611 LGPSGKLDRRAL 1622
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-669 |
1.50e-07 |
|
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: 54.28 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSivfagfsaeslcerildsscclLITT 214
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA----------------------LINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 215 DAfyRGEKLVNLKELADeslekcrekgfpVRCCIVvkhlgraelgmndspsqsppvkrpcpdvqicwnegvdlwwhelmq 294
Cdd:cd05940 61 NL--RGESLAHCLNVSS------------AKHLVV--------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 295 qagdecepewcdaeDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05940 82 --------------DAALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 375 NGATSVLFEGIPTypdeGRLWSIVDKYKVTKFYTAPTAIRMLMKfgdDPVTKHSRASlQVLGTVGEPINPEAWLWYHRVV 454
Cdd:cd05940 147 SGATLVIRKKFSA----SNFWDDIRKYQATIFQYIGELCRYLLN---QPPKPTERKH-KVRMIFGNGLRPDIWEEFKERF 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 455 GsqrCPIVDTFWQTETGGHMLTPLPGatpmKPGSAsfpffGVAPAILnesgeeleGEAEGYLVFK------QPW------ 522
Cdd:cd05940 219 G---VPRIAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLL--------RKVAPLALVKydlesgEPIrdaegr 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 --------PGIMRTVYGNHTRFE-------------TTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:cd05940 279 cikvprgePGLLISRINPLEPFDgytdpaatekkilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVST 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 582 AEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSptlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd05940 359 TEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGTF 435
|
....*....
gi 31980996 661 KIMRRVLRK 669
Cdd:cd05940 436 KQQKVDLRN 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
136-447 |
4.65e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.98 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhSIVfagfsaeslceriLDssccllittd 215
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV-PVL-------------VD---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 216 afyRGEKLVNLKELADESlekcREKGFpvrCCIVVKHLGRAELGmndspsqsppvkRPCPDVQICWNEGVDLWW-----H 290
Cdd:PRK09274 98 ---PGMGIKNLKQCLAEA----QPDAF---IGIPKAHLARRLFG------------WGKPSVRRLVTVGGRLLWggttlA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 291 ELMQ-QAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGgymLYVA--TTFKYVFDFHPEDVFWCTADIgwitghsY 367
Cdd:PRK09274 156 TLLRdGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG---MFEAqiEALREDYGIEPGEIDLPTFPL-------F 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 368 VTYGPlANGATSVLFEGIPTYP---DEGRLWSIVDKYKVTKFYTAPTAIRmlmkfgddPVTKHSRASLQVLGTV------ 438
Cdd:PRK09274 226 ALFGP-ALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLE--------RLGRYGEANGIKLPSLrrvisa 296
|
....*....
gi 31980996 439 GEPINPEAW 447
Cdd:PRK09274 297 GAPVPIAVI 305
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
307-601 |
6.71e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 52.46 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 307 AEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAtTFKYVFDFHPEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 386
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 387 TYP---DEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVgSQRCPIVD 463
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKML-SDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 464 TFWQTET------GGHMLTPLPGATPMKPGSA--SFPFFGVAPAILNESGEELEGEAEGYLVfkqPWPGIMR-TVYGN-- 532
Cdd:cd05910 232 PYGATEAlpvssiGSRELLATTTAATSGGAGTcvGRPIPGVRVRIIEIDDEPIAEWDDTLEL---PRGEIGEiTVTGPtv 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980996 533 ----HTRFETTYFKKFPG-----YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05910 309 tptyVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
131-673 |
7.30e-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: 52.28 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACarlgalhsiVFAGFSAeslcerildssccL 210
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFVP-------------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LITTDAFYRG-----EKLVNLKELADEslekcrekgfpvrcCIVvkhLGRAELGMNDSPSQSPpvkRPCPDVQICWNEgv 285
Cdd:cd05906 93 PLTVPPTYDEpnarlRKLRHIWQLLGS--------------PVV---LTDAELVAEFAGLETL---SGLPGIRVLSIE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 286 dlwwhELMQQAGDecePEW--CDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDVF--W------- 354
Cdd:cd05906 151 -----ELLDTAAD---HDLpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWvpldhvg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 355 -------------C------TADI--------GWITGHSY-VTYGPlaNGATSVLFEGIPTYPDegRLWSIvdkykvtkf 406
Cdd:cd05906 222 glvelhlravylgCqqvhvpTEEIladplrwlDLIDRYRVtITWAP--NFAFALLNDLLEEIED--GTWDL--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 407 ytapTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPinPEAwlwyhrvvgsqrcpIVDTFWQTETGGHMLTPLPGATPMKP 486
Cdd:cd05906 289 ----SSLRYLVNAGEAVVAKTIRRLLRLLEPYGLP--PDA--------------IRPAFGMTETCSGVIYSRSFPTYDHS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 487 GSASFPFFGvapailnesgeelegeaegylvfkQPWPGI-MRTVYGNHT--------RFETTYFKKFPGYY--------- 548
Cdd:cd05906 349 QALEFVSLG------------------------RPIPGVsMRIVDDEGQllpegevgRLQVRGPVVTKGYYnnpeanaea 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 549 VTGDGCRRDQD------GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE--AAVVGHPHPVKGECLYCFVtlcdg 620
Cdd:cd05906 405 FTEDGWFRTGDlgfldnGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIF----- 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 621 htFSPTLTE-----ELKKQIR----EKIGpiATPDYI----QNApgLPKTRSGKIMRRVLRKIAQN 673
Cdd:cd05906 480 --FVPEYDLqdalsETLRAIRsvvsREVG--VSPAYLiplpKEE--IPKTSLGKIQRSKLKAAFEA 539
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
129-662 |
1.65e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 50.93 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 129 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAESLCERILDssc 208
Cdd:cd17654 10 QTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGA----AYAPIDPASPEQRSLT--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 209 cLLITTDAFYrgeKLVNlkeladeslekcrekgfpvrccivvKHLGRAelgmndsPSQSPPVKRpcpdvqicwnegvdlw 288
Cdd:cd17654 83 -VMKKCHVSY---LLQN-------------------------KELDNA-------PLSFTPEHR---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 wHELMQQAGDECepewcdaedplFILYTSGSTGKPKGV---VHTIGGYMLYvattFKYVFDFHPEDVFWCTadigwitgh 365
Cdd:cd17654 111 -HFNIRTDECLA-----------YVIHTSGTTGTPKIVavpHKCILPNIQH----FRSLFNITSEDILFLT--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 366 SYVTYGP--------LANGATSVlfegipTYPDEGRLWS-----IVDK-YKVTKFYTAPTAIRMLMK--FGDDPVTKHSr 429
Cdd:cd17654 166 SPLTFDPsvveiflsLSSGATLL------IVPTSVKVLPskladILFKrHRITVLQATPTLFRRFGSqsIKSTVLSATS- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 430 aSLQVLGTVGE--PINPEAWLWYHRVVGSQRCPIVDTfwqTETGGHMLT--------PLPGATPMkpgsasfpffgVAPA 499
Cdd:cd17654 239 -SLRVLALGGEpfPSLVILSSWRGKGNRTRIFNIYGI---TEVSCWALAykvpeedsPVQLGSPL-----------LGTV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 500 ILNESGEELEGEAEGYLvfkqpwPGIMRTVY--GNHTRFETTYfkkfpgyYVTGDGCRRdQDGYYWITGRIDDMLNVSGH 577
Cdd:cd17654 304 IEVRDQNGSEGTGQVFL------GGLNRVCIldDEVTVPKGTM-------RATGDFVTV-KDGELFFLGRKDSQIKRRGK 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 578 LLSTAEVESALVEHEAVAEAAVVGHphpvKGECLYCFVTlcdghtfSPTLTEELKKQIREKIGPI-ATPDYIQNAPGLPK 656
Cdd:cd17654 370 RINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIV-------GESSSSRIHKELQLTLLSShAIPDTFVQIDKLPL 438
|
....*.
gi 31980996 657 TRSGKI 662
Cdd:cd17654 439 TSHGKV 444
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
299-382 |
1.81e-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: 51.06 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 299 ECEPEWCD--AEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDF-HPEDVfwctadigwitghsYVTYGPLAN 375
Cdd:cd17639 77 ECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDR--------------YLAYLPLAH 142
|
90
....*....|.
gi 31980996 376 ----GATSVLF 382
Cdd:cd17639 143 ifelAAENVCL 153
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
587-679 |
1.94e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 50.53 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSPTLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|...
gi 31980996 667 LRKIAQNDHDLGD 679
Cdd:PRK09188 322 LRLIAMNQIDELD 334
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
115-667 |
3.59e-06 |
|
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: 49.86 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 115 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:cd17645 9 ERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 195 SAESLCERILDSSCCLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhlgraelgmndspsqsppvkrpc 274
Cdd:cd17645 83 PGERIAYMLADSSAKILLT------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 275 pdvqicwnegvdlwwhelmqqagdecepewcDAEDPLFILYTSGSTGKPKGVV---HTIGGYMLYvattFKYVFDFHPED 351
Cdd:cd17645 102 -------------------------------NPDDLAYVIYTSGSTGLPKGVMiehHNLVNLCEW----HRPYFGVTPAD 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 352 VFWCTADIGWiTGHSYVTYGPLANGATsvlfegIPTYPDEGRLwsivDKYKVTK-FYTAPTAIRMLMKFGDDPVTKHSRA 430
Cdd:cd17645 147 KSLVYASFSF-DASAWEIFPHLTAGAA------LHVVPSERRL----DLDALNDyFNQEGITISFLPTGAAEQFMQLDNQ 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 431 SLQVLGTVGEPINpeawlwyhrVVGSQRCPIVDTFWQTETgghmlTPLPGATPMKPGSASFPFfGVAPA-----ILNESG 505
Cdd:cd17645 216 SLRVLLTGGDKLK---------KIERKGYKLVNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEAL 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 506 EELEGEAEGYLVFKQPwpGIMRtvyGNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:cd17645 281 QLQPIGVAGELCIAGE--GLAR---GYLNRPELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfSPTLT--EELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-------APEEIphEELREWLKNDLPDYMIPTYFVHLKALP 427
|
570
....*....|..
gi 31980996 656 KTRSGKIMRRVL 667
Cdd:cd17645 428 LTANGKVDRKAL 439
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
137-337 |
5.88e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.43 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARL-------------GALHSIV------FAgFSAE 197
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHslicvplydtlgpGAVDYIVdhaeidFV-FVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 198 SLCERILDSSCcllittDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHLGRaelgmnDSPSQ-SPPvkrpcpd 276
Cdd:PLN02430 157 KKIKELLEPDC------KSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGK------ENPSEtNPP------- 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980996 277 vqicwnegvdlwwhelmqQAGDECEpewcdaedplfILYTSGSTGKPKGVVHTIGGYMLYV 337
Cdd:PLN02430 218 ------------------KPLDICT-----------IMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
131-375 |
7.03e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 49.46 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCCL 210
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV-EFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 211 LittdAFYRGEKLVNLkeLAdeSLEKCREkgfpvrccivvkHLgRAELGMND-SPSQSPPVKrpcpdvqicwNEGVDLW- 288
Cdd:PLN02861 152 I----AFVQESKISSI--LS--CLPKCSS------------NL-KTIVSFGDvSSEQKEEAE----------ELGVSCFs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 289 WHELMQQAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFdfhpedvfwcTADIGWITGHSYV 368
Cdd:PLN02861 201 WEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK----------VTDRVATEEDSYF 270
|
....*..
gi 31980996 369 TYGPLAN 375
Cdd:PLN02861 271 SYLPLAH 277
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
309-660 |
1.07e-05 |
|
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: 48.07 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 309 DPLFILYTSGSTGKPKGVVHTIGGYMLYVattfkyvfdfhpedvfWCTADIGWITGHS-YVTYGPLANGATsvLFEGIPT 387
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQA----------------LVLAVLQAIDEGTvFLNSGPLFHIGT--LMFTLAT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 388 Y-----------PDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDpvTKHSRASLQVLgtvgepinPEAWLWYHRVvgs 456
Cdd:cd17636 63 FhaggtnvfvrrVDAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSS--------PAAPEWNDMA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 457 qrcPIVDTFW--------QTETGGhmLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrT 528
Cdd:cd17636 130 ---TVDTSPWgrkpggygQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGP------T 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 529 V---YGNhtRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:cd17636 199 VmagYWN--RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 31980996 606 VKGECLYCFVTLCDGHTFSPtltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17636 277 RWAQSVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
136-374 |
1.17e-05 |
|
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: 48.37 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQGI--QKGDRVAIYMPMILELVVAMLACARLGalhsivfagfsaeslcerildssccllIT 213
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYS---------------------------LV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 214 TDAFYrgeklvnlKELADESLEkcrekgfpvrccIVVKHlgrAELGMndspsqsppvkrpcpdvqICWNEGVDLW-WHEL 292
Cdd:cd05927 59 TVPLY--------DTLGPEAIE------------YILNH---AEISI------------------VFCDAGVKVYsLEEF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 293 MQQ-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFH---PEDVfwctadigwitghsYV 368
Cdd:cd05927 98 EKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDV--------------YI 163
|
....*.
gi 31980996 369 TYGPLA 374
Cdd:cd05927 164 SYLPLA 169
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
108-216 |
2.41e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.43 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 108 LDRNVHEkkLGDKVAFYW---EGNEPGETTKITYRELLVQVCQFSNVLrKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 31980996 185 ALHSIVFA----GfSAESLCERILDSSCCLLITTDA 216
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA 151
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
545-673 |
2.48e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.78 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 545 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 624
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 31980996 625 PTLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
306-672 |
5.32e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.88 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 383
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 384 GIPTYpdegrlwsivdkykvtkFYTAPTAIRML----------MKFGDDP-VTKHSRA-------SLQVLGTVGEPINPE 445
Cdd:PRK06814 860 GVKVF-----------------LYPSPLHYRIIpeliydtnatILFGTDTfLNGYARYahpydfrSLRYVFAGAEKVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 446 AWLWYHRVVGSQrcpIVDTFWQTETGghmltP-LPGATPM--KPGSASFPFFGVAPAIlnesgeelegeaegylvfkQPW 522
Cdd:PRK06814 923 TRQTWMEKFGIR---ILEGYGVTETA-----PvIALNTPMhnKAGTVGRLLPGIEYRL-------------------EPV 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 523 PGI-------MR--TVYGNHTRFETTYFKKFP--GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 591
Cdd:PRK06814 976 PGIdeggrlfVRgpNVMLGYLRAENPGVLEPPadGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAEL 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 592 EAVAEAAVVGHPHPVKGECLYCFVTlcdghtfSPTLT-EELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06814 1056 WPDALHAAVSIPDARKGERIILLTT-------ASDATrAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
...
gi 31980996 670 IAQ 672
Cdd:PRK06814 1129 LAE 1131
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
113-374 |
5.98e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.25 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 113 HEKKLGDKVAfywEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARlgalHSIVfa 192
Cdd:PLN02736 59 DYKYLGTRIR---VDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSA----YSYV-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 193 gfsaeslcerildsSCCLLIT--TDAFyrgEKLVNLKELAD--------ESLEKCREKGFPVRCCIVVkhlGRAELGMND 262
Cdd:PLN02736 130 --------------SVPLYDTlgPDAV---KFIVNHAEVAAifcvpqtlNTLLSCLSEIPSVRLIVVV---GGADEPLPS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 263 SPSQSppvkrpcpdvqicwneGVDLWWHELMQQAGDECEPEWC--DAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATT 340
Cdd:PLN02736 190 LPSGT----------------GVEIVTYSKLLAQGRSSPQPFRppKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGS 253
|
250 260 270
....*....|....*....|....*....|....
gi 31980996 341 fKYVFDFHPEDVfwctadigwitghsYVTYGPLA 374
Cdd:PLN02736 254 -SLSTKFYPSDV--------------HISYLPLA 272
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
306-602 |
1.52e-04 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 44.66 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 306 DAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 382
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 383 EGIPTYPDEgrlwsiVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTV---GE---PINPEAWLWYH----- 451
Cdd:cd17640 160 TSIRTLKDD------LKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFlsgGIfkfGISGGGALPPHvdtff 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 452 RVVGsqrCPIVDTFWQTETGghmltplPGATPMKP-----GSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIM 526
Cdd:cd17640 234 EAIG---IEVLNGYGLTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG-PQVM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 527 RTVYGNHtrfETTyfKKF---PGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGH 602
Cdd:cd17640 303 KGYYKNP---EAT--SKVldsDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
136-648 |
2.23e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.20 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 136 ITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL--CERildssCC--- 209
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLlhCFR-----CCgak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 210 -LLITTDafyrgeklvnLKELADESLEKCREKGfpVRCCIV--------VKHLGRAelgMNDSPSQSPPVKrpcPDVQIC 280
Cdd:cd05938 81 vLVVAPE----------LQEAVEEVLPALRADG--VSVWYLshtsntegVISLLDK---VDAASDEPVPAS---LRAHVT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 281 WNegvdlwwhelmqqagdecepewcdaeDPLFILYTSGSTGKPKGVVhtIGGYMLYVATTFKYVFDFHPEDVFWCTA--- 357
Cdd:cd05938 143 IK--------------------------SPALYIYTSGTTGLPKAAR--ISHLRVLQCSGFLSLCGVTADDVIYITLply 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 358 -DIGWITGHSyvtyGPLANGATSVLFEGIPTypdeGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLqvlg 436
Cdd:cd05938 195 hSSGFLLGIG----GCIELGATCVLKPKFSA----SQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL---- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 437 TVGEPINPEAWLWYHRVVGSQRcpIVDTFWQTEtgGHM----LTPLPGATpmkpGSAS------FPF------------- 493
Cdd:cd05938 263 AIGNGLRADVWREFLRRFGPIR--IREFYGSTE--GNIgffnYTGKIGAV----GRVSylykllFPFelikfdvekeepv 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 494 -----FGVA-----PAILnesgeelegeaEGYLVFKQPWPG-----------IMRTVygnhtrfettyFKKFPGYYVTGD 552
Cdd:cd05938 335 rdaqgFCIPvakgePGLL-----------VAKITQQSPFLGyagdkeqtekkLLRDV-----------FKKGDVYFNTGD 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 553 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSptlTEEL 631
Cdd:cd05938 393 LLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLKPGHEFD---GKKL 469
|
570
....*....|....*..
gi 31980996 632 KKQIREKIGPIATPDYI 648
Cdd:cd05938 470 YQHVREYLPAYARPRFL 486
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-326 |
4.17e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 43.35 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGalHSIVFAGFS--A 196
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSspA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 197 ESLcERILDSS-CCLLITTDAFYRGE---KLVNLKELADESLEKcrekgfpvrccivvkhlgraelgmnDSPSQSPPVKr 272
Cdd:PRK04813 89 ERI-EMIIEVAkPSLIIATEELPLEIlgiPVITLDELKDIFATG-------------------------NPYDFDHAVK- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 31980996 273 pcpdvqicwnegvdlwwhelmqqaGDecepewcdaeDPLFILYTSGSTGKPKGV 326
Cdd:PRK04813 142 ------------------------GD----------DNYYIIFTSGTTGKPKGV 161
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
132-186 |
4.98e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.02 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31980996 132 ETTKITYRELLVQVCQFSNVLR-KQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVV 66
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
132-190 |
5.10e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 40.43 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980996 132 ETTKITYRellvQVCQFSNV----LRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIV 190
Cdd:TIGR03443 267 KTRSFTYK----QINEASNIlahyLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
301-445 |
5.56e-03 |
|
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: 39.78 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 301 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTIGGYMLYVATTfkyvFDFHPEDVF--W--CTADIGWITGHsyvtYGP 372
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980996 373 LANGATSVLfegIPT--YPDEGRLW-SIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKH-SRASLQVLGTVGEPINPE 445
Cdd:cd05908 170 LIAGMNQYL---MPTrlFIRRPILWlKKASEHKATIVSSPNFGYKYFLKTLKPEKANDwDLSSIRMILNGAEPIDYE 243
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
273-331 |
5.78e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 39.85 E-value: 5.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980996 273 PCPDVQICWNEGVDLWWHEL----MQQAGDECEPEWcDAEDPLFILYTSGSTGKPKGVVHTIG 331
Cdd:PRK09029 97 PSLTLDFALVLEGENTFSALtslhLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQ 158
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
555-659 |
5.81e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.09 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980996 555 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAavVGHPHPVKGECL-YCFVTLCDGHTFSPT-LTEELk 632
Cdd:PRK07868 845 RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLA--VTYGVEVGGRQLaVAAVTLRPGAAITAAdLTEAL- 921
|
90 100
....*....|....*....|....*..
gi 31980996 633 kqirEKIGPIATPDYIQNAPGLPKTRS 659
Cdd:PRK07868 922 ----ASLPVGLGPDIVHVVPEIPLSAT 944
|
|
| |
