|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-682 |
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: 1199.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 28 EKYKELYIKSVESPEEFWADVAKDFFWKTKYTGKFLDYnfdvtKGEIYIKCMEGATTNICYNVLDRNVHERklGDRVAFY 107
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWS-----KGPPFIKWFEGGKLNISYNCLDRHLKER--GDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 108 WEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIM 187
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 188 DSQCCLLITADGFYRGDKLINLKLIADEALKKCrdksFPVEKCIMLKHLTKEdeassgslsppakracpdlqqekqkerv 267
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE---------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 268 rkvrpppqVPWNPEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSD 347
Cdd:cd05966 202 --------VPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 348 DVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRT 427
Cdd:cd05966 274 DIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 428 SLKILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEG 507
Cdd:cd05966 354 SLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 508 PSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 587
Cdd:cd05966 434 EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVA 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 588 HEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKI 667
Cdd:cd05966 514 HPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
650
....*....|....*
gi 1036086734 668 ACNERDLGDVSTLAD 682
Cdd:cd05966 594 AAGEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
15-693 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1133.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 15 PGDLKKEAHIpSFEKYKELYIKSVESPEEFWADVAKDFFWKTKYTgKFLDYNfdvtkgEIYIKCMEGATTNICYNVLDRN 94
Cdd:PRK00174 5 PAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKPFD-TVLDWN------APFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 95 VHERklGDRVAFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVF 174
Cdd:PRK00174 77 LKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 175 AGFSSESLCERIMDSQCCLLITADGFYRGDKLINLKLIADEALKKCRdksfPVEKCIMLKHlTKEDeassgslsppakra 254
Cdd:PRK00174 155 GGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRR-TGGD-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 255 cpdlqqekqkervrkvrpppqVPWNPEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYT 334
Cdd:PRK00174 216 ---------------------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 335 ASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLM 414
Cdd:PRK00174 275 AMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 415 KYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVV 494
Cdd:PRK00174 355 KEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 495 PAILNESGEELEGPSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGH 574
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 575 LLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKT 654
Cdd:PRK00174 515 RLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKT 594
|
650 660 670
....*....|....*....|....*....|....*....
gi 1036086734 655 RSGKIMRRVLRKIACNERDLGDVSTLADSSVIEHLFENR 693
Cdd:PRK00174 595 RSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKLIEAR 633
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
24-692 |
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: 1055.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 24 IPSFEKYKELYIKSVESPEEFWADVAKD-FFWKTKYTgKFLDYNFDVtkgeiYIKCMEGATTNICYNVLDRnvHERKLGD 102
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKPFT-KVLDWSFPP-----FYKWFVGGELNVSYNCVDR--HLEARPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 103 RVAFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESL 182
Cdd:TIGR02188 73 KVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 183 CERIMDSQCCLLITADGFYRGDKLINLKLIADEALKKCRDKsfpVEKCIMLKHltkedeasSGSlsppakracpdlqqek 262
Cdd:TIGR02188 153 ADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRR--------TGN---------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 263 qkervrkvrppPQVPWNPEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVF 342
Cdd:TIGR02188 206 -----------PVVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 343 DYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVH 422
Cdd:TIGR02188 275 DIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 423 KYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESG 502
Cdd:TIGR02188 355 KHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEG 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 503 EELEGPSE-GYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 581
Cdd:TIGR02188 435 NPVEGPGEgGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEI 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 582 ESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:TIGR02188 515 ESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
650 660 670
....*....|....*....|....*....|..
gi 1036086734 662 RVLRKIACNERD-LGDVSTLADSSVIEHLFEN 692
Cdd:TIGR02188 595 RLLRKIAAGEAEiLGDTSTLEDPSVVEELIEA 626
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
10-691 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 895.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 10 DVLHAPGDLKKEAHIPSFEKYKELYIKSVESPEEFWADVAKDFFWKTKYTG-KFLDYNFDVTKGEIYIKCMEGATTNICY 88
Cdd:PLN02654 12 DLVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGdEVCSENLDVRKGPISIEWFKGGKTNICY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 89 NVLDRNVhERKLGDRVAFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGA 168
Cdd:PLN02654 92 NCLDRNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 169 VHSIVFAGFSSESLCERIMDSQCCLLITADGFYRGDKLINLKLIADEALKKCRDKSFPVEKCimlkhLTKEDEASsgsls 248
Cdd:PLN02654 171 VHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGIC-----LTYENQLA----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 249 ppakracpdLQQEKQKervrkvrpppqvpWNPEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVS 328
Cdd:PLN02654 241 ---------MKREDTK-------------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 329 GYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPT 408
Cdd:PLN02654 299 GYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 409 AIRLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATF 488
Cdd:PLN02654 379 LVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 489 PFFGVVPAILNESGEELEGPSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDM 568
Cdd:PLN02654 459 PFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDV 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNA 648
Cdd:PLN02654 539 INVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1036086734 649 PGLPKTRSGKIMRRVLRKIACNERD-LGDVSTLADSSVIEHLFE 691
Cdd:PLN02654 619 PGLPKTRSGKIMRRILRKIASRQLDeLGDTSTLADPGVVDQLIA 662
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
80-689 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 874.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 80 EGATTNICYNVLDRNVHERklGDRVAFYWEGnEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVA 159
Cdd:COG0365 4 VGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 160 MLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADGFYRGDKLINLKLIADEALKKCRDksfpVEKCIMLKhltke 239
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVG----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 240 deassgslsppakracpdlqqekqkervrkvRPPPQVPWNPEVDmcWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGK 319
Cdd:COG0365 152 -------------------------------RTGADVPMEGDLD--WDELLAAASAEFEPEPTDADDPLFILYTSGTTGK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 320 PKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYH 399
Cdd:COG0365 199 PKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 400 VSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAaT 479
Cdd:COG0365 279 VTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-L 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 480 PMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYY 559
Cdd:COG0365 355 PVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYF 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 560 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAI 639
Cdd:COG0365 435 WILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPY 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1036086734 640 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAcNERDLGDVSTLADSSVIEHL 689
Cdd:COG0365 515 AYPREIEFVDELPKTRSGKIMRRLLRKIA-EGRPLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
30-660 |
0e+00 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 712.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 30 YKELYIKSVESPEEFWADVAKDFFWKTKYTGKfldYNFDVTKGEIYIKCMEGATTNICYNVLDRNVHERklGDRVAFYWE 109
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKV---KNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 110 GNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDS 189
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 190 QCCLLITADGFYRGDKLINLKLIADEALKKcrdKSFPVEKCIMLKhltkedeassgslsppakracpdlqqekqkervrk 269
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLK----------------------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 270 vRPPPQVPWNPEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDV 349
Cdd:cd17634 198 -RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSL 429
Cdd:cd17634 277 YWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 430 KILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPS 509
Cdd:cd17634 357 RILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGT 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 510 EGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 589
Cdd:cd17634 437 EGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036086734 590 AVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIM 660
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
30-689 |
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 1036086734 30 YKELYIKSVESPEEFWADVAKDFFWKTKYTgKFLDYNFDVtkgeiYIKCMEGATTNICYNVLDRNVhERKLGDRVAFYWE 109
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPE-KILDNSNPP-----FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 110 GNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDS 189
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 190 QCCLLITADGFYRGDKLINLKLIADEALKKCRDKSfpvEKCIMLkhltkedeassgslsppakracpdlqqekQKERVrk 269
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELSGHKP---HHVLVL-----------------------------NRPQV-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 270 vrppPQVPWNPEVDMCWHSLIGGAsEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDV 349
Cdd:cd05967 200 ----PADLTKPGRDLDWSELLAKA-EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTADIGWITGHSYITYGPLANGATSVLFEGLPT-YPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDP----VHKY 424
Cdd:cd05967 275 WWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRK--EDPdgkyIKKY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 425 KRTSLKILGTVGEPINPEAWQWYYNVVGEkrcPVVDTFWQTETGGHVMTPLP--AATPMKPGSATFPFFGVVPAILNESG 502
Cdd:cd05967 353 DLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVglEPLPIKAGSPGKPVPGYQVQVLDEDG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 503 EELEGPSEGYLVFKQPW-PGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 581
Cdd:cd05967 430 EPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 582 ESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN-QKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIM 660
Cdd:cd05967 510 EESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKIL 589
|
650 660
....*....|....*....|....*....
gi 1036086734 661 RRVLRKIaCNERDLGDVSTLADSSVIEHL 689
Cdd:cd05967 590 RRTLRKI-ADGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
28-687 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 576.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 28 EKYKELYIKSVESPEEFWADVAKDFFWKTKYTgKFLDYN---FdvtkgeiyIKCMEGATTNICYNVLDRNVHERklGDRV 104
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFT-QVLDYSnppF--------ARWFVGGRTNLCHNAVDRHLAKR--PEQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 105 AFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCE 184
Cdd:PRK10524 71 ALIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 185 RIMDSQCCLLITADGFYRGDKLINLKLIADEALKKCrdkSFPVEKCIMLKhltkedeassgslsppakracpdlqqekqk 264
Cdd:PRK10524 151 RIDDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALA---QHKPRHVLLVD------------------------------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 265 ervRKVRPppqVPWNPEVDMCWHSL---IGGASEECEpvWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMV 341
Cdd:PRK10524 198 ---RGLAP---MARVAGRDVDYATLraqHLGARVPVE--WLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 342 FDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPV 421
Cdd:PRK10524 270 FGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 422 HKYKRTSLKILGTVGEPINPEAWQWYYNVVGEkrcPVVDTFWQTETGGHVMTPLP--AATPMKPGSATFPFFGVVPAILN 499
Cdd:PRK10524 350 RKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARgvEDRPTRLGSPGVPMYGYNVKLLN 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 500 E-SGEELEGPSEGYLVFKQPW-PGVMRTVYGNHLRFETTYFKKF-PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLL 576
Cdd:PRK10524 427 EvTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRL 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 577 STAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN-----QKLEAELKKQVREKIGAIATPDYIQNAPGL 651
Cdd:PRK10524 507 GTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSAL 586
|
650 660 670
....*....|....*....|....*....|....*.
gi 1036086734 652 PKTRSGKIMRRVLRKIaCNERDLGDVSTLADSSVIE 687
Cdd:PRK10524 587 PKTRSGKLLRRAIQAI-AEGRDPGDLTTIEDPAALQ 621
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
45-682 |
3.37e-175 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 512.13 E-value: 3.37e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 45 WADVAKDFFWKTkyTGKFldynfdvtkgeiyikcmegattNICYNVLDRNVHErKLGDRVAFYWEGnePGDEKTVTYREL 124
Cdd:PRK04319 27 WEEVEKEFSWLE--TGKV----------------------NIAYEAIDRHADG-GRKDKVALRYLD--ASRKEKYTYKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 125 LQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADGFYR-- 202
Cdd:PRK04319 80 KELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLErk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 203 -GDKLINLK--LIADEalkkcrdksfpvekcimlkhltkEDEASSGSLSppakracpdlqqekqkervrkvrpppqvpwn 279
Cdd:PRK04319 160 pADDLPSLKhvLLVGE-----------------------DVEEGPGTLD------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 pevdmcWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHtVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWI 359
Cdd:PRK04319 186 ------FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLH-VHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 360 TGHSYITYGPLANGATSVLFEGlptYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPI 439
Cdd:PRK04319 259 TGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 440 NPEAWQWYYNVVGEkrcPVVDTFWQTETGGHVMTPLPAaTPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPW 519
Cdd:PRK04319 336 NPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYPA-MDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGW 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNHLRFETtYFKkfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGR 599
Cdd:PRK04319 412 PSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 600 PHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRkiaCNERDL--GDV 677
Cdd:PRK04319 489 PDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK---AWELGLpeGDL 565
|
....*
gi 1036086734 678 STLAD 682
Cdd:PRK04319 566 STMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-682 |
3.35e-168 |
|
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: 495.86 E-value: 3.35e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 27 FEKYKELYIKSVESPEEFWADVAKDF-FWKTKYTGKFLDynfdVTKGEIYIKCMEGATTNICYNVLDRnvHERKLGDRVA 105
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTLD----LSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 106 FYWEGnEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCER 185
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 186 IMDSQCCLLITADGFYRGDKLINLKLIADEALKKCrdksFPVEKCIMLKHLTKEDEASSGS-LSPPAKRACPDLQQEKQk 264
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFTPAKGRdLSYDEEKETAGDGAERT- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 265 ervrkvrpppqvpwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDY 344
Cdd:cd05968 234 --------------------------------------ESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 345 HSDD-VYWCTaDIGWITGhSYITYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHK 423
Cdd:cd05968 276 KPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 424 YKRTSLKILGTVGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHVMTPLPAaTPMKPGSATFPFFGVVPAILNESGE 503
Cdd:cd05968 354 HDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVLI-KPIKPSSFNGPVPGMKADVLDESGK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 504 ELEgPSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVES 583
Cdd:cd05968 433 PAR-PEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 584 ALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRV 663
Cdd:cd05968 512 VLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRV 591
|
650
....*....|....*....
gi 1036086734 664 LRKIACNErDLGDVSTLAD 682
Cdd:cd05968 592 IRAAYLGK-ELGDLSSLEN 609
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
120-668 |
1.06e-138 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 414.21 E-value: 1.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADG 199
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 FYRgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppaKRacpdlqqekqkervrkvrpppqvpwn 279
Cdd:cd05969 82 LYE-------------------------------------------------RT-------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 pevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHtVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWI 359
Cdd:cd05969 87 -----------------------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWV 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 360 TGHSYITYGPLANGATSVLFEGlptYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPI 439
Cdd:cd05969 143 TGTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 440 NPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAaTPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPW 519
Cdd:cd05969 220 NPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGW 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNHLRFETtYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGR 599
Cdd:cd05969 296 PSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGK 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 600 PHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:cd05969 373 PDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
119-666 |
1.14e-110 |
|
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: 341.24 E-value: 1.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 119 VTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSqccllitad 198
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 gfyrgdklinlkliadealkkcrdksfpVEKCIMlkhltkedeassgslsppakracpdlqqekqkervrkvrpppqvpw 278
Cdd:cd05972 72 ----------------------------GAKAIV---------------------------------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 279 npevdmcwhsliggaseecepvwCDSEDPLFILYTSGSTGKPKGVLHTVSgYMLYTASTFKMVFDYHSDDVYWCTADIGW 358
Cdd:cd05972 78 -----------------------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGW 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 359 ITGHSYITYGPLANGATSVLFEGLPTypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSdpvHKYKRTSLKILGTVGEP 438
Cdd:cd05972 134 AKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDL---SSYKFSHLRLVVSAGEP 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 439 INPEAWQWYYNVVGEkrcPVVDTFWQTETGGHVMTPLpaATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQP 518
Cdd:cd05972 209 LNPEVIEWWRAATGL---PIRDGYGQTETGLTVGNFP--DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 519 WPGVMRTVYGNHLRFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 598
Cdd:cd05972 284 PPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVG 360
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036086734 599 RPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05972 361 SPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-572 |
4.77e-109 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 336.59 E-value: 4.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 91 LDRNVheRKLGDRVAFywegnEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVH 170
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 171 SIVFAGFSSESLCERIMDSQCCLLITADGFYrgdklinlkliaDEALKKCRDKSFPVEKCIMLKHLtkedeassgslspp 250
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRD-------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 251 akracPDLQQEKQKERVRKVRPPPqvpwnpevdmcwhsliggaseeCEPVWCDSEDPLFILYTSGSTGKPKGVLHTVsGY 330
Cdd:pfam00501 128 -----PVLKEEPLPEEAKPADVPP----------------------PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 331 MLYTASTFKMV----FDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTyPDVSRMWEIVDKYHVSKFYTA 406
Cdd:pfam00501 180 LVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 407 PTAIRLLMKYGsdPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAATPM-KPGS 485
Cdd:pfam00501 259 PTLLNMLLEAG--APKRALLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 486 ATFPFFGVVPAILNESGEELEGPSE-GYLVFKQpwPGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGR 564
Cdd:pfam00501 334 VGRPLPGTEVKIVDDETGEPVPPGEpGELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGR 409
|
....*...
gi 1036086734 565 IDDMLNVS 572
Cdd:pfam00501 410 KKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
90-668 |
3.45e-91 |
|
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: 291.33 E-value: 3.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVHERklGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:COG0318 4 LLRRAAARH--PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 HSIVFAGFSSESLCERIMDSQCCLLITAdgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsp 249
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVTA---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 250 pakracpdlqqekqkervrkvrpppqvpwnpevdmcwhsliggaseecepvwcdsedplFILYTSGSTGKPKGVLHTVSG 329
Cdd:COG0318 104 -----------------------------------------------------------LILYTSGTTGRPKGVMLTHRN 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 330 yMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLfeglPTYPDVSRMWEIVDKYHVSKFYTAPTA 409
Cdd:COG0318 125 -LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTM 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 410 IRLLMKYgsDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFP 489
Cdd:COG0318 200 LARLLRH--PEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 490 FFGVVPAILNESGEELEGPSEGYLVFKQPWpgVMRTVYGNHlrfETTyFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDM 568
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDP---EAT-AEAFRdGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNA 648
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD---AEELRAFLRERLARYKVPRRVEFV 425
|
570 580
....*....|....*....|
gi 1036086734 649 PGLPKTRSGKIMRRVLRKIA 668
Cdd:COG0318 426 DELPRTASGKIDRRALRERY 445
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
306-660 |
1.31e-89 |
|
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: 283.41 E-value: 1.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMvFDYHSDDVYWCTADIGWItGHSYITYGPLANGATSVLFEGlpty 385
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 386 PDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYgsDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQT 465
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKA--PESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 466 ETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWpgVMRtVYGNhlRFETTYFKKFPGYY 545
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPS--VMK-GYWN--NPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 546 VTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqKLE 625
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD---LDA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 1036086734 626 AELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIM 660
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
41-666 |
9.37e-81 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 269.69 E-value: 9.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 41 PEEFWADVAKDF-FWKTKYTGKfldYNFDvtkgEIYIKCMEGATTNICYNVLDRNVHERKLGDRVAFYWEGnePGDEKTV 119
Cdd:PTZ00237 21 PESFWDEVAKKYvHWDKMYDKV---YSGD----EIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYEC--PYLKKTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 --TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITA 197
Cdd:PTZ00237 92 klTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 198 DGFYRGDKLINLKLIADEALKKcrdKSFPVEKCIMLKHLTKEDEASSGSL-SPPAKRACPDLQQEkqkerVRKVRPPPQV 276
Cdd:PTZ00237 172 NYGILNDEIITFTPNLKEAIEL---STFKPSNVITLFRNDITSESDLKKIeTIPTIPNTLSWYDE-----IKKIKENNQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 PWNPEVdmcwhsliggaseecePVwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWCTADI 356
Cdd:PTZ00237 244 PFYEYV----------------PV--ESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 357 GWITGHSYItYGPLANGATSVLFEGLPTYPDVSR--MWEIVDKYHVSKFYTAPTAIRLLMKYgsDP----VH-KYKRTSL 429
Cdd:PTZ00237 306 GWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKHIEddLWNTIEKHKVTHTLTLPKTIRYLIKT--DPeatiIRsKYDLSNL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 430 KILGTVGEPINPEAWQWYYNVVgekRCPVVDTFWQTETGghVMTPLPAATPMKPGSAT-FPFFGVVPAILNESGEELEGP 508
Cdd:PTZ00237 383 KEIWCGGEVIEESIPEYIENKL---KIKSSRGYGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 509 SEGYLVFKQPWP-GVMRTVYGNHLRFETTyFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 587
Cdd:PTZ00237 458 EIGEVAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 588 HEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQ----KLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRV 663
Cdd:PTZ00237 537 HPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQI 616
|
...
gi 1036086734 664 LRK 666
Cdd:PTZ00237 617 ISK 619
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
120-666 |
8.15e-77 |
|
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: 253.21 E-value: 8.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITadg 199
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 fyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpDLQQEkqkervrkvrpppqvpwn 279
Cdd:cd05973 79 ---------------------------------------------------------DAANR------------------ 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 pevdmcwHSLiggaseecepvwcdSEDPLFILYTSGSTGKPKGVLHTVSgYMLYTASTFKMVFDYHSDDVYWCTADIGWI 359
Cdd:cd05973 84 -------HKL--------------DSDPFVMMFTSGTTGLPKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWA 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 360 TGHSYITYGPLANGATSVLFEGLPTYPDVsrmWEIVDKYHVSKFYTAPTAIRLLMKYGSdPVHKYKRTSLKILGTVGEPI 439
Cdd:cd05973 142 YGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAGA-EVPARPKGRLRRVSSAGEPL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 440 NPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELeGPSEgylvfkqpw 519
Cdd:cd05973 218 TPEVIRWFDAALG---VPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDEL-GPGE--------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNH--LRFETTYFKKFP----GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 593
Cdd:cd05973 285 PGRLAIDIANSplMWFRGYQLPDTPaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAE 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 594 AAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05973 365 AAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
20-688 |
9.24e-77 |
|
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: 258.36 E-value: 9.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 20 KEAHIPSFEKYKELYIKSVESPEEFWADVaKDFF---WKTKYTgkfldyNFDVTKGEiyikcME------GATTNICYNV 90
Cdd:cd05943 9 NARHGLSLADYAALHRWSVDDPGAFWAAV-WDFSgvrGSKPYD------VVVVSGRI-----MPgarwfpGARLNYAENL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 91 LDRNVHErklgDRVAFYWEGNEPGDEktVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVH 170
Cdd:cd05943 77 LRHADAD----DPAAIYAAEDGERTE--VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 171 SIVFAGFSSESLCERIMDSQCCLLITADGFYRGDKLINlkliadealkkcrdksfpvekcimlkHLTKEDEASSGSLSPP 250
Cdd:cd05943 151 SSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHD--------------------------VREKVAELVKGLPSLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 251 AKRACPDLQQEKQKErvrkVRPPPQVPWnpevdmcWHSLIG-GASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSG 329
Cdd:cd05943 205 AVVVVPYTVAAGQPD----LSKIAKALT-------LEDFLAtGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 330 YMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYgpLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTA 409
Cdd:cd05943 274 TLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 410 IRLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEkrcpvvDTFWQTETGGhvmTPLPAA-------TPMK 482
Cdd:cd05943 352 LDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVY 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 483 PGSATFPFFGVVPAILNESGEELEGPSeGYLVFKQPWPGvmRTVY----GNHLRFETTYFKKFPGYYVTGDGCRRDKDGY 558
Cdd:cd05943 423 RGEIQCRGLGMAVEAFDEEGKPVWGEK-GELVCTKPFPS--MPVGfwndPDGSRYRAAYFAKYPGVWAHGDWIEITPRGG 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 559 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGA 638
Cdd:cd05943 500 VVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSP 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1036086734 639 IATPDYIQNAPGLPKTRSGKIMRRVLRKIACNeRDLGDVSTLADSSVIEH 688
Cdd:cd05943 580 RHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAG-RPVKNAGALANPESLDL 628
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
26-664 |
8.97e-73 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 248.17 E-value: 8.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 26 SFEKYKELYIKSVESPEEFWADVAkDFF---WKTKYT-----GKFLDYNFdvtkgeiyikcMEGATTNICYNVLdrnVHE 97
Cdd:PRK03584 32 SFDDYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYTvvlagRRMPGARW-----------FPGARLNYAENLL---RHR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RklGDRVAFYWEGnEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK03584 97 R--DDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITADGFYRGDKLINLKliadEALKKCRDKSFPVEKCIMLKHLTKEDEASsgslsppakracpd 257
Cdd:PRK03584 174 GVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRR----AKVAELRAALPSLEHVVVVPYLGPAAAAA-------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 lqqekqkervrkvRPPPQVPWNpevdmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAST 337
Cdd:PRK03584 236 -------------ALPGALLWE-------DFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 FKMVFDYHSDDVY-WCTAdIGWI------TGhsyitygpLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAI 410
Cdd:PRK03584 296 LGLHCDLGPGDRFfWYTT-CGWMmwnwlvSG--------LLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 411 RLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEkrcpvvDTFWQTETGG-HVMTPLPAATPMKP---GSA 486
Cdd:PRK03584 367 DACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNPLLPvyrGEI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 487 TFPFFGVVPAILNESGEELEGpSEGYLVFKQPWPGvMrTVY-----GNHlRFETTYFKKFPGYYVTGDGCRRDKDGYYWI 561
Cdd:PRK03584 441 QCRGLGMAVEAWDEDGRPVVG-EVGELVCTKPFPS-M-PLGfwndpDGS-RYRDAYFDTFPGVWRHGDWIEITEHGGVVI 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 562 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIAT 641
Cdd:PRK03584 517 YGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHV 596
|
650 660
....*....|....*....|....*..
gi 1036086734 642 PDYIQNAPGLPKTRSGKIM----RRVL 664
Cdd:PRK03584 597 PDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
114-665 |
2.41e-71 |
|
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: 238.49 E-value: 2.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITaDGfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrpp 273
Cdd:cd05971 82 LVT-DG-------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqvpwnpevdmcwhsliggaseecepvwcdSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDY--HSDDVYW 351
Cdd:cd05971 87 ------------------------------SDDPALIIYTSGTTGPPKGALHA-HRVLLGHLPGVQFPFNLfpRDGDLYW 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 CTADIGWItghsyityGPLANGATSVLFEGLP------TYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGsdPVHKYK 425
Cdd:cd05971 136 TPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQG--EQLKHA 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGTVGEPINPEAWQWYYNVVGEkrcPVVDTFWQTEtGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEEL 505
Cdd:cd05971 206 QVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPL 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 506 EGPSEGYLVFKQPWPGVMRTVYGNhlrfETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESA 584
Cdd:cd05971 282 PPGEVGEIAVELPDPVAFLGYWNN----PSATEKKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEC 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 585 LVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd05971 358 LLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
.
gi 1036086734 665 R 665
Cdd:cd05971 438 R 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
88-665 |
2.17e-67 |
|
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: 229.95 E-value: 2.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 88 YN---VLDRNVhERKLGDRVAFYwegnepGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACA 164
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 165 RIGAVhsivfagfsseslcerimdsqccllitadgfyrgDKLINLKLIADE---ALKKCRDKSFPVekcimlkhltkede 241
Cdd:cd05959 76 RAGIV----------------------------------PVPVNTLLTPDDyayYLEDSRARVVVV-------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 242 asSGSLSPPAKRACPDLQQEKqkerVRKVRPPPQVPWNPEVDMcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPK 321
Cdd:cd05959 108 --SGELAPVLAAALTKSEHTL----VVLIVSGGAGPEAGALLL--AELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 322 GVLHTVSGyMLYTASTF-KMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTyPDvsRMWEIVDKYHV 400
Cdd:cd05959 180 GVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 401 SKFYTAPTAIRLLMKygSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAAtp 480
Cdd:cd05959 256 TVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR-- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 481 MKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWPGVMrtvYGNhlRFETTYfKKFPGYYV-TGDGCRRDKDGYY 559
Cdd:cd05959 329 VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM---YWN--NRDKTR-DTFQGEWTrTGDKYVRDDDGFY 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 560 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAI 639
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPY 482
|
570 580
....*....|....*....|....*.
gi 1036086734 640 ATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05959 483 KYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
88-665 |
4.24e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 221.60 E-value: 4.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 88 YNVLDRNVheRKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIG 167
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 168 AVhsivfagfsseslcerimdsqcclLITadgfyrgdklINLKLIADEA---LKKCRDKSFPVEkcimlkhltkedeass 244
Cdd:PRK06187 81 AV------------------------LHP----------INIRLKPEEIayiLNDAEDRVVLVD---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 245 GSLSPPAKRACPDLqqekqkERVRKV---RPPPQVPWNPEVDmCWHSLIGGASEEcePVWCDSE--DPLFILYTSGSTGK 319
Cdd:PRK06187 111 SEFVPLLAAILPQL------PTVRTViveGDGPAAPLAPEVG-EYEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 320 PKGVLHTVSGYMLYTASTfKMVFDYHSDDVY-----------WctadiGWitghsyiTYGPLANGATSVlfeglptYP-- 386
Cdd:PRK06187 182 PKGVVLSHRNLFLHSLAV-CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV-------IPrr 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 387 -DVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGtvGEPINP---EAWQwyynvvgEK-RCPVVDT 461
Cdd:PRK06187 242 fDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPallREFK-------EKfGIDLVQG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 462 FWQTETGGHV-MTPLPAATP---MKPGSATFPFFGVVPAILNESGEELE--GPSEGYLVFKQPWpgVMRTVYGNHLRFET 535
Cdd:PRK06187 313 YGMTETSPVVsVLPPEDQLPgqwTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPW--LMQGYWNRPEATAE 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 536 TYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLN 615
Cdd:PRK06187 391 TIDG---GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK 467
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1036086734 616 DGINYNqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK06187 468 PGATLD---AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
85-666 |
1.35e-63 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 220.42 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 85 NICYNVLDRNVHERKLGDRV---AFYWEgNEPGDEKTVTYRELLQQVCKFANVL-KSQGVKKGDRVSIYMPMVVELVVAM 160
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 161 LACARIGavhsIVFAGFSSEslcerimdsqcclLITADGFYRgdklinlkLIADEAlkkcrdksfpveKCIMlkhltked 240
Cdd:cd05928 85 VACIRTG----LVFIPGTIQ-------------LTAKDILYR--------LQASKA------------KCIV-------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 241 eaSSGSLSPPAKRA---CPDLQQEKQkervrkVRPPPQVPWnpevdMCWHSLIGGASEECEPVWCDSEDPLFILYTSGST 317
Cdd:cd05928 120 --TSDELAPEVDSVaseCPSLKTKLL------VSEKSRDGW-----LNFKELLNEASTEHHCVETGSQEPMAIYFTSGTT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 318 GKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATsVLFEGLPTYpDVSRMWEIVDK 397
Cdd:cd05928 187 GSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 398 YHVSKFYTAPTAIRLLMKygsDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPlpA 477
Cdd:cd05928 265 YPITTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG---LDIYEGYGQTETGLICANF--K 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 478 ATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVF--KQPWPGVMRTVY-GNHLRFETTYFKKFpgyYVTGDGCRRD 554
Cdd:cd05928 337 GMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 555 KDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLN-DGINYNQ-KLEAELKKQV 632
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQFLSHDPeQLTKELQQHV 493
|
570 580 590
....*....|....*....|....*....|....
gi 1036086734 633 REKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05928 494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
91-661 |
3.25e-62 |
|
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: 214.01 E-value: 3.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 91 LDRNVheRKLGDRVAFYWEGNepgdekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVH 170
Cdd:cd17631 1 LRRRA--RRHPDRTALVFGGR------SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 171 SivfagfsseslcerimdsqccllitadgfyrgdkLINLKLIADEalkkcrdksfpvekcimLKHLTKEDEAssgslspp 250
Cdd:cd17631 73 V----------------------------------PLNFRLTPPE-----------------VAYILADSGA-------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 251 akracpdlqqekqkervrKVrpppqvpwnpevdmcwhsLIggaseecepvwcdsEDPLFILYTSGSTGKPKGVLHTvSGY 330
Cdd:cd17631 94 ------------------KV------------------LF--------------DDLALLMYTSGTTGRPKGAMLT-HRN 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 331 MLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGlptyPDVSRMWEIVDKYHVSKFYTAPTAI 410
Cdd:cd17631 123 LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMI 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 411 RLLMKYGSDPvhKYKRTSLKILGTVGEPINP---EAWQwyynvvgEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSAT 487
Cdd:cd17631 199 QALLQHPRFA--TTDLSSLRAVIYGGAPMPErllRALQ-------ARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAG 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 488 FPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRtvyGNHLRFETT--YFKKfpGYYVTGDGCRRDKDGYYWITGRI 565
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVMA---GYWNRPEATaaAFRD--GWFHTGDLGRLDEDGYLYIVDRK 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 566 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYI 645
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG---AELDEDELIAHCRERLARYKIPKSV 419
|
570
....*....|....*.
gi 1036086734 646 QNAPGLPKTRSGKIMR 661
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
85-665 |
1.13e-59 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 210.04 E-value: 1.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 85 NICYNVLDRNVHERKlgDRVAFYWeGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACA 164
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 165 RIGAvhsivfagfsseslcerIMDSQCCLLITADGFYRGDKlINLKLIAdealkkcrdksfpvekCIMLKHLTKEDEASS 244
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYRIES-ADIKMIV----------------AIAEDNIPEEIEKAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 245 GSLSPPAKRAcpdlqqekqkervrKVRPPPQVPWnpevdMCWHSLIGGASEECEP----VWCDSEDPLFILYTSGSTGKP 320
Cdd:cd05970 140 PECPSKPKLV--------------WVGDPVPEGW-----IDFRKLIKNASPDFERptanSYPCGEDILLVYFSSGTTGMP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 321 KGVLHtVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTYPDvsRMWEIVDKYHV 400
Cdd:cd05970 201 KMVEH-DFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 401 SKFYTAPTAIRLLMKygsDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKrcpVVDTFWQTETGGHVMTpLPAATP 480
Cdd:cd05970 278 TTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 481 mKPGSATFPFFGVVPAILNESGEELEGPSEGYLVF----KQPWpGVMRTVYGNHLRFETTYFKkfpGYYVTGDGCRRDKD 556
Cdd:cd05970 351 -KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDED 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 557 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKI 636
Cdd:cd05970 426 GYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVT 505
|
570 580
....*....|....*....|....*....
gi 1036086734 637 GAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05970 506 APYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
21-667 |
4.69e-58 |
|
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: 208.20 E-value: 4.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 21 EAHIPSFEKYKELYIKSVESPEEFWADVAKdffWKTKYTGKFLDYNFDVTKGeIYIKCMEGATTNICYNVLdrnvheRKL 100
Cdd:TIGR01217 28 EHHGAAEGGYDALHRWSVDELDTFWKAVWE---WFDVRFSTPCARVVDDRTM-PGAQWFPGARLNYAENLL------RAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 101 G-DRVAFYW-EGNEPGdekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFS 178
Cdd:TIGR01217 98 GtEPALLYVdETHEPA---PVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 179 SESLCERIMDSQCCLLITADGFYRGDKlinlKLIADEALKKCRdKSFPVEKCIMLKHLtkedeassgsLSPPAKRAcpdl 258
Cdd:TIGR01217 175 ARGVLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPTLRAVVHIPY----------LGPRETEA---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 259 qqekqkervrkvrppPQVPWNpevdMCWHSLIGGAsEECEPVW--CDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAS 336
Cdd:TIGR01217 236 ---------------PKIDGA----LDLEDFTAAA-QAAELVFeqLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 337 TFKMVFDYHSDDVYWCTADIGWITGHSYITygPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKY 416
Cdd:TIGR01217 296 EHGLHCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 417 GSDPVHKYKRTSLKILGTVGEPINPEAWQWYYnvvgekRCPVVDTFWQTETGG-HVMTPLPAATPMKP---GSATFPFFG 492
Cdd:TIGR01217 374 GVHPARTHDLSALQCVASTGSPLPPDGFRWVY------DEIKADVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 493 VVPAILNESGEELEGPSeGYLVFKQPWPGvMRTVYGNH---LRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML 569
Cdd:TIGR01217 448 TAVQSWDPEGKPVTGEV-GELVCTNPMPS-MPIRFWNDpdgSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTL 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 570 NVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAP 649
Cdd:TIGR01217 526 NPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVP 605
|
650
....*....|....*...
gi 1036086734 650 GLPKTRSGKIMRRVLRKI 667
Cdd:TIGR01217 606 GIPHTLTGKRVEVAVKRV 623
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
88-665 |
2.40e-57 |
|
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: 201.64 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 88 YNVLDRNVheRKLGDRVAFYWegnepgDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIG 167
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 168 AvhsIVFagfsseslcerimdsqccllitadgfyrgdkLINLKLIADEalkkcrdksfpvekcimLKHLTKEDEASSGsl 247
Cdd:cd05936 74 A---VVV-------------------------------PLNPLYTPRE-----------------LEHILNDSGAKAL-- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 248 sppakracpdlqqekqkervrkvrpppqvpwnpEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTv 327
Cdd:cd05936 101 ---------------------------------IVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLT- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 328 SGYMLYTASTFKMVF--DYHSDDVYWCTADIgwitghsYITYG-------PLANGATSVLfegLPTyPDVSRMWEIVDKY 398
Cdd:cd05936 147 HRNLVANALQIKAWLedLLEGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEIRKH 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 HVSKFYTAPTAIRLLMkyGSDPVHKYKRTSLKILGTVGEPINPE-AWQWyynvvgEKR--CPVVDTFWQTETGghvmtPL 475
Cdd:cd05936 216 RVTIFPGVPTMYIALL--NAPEFKKRDFSSLRLCISGGAPLPVEvAERF------EELtgVPIVEGYGLTETS-----PV 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 476 PAATPM----KPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRtvyGNHLRFETT--YFKKfpGYYVTGD 549
Cdd:cd05936 283 VAVNPLdgprKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMK---GYWNRPEETaeAFVD--GWLRTGD 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 550 GCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqKLEAELK 629
Cdd:cd05936 356 IGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS---LTEEEII 432
|
570 580 590
....*....|....*....|....*....|....*.
gi 1036086734 630 KQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05936 433 AFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
115-665 |
2.84e-56 |
|
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: 198.07 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSivfagfsseslcerimdsqccll 194
Cdd:cd05919 7 ADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAV----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 itadgfyrgdkLINLKLIADEALKKCRDKsfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrppp 274
Cdd:cd05919 64 -----------VINPLLHPDDYAYIARDC--------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qvpwnpevdmcwhsliggaseECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWCTA 354
Cdd:cd05919 82 ---------------------EARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 355 DI--GWITGHSYItyGPLANGATSVLFeglPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKrtSLKIL 432
Cdd:cd05919 141 KMffGYGLGNSLW--FPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALR--SLRLC 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 433 GTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAAtpMKPGSATFPFFGVVPAILNESGEELEGPSEGY 512
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFG---GPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGD 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 513 LVFKQPWPGVMrtvYGNhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 592
Cdd:cd05919 289 LLVRGPSAAVG---YWN--NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 593 EAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05919 364 EAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
113-666 |
6.03e-56 |
|
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: 198.69 E-value: 6.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 113 PGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCC 192
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 193 LLITADGFyrgdklinlKLIADEALKKCRdksfpvekcimLKHLTKEDEASSGSLSPPAKracpDLQQEKQKERVRKVRP 272
Cdd:cd05926 89 LVLTPKGE---------LGPASRAASKLG-----------LAILELALDVGVLIRAPSAE----SLSNLLADKKNAKSEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 273 PPQvpwnpevdmcwhsliggaseecepvwcdSEDPLFILYTSGSTGKPKGVLHT---VSGYMLYTASTFKMVFD------ 343
Cdd:cd05926 145 VPL----------------------------PDDLALILHTSGTTGRPKGVPLThrnLAASATNITNTYKLTPDdrtlvv 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 344 ---YHsddvywctadigwITGhsyitygpLANGATSVLFEG----LPTYPDVSRMWEIVDKYHVSkFYTA-PTAIR-LLM 414
Cdd:cd05926 197 mplFH-------------VHG--------LVASLLSTLAAGgsvvLPPRFSASTFWPDVRDYNAT-WYTAvPTIHQiLLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 415 KYGSDPVHKYkrTSLKILGTVGEPINP---EAWQWYYnvvgekRCPVVDTFWQTETGgHVMT--PLPAaTPMKPGSATFP 489
Cdd:cd05926 255 RPEPNPESPP--PKLRFIRSCSASLPPavlEALEATF------GAPVLEAYGMTEAA-HQMTsnPLPP-GPRKPGSVGKP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 490 FfGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGNHlrfETT--YFKKFpGYYVTGDGCRRDKDGYYWITGRIDD 567
Cdd:cd05926 325 V-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNP---EANaeAAFKD-GWFRTGDLGYLDADGYLFLTGRIKE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 568 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQN 647
Cdd:cd05926 398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG---ASVTEEELRAFCRKHLAAFKVPKKVYF 474
|
570
....*....|....*....
gi 1036086734 648 APGLPKTRSGKIMRRVLRK 666
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
117-660 |
6.93e-52 |
|
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: 187.03 E-value: 6.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLIT 196
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADGFYrgDKLInlkliadEALKKCrdksFPVEKCIMLKHltkedeassgslSPPAKRACPDLQQEKQKERVRKVRPPPQV 276
Cdd:cd05911 89 DPDGL--EKVK-------EAAKEL----GPKDKIIVLDD------------KPDGVLSIEDLLSPTLGEEDEDLPPPLKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 PwnpevdmcwhsliggaseecepvwcdSEDPLFILYTSGSTGKPKGVLHT----VSGYMLYTASTFKMvfdYHSDDVYWC 352
Cdd:cd05911 144 G--------------------------KDDTAAILYSSGTTGLPKGVCLShrnlIANLSQVQTFLYGN---DGSNDVILG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 TADIGWITGHSYITYGPLaNGATSVLFEGlptyPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSdpVHKYKRTSLKIL 432
Cdd:cd05911 195 FLPLYHIYGLFTTLASLL-NGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 433 GTVGEPINPEAwqwyYNVVGEKRCPVVDTF-W-QTETGGHVMTPLPaaTPMKPGSATFPFFGVVPAILNESGEELEGPSE 510
Cdd:cd05911 268 LSGGAPLSKEL----QELLAKRFPNATIKQgYgMTETGGILTVNPD--GDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 511 -GYLVFKQPwpGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 589
Cdd:cd05911 342 pGEICVRGP--QVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHP 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 590 AVAEAAVVGRPHPVKGESLYCFVTLNDGinynQKL-EAELKKQVREKI--------GAIATPDyiqnapgLPKTRSGKIM 660
Cdd:cd05911 418 GVADAAVIGIPDEVSGELPRAYVVRKPG----EKLtEKEVKDYVAKKVasykqlrgGVVFVDE-------IPKSASGKIL 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
85-666 |
5.86e-51 |
|
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: 185.04 E-value: 5.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 85 NICYNVLDRNVhERKLGDRVAFYwegnepGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACA 164
Cdd:TIGR02262 4 NAAEDLLDRNV-VEGRGGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 165 RIGAVhsivfagfsseslcerimdsqccllitadgfyrgDKLINLKLIADE---ALKKCRDKSFPVekcimlkhltkede 241
Cdd:TIGR02262 77 RAGIV----------------------------------PVALNTLLTADDyayMLEDSRARVVFV-------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 242 asSGSLSPPAKRACPDLQQEKQkeRVRKVRPPPqvpwnPEVDMCwhSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPK 321
Cdd:TIGR02262 109 --SGALLPVIKAALGKSPHLEH--RVVVGRPEA-----GEVQLA--ELLATESEQFKPAATQADDPAFWLYSSGSTGMPK 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 322 GVLHTVSGyMLYTASTF-KMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLPTyPDvsRMWEIVDKYHV 400
Cdd:TIGR02262 178 GVVHTHSN-PYWTAELYaRNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 401 SKFYTAPTAIRLLMkygSDPVHKYKR-TSLKILGTVGEPInPEA----WQWYYNVvgekrcPVVDTFWQTETGGHVMTPL 475
Cdd:TIGR02262 254 TIFYGVPTLYAAML---ADPNLPSEDqVRLRLCTSAGEAL-PAEvgqrWQARFGV------DIVDGIGSTEMLHIFLSNL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 476 PAAtpMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWPGVMrtVYGNHLRFETTYFKkfpGYYVTGDGCRRDK 555
Cdd:TIGR02262 324 PGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRND 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 556 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREK 635
Cdd:TIGR02262 397 DGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG---QTALETELKEHVKDR 473
|
570 580 590
....*....|....*....|....*....|.
gi 1036086734 636 IGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:TIGR02262 474 LAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
98-666 |
6.72e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 185.14 E-value: 6.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEgnepgdEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK08316 22 RRYPDKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITADGFYRgdklinlklIADEALKKCRDKSFPVEKcimlkhltkedeASSGSLSPPAKRACPD 257
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAP---------TAEAALALLPVDTLILSL------------VLGGREAPGGWLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEkqkervrkvRPPPQvpwnPEVDMcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHT----VSGYMly 333
Cdd:PRK08316 155 WAEA---------GSVAE----PDVEL------------------ADDDLAQILYTSGTESLPKGAMLThralIAEYV-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 334 taSTFkMVFDYHSDDV-------YWCTADigwitgHSYItyGP-LANGATSVLFEGlptyPDVSRMWEIVDKYHVSKFYT 405
Cdd:PRK08316 202 --SCI-VAGDMSADDIplhalplYHCAQL------DVFL--GPyLYVGATNVILDA----PDPELILRTIEAERITSFFA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 406 APTA-IRLLmkyGSDPVHKYKRTSLKiLGTVGEPINPEAwqwyynVVGE--KRCPVVdTFW----QTETGghvmtplPAA 478
Cdd:PRK08316 267 PPTVwISLL---RHPDFDTRDLSSLR-KGYYGASIMPVE------VLKElrERLPGL-RFYncygQTEIA-------PLA 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 479 TPM-------KPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpgvmrtvygnHLRfeTTYFKKfP--------- 542
Cdd:PRK08316 329 TVLgpeehlrRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP-----------QLM--LGYWDD-Pektaeafrg 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQ 622
Cdd:PRK08316 395 GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG---AT 471
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1036086734 623 KLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK08316 472 VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
306-665 |
6.60e-48 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 174.40 E-value: 6.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSgYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLfegLPTY 385
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHA-NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 386 pDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPvhkyKRTSLKILGTVGEPINPEAWQWYynvvgEKR--CPVVDTFW 463
Cdd:cd05934 158 -SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHEEF-----EERfgVRLLEGYG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 464 QTETGGHVMTPLPAATPmkPGSATFPFFGVVPAILNESGEELEGPSEGYLVFK-QPWPGVMRTVYGNhlrfETTYFKKFP 542
Cdd:cd05934 228 MTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYYNM----PEATAEAMR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 -GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyn 621
Cdd:cd05934 302 nGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG---- 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1036086734 622 QKL-EAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05934 378 ETLdPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
98-666 |
5.48e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 173.94 E-value: 5.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAfYWEGnepgdEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivfagf 177
Cdd:PRK07656 16 RRFGDKEA-YVFG-----DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 sseslcerimdsqcclLITadgfyrgdklINLKLIADEA---LKKCRDKSFpvekcIMLKHLTKEDEASSGSLsppakra 254
Cdd:PRK07656 82 ----------------VVP----------LNTRYTADEAayiLARGDAKAL-----FVLGLFLGVDYSATTRL------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 255 cPDLQqekqkervRKVRPPPQVPWNPEVDMC-WHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTvSGYMLY 333
Cdd:PRK07656 124 -PALE--------HVVICETEEDDPHTEKMKtFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLT-HRQLLS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 334 TASTFKMVFDYHSDDVYWC----------TAdiGWITghsyitygPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKF 403
Cdd:PRK07656 194 NAADWAEYLGLTEGDRYLAanpffhvfgyKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 404 YTAPTAIRLLmkYGSDPVHKYKRTSLKILGTVGEPINPEAWQwyyNVVGEKRCPVVDT-FWQTETGGHV-MTPL--PAAT 479
Cdd:PRK07656 260 PGPPTMYNSL--LQHPDRSAEDLSSLRLAVTGAASMPVALLE---RFESELGVDIVLTgYGLSEASGVTtFNRLddDRKT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 480 PmkPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGnhLRFETTYFKKFPGYYVTGDGCRRDKDGYY 559
Cdd:PRK07656 335 V--AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYD--DPEATAAAIDADGWLHTGDLGRLDEEGYL 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 560 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAI 639
Cdd:PRK07656 409 YIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELT---EEELIAYCREHLAKY 485
|
570 580
....*....|....*....|....*..
gi 1036086734 640 ATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK07656 486 KVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
84-664 |
4.17e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 166.67 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 84 TNICYNVldrNVHERKLGDRVAFYWEGNEpgdektVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLA 162
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 163 CARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADGFYrgDKLinLKLIADEALKkcrdksfpvekCIMLKHLtkedea 242
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELA--PKV--APAVGNLRLR-----------HVIVAQY------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 243 sSGSLSPPAKRACPDLQQekqkervrkVRPPPQVPWNPEVdMCWHSLIGgASEECEPVWCDSEDPLFILYTSGSTGKPKG 322
Cdd:PRK08314 140 -SDYLPAEPEIAVPAWLR---------AEPPLQALAPGGV-VAWKEALA-AGLAPPPHTAGPDDLAVLPYTSGTTGVPKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 323 VLHTVSGYMlYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSK 402
Cdd:PRK08314 208 CMHTHRTVM-ANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERYRVTH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 403 FYTAPTAIRLLMkygSDP-VHKYKRTSLKILGTVGEPInPEAwqwyynvVGEK---RC--PVVDTFWQTETgghvMTPL- 475
Cdd:PRK08314 283 WTNIPTMVVDFL---ASPgLAERDLSSLRYIGGGGAAM-PEA-------VAERlkeLTglDYVEGYGLTET----MAQTh 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 476 --PAATPmKPGSATFPFFGVVPAILN-ESGEELEGPSEGYLVFKQPwpGVMRTVYGNHlrfETT--YFKKFPG--YYVTG 548
Cdd:PRK08314 348 snPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGP--QVFKGYWNRP---EATaeAFIEIDGkrFFRTG 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 549 DGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinYNQKLEAE- 627
Cdd:PRK08314 422 DLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPE--ARGKTTEEe 499
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 628 LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:PRK08314 500 IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
304-668 |
2.22e-43 |
|
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: 161.97 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 304 SEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVfDYHSDDVYWCTADIGWiTGHSYIT-YGPLANGATSVLFegl 382
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 pTYP--DVSRMWEIVDKYHVSKFYTAPTAIRLLMKygsDPVHKYKRTSLKILGTvGEPINPEAWQWYYNVVGEKrcpVVD 460
Cdd:cd05974 159 -NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEVIEQVRRAWGLT---IRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 461 TFWQTETGGHV-MTPlpaATPMKPGSATFPFFGVVPAILNESGEEL-EGpsEGYLVFKQPWP-GVMRTVYGNHLRfetTY 537
Cdd:cd05974 231 GYGQTETTALVgNSP---GQPVKAGSMGRPLPGYRVALLDPDGAPAtEG--EVALDLGDTRPvGLMKGYAGDPDK---TA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 538 FKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDG 617
Cdd:cd05974 303 HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1036086734 618 INYNQKLEAELKKQVREKIGAIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 668
Cdd:cd05974 383 YEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
304-665 |
2.88e-43 |
|
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: 161.88 E-value: 2.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 304 SEDPLFILYTSGSTGKPKGVLHTVSGYMLyTASTF-KMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGl 382
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLA-SADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 pTYPDvsRMWEIVDKYHVSKFYTAPTAIRLLMkyGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTF 462
Cdd:cd05958 174 -ATPD--LLLSAIARYKPTVLFTAPTAYRAML--AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 463 WQTETGgHVMTplpAATP--MKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpgvmrTVY-GNHLRFETTYFK 539
Cdd:cd05958 246 GSTEMF-HIFI---SARPgdARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 540 KfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGIN 619
Cdd:cd05958 316 G--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1036086734 620 YNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05958 394 PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
115-664 |
5.39e-42 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 158.46 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAvhsivfagfsseslcerimdsqCCLL 194
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----------------------AYVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ItadgfyrgdklinlkliadealkkcrDKSFPVEKCIMLkhltkedeassgslsppAKRACPDLqqekqkervrkvrppp 274
Cdd:cd05930 67 L--------------------------DPSYPAERLAYI-----------------LEDSGAKL---------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qvpwnpevdmcwhsliggaseecepVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAStFKMVFDYHSDDVYWCTA 354
Cdd:cd05930 88 -------------------------VLTDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFT 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 355 DIGWItGHSYITYGPLANGATSVLFEGLpTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHkykrTSLKILGT 434
Cdd:cd05930 142 SFSFD-VSVWEIFGALLAGATLVVLPEE-VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 435 VGEPINPEAWQ-WY--------YNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMkPGSATFpffgvvpaILNESGEEL 505
Cdd:cd05930 216 GGEALPPDLVRrWRellpgarlVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLDENLRPV 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 506 --EGPSEGYLVfkqpWPGVMRtvyGNHLRFETTYFK-----KFPG--YYVTGDGCRRDKDG--YYwiTGRIDDMLNVSGH 574
Cdd:cd05930 287 ppGVPGELYIG----GAGLAR---GYLNRPELTAERfvpnpFGPGerMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGY 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 575 LLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKT 654
Cdd:cd05930 358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG---GELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
570
....*....|
gi 1036086734 655 RSGKIMRRVL 664
Cdd:cd05930 435 PNGKVDRKAL 444
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
118-668 |
5.43e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.97 E-value: 5.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 118 TVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLAcariGAVHSIVFA---GFSSESLCERIMDSQCCLL 194
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITADGFYRGDklinlklIADEALKKcrdksfpVEKCIMLKHLTKEDeaSSGSLSPPAKRAcpdlqqekqkerVRKVRPPP 274
Cdd:PRK07529 134 VTLGPFPGTD-------IWQKVAEV-------LAALPELRTVVEVD--LARYLPGPKRLA------------VPLIRRKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVP---WNPEVDMCWH-SLIGGASEEcepvwcdSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVY 350
Cdd:PRK07529 186 HARildFDAELARQPGdRLFSGRPIG-------PDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 351 WCTADIGWITGHSYITYGPLANGAtSVLFEGLPTYPD---VSRMWEIVDKYHVSKFYTAPTAIRLLMKYgsdPVHKYKRT 427
Cdd:PRK07529 258 FCGLPLFHVNALLVTGLAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALLQV---PVDGHDIS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 428 SLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTE-TGGHVMTPlpAATPMKPGSA--TFPFFGVVPAILNESGEE 504
Cdd:PRK07529 334 SLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNP--PDGERRIGSVglRLPYQRVRVVILDDAGRY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 505 LE--GPSE-GYLVFKQP--WPGVMRTVYGNHLRFEttyfkkfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTA 579
Cdd:PRK07529 409 LRdcAVDEvGVLCIAGPnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 580 EVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIG--AiATPDYIQNAPGLPKTRSG 657
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG---ASATEAELLAFARDHIAerA-AVPKHVRILDALPKTAVG 557
|
570
....*....|.
gi 1036086734 658 KIMRRVLRKIA 668
Cdd:PRK07529 558 KIFKPALRRDA 568
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
24-666 |
1.25e-40 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 159.09 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 24 IPSFEKYKELyikSVESPEEFWADVAKDffwktkytgkfLDYNFDV-------TKGEIYI--KCMEGATTNICYNVLDRN 94
Cdd:PLN03052 119 ISSFSEFQRF---SVENPEVYWSIVLDE-----------LSLVFSVpprcildTSDESNPggQWLPGAVLNVAECCLTPK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 95 VHERklGDRVAFYW--EGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLAcarigavhsI 172
Cdd:PLN03052 185 PSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLA---------I 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 173 VFAG---------FSSESLCERIMDSQCCLLITADGFYRGDKlinlkliadealkkcrdkSFPVEKCIMlkhltkeDEAS 243
Cdd:PLN03052 254 ILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGK------------------SIPLYSRVV-------EAKA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 244 SGSLSPPAKRACPDLQQEKQkervrkvrpppqvpwnpevDMCWHSLIGGAS-----EECEPVWCDSEDPLFILYTSGSTG 318
Cdd:PLN03052 309 PKAIVLPADGKSVRVKLREG-------------------DMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 319 KPKGVLHTvsgymlyTASTFKMVFD--YHSD----DVY-WCTaDIGWITGHsYITYGPLANGATSVLFEGLPTYPDVSRM 391
Cdd:PLN03052 370 EPKAIPWT-------QLTPLRAAADawAHLDirkgDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAKF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 392 weiVDKYHVSKFYTAPTAIRLLMKYGSdpVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKrcPVVDTFWQTETGGHV 471
Cdd:PLN03052 441 ---VQDAKVTMLGTVPSIVKTWKNTNC--MAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTELGGGF 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 472 MTplpaATPMKPGS-ATF--PFFGVVPAILNESGEEL--EGPSEGYLVFKQPWPGVMRTVY-GNHlrfETTYFKKFPGYY 545
Cdd:PLN03052 514 VT----GSLLQPQAfAAFstPAMGCKLFILDDSGNPYpdDAPCTGELALFPLMFGASSTLLnADH---YKVYFKGMPVFN 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 546 VT-----GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHEAVAEAAVVGRPHPVKG-ESLYCFVTLN 615
Cdd:PLN03052 587 GKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DESVLETAAIGVPPPGGGpEQLVIAAVLK 663
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1036086734 616 DGINYNQKLEaELKK----QVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PLN03052 664 DPPGSNPDLN-ELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
150-665 |
4.36e-40 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 154.20 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 150 MPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADGFYRGDKLINL--KLIadealkkcrdKSFPv 227
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLysKVV----------EAAP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 228 EKCIMLKhltkedeASSGSLSPPAKracpdlqqekqkervrkvrpppqvpwnpEVDMCWHSLIGGASE-------ECEPV 300
Cdd:PLN03051 70 AKAIVLP-------AAGEPVAVPLR----------------------------EQDLSWCDFLGVAAAqgsvggnEYSPV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 301 WCDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGWITGhSYITYGPLANGATSVLFE 380
Cdd:PLN03051 115 YAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 381 GLPTYPDVSrmwEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRcPVVD 460
Cdd:PLN03051 193 GAPLGRGFG---KFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 461 TFWQTETGGHVM--TPLpaaTPMKPGSATFPFFGVVPAILNESGEEL--EGPSEGYLVFKQPWPGVM-RTVYGNHlrfET 535
Cdd:PLN03051 269 YCGGTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASdRLLNADH---DK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 536 TYFKKFPGYYVTGDGCRRDKD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGRPHPVKG-E 606
Cdd:PLN03051 343 VYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpE 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036086734 607 SLYCFVTLND-GINYNQKLEAELKKQVREKIGAIATP----DYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PLN03051 423 LLVIFLVLGEeKKGFDQARPEALQKKFQEAIQTNLNPlfkvSRVKIVPELPRNASNKLLRRVLR 486
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
117-664 |
1.08e-38 |
|
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: 150.08 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLIT 196
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADgfyrgdklinlkliadEALKKCRDKSFPVEkcimlkhLTKEDEASSGSLSPPAKRACPDlqqekqkervrkvrPPPQV 276
Cdd:cd05904 111 TA----------------ELAEKLASLALPVV-------LLDSAEFDSLSFSDLLFEADEA--------------EPPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 PWNPEvdmcwhsliggaseecepvwcdseDPLFILYTSGSTGKPKGVLHT-------VSGYMLYTASTFkmvfdyHSDDV 349
Cdd:cd05904 154 VIKQD------------------------DVAALLYSSGTTGRSKGVMLThrnliamVAQFVAGEGSNS------DSEDV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTADIGWITGHSYITYGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDPVHKYKRTSL 429
Cdd:cd05904 204 FLCVLPMFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 430 KILGTVGEPINPEAWQWYynvvgEKRCPVVDtFWQ----TETGGHV-MTPLPAATPMKPGSATFPFFGVVPAILN-ESGE 503
Cdd:cd05904 278 RQIMSGAAPLGKELIEAF-----RAKFPNVD-LGQgygmTESTGVVaMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 504 ELEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVES 583
Cdd:cd05904 352 SLPPNQTGELWIRGP--SIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 584 ALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELK----KQVR--EKIGAIATPDYIqnapglPKTRSG 657
Cdd:cd05904 428 LLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLT---EDEIMdfvaKQVApyKKVRKVAFVDAI------PKSPSG 498
|
....*..
gi 1036086734 658 KIMRRVL 664
Cdd:cd05904 499 KILRKEL 505
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
102-667 |
7.02e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 144.72 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEgnepgdEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsIVFAG--FSS 179
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 180 ESLCERIMDSQCCLLITADGFyrgdklinlkliadealkkcRDKSFPVEKCIMlkhltkedeassgslsppakracPDLQ 259
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF--------------------EAKLIPGISVKF-----------------------AELM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 260 QEKQKErvrkvrPPPQVPWnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVsGYMLYTASTFK 339
Cdd:PRK03640 126 NGPKEE------AEIQEEF------------------------DLDEVATIMYTSGTTGKPKGVIQTY-GNHWWSAVGSA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 340 MVFDYHSDDVYWCTADIGWITGHSyITYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAI-RLLMKYGS 418
Cdd:PRK03640 175 LNLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLqRLLERLGE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 419 DPVHKYKRTSLkiLGtvGEPINPEAWQwyynVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGV----- 493
Cdd:PRK03640 250 GTYPSSFRCML--LG--GGPAPKPLLE----QCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCelkie 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 494 ---VPAILNESGE-ELEGPS--EGYLvfKQPWPgvmrtvygNHLRFETTYFKkfpgyyvTGDGCRRDKDGYYWITGRIDD 567
Cdd:PRK03640 322 kdgVVVPPFEEGEiVVKGPNvtKGYL--NREDA--------TRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSD 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 568 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklEAELKKQVREKIGAIATPDYIQN 647
Cdd:PRK03640 385 LIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT-----EEELRHFCEEKLAKYKVPKRFYF 459
|
570 580
....*....|....*....|
gi 1036086734 648 APGLPKTRSGKIMRRVLRKI 667
Cdd:PRK03640 460 VEELPRNASGKLLRHELKQL 479
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
98-666 |
7.28e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 145.18 E-value: 7.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWegnepgDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsIVFAGF 177
Cdd:PRK07470 18 RRFPDRIALVW------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 sseslceRIMDSQCCLLITADGfyrgdklinlkliadealkkcrdksfpveKCIMLKHLTKEDEASSgslsppAKRACPD 257
Cdd:PRK07470 90 -------RQTPDEVAYLAEASG-----------------------------ARAMICHADFPEHAAA------VRAASPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LqqekqkervRKVRPPPQVPWNPEVDmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTvSGYMLYtast 337
Cdd:PRK07470 128 L---------THVVAIGGARAGLDYE---ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAF---- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 fkmVFDYHSDDVYWCTadigwiTGHS-YITYGPL------------ANGATSVLfegLPTYP-DVSRMWEIVDKYHVSKF 403
Cdd:PRK07470 191 ---VITNHLADLMPGT------TEQDaSLVVAPLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 404 YTAPTAIRLLMKYGSdpVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKrcpVVDTFWQTETGGHvMTPLPAA----- 478
Cdd:PRK07470 259 FTVPTILKMLVEHPA--VDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGN-ITVLPPAlhdae 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 479 -TPM-KPGSATFPFFGVVPAILNESGEELeGPSE-------GylvfkqpwPGVMRTVYGNHlrfETTYfKKF-PGYYVTG 548
Cdd:PRK07470 333 dGPDaRIGTCGFERTGMEVQIQDDEGREL-PPGEtgeicviG--------PAVFAGYYNNP---EANA-KAFrDGWFRTG 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 549 DGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAEL 628
Cdd:PRK07470 400 DLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD---EAEL 476
|
570 580 590
....*....|....*....|....*....|....*...
gi 1036086734 629 KKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
117-666 |
2.15e-36 |
|
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: 143.77 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLIT 196
Cdd:TIGR03098 24 RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADGfyRGDKLinlkliaDEALKKCRDksfpvekcimLKHLTKEDEASSGSLSPPAKRAcpdlqqekqkervrkvrpppqv 276
Cdd:TIGR03098 104 SSE--RLDLL-------HPALPGCHD----------LRTLIIVGDPAHASEGHPGEEP---------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 pwnpevdMCWHSLIGgASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADI 356
Cdd:TIGR03098 143 -------ASWPKLLA-LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRN-LVAGAQSVATYLENRPDDRLLAVLPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 357 GWITGHSYITYGpLANGATSVLFEGLpTYPDVSRMweiVDKYHVSKFYTAPTairLLMKYGSDPVHKYKRTSLKILGTVG 436
Cdd:TIGR03098 214 SFDYGFNQLTTA-FYVGATVVLHDYL-LPRDVLKA---LEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNSG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 437 EPINPEAWQWYynvvgEKRCPVVDTFWQ---TETGGHVMTPlPAATPMKPGS--ATFPFFGVVpaILNESGEELEGPSEG 511
Cdd:TIGR03098 286 GAMPRATLSRL-----RSFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEVL--VLREDGSECAPGEEG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 512 YLVFKQPwpgVMRTVYGNHLRFETTYFKKFPGYYV----------TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 581
Cdd:TIGR03098 358 ELVHRGA---LVAMGYWNDPEKTAERFRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 582 ESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQkleAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:TIGR03098 435 EEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKIDR 511
|
....*
gi 1036086734 662 RVLRK 666
Cdd:TIGR03098 512 KALAK 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
119-664 |
1.29e-35 |
|
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: 139.92 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 119 VTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsIVfagfsseslcerimdsqccllitad 198
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV--VV------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 gfyrgdkLINLKLIADEalkkcrdksfpvekcimLKHLTKEDEASSgslsppakracpdlqqekqkervrkvrpppqvpw 278
Cdd:cd05935 55 -------PINPMLKERE-----------------LEYILNDSGAKV---------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 279 npevdmcwhsLIGGASEEcepvwcdseDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHSDDVYWCTADIGW 358
Cdd:cd05935 77 ----------AVVGSELD---------DLALIPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 359 ITGHSYITYGPLANGATSVLFeglpTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMkygSDP-VHKYKRTSLKILGTVGE 437
Cdd:cd05935 137 VTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL---ATPeFKTRDLSSLKVLTGGGA 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 438 PINPEAWQWYYNVVGEKrcpVVDTFWQTETgghvMTPLPAATPMKPGSATF--PFFGVVPAILN-ESGEELEGPSEGYLV 514
Cdd:cd05935 210 PMPPAVAEKLLKLTGLR---FVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDiETGRELPPNEVGEIV 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 515 FKQPwpGVMRTvYGNHLRFETTYFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 592
Cdd:cd05935 283 VRGP--QIFKG-YWNRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI* 359
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 593 EAAVVGRPHPVKGESLYCFVTLNDGinYNQKLEAE-LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd05935 360 EVCVISVPDERVGEEVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
118-666 |
1.70e-35 |
|
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: 139.44 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 118 TVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivfagfsseslcerimdsqCCLLITa 197
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---------------------TNPILP- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 198 dgFYRGDKLINLkliadeaLKKCRDKSFPVekcimlkhltkedeassgslsppakracpdlqqekqKERVRKVRPPPQvp 277
Cdd:cd05903 59 --FFREHELAFI-------LRRAKAKVFVV------------------------------------PERFRQFDPAAM-- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 278 wnpevdmcwhsliggaseecepvwcdSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHSDDVYWCTADIG 357
Cdd:cd05903 92 --------------------------PDAVALLLFTSGTTGEPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMA 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 358 WITGHSYITYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPT----AIRLLMKYGSDPVHkykrtsLKILG 433
Cdd:cd05903 145 HQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREHGVTFMMGATPfltdLLNAVEEAGEPLSR------LRTFV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 434 TVGEPINP----EAWQwyynVVGEKRCPVvdtFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPS 509
Cdd:cd05903 215 CGGATVPRslarRAAE----LLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 510 EGYLVFKQPwpgvmrTVYGNHLRFETTYFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 588
Cdd:cd05903 288 EGELLSRGP------SVFLGYLDRPDLTADAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 589 EAVAEAAVVGRPHPVKGESLYCFVTLNDG--INYNQKLEAELKKQV-REKIgaiatPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05903 362 PGVIEAAVVALPDERLGERACAVVVTKSGalLTFDELVAYLDRQGVaKQYW-----PERLVHVDDLPRTPSGKVQKFRLR 436
|
.
gi 1036086734 666 K 666
Cdd:cd05903 437 E 437
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
90-668 |
7.67e-35 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 139.51 E-value: 7.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVHERklGDRVAFYwegnepGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:COG1021 30 LLRRRAERH--PDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 HsiVFAGFS---SE--SLCERimdSQCCLLITAD---GF-YRGdklinlklIADEALKKCRDksfpvekcimLKHLTKED 240
Cdd:COG1021 102 P--VFALPAhrrAEisHFAEQ---SEAVAYIIPDrhrGFdYRA--------LARELQAEVPS----------LRHVLVVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 241 EASSG-SLSppakracpdlqqekqkervrkvrpppqvpwnpevdmcwhSLIGGASEECEPVwCDSEDPLFILYTSGSTGK 319
Cdd:COG1021 159 DAGEFtSLD---------------------------------------ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 320 PKGVLHTVSGYmLYTASTFKMVFDYHSDDVYWCTADIGwitgHSYitygPLAN-GATSVLFEG----LPTYPDVSRMWEI 394
Cdd:COG1021 199 PKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPAA----HNF----PLSSpGVLGVLYAGgtvvLAPDPSPDTAFPL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 395 VDKYHVSkfYTA--PTAIRLLMKYGSDpvHKYKRTSLKILGTVGEPINPEAwqwYYNVVGEKRCPVVDTFWQTEtgGHV- 471
Cdd:COG1021 270 IERERVT--VTAlvPPLALLWLDAAER--SRYDLSSLRVLQVGGAKLSPEL---ARRVRPALGCTLQQVFGMAE--GLVn 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 472 MTPL--PAAT-------PMKPGSATFpffgvvpaILNESGEELEGPSEGYLVFKQPWpgvmrTVYGnhlrfettYFKKfP 542
Cdd:COG1021 341 YTRLddPEEVilttqgrPISPDDEVR--------IVDEDGNPVPPGEVGELLTRGPY-----TIRG--------YYRA-P 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 ----------GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFV 612
Cdd:COG1021 399 ehnaraftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV 478
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 613 TLNDGinyNQKLeAELKKQVREKigAIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:COG1021 479 VPRGE---PLTL-AELRRFLRER--GLAAfklPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
101-666 |
3.55e-34 |
|
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: 137.38 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 101 GDRVAFYWEGnePGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV-HSIVFagfss 179
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 180 eslceRIMDSQccLLITADgfYRGDKLinlkLIADEAL----KKCRDKSFPVEKCIMLKHLTKEDEassgslsPPAKRAC 255
Cdd:cd12119 83 -----RLFPEQ--IAYIIN--HAEDRV----VFVDRDFlpllEAIAPRLPTVEHVVVMTDDAAMPE-------PAGVGVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 256 pdlqqekqkervrkvrpppqvpwnpevdmCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYT- 334
Cdd:cd12119 143 -----------------------------AYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAm 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 335 ASTFKMVFDYHSDDVY-----------WCTADIGWITGHSYITYGPLANGATSVlfeglptypdvsrmwEIVDKYHVSKF 403
Cdd:cd12119 194 AALLTDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPASLA---------------ELIEREGVTFA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 404 YTAPTAIRLLMKYGSDpvHKYKRTSLKILGTVGEPINP---EAWQwyynvvgEKRCPVVDTFWQTETG--GHVMTPLPAA 478
Cdd:cd12119 259 AGVPTVWQGLLDHLEA--NGRDLSSLRRVVIGGSAVPRsliEAFE-------ERGVRVIHAWGMTETSplGTVARPPSEH 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 479 TPMKPG-------SATFPFFGVVPAILNESGEELE--GPSEGYLVFKQPWpgVMRTVYGNHlrfETTYFKKFPGYYVTGD 549
Cdd:cd12119 330 SNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPW--VTKSYYKND---EESEALTEDGWLRTGD 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 550 GCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKleaELK 629
Cdd:cd12119 405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELL 481
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 630 KQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd12119 482 EFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
312-668 |
6.31e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 133.37 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 312 YTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGAtSVLFEGLPTYPD---V 388
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAGYRNpglF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 389 SRMWEIVDKYHVSKFYTAPTAIRLLMKYgsdPVHKyKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTE-T 467
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQV---PVNA-DISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEaT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 468 GGHVMTPlpAATPMKPGSA--TFPFFGVVPAILNESGEELE--GPSE-GYLVFKQPwpgvmrTVYGNHLRFETTYFKKF- 541
Cdd:cd05944 160 CLVAVNP--PDGPKRPGSVglRLPYARVRIKVLDGVGRLLRdcAPDEvGEICVAGP------GVFGGYLYTEGNKNAFVa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 542 PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN 621
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1036086734 622 qklEAELKKQVREKIGA-IATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:cd05944 312 ---EEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
102-664 |
1.00e-33 |
|
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: 134.68 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVfagfsses 181
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 lcerimdsqccllitadgfyrgdklinlkliadealkkcrDKSFPVEkcimlkhltkedeassgslsppakracpdlqqe 261
Cdd:cd05945 72 ----------------------------------------DASSPAE--------------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 262 kqkeRVRKVrpppqvpwnpeVDMCwhsliggaseECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAStfkMV 341
Cdd:cd05945 79 ----RIREI-----------LDAA----------KPALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNW---ML 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 342 --FDYHSDDVYWCTA---------DIgwitghsyitYGPLANGATSV------------LFEGLPTYPdvsrmweivdky 398
Cdd:cd05945 131 sdFPLGPGDVFLNQApfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG------------ 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 hVSKFYTAPTAIRLLMKYGSDPVHKYK--RTSLKIlgtvGEPI-NPEAWQWyynvvgEKR---CPVVDTFWQTET----G 468
Cdd:cd05945 189 -ITVWVSTPSFAAMCLLSPTFTPESLPslRHFLFC----GEVLpHKTARAL------QQRfpdARIYNTYGPTEAtvavT 257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 469 GHVMTPLPAATpMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKkFPGY--YV 546
Cdd:cd05945 258 YIEVTPEVLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGP--SVSKGYLNNPEKTAAAFFP-DEGQraYR 333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 547 TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInyNQKLEA 626
Cdd:cd05945 334 TGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA--EAGLTK 411
|
570 580 590
....*....|....*....|....*....|....*...
gi 1036086734 627 ELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd05945 412 AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
102-668 |
6.90e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 133.64 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSES 181
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 LCERIMDSQCCLLITADGFyRG-DKlinlkliadEALKKCRDKSFPvekciMLKHLTKEDEASSGS----LSPPAKRACP 256
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGfDH---------AAMARRLRPELP-----ALRHVVVVGGDGADSfealLITPAWEQEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 257 DLQQEkqkerVRKVRPPPqvpwnpevdmcwhsliggaseecepvwcdsEDPLFILYTSGSTGKPKGVLHT----VSGYML 332
Cdd:PRK13295 184 DAPAI-----LARLRPGP------------------------------DDVTQLIYTSGTTGEPKGVMHTantlMANIVP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 333 YTAStfkmvFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSkFYTAPTAIRL 412
Cdd:PRK13295 229 YAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIW----DPARAAELIRTEGVT-FTMASTPFLT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 413 LM----KYGSDPVhkykrTSLKILGTVGEPINP----EAWQwyynVVGEKrcpVVDTFWQTETGGhVMTPLPAATPMKpG 484
Cdd:PRK13295 299 DLtravKESGRPV-----SSLRTFLCAGAPIPGalveRARA----ALGAK---IVSAWGMTENGA-VTLTKLDDPDER-A 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 485 SAT--FPFFGVVPAILNESGEELEGPSEGYLVFKQPwpgvmrTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWIT 562
Cdd:PRK13295 365 STTdgCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 563 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAE-LKKQvreKIGAIAT 641
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEfLKAQ---KVAKQYI 515
|
570 580
....*....|....*....|....*..
gi 1036086734 642 PDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK13295 516 PERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
102-664 |
1.23e-32 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 131.66 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSES 181
Cdd:cd17643 2 EAVAVVDED------RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 LCERIMDSQCCLLITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqe 261
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 262 kqkervrkvrpppqvpwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHT---VSGymLYTASTf 338
Cdd:cd17643 91 -----------------------------------------DPDDLAYVIYTSGSTGRPKGVVVShanVLA--LFAATQ- 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 339 kMVFDYHSDDVywctadigWITGHSYI-------TYGPLANGATSVLFEglptyPDVSR----MWEIVDKYHVSKFYTAP 407
Cdd:cd17643 127 -RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLVVVP-----YEVARspedFARLLRDEGVTVLNQTP 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 408 TAIRLLMKYGSDPVHKYKRTSLKILGtvGEPINPEAWQWYYNVVGEKRCPVVDTFWQTETGGHV----MTP--LPAATpM 481
Cdd:cd17643 193 SAFYQLVEAADRDGRDPLALRYVIFG--GEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-A 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 482 KPGSATFPFFGVvpAILNESGEELE--GPSEGYLvfkqPWPGVMRtvyGNHLRFETTYfKKF-------PG--YYVTGDG 550
Cdd:cd17643 270 SPIGRPLPGLRV--YVLDADGRPVPpgVVGELYV----SGAGVAR---GYLGRPELTA-ERFvanpfggPGsrMYRTGDL 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 551 CRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKK 630
Cdd:cd17643 340 ARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRA 416
|
570 580 590
....*....|....*....|....*....|....*....
gi 1036086734 631 QVREKIgaiatPDYIQNA-----PGLPKTRSGKIMRRVL 664
Cdd:cd17643 417 LLKELL-----PDYMVPAryvplDALPLTVNGKLDRAAL 450
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
117-664 |
1.49e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 132.85 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSqccllit 196
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDS------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 adgfyrGDKLInlkliadealkKCRDKSFP----VEKCIMLKHLTKEDEAssgSLSPPAKRACPDLQQEKQKERVRKVRp 272
Cdd:PRK06710 121 ------GAKVI-----------LCLDLVFPrvtnVQSATKIEHVIVTRIA---DFLPFPKNLLYPFVQKKQSNLVVKVS- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 273 ppqvpwNPEVDMCWHSLIGGASEECEpVWCDSEDPLFIL-YTSGSTGKPKGVLHTVSGYMLYTASTFKMVFD-YHSDDVY 350
Cdd:PRK06710 180 ------ESETIHLWNSVEKEVNTGVE-VPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 351 WCTADIGWITGHSYITYGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDPVHKYKRTSLK 430
Cdd:PRK06710 253 LGVLPFFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 431 ILGTVGEPINPEAWQWYYNVVGEKrcpVVDTFWQTETgghvmTPLPAATPM----KPGSATFPFFGVVPAILN-ESGEEL 505
Cdd:PRK06710 327 ACISGSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSlETGEAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 506 EGPSEGYLVFKQPwpgvmRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESAL 585
Cdd:PRK06710 399 PPGEIGEIVVKGP-----QIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 586 VEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:PRK06710 474 YEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
102-659 |
1.51e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 132.86 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSES 181
Cdd:PRK06178 48 QRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 LCERIMDSQCCLLITADGFYrgdklinlkliadEALKKCRDKSfPVEKCIMlkhltkedeASSGSLSPPA-KRACPDLQQ 260
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA-------------PVVEQVRAET-SLRHVIV---------TSLADVLPAEpTLPLPDSLR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 261 EkqkervrkvrPPPQVPwnpevdmCWHSLIGGASEECEPVWC---DSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTAST 337
Cdd:PRK06178 179 A----------PRLAAA-------GAIDLLPALRACTAPVPLpppALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 FKMV-FDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLfegLPTYPDVSRMwEIVDKYHVSK-FYTAPTAIRLLMK 415
Cdd:PRK06178 241 AYAVaVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVL---LARWDAVAFM-AAVERYRVTRtVMLVDNAVELMDH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 416 YGsdpVHKYKRTSLKILGTVG--EPINPEAWQWYYNVVGekrCPVVDTFW-QTETggHVmtplpaatpmkpgSATF---- 488
Cdd:PRK06178 317 PR---FAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTET--HT-------------CDTFtagf 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 489 ----------PFF-GV-VPA----ILN-ESGEELEGPSEGYLVFKQPwpgVMRTVYGNHLRFETTYFKKfpGYYVTGDGC 551
Cdd:PRK06178 376 qdddfdllsqPVFvGLpVPGtefkICDfETGELLPLGAEGEIVVRTP---SLLKGYWNKPEATAEALRD--GWLHTGDIG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 552 RRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQ 631
Cdd:PRK06178 451 KIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTAAALQAW 527
|
570 580
....*....|....*....|....*....
gi 1036086734 632 VREKIGAIATPD-YIQNApgLPKTRSGKI 659
Cdd:PRK06178 528 CRENMAVYKVPEiRIVDA--LPMTATGKV 554
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
114-665 |
2.25e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 131.56 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGavhsivfagfsseslcerimdsqccL 193
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSG-------------------------L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITAdgfyrgdklINLKLIADEA---LKKCRDKSFPVekcimlkhltkedeasSGSLSPPAKRACPDLQQEkqkERVRKV 270
Cdd:PRK08276 62 YYTP---------INWHLTAAEIayiVDDSGAKVLIV----------------SAALADTAAELAAELPAG---VPLLLV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 271 RPPPQVPWNPevdmcWHSLIGGASEEcepvwcDSEDPLF---ILYTSGSTGKPKGVL--------HTVSGYMLytastFK 339
Cdd:PRK08276 114 VAGPVPGFRS-----YEEALAAQPDT------PIADETAgadMLYSSGTTGRPKGIKrplpgldpDEAPGMML-----AL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 340 MVFDYHS--DDVYWC------TADIGWITGhsyitygPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAIR 411
Cdd:PRK08276 178 LGFGMYGgpDSVYLSpaplyhTAPLRFGMS-------ALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 412 LLMKYGSDPVHKYKRTSLKILGTVGEPINPE------AWqWyynvvGekrcPVVD-TFWQTETGGH-VMTPLPAATpmKP 483
Cdd:PRK08276 247 RMLKLPEEVRARYDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVtVITSEDWLA--HP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 484 GSATFPFFGVVpAILNESGEELEGPSEGYLVFKQPWPGVmrTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITG 563
Cdd:PRK08276 315 GSVGKAVLGEV-RILDEDGNELPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTD 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 564 RIDDMLnVSGHL-LSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATP 642
Cdd:PRK08276 390 RKSDMI-ISGGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCP 468
|
570 580
....*....|....*....|...
gi 1036086734 643 DYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK08276 469 RSIDFEDELPRTPTGKLYKRRLR 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
120-596 |
2.57e-32 |
|
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: 129.69 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLcERIM-DSQCCLLITA 197
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 198 DGFyrgdklinlkliadealkkCRDKSFPVEKCIMLKHLTKEDEASSGSLSPPAKRACPDlqqekqkervrkvrpppqvp 277
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPD-------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 278 wnpevdmcwhsliggaseecepvwcdseDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIG 357
Cdd:TIGR01733 121 ----------------------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 358 WITGHSYItYGPLANGATSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLmkygsDPVHKYKRTSLKILGTVGE 437
Cdd:TIGR01733 172 FDASVEEI-FGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL-----AAALPPALASLRLVILGGE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 438 PINPEAWQWYYNVVGEKRcpVVDTFWQTETGGHVM---TPLPAATPMKPGSATFPFFGVVPAILNESGE--------EL- 505
Cdd:TIGR01733 246 ALTPALVDRWRARGPGAR--LINLYGPTETTVWSTatlVDPDDAPRESPVPIGRPLANTRLYVLDDDLRpvpvgvvgELy 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 506 -EGP--SEGYLvfKQpwPGVMRTVYGNHLRFETTyfkkFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVE 582
Cdd:TIGR01733 324 iGGPgvARGYL--NR--PELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
490
....*....|....
gi 1036086734 583 SALVEHEAVAEAAV 596
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
98-665 |
6.13e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.49 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWegnepgDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK06188 23 KRYPDRPALVL------GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITADGFY--RGDKLinlkliadealkkcrdksfpVEKCIMLKHLTKEDEASSGslsppakrac 255
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFveRALAL--------------------LARVPSLKHVLTLGPVPDG---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 256 PDLQQEkqkerVRKVRPPPQVPWNpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTA 335
Cdd:PRK06188 147 VDLLAA-----AAKFGPAPLVAAA-----------------------LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 336 stfkmvfdyhsddvyWCTADIGWITGHSYITYGPLANGATS----VLFEG-----LPTYpDVSRMWEIVDKYHVSKFYTA 406
Cdd:PRK06188 199 ---------------IQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGgtvivLAKF-DPAEVLRAIEEQRITATFLV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 407 PTAIRLLMKYGSDPvhkykRTSLKILGTV---GEPINP----EAwqwyynvvGEKRCPV-VDTFWQTETGgHVMTPLP-- 476
Cdd:PRK06188 263 PTMIYALLDHPDLR-----TRDLSSLETVyygASPMSPvrlaEA--------IERFGPIfAQYYGQTEAP-MVITYLRkr 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 ---AATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRtvyGNHLRFETT--YFKKfpGYYVTGDGC 551
Cdd:PRK06188 329 dhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVA 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 552 RRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQ 631
Cdd:PRK06188 402 REDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVD---AAELQAH 478
|
570 580 590
....*....|....*....|....*....|....
gi 1036086734 632 VREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK06188 479 VKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
90-666 |
3.07e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 128.96 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVheRKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:PRK05605 37 LYDNAV--ARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 ---HSIVFAGFSSESLCErimDSQCCLLITADGfyrgdklinlklIADEALKKCRDKsfPVEKcIMLKHLTKedeassgs 246
Cdd:PRK05605 109 vveHNPLYTAHELEHPFE---DHGARVAIVWDK------------VAPTVERLRRTT--PLET-IVSVNMIA-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 247 lsppakrACPDLQQEKQK---ERVRKVR------PPPQVPWNPEVDmcwhSLIGGASEECEPVWCDSEDPLFILYTSGST 317
Cdd:PRK05605 163 -------AMPLLQRLALRlpiPALRKARaaltgpAPGTVPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 318 GKPKGVLHTvsgymlytastfkmvfdyHSDDVYWCTADIGWITG---------------HSY-----ITYGPLAnGATSV 377
Cdd:PRK05605 232 GKPKGAQLT------------------HRNLFANAAQGKAWVPGlgdgpervlaalpmfHAYgltlcLTLAVSI-GGELV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 378 LFeglPTyPDVSRMWEIVDKyHVSKFYTA-PTAIRLLMKygsdpVHKYKRTSLKILgtvgepinpeawqwYYNVVGEKRC 456
Cdd:PRK05605 293 LL---PA-PDIDLILDAMKK-HPPTWLPGvPPLYEKIAE-----AAEERGVDLSGV--------------RNAFSGAMAL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 457 PV--VDTfWQTETGGHV-----MT---PLPAATPM----KPGSATFPFFGVVPAILN--ESGEELEGPSEGYLVFKQPwp 520
Cdd:PRK05605 349 PVstVEL-WEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGP-- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 521 gvmrTVYGNHLRFETTYFKKF-PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGR 599
Cdd:PRK05605 426 ----QVFKGYWNRPEETAKSFlDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 600 PHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK05605 502 PREDGSEEVVAAVVLEPGAALD---PEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
115-667 |
3.27e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 128.89 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESL---CERimdsqc 191
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLaevAAR------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 192 cllitaDGfyrgdklINLKLIADEALKKCRDKSFPVEKCIMLKHLTKEDeassgslsPPAKRACPDLQQekqkervrkvr 271
Cdd:PRK07788 145 ------EG-------VKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDD--------EPSGSTDETLDD----------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 272 pppqvpwnpevdmcwhsLIGGASEECEPVWcdSEDPLFILYTSGSTGKPKGVLH------TVSGYMLyTASTFKMvfdyh 345
Cdd:PRK07788 193 -----------------LIAGSSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRpepsplAPLAGLL-SRVPFRA----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 346 sDDVYWCTADIGWITGHSYITYGpLANGATSVL---FeglptypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVH 422
Cdd:PRK07788 248 -GETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 423 KYKRTSLKILGTVGEPINPEawqwYYNVVGEKRCPVVDTFW-QTETGghVMTplpAATP----MKPGSATFPFFGVVPAI 497
Cdd:PRK07788 319 KYDTSSLKIIFVSGSALSPE----LATRALEAFGPVLYNLYgSTEVA--FAT---IATPedlaEAPGTVGRPPKGVTVKI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 498 LNESGEELEgpsegylvfkqpwPGVMRTVY-GNHLRFETtYF-----KKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNV 571
Cdd:PRK07788 390 LDENGNEVP-------------RGVVGRIFvGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 572 SGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNAPGL 651
Cdd:PRK07788 456 GGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD---EDAIKDYVRDNLARYKVPRDVVFLDEL 532
|
570
....*....|....*.
gi 1036086734 652 PKTRSGKIMRRVLRKI 667
Cdd:PRK07788 533 PRNPTGKVLKRELREM 548
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
95-665 |
9.10e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 127.11 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 95 VHERKLGDRVAFYWegnePGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVF 174
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 175 AGFSSESLCERIMDSQCCLLITAdgfyrGDKLInlklIADEALKKCRDksfpVEKCIMLKhltkEDEASSGSLS-PPAKR 253
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITS-----AAKLD----VARALLKQCPG----VRHRLVLD----GDGELEGFVGyAEAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 254 ACPDLQQEKQKErvrkvrpppqvpwnpevdmcwhsliGGAseecepvwcdsedplfILYTSGSTGKPKGVLHTVSGYMLY 333
Cdd:PRK13391 144 GLPATPIADESL-------------------------GTD----------------MLYSSGTTGRPKGIKRPLPEQPPD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 334 TAST----FKMVFDYHSDDVYWCTADIGwitgHSyityGPLA-------NGATSVLFEGLptypDVSRMWEIVDKYHVSK 402
Cdd:PRK13391 183 TPLPltafLQRLWGFRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 403 FYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPINPE------AWqWyynvvgekrCPVVDTFW-QTETGGhvMTPL 475
Cdd:PRK13391 251 TQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYaATEGLG--FTAC 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 476 PAATPM-KPGSATFPFFGVvPAILNESGEELegpsegylvfkqPwPGVMRTVYgnhlrFET-TYFKKF------------ 541
Cdd:PRK13391 319 DSEEWLaHPGTVGRAMFGD-LHILDDDGAEL------------P-PGEPGTIW-----FEGgRPFEYLndpaktaearhp 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 542 -PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINY 620
Cdd:PRK13391 380 dGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDP 459
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1036086734 621 NQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK13391 460 GPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
114-665 |
1.63e-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: 125.92 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITADGFyrgdklinlkliADEALkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkVRPP 273
Cdd:cd17651 96 VLTHPAL------------AGELA----------------------------------------------------VELV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 PQVPWNPEVDmcwhSLIGGASEECEPvwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTfKMVFDYHSDDVYWCT 353
Cdd:cd17651 112 AVTLLDQPGA----AAGADAEPDPAL---DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQ-ARASSLGPGARTLQF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 354 ADIGWITGHSYItYGPLANGATSVLfeglPT---YPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygsDPVHKYKR-TSL 429
Cdd:cd17651 184 AGLGFDVSVQEI-FSTLCAGATLVL----PPeevRTDPPALAAWLDEQRISRVFLPTVALRALAE---HGRPLGVRlAAL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 430 KILGTVGEP-INPEAWQWYYNVVGEKRcpVVDTFWQTETggHVMT----PLPAATPMKPGSATFPFFGVVPAILNESGEE 504
Cdd:cd17651 256 RYLLTGGEQlVLTEDLREFCAGLPGLR--LHNHYGPTET--HVVTalslPGDPAAWPAPPPIGRPIDNTRVYVLDAALRP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 505 LEGPSEGYLVFKQPwpGVMRtvyGNHLRFETTYfKKF------PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLL 576
Cdd:cd17651 332 VPPGVPGELYIGGA--GLAR---GYLNRPELTA-ERFvpdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 577 STAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRS 656
Cdd:cd17651 406 ELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE---APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPN 482
|
....*....
gi 1036086734 657 GKIMRRVLR 665
Cdd:cd17651 483 GKLDRRALP 491
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
305-665 |
3.14e-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: 124.47 E-value: 3.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 305 EDPLFILYTSGSTGKPKGVLhtVSGY-MLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGpLANGATSVLfEGLP 383
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVR--LSHQnLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVL-TNDG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 384 TYPDVsrMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVhkyKRTSLKILGTVGEPINPEawqwyynVVGEKRCPVVDT-- 461
Cdd:cd05922 193 VLDDA--FWEDLREHGATGLAGVPSTYAMLTRLGFDPA---KLPSLRYLTQAGGRLPQE-------TIARLRELLPGAqv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 462 ---FWQTETGGHvMTPLPAATPM-KPGSATFPFFGVVPAILNESGEElEGPSE-GYLVFKQPWpgVMRTvYGNHLRFETT 536
Cdd:cd05922 261 yvmYGQTEATRR-MTYLPPERILeKPGSIGLAIPGGEFEILDDDGTP-TPPGEpGEIVHRGPN--VMKG-YWNDPPYRRK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 537 YfKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVkGESLYCFVTLND 616
Cdd:cd05922 336 E-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPD 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1036086734 617 GINynqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05922 414 KID-----PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
296-666 |
4.38e-30 |
|
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: 123.94 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 296 ECEPVWCDSE-----DPLFILYTSGSTGKPKGVLHTVSGymlyTASTFKMVFD---YHSDDVYWCTADIGWITGHSYITY 367
Cdd:cd05941 75 ELEYVITDSEpslvlDPALILYTSGTTGRPKGVVLTHAN----LAANVRALVDawrWTEDDVLLHVLPLHHVHGLVNALL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 368 GPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTA-IRLL-----MKYGSDPVHKY--KRTSLKILGTVGEPI 439
Cdd:cd05941 151 CPLFAGASVEF---LPKF-DPKEVAISRLMPSITVFMGVPTIyTRLLqyyeaHFTDPQFARAAaaERLRLMVSGSAALPV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 440 nP--EAWQwyyNVVGEkrcPVVDTFWQTETGGHVMTPLPAatPMKPGSATFPFFGVVPAIL-NESGEELEGPSEGYLVFK 516
Cdd:cd05941 227 -PtlEEWE---AITGH---TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 517 QPwpgvmrTVYgnhlrfeTTYFKKfP----------GYYVTGDGCRRDKDGYYWITGRI-DDMLNVSGHLLSTAEVESAL 585
Cdd:cd05941 298 GP------SVF-------KEYWNK-PeatkeeftddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 586 VEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05941 364 LAHPGVSECAVIGVPDPDWGERVVAVVVLRAGA--AALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
.
gi 1036086734 666 K 666
Cdd:cd05941 442 K 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
580-658 |
1.01e-29 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 112.25 E-value: 1.01e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 580 EVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGK 658
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
310-666 |
1.07e-29 |
|
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: 122.07 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 310 ILYTSGSTGKPKGVLHTVsGYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGpLANGATSVLFEGLptypDVS 389
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTF-GNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 390 RMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLkiLGtvGEPINPEAWQwyynVVGEKRCPVVDTFWQTETGG 469
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPAPKPLLE----QCKEKGIPVYQSYGMTETCS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 470 HVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEgpsEGYLVFKQPwpGVMRTVYG----NHLRFETTYFKkfpgyy 545
Cdd:cd05912 228 QIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGP--NVTKGYLNrpdaTEESFENGWFK------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 546 vTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklE 625
Cdd:cd05912 297 -TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-----E 370
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1036086734 626 AELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05912 371 EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
120-672 |
5.62e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.07 E-value: 5.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADG 199
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 FYRGdKLINLKLIAdealkkcrdksfpvekcimlkhLTKEDEASSGSLSPPAkracpdlqqekqkervrkvrpppqvpwn 279
Cdd:PRK09088 104 VAAG-RTDVEDLAA----------------------FIASADALEPADTPSI---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 pevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTAD---- 355
Cdd:PRK09088 133 -----------------------PPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhi 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 356 IGWITGHSYItygpLANGATSVLFEGLPtyPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKY-GSDPVhkyKRTSLKILGT 434
Cdd:PRK09088 189 IGLITSVRPV----LAVGGSILVSNGFE--PKRTLGRLGDPALGITHYFCVPQMAQAFRAQpGFDAA---ALRHLTALFT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 435 VGEPINPEAWQWYYnvvgEKRCPVVDTFWQTETGGHVMTPL-PAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYL 513
Cdd:PRK09088 260 GGAPHAAEDILGWL----DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 514 VFKQP--WPGVMRTVYgnhlrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 591
Cdd:PRK09088 336 LLRGPnlSPGYWRRPQ------ATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGI 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 592 AEAAVVGRPHPVKGESLYCFVTLNDGINYNQkleAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIACNE 671
Cdd:PRK09088 410 RECAVVGMADAQWGEVGYLAIVPADGAPLDL---ERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAG 486
|
.
gi 1036086734 672 R 672
Cdd:PRK09088 487 R 487
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
102-667 |
1.39e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 119.96 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYwegnepGDEKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGavhsivfagfsse 180
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVE------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 181 slcerimdsqcCLLITadgfyrgdklINLKLIADEALKKCRDKSFPVEKCIMLKHLTKEDEASSGSLSPPAKraCPDLQQ 260
Cdd:PRK06839 78 -----------CIAVP----------LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVIS--ITSLKE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 261 EKQKERVRKVRPppqvpwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKG-VLHTVSgyMLYTASTFK 339
Cdd:PRK06839 135 IEDRKIDNFVEK------------------------------NESASFIICYTSGTTGKPKGaVLTQEN--MFWNALNNT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 340 MVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLfeglPTYPDVSRMWEIVDKYHVSKFYTAPTairllmkygsd 419
Cdd:PRK06839 183 FAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV----PRKFEPTKALSMIEKHKVTVVMGVPT----------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 420 pVHKYKRTSLKILGTvgepiNPEAWQWYYNvvGEKRCPVV-------------DTFWQTETGGHVMTPLPAATPMKPGSA 486
Cdd:PRK06839 248 -IHQALINCSKFETT-----NLQSVRWFYN--GGAPCPEElmrefidrgflfgQGFGMTETSPTVFMLSEEDARRKVGSI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 487 TFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMrTVYGNhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRID 566
Cdd:PRK06839 320 GKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVM-KEYWN--RPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKK 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 567 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYnqkLEAELKKQVREKIGAIATPDYIQ 646
Cdd:PRK06839 395 EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL---IEKDVIEHCRLFLAKYKIPKEIV 471
|
570 580
....*....|....*....|.
gi 1036086734 647 NAPGLPKTRSGKIMRRVLRKI 667
Cdd:PRK06839 472 FLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
120-666 |
3.17e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.47 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV-HSIVFAgfsseslcerimdsqccllitad 198
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVsVPLLPS----------------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 gfYRGDKLInlkliadEALKKCRDKSFPVEkcimlkhlTKEDEASSGSLSPPAKRACPDLQQEKQkerVRKVRPPPQVPW 278
Cdd:PRK06087 108 --WREAELV-------WVLNKCQAKMFFAP--------TLFKQTRPVDLILPLQNQLPQLQQIVG---VDKLAPATSSLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 279 NPEVDMCWHSLiggaseeCEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGW 358
Cdd:PRK06087 168 LSQIIADYEPL-------TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 359 ITGHSYITYGPLANGATSVLFEglptypdvsrmweivdkyhvskFYTAPTAIRLLMK------YGSDPV----------H 422
Cdd:PRK06087 240 ATGFLHGVTAPFLIGARSVLLD----------------------IFTPDACLALLEQqrctcmLGATPFiydllnllekQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 423 KYKRTSLKIL----GTVGEPINPEAWQWyynvvGEKRCPVvdtFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAIL 498
Cdd:PRK06087 298 PADLSALRFFlcggTTIPKKVARECQQR-----GIKLLSV---YGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 499 NES------GEELEGPSEGYLVFkqpwpgvmrTVYGNHLRfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVS 572
Cdd:PRK06087 370 DEArktlppGCEGEEASRGPNVF---------MGYLDEPE-LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 573 GHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINyNQKLEAELKKQVREKIGAIATPDYIQNAPGLP 652
Cdd:PRK06087 440 GENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH-SLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLP 518
|
570
....*....|....
gi 1036086734 653 KTRSGKIMRRVLRK 666
Cdd:PRK06087 519 RTASGKIQKFLLRK 532
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
98-665 |
4.00e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 119.02 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEgNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK08008 18 DVYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESlCERIMD-SQCCLLITADGFYrgdklinlkliadEALKKCRDksfpvEKCIMLKHLTKEDEASsgslspPAKRACP 256
Cdd:PRK08008 97 LREE-SAWILQnSQASLLVTSAQFY-------------PMYRQIQQ-----EDATPLRHICLTRVAL------PADDGVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 257 DLQQEKQKErvrkvrpppqvpwnpevdmcwhsliggASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT-----VSGYm 331
Cdd:PRK08008 152 SFTQLKAQQ---------------------------PATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 332 lYTASTFKMVFD---------YHSDdvYWCTADIGWITGhsyitygplanGATSVLFEglpTYpDVSRMWEIVDKYHVSK 402
Cdd:PRK08008 204 -YSAWQCALRDDdvyltvmpaFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 403 FYTAPTAIRLLMKygsdpvhkykrtslkilgtvgEPINPEAWQ-------WYYNV-VGEK-----RCPV--VDTFWQTET 467
Cdd:PRK08008 266 TECIPMMIRTLMV---------------------QPPSANDRQhclrevmFYLNLsDQEKdafeeRFGVrlLTSYGMTET 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 468 GGHVMTPLPAATPMKPgSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwPGvmRTVY-GNHLRFETTYFKKFP-GYY 545
Cdd:PRK08008 325 IVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV-PG--KTIFkEYYLDPKATAKVLEAdGWL 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 546 VTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklE 625
Cdd:PRK08008 401 HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS---E 477
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1036086734 626 AELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK08008 478 EEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
114-664 |
4.97e-27 |
|
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: 114.72 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKtVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:cd12115 21 GDES-LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrpp 273
Cdd:cd12115 100 VLT----------------------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqvpwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGymlytASTFkmvfdyhsddVYWCT 353
Cdd:cd12115 103 -----------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAF----------LQWAA 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 354 ADIG-----WITGHSYITY--------GPLANGATSVLFEGLPTYPDVSRMWEivdkyhVSKFYTAPTAIRLLMKYGSDP 420
Cdd:cd12115 139 AAFSaeelaGVLASTSICFdlsvfelfGPLATGGKVVLADNVLALPDLPAAAE------VTLINTVPSAAAELLRHDALP 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 421 vhkykrTSLKILGTVGEPINPEAWQWYYNVVGEKRcpVVDTFWQTETgghvmTPLPAATPMKPGSAT-----FPFFGVVP 495
Cdd:cd12115 213 ------ASVRVVNLAGEPLPRDLVQRLYARLQVER--VVNLYGPSED-----TTYSTVAPVPPGASGevsigRPLANTQA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 496 AILNESGEEL------------EGPSEGYLvfKQPwpgvMRTVYgnhlRFETTYFkkFPG--YYVTGDGCRRDKDGYYWI 561
Cdd:cd12115 280 YVLDRALQPVplgvpgelyiggAGVARGYL--GRP----GLTAE----RFLPDPF--GPGarLYRTGDLVRWRPDGLLEF 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 562 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIAT 641
Cdd:cd12115 348 LGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYMV 424
|
570 580
....*....|....*....|...
gi 1036086734 642 PDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
102-665 |
6.23e-27 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 117.65 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGNepgdekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHsivfagfsses 181
Cdd:COG1020 491 DAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY----------- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 L-------CERI--M--DSQCCLLITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslspp 250
Cdd:COG1020 554 VpldpaypAERLayMleDAGARLVLT------------------------------------------------------ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 251 akracpdlqQEKQKERVrkvrPPPQVPWnPEVDmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVL---HTV 327
Cdd:COG1020 580 ---------QSALAARL----PELGVPV-LALD---ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMvehRAL 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 328 SGYMLYTASTfkmvFDYHSDDVywctadigwITGHSYIT--------YGPLANGATSVLF--EGLptyPDVSRMWEIVDK 397
Cdd:COG1020 643 VNLLAWMQRR----YGLGPGDR---------VLQFASLSfdasvweiFGALLSGATLVLAppEAR---RDPAALAELLAR 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 398 YHVSKFYTAPTAIRLLMKYGSDPVHkykrtSLKILGTVGEPINPEAWQWYYNVVGEKR---------CPVVDTFWQTETG 468
Cdd:COG1020 707 HRVTVLNLTPSLLRALLDAAPEALP-----SLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPP 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 469 GHVMTPLPAATPMkPGSATFpffgvvpaILNESGE--------EL----EGPSEGYLvfKQPwpgvmrtvygnHL---RF 533
Cdd:COG1020 782 DADGGSVPIGRPI-ANTRVY--------VLDAHLQpvpvgvpgELyiggAGLARGYL--NRP-----------ELtaeRF 839
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 534 ETTYFkKFPG--YYVTGDGCRRDKDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESL 608
Cdd:COG1020 840 VADPF-GFPGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRL 915
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 609 YCFVTLNDGInynQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:COG1020 916 VAYVVPEAGA---AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
115-665 |
6.79e-27 |
|
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: 114.39 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:cd17649 9 GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITADGfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrppp 274
Cdd:cd17649 89 LTHHP--------------------------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qvpwnpevdmcwhsliggaseecepvwcdsEDPLFILYTSGSTGKPKGVL--H-TVSGYMLYTASTFKMvfdyHSDDVYW 351
Cdd:cd17649 94 ------------------------------RQLAYVIYTSGSTGTPKGVAvsHgPLAAHCQATAERYGL----TPGDREL 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 CTADIGWITGHSYItYGPLANGAtSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDpVHKYKRTSLKI 431
Cdd:cd17649 140 QFASFNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRL 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 432 LGTVGEPINPE-AWQWyynvvGEKRCPVVDTFWQTETgghVMTPL--PAATPMKPGSATFPFFGVVPA----ILNESGEE 504
Cdd:cd17649 217 YIFGGEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPIGRPLGGrsayILDADLNP 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 505 LE--GPSEGYLvfkqPWPGVMRtvyGNHLRFETTYfKKF-------PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSG 573
Cdd:cd17649 289 VPvgVTGELYI----GGEGLAR---GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 574 HLLSTAEVESALVEHEAVAEAAVVGRPHPVkGESLYCFVTLNDGiNYNQKLEAELKKQVREKIgaiatPDYIQNA----- 648
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAA-AAQPELRAQLRTALRASL-----PDYMVPAhlvfl 433
|
570
....*....|....*..
gi 1036086734 649 PGLPKTRSGKIMRRVLR 665
Cdd:cd17649 434 ARLPLTPNGKLDRKALP 450
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
91-664 |
9.91e-27 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 114.35 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 91 LDRNVHE--RKLGDRVAFYwegnepGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGA 168
Cdd:cd05920 17 LGDLLARsaARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 169 VhsIVFAGFS---SE--SLCERimdSQCCLLITADGFYRGDklinlkliadealkkcrdksfpvekcimlkhltkedeas 243
Cdd:cd05920 91 V--PVLALPShrrSElsAFCAH---AEAVAYIVPDRHAGFD--------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 244 SGSLSPPAKRACPDlqqekqkervrkvrpppqvpwnpevdmcwhsliggaseecepvwcdsedPLFILYTSGSTGKPKGV 323
Cdd:cd05920 127 HRALARELAESIPE-------------------------------------------------VALFLLSGGTTGTPKLI 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 324 LHTVSGYmLYTASTFKMVFDYHSDDVYWCTADIGwitgHSYITYGP-----LANGATSVLfeglPTYPDVSRMWEIVDKY 398
Cdd:cd05920 158 PRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIERE 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 HVSKFYTAPTAIRLLMKYGSDPvhKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTEtGGHVMTPL--P 476
Cdd:cd05920 229 GVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPALARRVPPVLG---CTLQQVFGMAE-GLLNYTRLddP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 AAT-------PMKPGSATFpffgvvpaILNESGEELEGPSEGYLVFKQPWpgvmrTVYGnHLRFETTYFKKFP--GYYVT 547
Cdd:cd05920 303 DEViihtqgrPMSPDDEIR--------VVDEEGNPVPPGEEGELLTRGPY-----TIRG-YYRAPEHNARAFTpdGFYRT 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 548 GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDginynQKLEA- 626
Cdd:cd05920 369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-----PPPSAa 443
|
570 580 590
....*....|....*....|....*....|....*....
gi 1036086734 627 ELKKQVREK-IGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd05920 444 QLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
114-615 |
1.27e-26 |
|
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: 113.46 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsIVFAGFSSeslcerimdsqccl 193
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV--PVPIYPTS-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 litadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrPP 273
Cdd:cd05907 65 ------------------------------------------------------------------------------SA 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 PQVPW---NPEVDMCwhslIGGaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMlytaSTFKMVFDYHS---D 347
Cdd:cd05907 67 EQIAYilnDSEAKAL----FVE----------DPDDLATIIYTSGTTGRPKGVMLSHRNIL----SNALALAERLPateG 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 348 DVYWCTADIGWITGHSYITYGPLANGATSV-------LFEGL----PTY-PDVSRMWE-IVDKYHVSKfytAPTAIRLLM 414
Cdd:cd05907 129 DRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetLLDDLsevrPTVfLAVPRVWEkVYAAIKVKA---VPGLKRKLF 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 415 KYGSDPvhkykrtSLKILGTVGEPINPEAWQWyYNVVGekrCPVVDTFWQTETGGHV-MTPLPAATPMKPGSatfPFFGV 493
Cdd:cd05907 206 DLAVGG-------RLRFAASGGAPLPAELLHF-FRALG---IPVYEGYGLTETSAVVtLNPPGDNRIGTVGK---PLPGV 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 494 VPAIlNESGE-ELEGPSegylvfkqpwpgVMRTVYGNHLrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML-NV 571
Cdd:cd05907 272 EVRI-ADDGEiLVRGPN------------VMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTS 336
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1036086734 572 SGHLLSTAEVESALVEHEAVAEAAVVG--RPHPVkgeslyCFVTLN 615
Cdd:cd05907 337 GGKNISPEPIENALKASPLISQAVVIGdgRPFLV------ALIVPD 376
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
289-666 |
1.28e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 113.93 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 289 LIGGASEECEPVWCDSE-DPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFkMVFDYHSDDVYWCTADI----GWItghs 363
Cdd:cd12118 116 LLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYLNALANI-LEWEMKQHPVYLWTLPMfhcnGWC---- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 364 yITYGPLANGATSVLFEGLpTYPDVsrmWEIVDKYHVSKFYTAPTAIRLLMKYgsdPVHKYKRTSLKILGTVGEPINPEA 443
Cdd:cd12118 191 -FPWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLANA---PPSDARPLPHRVHVMTAGAPPPAA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 444 WQWYYNVVGEKrcpVVDTFWQTETGGHVmtplpAATPMKPGSATFPFF---------GVvpAILNESGEELEGPSEGYLV 514
Cdd:cd12118 263 VLAKMEELGFD---VTHVYGLTETYGPA-----TVCAWKPEWDELPTEerarlkarqGV--RYVGLEEVDVLDPETMKPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 515 fkqPWPG------VMR--TVYGNHLRFETTYFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESAL 585
Cdd:cd12118 333 ---PRDGktigeiVFRgnIVMKGYLKNPEATAEAFRgGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 586 VEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPgLPKTRSGKIMRRVLR 665
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEG---AKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
.
gi 1036086734 666 K 666
Cdd:cd12118 486 D 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
98-664 |
1.32e-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: 113.84 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkeDEASSGSLsppAKRACPD 257
Cdd:cd12117 82 PAERLAFMLADAGAKVLLT-------------------------------------------DRSLAGRA---GGLEVAV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKqkervrkvrPPPQVPWNPEVDmcwhsliggaseecepvwCDSEDPLFILYTSGSTGKPKGVLHTVSG-------- 329
Cdd:cd12117 116 VIDEA---------LDAGPAGNPAVP------------------VSPDDLAYVMYTSGSTGRPKGVAVTHRGvvrlvknt 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 330 -YMLYTAstfkmvfdyhsDDVYWCTADIGWiTGHSYITYGPLANGATSVLFEGlPTYPDVSRMWEIVDKYHVSK-FYTAP 407
Cdd:cd12117 169 nYVTLGP-----------DDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 408 TaIRLLMKYGSDPVhkykrTSLKILGTVGEPINPEAW-QWYynvvgeKRCP---VVDTFWQTETGG----HVMTPLPAAT 479
Cdd:cd12117 236 L-FNQLADEDPECF-----AGLRELLTGGEVVSPPHVrRVL------AACPglrLVNGYGPTENTTfttsHVVTELDEVA 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 480 PMKP-GSatfPFFGVVPAILNESGE--------EL----EGPSEGYL--------VFKQ-PWPGVMRtvygnhlrfetty 537
Cdd:cd12117 304 GSIPiGR---PIANTRVYVLDEDGRpvppgvpgELyvggDGLALGYLnrpaltaeRFVAdPFGPGER------------- 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 538 fkkfpgYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDG 617
Cdd:cd12117 368 ------LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA 441
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1036086734 618 INYnqkleAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd12117 442 LDA-----AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
101-664 |
1.93e-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: 113.52 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 101 GDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSE 180
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 181 SLCERIMDSQCCLLitadgfyrgdklinlkliadealkkcrdksfpvekcimlkhLTKEDEASSGSLSPPAKRACPdlqq 260
Cdd:cd17646 86 RLAYMLADAGPAVV-----------------------------------------LTTADLAARLPAGGDVALLGD---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 261 ekqkerVRKVRPPPQVPWNPEvdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVL---HTVSGYMLYtast 337
Cdd:cd17646 121 ------EALAAPPATPPLVPP---------------------RPDNLAYVIYTSGSTGRPKGVMvthAGIVNRLLW---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 fkMVFDY---HSDDVYWCTA---DI-GWITghsyitYGPLANGATSVLFE-GLPTypDVSRMWEIVDKYHVSKFYTAPTA 409
Cdd:cd17646 170 --MQDEYplgPGDRVLQKTPlsfDVsVWEL------FWPLVAGARLVVARpGGHR--DPAYLAALIREHGVTTCHFVPSM 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 410 IRLLMKYGSDPvhkyKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTET----------GGHVMTPLPAAT 479
Cdd:cd17646 240 LRVFLAEPAAG----SCASLRRVFCSGEALPPELAARFLALPG---AELHNLYGPTEAaidvthwpvrGPAETPSVPIGR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 480 PMkPGSATFpffgvvpaILNESGEelegpsegylvfKQPwPGVMRTVY--GNHL-------------RFETTYFKKFPGY 544
Cdd:cd17646 313 PV-PNTRLY--------VLDDALR------------PVP-VGVPGELYlgGVQLargylgrpaltaeRFVPDPFGPGSRM 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 545 YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinYNQKL 624
Cdd:cd17646 371 YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAG--AAGPD 448
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1036086734 625 EAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd17646 449 TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
102-684 |
2.57e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.72 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGNepgdekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVfagfsses 181
Cdd:PRK07786 32 DAPALRFLGN------TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPV-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 lcerimdsqccllitadgfyrgdkliNLKLIADEAlkkcrdkSFPVEKCIMLKHLTkedEASSGSLSPPAKRACPDLqqe 261
Cdd:PRK07786 98 --------------------------NFRLTPPEI-------AFLVSDCGAHVVVT---EAALAPVATAVRDIVPLL--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 262 kqkERVRKVRPPPQvpwnpEVDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYmlyTASTFKMV 341
Cdd:PRK07786 139 ---STVVVAGGSSD-----DSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL---TGQAMTCL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 342 FDYHSD---DVYWCTADIGWITGhsyitygpLANGATSVLFeGLPT--YP----DVSRMWEIVDKYHVSKFYTAPTAIRL 412
Cdd:PRK07786 208 RTNGADinsDVGFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 413 LMkygSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRcpVVDTFWQTEtgghvMTPLpaaTPM--------KPG 484
Cdd:PRK07786 279 VC---AEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQ--ILAAFGQTE-----MSPV---TCMllgedairKLG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 485 SATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpgVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGR 564
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP---TLMSGYWNNPEATAEAFAG--GWFHSGDLVRQDEEGYVWVVDR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 565 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLE-AELKKQVREKIGAIATPD 643
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPK 497
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1036086734 644 YIQNAPGLPKTRSGKIMRRVLRKI--ACNERDLGDVSTLADSS 684
Cdd:PRK07786 498 ALEIVDALPRNPAGKVLKTELRERygACVNVERRSASAGFTER 540
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
119-664 |
3.66e-26 |
|
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: 112.60 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 119 VTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSivfagfsseslcerimdsqccllitad 198
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA--------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 gfyrgdkLINLKLIADEalkkcrdksfpvekcimLKHLTKEDEASSGSLSPPAKRACPDLQQEKQKERVrKVRPPPQVPW 278
Cdd:cd05923 82 -------LINPRLKAAE-----------------LAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLAL-SDLVGLGEPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 279 NpevdmcwhsliggASEECEPVWCDSEDPLFILYTSGSTGKPKGVL---HTVSGYMLYTASTFKMVFDYHSddvywctAD 355
Cdd:cd05923 137 S-------------AGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHN-------VV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 356 IGWITghSYITYGPLANGATSVLFEG---LPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMkyGSDPVHKYKRTSLKIL 432
Cdd:cd05923 197 LGLMP--LYHVIGFFAVLVAALALDGtyvVVEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 433 GTVGEPINPEAWQwyyNVVGEKRCPVVDTFWQTETGGHVMTPLPAA-TPMKPGsatfpFFG---VVPaILNESGEELEGP 508
Cdd:cd05923 273 TFAGATMPDAVLE---RVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEALANG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 509 SEGYLVFKQP----WPGVMRtvygnhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESA 584
Cdd:cd05923 344 EEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERV 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 585 LVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEA-----ELKKQVREKIGAIATPdyiqnapgLPKTRSGKI 659
Cdd:cd05923 417 LSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQfcrasELADFKRPRRYFFLDE--------LPKNAMNKV 488
|
....*
gi 1036086734 660 MRRVL 664
Cdd:cd05923 489 LRRQL 493
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
115-664 |
4.11e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 112.38 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITadgfyrgdklinlkliaDEALKkcrdksFPVEKCIMLKHLTKEDEASSGSlsppakracpdlqqekqkervrkVRPPP 274
Cdd:cd12116 89 LT-----------------DDALP------DRLPAGLPVLLLALAAAAAAPA-----------------------APRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVPwnpevdmcwhsliggaseecepvwcdsEDPLFILYTSGSTGKPKGVLHT---VSGYMLYTASTFKMvfdyhsddvyw 351
Cdd:cd12116 123 VSP---------------------------DDLAYVIYTSGSTGRPKGVVVShrnLVNFLHSMRERLGL----------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 cTADIGWITGHSY---IT----YGPLANGATSVLFEGLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPvhky 424
Cdd:cd12116 165 -GPGDRLLAVTTYafdISllelLLPLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 425 kRTSLKIL-GtvGEPINP-----------EAWqwyyNVVGekrcPVVDTFWQT-----ETGGHVM--TPLP--------- 476
Cdd:cd12116 239 -RAGLTALcG--GEALPPdlaarllsrvgSLW----NLYG----PTETTIWSTaarvtAAAGPIPigRPLAntqvyvlda 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 AATPMKPGsatfpffgvVPAILNESGEeleGPSEGYlvfkqpwpgvmrtvygnHLRFETTyFKKF-------PG--YYVT 547
Cdd:cd12116 308 ALRPVPPG---------VPGELYIGGD---GVAQGY-----------------LGRPALT-AERFvpdpfagPGsrLYRT 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 548 GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGEsLYCFVTLNDGINYNqklEAE 627
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAA 433
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 628 LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd12116 434 LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
90-636 |
5.67e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 113.27 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVheRKLGDRVAFYWEGNepGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 HSIVFAGfSSESLCERIM-DSQCCLLITADGFYRgDKLInlkliadEALKKCRDksfpVEKCIMLKHLTKEDEASSGSLS 248
Cdd:COG1022 92 TVPIYPT-SSAEEVAYILnDSGAKVLFVEDQEQL-DKLL-------EVRDELPS----LRHIVVLDPRGLRDDPRLLSLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 249 ppakracpDLQqekqkERVRKVRPPpqvpwnPEVDMCWHSLiggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTvS 328
Cdd:COG1022 159 --------ELL-----ALGREVADP------AELEARRAAV-------------KPDDLATIIYTSGTTGRPKGVMLT-H 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 329 GYMLYTASTFKMVFDYHSDDVY-----WCtadigWITGHSyITYGPLANGATSVLFEGLPTYPD------------VSRM 391
Cdd:COG1022 206 RNLLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkptfmlaVPRV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 392 WEivdkyhvsKFYTA----------------PTAIRLLMKYG-----SDPVHKYKRTSLKI------------LG----- 433
Cdd:COG1022 280 WE--------KVYAGiqakaeeagglkrklfRWALAVGRRYArarlaGKSPSLLLRLKHALadklvfsklreaLGgrlrf 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 434 --TVGEPINPEAWQWYYNV-VgekrcPVVDTFWQTETGGHVMTPLPAAtpMKPGSATFPFFGVVPAIlNESGEelegpse 510
Cdd:COG1022 352 avSGGAALGPELARFFRALgI-----PVLEGYGLTETSPVITVNRPGD--NRIGTVGPPLPGVEVKI-AEDGE------- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 511 gyLVFKQpwPGVMRtvyGnhlrfettYFKKfP----------GYYVTGD-GcRRDKDGYYWITGRIDDMLNVS-GHLLST 578
Cdd:COG1022 417 --ILVRG--PNVMK---G--------YYKN-PeataeafdadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAP 479
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVG--RPHPVkgeslyCFVTLND----------GINYNQKLEAELKKQVREKI 636
Cdd:COG1022 480 QPIENALKASPLIEQAVVVGdgRPFLA------ALIVPDFealgewaeenGLPYTSYAELAQDPEVRALI 543
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
310-665 |
6.18e-26 |
|
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: 111.70 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 310 ILYTSGSTGKPKGVLHTVSGYMLYTAS--TFKMVFDYHSDDVYWCTADIGWITGHSYiTYGPLANGATSVLFEGLptypD 387
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 388 VSRMWEIVDKYHVSKFYTAPTA-IRLLMKYGSDPvHKYKRTSLKILGTVGEPINP---EAW-QWYynvvgekrCPVVDTF 462
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMfVRLLKLPEAVR-NAYDLSSLKRVIHAAAPCPPwvkEQWiDWG--------GPIIWEY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 463 WQ-TETGGhvMTPLPAATPMK-PGSATFPFFGVVpAILNESGEELEGPSEGYLVFKQPWPgvmrtvYGNHLRFETTYFKK 540
Cdd:cd05929 276 YGgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 541 FPGYYVT-GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGIN 619
Cdd:cd05929 347 NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAD 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1036086734 620 YNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05929 427 AGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
98-667 |
6.19e-26 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 112.54 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWegnepgDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK06155 32 ERYPDRPLLVF------GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITADGFYrgdklinlkliadEALKKCRDKSFPVEKCIMLkhltkeDEASSGSLsPPAKRACPd 257
Cdd:PRK06155 106 RGPQLEHILRNSGARLLVVEAALL-------------AALEAADPGDLPLPAVWLL------DAPASVSV-PAGWSTAP- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 lqqekqkervrkvrPPPqvpwnpevdmcwhsliGGASEECEPVwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAST 337
Cdd:PRK06155 165 --------------LPP----------------LDAPAPAAAV--QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 FKMVfDYHSDDVYWCTADIGWITGHSYItYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYG 417
Cdd:PRK06155 213 AEDL-EIGADDVLYTTLPLFHTNALNAF-FQALLAGATYVLEPRF----SASGFWPAVRRHGATVTYLLGAMVSILLSQP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 418 SDPVHKYKRTSLKiLGTVGEPINPEAWQWYYNVvgekrcPVVDTFWQTETGGHVMTPLPAAtpmKPGSATFPFFGVVPAI 497
Cdd:PRK06155 287 ARESDRAHRVRVA-LGPGVPAALHAAFRERFGV------DLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEARV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 498 LNESGEELEGPSEGYLVFKQPWPGVMRTVYGNHLRFETTYFKKFpgYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLS 577
Cdd:PRK06155 357 VDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKTVEAWRNL--WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENIS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 578 TAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinynQKLE-AELKKQVREKIGAIATPDYIQNAPGLPKTRS 656
Cdd:PRK06155 435 SFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG----TALEpVALVRHCEPRLAYFAVPRYVEFVAALPKTEN 510
|
570
....*....|.
gi 1036086734 657 GKIMRRVLRKI 667
Cdd:PRK06155 511 GKVQKFVLREQ 521
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
306-668 |
1.21e-25 |
|
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: 108.19 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGWITGHsYITYGPLANGATSVLFEGLPty 385
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 386 pDVSRMWEIVDKYHVSkfyTAPTAIRLLMKYGSDPvhkykrTSLKILGTV---GEPINPEAWQwyynVVGEKRCPVVDTF 462
Cdd:cd17630 77 -ALAEDLAPPGVTHVS---LVPTQLQRLLDSGQGP------AALKSLRAVllgGAPIPPELLE----RAADRGIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 463 WQTETGGHVMTPLPAATpmKPGSATFPFFGVVPAILNESGEELEGPSegylVFKQPWPGVMRTVYGNhlrfettyfkkfP 542
Cdd:cd17630 143 GMTETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEIWVGGAS----LAMGYLRGQLVPEFNE------------D 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInynq 622
Cdd:cd17630 205 GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA---- 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1036086734 623 kLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:cd17630 281 -DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
120-668 |
1.23e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 111.79 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADG 199
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 FyRGDKLINlkliadealkkcrdksfpvekciMLKHLTKEDeassgSLSPPAKRACPDLQQEKQKERVRKVRPPPQVPWn 279
Cdd:PRK12583 127 F-KTSDYHA-----------------------MLQELLPGL-----AEGQPGALACERLPELRGVVSLAPAPPPGFLAW- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 PEVDMCWHSLIGGASEECEPVwCDSEDPLFILYTSGSTGKPKGVL---HTV--SGYMLYTAstfkMVFDYHSDDV----- 349
Cdd:PRK12583 177 HELQARGETVSREALAERQAS-LDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES----LGLTEHDRLCvpvpl 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTadigwitGHSYITYGPLANGATSVL----FEGLPTYpdvsrmwEIVDKYHVSKFYTAPTAirLLMKYGSDPVHKYK 425
Cdd:PRK12583 252 YHCF-------GMVLANLGCMTVGACLVYpneaFDPLATL-------QAVEEERCTALYGVPTM--FIAELDHPQRGNFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGTVGEPINPEAWQwyyNVVGEKRCP-VVDTFWQTETGGhVMTPLPAATPMKPGSATF-------------PFF 491
Cdd:PRK12583 316 LSSLRTGIMAGAPCPIEVMR---RVMDEMHMAeVQIAYGMTETSP-VSLQTTAADDLERRVETVgrtqphlevkvvdPDG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 492 GVVPailneSGEELEGPSEGYLVfkqpwpgvMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNV 571
Cdd:PRK12583 392 ATVP-----RGEIGELCTRGYSV--------MKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 572 SGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGL 651
Cdd:PRK12583 457 GGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG---HAASEEELREFCKARIAHFKVPRYFRFVDEF 533
|
570
....*....|....*..
gi 1036086734 652 PKTRSGKIMRRVLRKIA 668
Cdd:PRK12583 534 PMTVTGKVQKFRMREIS 550
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
114-668 |
2.82e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 110.60 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITADGFYRGDKLINLKLIADEALKkcrdksfPVEKCIMLkhltkeDEASSGSLSPPAKRACPDLQQEKQkervrkvrPP 273
Cdd:PRK06164 111 LVVWPGFKGIDFAAILAAVPPDALP-------PLRAIAVV------DDAADATPAPAPGARVQLFALPDP--------AP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 PQVPWNPEVDmcwhsliggaseecepvwcdsEDPLFILY-TSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWC 352
Cdd:PRK06164 170 PAAAGERAAD---------------------PDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 TADIGWITGHSYITyGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVhkyKRTSLKIL 432
Cdd:PRK06164 228 ALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGERA---DFPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 433 GTVG-EPINPEAWQWyynvVGEKRCPVVDTFWQTET----GGHVMTP------LPAATPMKPGsatfpffGVVPAILNES 501
Cdd:PRK06164 300 GFASfAPALGELAAL----ARARGVPLTGLYGSSEVqalvALQPATDpvsvriEGGGRPASPE-------ARVRARDPQD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 502 GEELEGPSEGYLVFKQpwPGVMRTVYGNHlrfETTYFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAE 580
Cdd:PRK06164 369 GALLPDGESGEIEIRA--PSLMRGYLDNP---DATARALTDdGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 581 VESALVEHEAVAEAAVVGRPHPVKGESlYCFVTLNDGInynQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSG--- 657
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDGA---SPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAnga 519
|
570
....*....|.
gi 1036086734 658 KIMRRVLRKIA 668
Cdd:PRK06164 520 KIQKHRLREMA 530
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
306-661 |
2.63e-24 |
|
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: 104.41 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSGYMlytAStfkmvFDYHSDDVYWCTADIGWITG---HSYITYGplangATSVLFEG- 381
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI---ES-----FVCNEDLFNISGEDAILAPGplsHSLFLYG-----AISALYLGg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 382 ---LPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSdPVHKykrtsLKILGTVGEPINPEAWQWYYNvvGEKRCPV 458
Cdd:cd17633 68 tfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLE-PESK-----IKSIFSSGQKLFESTKKKLKN--IFPKANL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 459 VDTFWQTETGghVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELegpseGYLVFKQPWpgvmrtVYGNHLRFEttyF 538
Cdd:cd17633 140 IEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEM------VFSGYVRGG---F 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 539 KKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGEsLYCFVTLNDGI 618
Cdd:cd17633 204 SNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSGDKL 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1036086734 619 NYNQKLEAELKKQVREKIgaiatPDYIQNAPGLPKTRSGKIMR 661
Cdd:cd17633 283 TYKQLKRFLKQKLSRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
100-658 |
2.87e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 107.28 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 100 LGDRVAFYWegnepGDEKtVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSS 179
Cdd:PRK07798 16 VPDRVALVC-----GDRR-LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 180 ESLCERIMDSQCCLLITADGFyrGDKLINLKliadEALKKcrdksfpvekcimLKHLTKEDEASSGSLSPPAkracpdlq 259
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVL----PRLPK-------------LRTLVVVEDGSGNDLLPGA-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 260 qekqkervrkvrpppqVPWNpevdmcwhSLIGGASEECEPVwCDSEDPLFILYTSGSTGKPKGVLHT------VS--GYM 331
Cdd:PRK07798 143 ----------------VDYE--------DALAAGSPERDFG-ERSPDDLYLLYTGGTTGMPKGVMWRqedifrVLlgGRD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 332 LYTASTFKmvfdyhsdDVYWCTADIGWITGHSYITYGPLANGAT-----SVLFEG--LPTYPDVS----RMWEIVDKYHV 400
Cdd:PRK07798 198 FATGEPIE--------DEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSGqtVVLLPDVRfdadEVWRTIEREKV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 401 SKF------YTAPTAIRLlmkygsDPVHKYKRTSLKILGTVGEPINPEAWQ----WYYNVVgekrcpVVDTFWQTETG-- 468
Cdd:PRK07798 270 NVItivgdaMARPLLDAL------EARGPYDLSSLFAIASGGALFSPSVKEalleLLPNVV------LTDSIGSSETGfg 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 469 GHVMTplpAATPMKPGSATFPfFGVVPAILNESGEELEGPSE--GYLVFKQPWP-GvmrtVYGNHLRFETTyFKKFPG-- 543
Cdd:PRK07798 338 GSGTV---AKGAVHTGGPRFT-IGPRTVVLDEDGNPVEPGSGeiGWIARRGHIPlG----YYKDPEKTAET-FPTIDGvr 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 544 YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqk 623
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPD-- 486
|
570 580 590
....*....|....*....|....*....|....*
gi 1036086734 624 lEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGK 658
Cdd:PRK07798 487 -LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
115-665 |
3.17e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 107.15 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEK-TVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQccl 193
Cdd:PRK13382 64 DELgTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREG--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 litADGfyrgdklinlkLIADEALKKCRDKSFpvekcimlkhltkedeassgslsppakRACPDlqqekqKERVrkvrpp 273
Cdd:PRK13382 141 ---VDT-----------VIYDEEFSATVDRAL---------------------------ADCPQ------ATRI------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqVPWNPEVDMCWHSLIGGASEECEPVWCDSEDPLfILYTSGSTGKPKGVLHTVSGymlyTASTFKMVFDyhsddvywct 353
Cdd:PRK13382 168 --VAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSGPG----GIGTLKAILD---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 354 aDIGWITGHSYITYGPL--ANGATSVLFEGLPTYPDVSR-------MWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKY 424
Cdd:PRK13382 231 -RTPWRAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 425 KRTSLKILGTVGEPINPEAWQWYYNVVGekrcPVVDTFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEE 504
Cdd:PRK13382 310 SGRSLRFAAASGSRMRPDVVIAFMDQFG----DVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFRE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 505 LegpsegylvfkqPWPGVMRTVYGNHLRFE-----TTyfKKF-PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLST 578
Cdd:PRK13382 386 V------------PTGEVGTIFVRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInynQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGK 658
Cdd:PRK13382 452 IEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA---SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
....*..
gi 1036086734 659 IMRRVLR 665
Cdd:PRK13382 529 ILRRELQ 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
119-662 |
2.94e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 119 VTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQC-CLLITA 197
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGArVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 198 DGfyrgdklinlklIADEALKKCRDKSFPVEkcimlkhLTKEDEASSGSLSPpakracpdlqqekqkERVRKVRPPPQVp 277
Cdd:PRK05852 124 DG------------PHDRAEPTTRWWPLTVN-------VGGDSGPSGGTLSV---------------HLDAATEPTPAT- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 278 wnpevdmcwhsligGASEECEPvwcdseDPLFILYTSGSTGKPKGVLHT-----------VSGYML--YTASTFKMVFdY 344
Cdd:PRK05852 169 --------------STPEGLRP------DDAMIMFTGGTTGLPKMVPWThaniassvraiITGYRLspRDATVAVMPL-Y 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 345 HsddvywctadigwitGHSYIT--YGPLANGATsVLfegLPTYPDVS--RMWEIVDKYHVSKFYTAPTAIRLLMKYGSDP 420
Cdd:PRK05852 228 H---------------GHGLIAalLATLASGGA-VL---LPARGRFSahTFWDDIKAVGATWYTAVPTIHQILLERAATE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 421 VHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPL---------PAATPMKPGSATFPFF 491
Cdd:PRK05852 289 PSGRKPAALRFIRSCSAPLTAETAQALQTEFA---APVVCAFGMTEATHQVTTTQiegigqtenPVVSTGLVGRSTGAQI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 492 GVVpailNESGEELEGPSEGylvfkQPW---PGVMRTVYGNHlrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDM 568
Cdd:PRK05852 366 RIV----GSDGLPLPAGAVG-----EVWlrgTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKleaELKKQVREKIGAIATPDYIQNA 648
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEA 510
|
570
....*....|....
gi 1036086734 649 PGLPKTRSGKIMRR 662
Cdd:PRK05852 511 SGLPHTAKGSLDRR 524
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
93-666 |
4.00e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.81 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 93 RNVHE------RKLGDRVAFYWegnepgDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARI 166
Cdd:PRK12316 4551 RCVHQlvaeraRMTPDAVAVVF------DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 167 GAVHSIVFAGFSSESLCERIMDSQCCLLITAdgfyrgdklinlkliadealkkcrdksfpvekcimlKHLTKEdeassgs 246
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLTQ------------------------------------SHLLQR------- 4661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 247 LSPPAKRACPDLQQEKQkervrkvrpppqvpWNpevdmcwhsligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT 326
Cdd:PRK12316 4662 LPIPDGLASLALDRDED--------------WE------------GFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 327 VSGYMLYTASTFKMvfdyhsddvYWCTADIGWITGHSYI-------TYGPLANGAtSVLFEGlPTYPDVSRMWEIVDKYH 399
Cdd:PRK12316 4716 HGSLVNHLHATGER---------YELTPDDRVLQFMSFSfdgshegLYHPLINGA-SVVIRD-DSLWDPERLYAEIHEHR 4784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 400 VSKFYTAPTAIRLLMKygsDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRcpVVDTFWQTETgghVMTPLPAAT 479
Cdd:PRK12316 4785 VTVLVFPPVYLQQLAE---HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVY--LFNGYGPTET---TVTVLLWKA 4856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 480 P--MKPGSATFPFFGVVPA----ILNESGE--------EL----EGPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKf 541
Cdd:PRK12316 4857 RdgDACGAAYMPIGTPLGNrsgyVLDGQLNplpvgvagELylggEGVARGYL----ERPALTAE------RFVPDPFGA- 4925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 542 PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVkGESLYCFVTLND-GI 618
Cdd:PRK12316 4926 PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDpAL 5004
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 619 NYNQKLEAELKKQVREKIGAiATPDYIQNA-----PGLPKTRSGKIMRRVLRK 666
Cdd:PRK12316 5005 ADADEAQAELRDELKAALRE-RLPEYMVPAhlvflARMPLTPNGKLDRKALPQ 5056
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
286-665 |
1.12e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.41 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 286 WHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLhTVSGYMLYTASTFKMVFDYHSDDVYWCTADI--------G 357
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTERFGLTRDDVCYVSMPLfhsnavmaG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 358 WitghsyityGP-LANGATSVL---FEGLPTYPDVSRmweivdkYHVSKFYTAPTAIRLLMkygSDPVHKYKR-TSLKI- 431
Cdd:PRK13388 210 W---------APaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYIL---ATPERPDDAdNPLRVa 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 432 LGTVGEPINPEAWQWYYnvvgekRCPVVDTFWQTETGGHVMtpLPAATPmkPGSATFPFFGVV-----------PAILNE 500
Cdd:PRK13388 271 FGNEASPRDIAEFSRRF------GCQVEDGYGSSEGAVIVV--REPGTP--PGSIGRGAPGVAiynpetltecaVARFDA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 501 SGEeLEGPSE--GYLVFKQPwPGVMRTVYGNHlrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLST 578
Cdd:PRK13388 341 HGA-LLNADEaiGELVNTAG-AGFFEGYYNNP---EATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN-QKLEAELKKQvrEKIGAIATPDYIQNAPGLPKTRSG 657
Cdd:PRK13388 416 APIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFLAAQ--PDLGTKAWPRYVRIAADLPSTATN 493
|
....*...
gi 1036086734 658 KIMRRVLR 665
Cdd:PRK13388 494 KVLKRELI 501
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
303-668 |
2.03e-22 |
|
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: 101.25 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGAtSVLFEGL 382
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 PTYPDvsRMWEIVDKYHVSKFYTAPTAIRLLMKYgsdpVHKYKRTSLKILGTVGEPINP---EAWQWYYNVvgekrcPVV 459
Cdd:cd05909 223 PLDYK--KIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDtlrQEFQEKFGI------RIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 460 DTFWQTEtgghvMTPLPAAT----PMKPGSATFPFFGVVPAILN-ESGEELEGPSEGYLVFKQpwPGVMRTVYGNHlrfE 534
Cdd:cd05909 291 EGYGTTE-----CSPVISVNtpqsPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRG--PNVMLGYLNEP---E 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 535 TTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVGRPHPVKGESLYCFVT 613
Cdd:cd05909 361 LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1036086734 614 LNDGInynqklEAELKKQVRE-KIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:cd05909 441 TTDTD------PSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
116-670 |
2.16e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 101.01 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGvKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLI 195
Cdd:PRK07638 24 DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 196 TaDGFYRGDklinlklIADEalkKCRdksfpvekCIMLKHltkedeassgslsppakracpdlqqekqkervrkvrpppq 275
Cdd:PRK07638 103 T-ERYKLND-------LPDE---EGR--------VIEIDE---------------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 vpwnpevdmcWHSLIGGASEECEPVwCDSE-DPLFILYTSGSTGKPKGVLHTVSGYMLY---TASTFKMVfdyHSDDVYw 351
Cdd:PRK07638 124 ----------WKRMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWLHSfdcNVHDFHMK---REDSVL- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 ctadigwITG---HSYITYGplangATSVLFEG-----LPTYPDVsRMWEIVDKYHVSKFYTAPTAIRLLMKygsdpVHK 423
Cdd:PRK07638 189 -------IAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFIPN-QVLDKLETENISVMYTVPTMLESLYK-----ENR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 424 YKRTSLKIL--GTVGEPINPEAWQ--WYYNVVGEkrcpvvdtFWQTETGGHVMTPLPAATPMKPGSATFPFFGVVPAILN 499
Cdd:PRK07638 251 VIENKMKIIssGAKWEAEAKEKIKniFPYAKLYE--------FYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICN 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 500 ESGEELEGPSEGYLVFKQPWPgVMRTVYGNHLRFETTYfkkfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTA 579
Cdd:PRK07638 323 EAGEEVQKGEIGTVYVKSPQF-FMGYIIGGVLARELNA----DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 580 EVESALVEHEAVAEAAVVGRPHPVKGESLycfVTLNDGiNYNQKleaELKKQVREKIGAIATPDYIQNAPGLPKTRSGKI 659
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKG-SATKQ---QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKI 470
|
570
....*....|.
gi 1036086734 660 MRRVLRKIACN 670
Cdd:PRK07638 471 ARMEAKSWIEN 481
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
98-665 |
5.22e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 100.48 E-value: 5.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK07059 34 RQYADRPAFICMG------KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITadgfyrgdkLINLKLIADEALKKcrdksfpvekcIMLKHLTKedeASSGslsppakracpD 257
Cdd:PRK07059 108 TPRELEHQLKDSGAEAIVV---------LENFATTVQQVLAK-----------TAVKHVVV---ASMG-----------D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKQK------ERVRKVRP----PPQVPWNpevdmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKG--VLH 325
Cdd:PRK07059 154 LLGFKGHivnfvvRRVKKMVPawslPGHVRFN-------DALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGatLLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 326 -TVSGYMLYTASTFKMVFDY--HSDDVYWCTA----DIGWITGHSYITygpLANGATSVLfegLPTYPDVSRMWEIVDKY 398
Cdd:PRK07059 227 rNIVANVLQMEAWLQPAFEKkpRPDQLNFVCAlplyHIFALTVCGLLG---MRTGGRNIL---IPNPRDIPGFIKELKKY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 HVSKFYTAPTAIRLLMKygSDPVHKYKRTSLKI-LG---TVGEPInpeAWQWYyNVVGekrCPVVDTFWQTETGGhVMTP 474
Cdd:PRK07059 301 QVHIFPAVNTLYNALLN--NPDFDKLDFSKLIVaNGggmAVQRPV---AERWL-EMTG---CPITEGYGLSETSP-VATC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 475 LPAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTvYGNhlRFETTYFKKFP-GYYVTGDGCRR 553
Cdd:PRK07059 371 NPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP--QVMAG-YWN--RPDETAKVMTAdGFFRTGDVGVM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 554 DKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDginynQKL-EAELKKQV 632
Cdd:PRK07059 446 DERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----PALtEEDVKAFC 520
|
570 580 590
....*....|....*....|....*....|...
gi 1036086734 633 REKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK07059 521 KERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
96-665 |
8.13e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 99.70 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 96 HERKLGDRVAFYWEgnEPGDekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGavhsivfa 175
Cdd:PRK13390 6 HAQIAPDRPAVIVA--ETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 176 gfsseslcerimdsqccLLITAdgfyrgdklINLKLIADEALKKCRDKSFPVEkcimlkhltkedeASSGSLSPPAKRAC 255
Cdd:PRK13390 74 -----------------LYITA---------INHHLTAPEADYIVGDSGARVL-------------VASAALDGLAAKVG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 256 PDLqqekqkervrkvrpPPQVPWNPEVD--MCWHSLIGGASEECEPVWCDSedplFILYTSGSTGKPKGVLHTVSGY--- 330
Cdd:PRK13390 115 ADL--------------PLRLSFGGEIDgfGSFEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIQPDLPGRdvd 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 331 -----MLYTASTFkmvFDYHSDDVYWCTADIGwitgHSyityGPL-------ANGATSVLFEGLptypDVSRMWEIVDKY 398
Cdd:PRK13390 177 apgdpIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 HVSKFYTAPTAIRLLMKYGSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrcPVVDTFWQTeTGGHVMTPLPAA 478
Cdd:PRK13390 242 RITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG----PIVYEYYSS-TEAHGMTFIDSP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 479 TPMK-PGSATFPFFGVVpAILNESGEELEGPSEGYLVFKQPwpgvmRTVYGNHLRFETTYFKKFPG---YYVTGDGCRRD 554
Cdd:PRK13390 317 DWLAhPGSVGRSVLGDL-HICDDDGNELPAGRIGTVYFERD-----RLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVD 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 555 KDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVRE 634
Cdd:PRK13390 391 EDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRS 470
|
570 580 590
....*....|....*....|....*....|.
gi 1036086734 635 KIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK13390 471 RIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
286-666 |
8.80e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 99.76 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 286 WHSLIGG-ASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT-----VSGYMLYTAstfkmvFDYHSDDVYWCTADI--- 356
Cdd:PRK07867 132 WADELAAhRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCThrkvaSAGVMLAQR------FGLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 357 -----GWITGhsyitygpLANGATSVL---FEGLPTYPDVSRmweivdkYHVSKF-YTA-PTAIRLlmkyGSDPVHKYKR 426
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnYVGkPLSYVL----ATPERPDDAD 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 427 TSLKIL-GTVGEPINPEAWqwyynvvgEKR--CPVVDTFWQTEtGGHVMTPLPAaTPmkPGSATFPFFGVvpAILN-ESG 502
Cdd:PRK07867 267 NPLRIVyGNEGAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGV--AIVDpDTG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 503 EELeGPSE-------------GYLVFKQPwPGVMRTVYGNHlrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML 569
Cdd:PRK07867 333 TEC-PPAEdadgrllnadeaiGELVNTAG-PGGFEGYYNDP---EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWM 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 570 NVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQ-KLEAELKKQvrEKIGAIATPDYIQNA 648
Cdd:PRK07867 408 RVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPKQWPSYVRVC 485
|
410
....*....|....*...
gi 1036086734 649 PGLPKTRSGKIMRRVLRK 666
Cdd:PRK07867 486 AELPRTATFKVLKRQLSA 503
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
306-661 |
9.62e-22 |
|
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: 96.96 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSyITYGPLANGATSVLFEGLpty 385
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 386 pDVSRMWEIVDKYHVSKFYT-APTAIRLLMKYGSDPVhkyKRTSLKILGTVGEPINPEAWqwyynvvgEKRCPVvdTFW- 463
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF--------EETTGA--TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 464 ---QTETGGHVmTPLPAATpmKPGSATFPFFGVVPAILNESGEELE----------GPsegyLVFKQPWpgvmrtvygnH 530
Cdd:cd17637 142 lygQTETSGLV-TLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPagetgeivvrGP----LVFQGYW----------N 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 531 LRFETTY-FKKfpGYYVTGDGCRRDKDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGES 607
Cdd:cd17637 205 LPELTAYtFRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1036086734 608 LYCFVTLNDGinynQKLEA-ELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:cd17637 283 IKAVCVLKPG----ATLTAdELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
98-665 |
1.06e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 99.45 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAG 176
Cdd:PRK05677 35 QRFADKPAFSNLG------KTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 177 FSSESLCERIMDSQCCLLITadgfyrgdkLINLKLIADEALKKCRDKSFPVekcimlkhltkedeASSGSLSPPAKRACP 256
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTGVKHVIV--------------TEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 257 DLQQEKQKERVRKVRPPPQVPWNpevdmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT---VSGYMLY 333
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFN-------DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 334 TASTFKMVFD------------YHsddvywctadIGWITGHSYITygpLANGATSVLfegLPTYPDVSRMWEIVDKYHVS 401
Cdd:PRK05677 239 CRALMGSNLNegceiliaplplYH----------IYAFTFHCMAM---MLIGNHNIL---ISNPRDLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 402 KFYTAPTAIRLLMKygSDPVHKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETgghvmTPLPAATPM 481
Cdd:PRK05677 303 GFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVNPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 482 K---PGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGNhlRFETTYFKKFPGYYVTGDGCRRDKDGY 558
Cdd:PRK05677 373 QaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQR--PEATDEILDSDGWLKTGDIALIQEDGY 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 559 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGA 638
Cdd:PRK05677 449 MRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTG 525
|
570 580
....*....|....*....|....*..
gi 1036086734 639 IATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK05677 526 YKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
96-665 |
5.27e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 96.88 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 96 HERKLGDRVAFYWEGNEpgdektVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivfa 175
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAV------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 176 gfsseslcerIMDsqccllitadgfyrgdklINLKLIADEALKKCRDKSfpvEKCIMLkhltkeDEASSGSLSPPAKRAC 255
Cdd:PRK06145 79 ----------FLP------------------INYRLAADEVAYILGDAG---AKLLLV------DEEFDAIVALETPKIV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 256 PDLQQEKQKERvrkvrpppqvpwnpevdmcwhslIGGASEECEPVWCDSEDPLF-ILYTSGSTGKPKGVLHTVsgymlyt 334
Cdd:PRK06145 122 IDAAAQADSRR-----------------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSY------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 335 astfkmvfdyhsDDVYWCTAD----IGWITGHSYITYGPLAN-GA-----TSVLFEG----LPTYPDVSRMWEIVDKYHV 400
Cdd:PRK06145 172 ------------GNLHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 401 SKFYTAPTAI-RLLMKYGSDpvhKYKRTSLKILGTVGEPiNPE----AWQWYYnvvgeKRCPVVDTFWQTET-GGHvmTP 474
Cdd:PRK06145 240 TCAWMAPVMLsRVLTVPDRD---RFDLDSLAWCIGGGEK-TPEsrirDFTRVF-----TRARYIDAYGLTETcSGD--TL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 475 LPAATPM-KPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpgvmRTVYGNHLRFETTYFKKFPGYYVTGDGCRR 553
Cdd:PRK06145 309 MEAGREIeKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP-----KVTKGYWKDPEKTAEAFYGDWFRSGDVGYL 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 554 DKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinynQKLE-AELKKQV 632
Cdd:PRK06145 384 DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG----ATLTlEALDRHC 459
|
570 580 590
....*....|....*....|....*....|...
gi 1036086734 633 REKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK06145 460 RQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
99-667 |
5.54e-21 |
|
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: 97.21 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 99 KLGDRVAFywegNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFS 178
Cdd:cd17642 29 SVPGTIAF----TDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 179 SESLCERIMDSQCCLLITAD-GFyrgDKLINLKliadealkkcrDKSFPVEKCIMLKhlTKEDeassgslsppakracpd 257
Cdd:cd17642 105 ERELDHSLNISKPTIVFCSKkGL---QKVLNVQ-----------KKLKIIKTIIILD--SKED----------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 lQQEKQKERVRKVRPPPqvpwnpevdmcwhslIGGASEECEPVWCDSEDPL-FILYTSGSTGKPKGVlhtvsgyMLyTAS 336
Cdd:cd17642 152 -YKGYQCLYTFITQNLP---------------PGFNEYDFKPPSFDRDEQVaLIMNSSGSTGLPKGV-------QL-THK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 337 TFKMVFDYHSDDVYWC-----TADIGWITGHS----YITYGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAP 407
Cdd:cd17642 208 NIVARFSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRVVL---MYKF-EEELFLRSLQDYKVQSALLVP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 408 TAIRLLMKygSDPVHKYKRTSLKILGTVGEPINPEawqwyynvVGE---KR--CPVV-DTFWQTETGGHVM-TPlpaATP 480
Cdd:cd17642 284 TLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE--------VGEavaKRfkLPGIrQGYGLTETTSAILiTP---EGD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 481 MKPGSA--TFPFFGVvpAILNESGEELEGPSE-GYLVFKQPwpGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDG 557
Cdd:cd17642 351 DKPGAVgkVVPFFYA--KVVDLDTGKTLGPNErGELCVKGP--MIMKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 558 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQKL-------EAELKK 630
Cdd:cd17642 425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEvmdyvasQVSTAK 504
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 631 QVRekiGAIATPDYIqnapglPKTRSGKIMRRVLRKI 667
Cdd:cd17642 505 RLR---GGVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
305-661 |
5.75e-21 |
|
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: 94.63 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 305 EDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATsVLFEGLPT 384
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 385 YPDVsrmWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYKrtSLKILGTVGE-PINPEAwqwyYNVVGEKRCPVVDTFW 463
Cdd:cd17635 80 YKSL---FKILTTNAVTTTCLVPTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAADV----RFIEATGLTNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 464 QTETGghVMTPLPAATPMKP-GSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWpgVMRTVYGNHLRFETTYFKkfp 542
Cdd:cd17635 151 LSETG--TALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLID--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQ 622
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENA 303
|
330 340 350
....*....|....*....|....*....|....*....
gi 1036086734 623 KleAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:cd17635 304 I--RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-664 |
6.38e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLI 195
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 196 TAdgfyrgdklinlkliadealkkcrdksfpvekcimlKHLTKEDEASSGslsppAKRACPDlqqekqkervrkvRPPPQ 275
Cdd:PRK12316 614 SQ------------------------------------SHLGRKLPLAAG-----VQVLDLD-------------RPAAW 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 VPwnpevdmcwhsligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT---VSGYMLYTASTFKMVFdyhSDDVYWC 352
Cdd:PRK12316 640 LE--------------GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRhraLSNRLCWMQQAYGLGV---GDTVLQK 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 T---ADIGwitghSYITYGPLANGATSVLF-EGLPTYPDvsRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPvhkyKRTS 428
Cdd:PRK12316 703 TpfsFDVS-----VWEFFWPLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTS 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 429 LKILGTVGEPINPEAWQW---------YYNVVGEKRCPVVDTFWQ--TETGGHVmtplPAATPMKPGSATF--PFFGVVP 495
Cdd:PRK12316 772 LRRIVCSGEALPADAQEQvfaklpqagLYNLYGPTEAAIDVTHWTcvEEGGDSV----PIGRPIANLACYIldANLEPVP 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 496 AilNESGEEL---EGPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVS 572
Cdd:PRK12316 848 V--GVLGELYlagRGLARGYH----GRPGLTAE------RFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR 915
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 573 GHLLSTAEVESALVEHEAVAEAAVVGrphpVKGESLYCFVTLND-GINYNQKLEAELKKQVREKIgaiaTPDYIQNAPGL 651
Cdd:PRK12316 916 GLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESeGGDWREALKAHLAASLPEYM----VPAQWLALERL 987
|
570
....*....|...
gi 1036086734 652 PKTRSGKIMRRVL 664
Cdd:PRK12316 988 PLTPNGKLDRKAL 1000
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
115-664 |
8.49e-21 |
|
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: 96.19 E-value: 8.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITadgfyrgdklinlkliadealkkCRDKSFPVEKCIMLKHLTKEDEASSGslsppakracpdlqqekqkervrkvRPPP 274
Cdd:cd12114 89 LT-----------------------DGPDAQLDVAVFDVLILDLDALAAPA-------------------------PPPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVPwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCTA 354
Cdd:cd12114 121 VDV-------------------------APDDLAYVIFTSGSTGTPKGVMISHRA-ALNTILDINRRFAVGPDDRVLALS 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 355 ---------DIgwitghsyitYGPLANGATSVLFEGLPTyPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYK 425
Cdd:cd12114 175 slsfdlsvyDI----------FGALSAGATLVLPDEARR-RDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGtvGEPIN---PEAWQwyynvvgeKRCP---VVDTFWQTETG----GHVMTPLPAATPMKP-GsatFPFFGVV 494
Cdd:cd12114 244 SLRLVLLS--GDWIPldlPARLR--------ALAPdarLISLGGATEASiwsiYHPIDEVPPDWRSIPyG---RPLANQR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 495 PAILNESGEELEGPSEGYLvfkqpW---PGVMRTVYGNHLRFETTYFKKFPG--YYVTGD-GCRRDkDGYYWITGRIDDM 568
Cdd:cd12114 311 YRVLDPRGRDCPDWVPGEL-----WiggRGVALGYLGDPELTAARFVTHPDGerLYRTGDlGRYRP-DGTLEFLGRRDGQ 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPvKGESLYCFVTLNDGinYNQKLEAELKKQVREKIGAIATPDYIQNA 648
Cdd:cd12114 385 VKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDND--GTPIAPDALRAFLAQTLPAYMIPSRVIAL 461
|
570
....*....|....*.
gi 1036086734 649 PGLPKTRSGKIMRRVL 664
Cdd:cd12114 462 EALPLTANGKVDRAAL 477
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-665 |
1.14e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.92 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITADGFYRGdklinlklIADEALKKCRDKSFPvekcimlkhlTKEDEASSGSLSPPAKRAcpdlqqekqkervrkvrPPP 274
Cdd:PRK12406 88 IAHADLLHG--------LASALPAGVTVLSVP----------TPPEIAAAYRISPALLTP-----------------PAG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVPWNPevdmcWhsLIGGASEECEPVwcdsEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHsddvywcta 354
Cdd:PRK12406 133 AIDWEG-----W--LAQQEPYDGPPV----PQPQSMIYTSGTTGHPKGVRRA-APTPEQAAAAEQMRALIY--------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 355 diGWITGHSYITYGPLANGATSV-------LFEGLPTYP--DVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYK 425
Cdd:PRK12406 192 --GLKPGIRALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGTVGEPINPEAWQ----WYYNVVGEkrcpvvdTFWQTETGGhVMTPLPAATPMKPGSATFPFFGVVPAILNES 501
Cdd:PRK12406 270 VSSLRHVIHAAAPCPADVKRamieWWGPVIYE-------YYGSTESGA-VTFATSEDALSHPGTVGKAAPGAELRFVDED 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 502 GEELEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 581
Cdd:PRK12406 342 GRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 582 ESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD---EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFK 494
|
....
gi 1036086734 662 RVLR 665
Cdd:PRK12406 495 RRLR 498
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
112-665 |
1.19e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 95.71 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 112 EPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHsivfagfsseslcerimdsqc 191
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVF--------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 192 cL-LITAdgfYRGDKLINLKLIADEALKKCRDKSFPVEKCIMLKHLTKE----DEASSGSLSppakracpdlqqekqkER 266
Cdd:PRK07514 81 -LpLNTA---YTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHvetlDADGTGSLL----------------EA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 267 VRkvrpppqvpwnpevdmcwhsligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHS 346
Cdd:PRK07514 141 AA-----------------------AAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLS-HGNLLSNALTLVDYWRFTP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 347 DDVYWCTADIGWITGHSYITYGPLANGAtSVLFegLPTY-PD--VSRMWEIVDKYHVSKFYTaptaiRLL---------- 413
Cdd:PRK07514 197 DDVLIHALPIFHTHGLFVATNVALLAGA-SMIF--LPKFdPDavLALMPRATVMMGVPTFYT-----RLLqeprltreaa 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 414 --MKY---GSDPV----HK--YKRTSLKILGTVGepinpeawqwyynvvgekrcpvvdtfwQTETGghVMTPLPAATPMK 482
Cdd:PRK07514 269 ahMRLfisGSAPLlaetHRefQERTGHAILERYG---------------------------MTETN--MNTSNPYDGERR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 483 PGSATFPFFGVVPAILN-ESGEELE----------GPSegylVFKQPW--PgvmrtvygnhlrfETTY--FKKfPGYYVT 547
Cdd:PRK07514 320 AGTVGFPLPGVSLRVTDpETGAELPpgeigmievkGPN----VFKGYWrmP-------------EKTAeeFRA-DGFFIT 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 548 GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAE 627
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALD---EAA 458
|
570 580 590
....*....|....*....|....*....|....*...
gi 1036086734 628 LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK07514 459 ILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
114-664 |
1.38e-20 |
|
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: 95.47 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEkTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:cd17655 19 EDQ-TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITadgfyrgdklinlkliaDEALKKCRDKSfpvEKCIMLKHLTKEDEASSgSLSPPAKracpdlqqekqkervrkvrpp 273
Cdd:cd17655 98 LLT-----------------QSHLQPPIAFI---GLIDLLDEDTIYHEESE-NLEPVSK--------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqvpwnpevdmcwhsliggaseecepvwcdSEDPLFILYTSGSTGKPKGVL-------HTVSG----YMLYTASTFKMVF 342
Cdd:cd17655 136 ------------------------------SDDLAYVIYTSGSTGKPKGVMiehrgvvNLVEWankvIYQGEHLRVALFA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 343 DYHSDdvywctADIGWItghsyitYGPLANGATSVLfeglptYPDVSRMW-----EIVDKYHVSKFYTAPTAIRLLmkyg 417
Cdd:cd17655 186 SISFD------ASVTEI-------FASLLSGNTLYI------VRKETVLDgqaltQYIRQNRITIIDLTPAHLKLL---- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 418 sDPVHKYKRTSLKILGTVGEPINPE-AWQW---------YYNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMKPGSAT 487
Cdd:cd17655 243 -DAADDSEGLSLKHLIVGGEALSTElAKKIielfgtnptITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 488 fpffgvvpaILNESGE--------EL----EGPSEGYLvfKQPwpgvmrtvygnhlrfETTYfKKF------PG--YYVT 547
Cdd:cd17655 322 ---------ILDQYGRpqpvgvagELyiggEGVARGYL--NRP---------------ELTA-EKFvddpfvPGerMYRT 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 548 GDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklEAE 627
Cdd:cd17655 375 GDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP-----VAQ 449
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 628 LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd17655 450 LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
98-668 |
1.84e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 95.66 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAG 176
Cdd:PRK12492 35 KKFADRPAFSNLG------VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 177 FSSESLCERIMDSQCCLLITADGFyrgDKLINlKLIADEALKkcrdksfpvekcimlkHLTkedEASSGSLSPPAKRACP 256
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIE----------------YLI---EAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 257 DLQQEKQKERVRKVRPPPQVPWNpevdmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTAS 336
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFK-------QALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLT-HGNLVANML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 337 TFKMVFDYHSDDvywctadigwitGHsyitygPLANGATSVLFEGLPTY------------------------P-DVSRM 391
Cdd:PRK12492 238 QVRACLSQLGPD------------GQ------PLMKEGQEVMIAPLPLYhiyaftancmcmmvsgnhnvlitnPrDIPGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 392 WEIVDKYHVSKFYTAPTAIRLLMKYGSdpVHKYKRTSLKILGTVGEPI---NPEAWQwyyNVVGekrCPVVDTFWQTETG 468
Cdd:PRK12492 300 IKELGKWRFSALLGLNTLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWE---QLTG---CTIVEGYGLTETS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 469 GhVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTvYGNHLRfETTYFKKFPGYYVTG 548
Cdd:PRK12492 372 P-VASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMKG-YWQQPE-ATAEALDAEGWFKTG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 549 DGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEaEL 628
Cdd:PRK12492 447 DIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP---GLSVE-EL 522
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1036086734 629 KKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK12492 523 KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
98-673 |
2.20e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 95.51 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAG 176
Cdd:PRK08974 34 ARYADQPAFINMG------EVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 177 FSSESLCERIMDSQCCLLITADGFYRgdklinlkliadeALKKCRDKSfPVEKCImlkhLTkedeaSSGSLSPPAKRACP 256
Cdd:PRK08974 108 YTPRELEHQLNDSGAKAIVIVSNFAH-------------TLEKVVFKT-PVKHVI----LT-----RMGDQLSTAKGTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 257 DLQQEKQKERVRKVRPPPQVPWNPEVDmcwhslIGGASEECEPVwCDSEDPLFILYTSGSTGKPKGVLHTvSGYMLytas 336
Cdd:PRK08974 165 NFVVKYIKRLVPKYHLPDAISFRSALH------KGRRMQYVKPE-LVPEDLAFLQYTGGTTGVAKGAMLT-HRNML---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 337 tfkmvfdyhsDDVYWCTAdigwitghsyiTYGPLANGATSVLFEGLPTY------------------------P-DVSRM 391
Cdd:PRK08974 233 ----------ANLEQAKA-----------AYGPLLHPGKELVVTALPLYhifaltvncllfielggqnllitnPrDIPGF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 392 WEIVDKYHvskfYTAPTAIRLLMK--YGSDPVHKYKRTSLKILGTVGEPINpeawqwyyNVVGEKrcpvvdtfWQTETGG 469
Cdd:PRK08974 292 VKELKKYP----FTAITGVNTLFNalLNNEEFQELDFSSLKLSVGGGMAVQ--------QAVAER--------WVKLTGQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 470 HV-----MT---PLPAATPMK----PGSATFPffgvVPA----ILNESGEELEGPSEGYLVFKQPwpGVMRtvyGNHLRF 533
Cdd:PRK08974 352 YLlegygLTecsPLVSVNPYDldyySGSIGLP----VPSteikLVDDDGNEVPPGEPGELWVKGP--QVML---GYWQRP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 534 ETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVT 613
Cdd:PRK08974 423 EATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 614 LNDginyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIACNERD 673
Cdd:PRK08974 503 KKD----PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVD 558
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
291-667 |
4.13e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.00 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 291 GGASEECEPVWCDSEDPLFILYTSGSTGKPKGV----------LHTVSGYMLYTASTFKMVFDYHSDDVYwctadigwit 360
Cdd:PRK12467 3223 NGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVgvrhgalanhLCWIAEAYELDANDRVLLFMSFSFDGA---------- 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 361 ghSYITYGPLANGATSVLFEGLPTYPDvsRMWEIVDKYHVSKFYTAPTAIRLLMKYGSdpVHKYkrTSLKILGTVGEPIN 440
Cdd:PRK12467 3293 --QERFLWTLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG--GADC--ASLDIYVFGGEAVP 3364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 441 PEAWQWY---------YNVVGEKRCPVVDTFWQTETGGhvmTPLPAATPMKPGSAtfpffGVVPAILNESGE-------- 503
Cdd:PRK12467 3365 PAAFEQVkrklkprglTNGYGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIYVLDGQLNpvpvgvag 3436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 504 EL----EGPSEGYlvFKQPwpGVMRTvygnhlRFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLST 578
Cdd:PRK12467 3437 ELyiggVGLARGY--HQRP--SLTAE------RFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 3506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVGRPhPVKGESLYCFVTLNDginYNQKLEAELKKQVREKIgaiatPDYIQNA-----PGLPK 653
Cdd:PRK12467 3507 GEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPAD---PQGDWRETLRDHLAASL-----PDYMVPAqllvlAAMPL 3577
|
410
....*....|....
gi 1036086734 654 TRSGKIMRRVLRKI 667
Cdd:PRK12467 3578 GPNGKVDRKALPDP 3591
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
99-668 |
8.25e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 93.79 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 99 KLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:PRK08751 37 KFADRPAYHSFG------KTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLCERIMDSQCCLLITADGFyrGDKLinLKLIADEalkkcrdksfPVEKCIMlkhltkedeASSGSLSPPAKRACPD 257
Cdd:PRK08751 111 TPRELKHQLIDSGASVLVVIDNF--GTTV--QQVIADT----------PVKQVIT---------TGLGDMLGFPKAALVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKQKERVRKVRPPPQVPWNpevdmcwHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTvsgymlytast 337
Cdd:PRK08751 168 FVVKYVKKLVPEYRINGAIRFR-------EALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLT----------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 fkmvfdyHSDDVYWCTADIGWITGHSYITYG--------PL-------ANGATSVLFEGLPTYPDVSR-MWEIVDKYHVS 401
Cdd:PRK08751 230 -------HRNLVANMQQAHQWLAGTGKLEEGcevvitalPLyhifaltANGLVFMKIGGCNHLISNPRdMPGFVKELKKT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 402 KFyTAPTAIR-----LLMKYGSDpvhKYKRTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETgghvmTPLP 476
Cdd:PRK08751 303 RF-TAFTGVNtlfngLLNTPGFD---QIDFSSLKMTLGGGMAVQRSVAERWKQVTG---LTLVEAYGLTET-----SPAA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 AATPMK----PGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGNHLrfETTYFKKFPGYYVTGDGCR 552
Cdd:PRK08751 371 CINPLTlkeyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIAR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 553 RDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDginynQKLEAE-LKKQ 631
Cdd:PRK08751 447 MDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTAEdVKAH 521
|
570 580 590
....*....|....*....|....*....|....*..
gi 1036086734 632 VREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK08751 522 ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
303-664 |
1.98e-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: 91.76 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVL-------HTVSGY------------MLYTAStfkMVFDYHSDDvyWCTAdigwitghs 363
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD--FARS--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 364 yitygpLANGATSVLfegLP--TYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDpvHKYKRTSLKILgTVGEPINP 441
Cdd:cd17650 157 ------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLL-IVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 442 EAW-QWYY----------NVVGEKRCPVVDTFWQTEtgghvMTPLPAATPMKPGSatfPFFGVVPAILNESGE------- 503
Cdd:cd17650 225 AQDfKTLAarfgqgmriiNSYGVTEATIDSTYYEEG-----RDPLGDSANVPIGR---PLPNTAMYVLDERLQpqpvgva 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 504 -EL----EGPSEGYLvfKQPWPGVMRTVygnHLRFEttyfkkfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLL 576
Cdd:cd17650 297 gELyiggAGVARGYL--NRPELTAERFV---ENPFA-------PGerMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 577 STAEVESALVEHEAVAEAAVVGRpHPVKGESLYC-FVTLNDGINYNqkleaELKKQVREKIGAIATPDYIQNAPGLPKTR 655
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVR-EDKGGEARLCaYVVAAATLNTA-----ELRAFLAKELPSYMIPSYYVQLDALPLTP 438
|
....*....
gi 1036086734 656 SGKIMRRVL 664
Cdd:cd17650 439 NGKVDRRAL 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
120-677 |
2.14e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 92.21 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITADG 199
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 FYRgdklinlklIADEALKKCRDKSFPVEKCIMLKhLTKEDEASSGSLSPPAKRACpdLQQEKQKERvrkvrPPPQVPWN 279
Cdd:PLN02479 127 FFT---------LAEEALKILAEKKKSSFKPPLLI-VIGDPTCDPKSLQYALGKGA--IEYEKFLET-----GDPEFAWK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 PEVDMcWHSLIGGaseecepvwcdsedplfilYTSGSTGKPKGV-LHTVSGYMLytASTFKMVFDYHSDDVYWCTADIGW 358
Cdd:PLN02479 190 PPADE-WQSIALG-------------------YTSGTTASPKGVvLHHRGAYLM--ALSNALIWGMNEGAVYLWTLPMFH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 359 ITGHSYiTYGPLANGATSVLFEGLPTypdvSRMWEIVDKYHVSKFYTAPTAIRLL------------------MKYGSDP 420
Cdd:PLN02479 248 CNGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhvMTAGAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 421 ----VHKYKRTSLKILGTVG--EPINPE---AWQWYYN-----------------VVGEKRCPVVDTfwqtetgghvmtp 474
Cdd:PLN02479 323 ppsvLFAMSEKGFRVTHTYGlsETYGPStvcAWKPEWDslppeeqarlnarqgvrYIGLEGLDVVDT------------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 475 lpaaTPMKPgsatfpffgvVPAilnesgeelEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKkfpGYYVTGDGCRRD 554
Cdd:PLN02479 390 ----KTMKP----------VPA---------DGKTMGEIVMRGN--MVMKGYLKNPKANEEAFAN---GWFHSGDLGVKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 555 KDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN--QKLEAELKKQV 632
Cdd:PLN02479 442 PDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALAEDIMKFC 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1036086734 633 REKIGAIATPDYIQNAPgLPKTRSGKIMRRVLRKIAcneRDLGDV 677
Cdd:PLN02479 522 RERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKA---KEMGPV 562
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
303-668 |
3.56e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 91.62 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFkMVFDYHSDDVYWCTADIGWITGHSYiTYGPLANGATSVLFEGL 382
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI-IGWEMGTCPVYLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 pTYPDVSRMWEIVDKYHVSkfyTAPTAIRLLMKyGSDPVHKYKRTSLKILgTVGEPinPEA------WQWYYNVV----- 451
Cdd:PLN03102 262 -TAPEIYKNIEMHNVTHMC---CVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP--PPAalvkkvQRLGFQVMhaygl 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 452 GEKRCPVVDTFWQTEtgghvMTPLPAATPM----KPGSATFPFFGVvpAILNESGEE---LEGPSEGYLVFKQpwpgvmR 524
Cdd:PLN03102 334 TEATGPVLFCEWQDE-----WNRLPENQQMelkaRQGVSILGLADV--DVKNKETQEsvpRDGKTMGEIVIKG------S 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 525 TVYGNHLRFETTYFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPV 603
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036086734 604 KGESLYCFVTLNDGINYNQKL-------EAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
116-666 |
8.80e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLI 195
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 196 TADgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgSLSPPAKRACPDLQQEKQKErvrkvrpppq 275
Cdd:PRK12316 3160 SQS-----------------------------------------------HLRLPLAQGVQVLDLDRGDE---------- 3182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 vpwnpevdmcwhsligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMvFDYHSDDVYWCTAD 355
Cdd:PRK12316 3183 ----------------NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTT 3245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 356 IGWiTGHSYITYGPLANGATSVLfEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDPVHKYkrTSLKILGTV 435
Cdd:PRK12316 3246 FSF-DVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE--EEDAHRC--TSLKRIVCG 3319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 436 GEPINPE------AWQWYYNVVGEKRCPVVDTFWQTETGGhvMTPLPAATPMKPGSATFPFFGVVPAILNESGEEL---E 506
Cdd:PRK12316 3320 GEALPADlqqqvfAGLPLYNLYGPTEATITVTHWQCVEEG--KDAVPIGRPIANRACYILDGSLEPVPVGALGELYlggE 3397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 507 GPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 586
Cdd:PRK12316 3398 GLARGYH----NRPGLTAE------RFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 587 EHEAVAEAAVVGrphpVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIgaiatPDYIQNA-----PGLPKTRSGKIMR 661
Cdd:PRK12316 3468 EHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflERMPLTPNGKLDR 3535
|
....*
gi 1036086734 662 RVLRK 666
Cdd:PRK12316 3536 KALPR 3540
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
291-666 |
1.35e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.86 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 291 GGASEECEPVWCdSEDPLFILYTSGSTGKPKGVlhTVSGYMLYTASTFKMVF-DYHSDDVYWCTADIGWITGHSyityGP 369
Cdd:PLN02860 159 ALGTTELDYAWA-PDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGLS----SA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 370 LAN---GATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYG----SDPVHKYKRTSLKILGTVGEPINPE 442
Cdd:PLN02860 232 LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTrksmTWKVFPSVRKILNGGGSLSSRLLPD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 443 AWQWYynvvgeKRCPVVDTFWQTETGGHvMTPLPAATPmkpgsaTFPFFGVVPAILNESGEELEGPSEGYLVFKQP---- 518
Cdd:PLN02860 308 AKKLF------PNAKLFSAYGMTEACSS-LTFMTLHDP------TLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAphve 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 519 -----------------WPGVMRTVYGNHLrfETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEV 581
Cdd:PLN02860 375 lkigldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 582 ESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDG--------INYNQKL---EAELKKQVREK-IGAIATPD-YIQNA 648
Cdd:PLN02860 453 EAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekENAKKNLtlsSETLRHHCREKnLSRFKIPKlFVQWR 532
|
410
....*....|....*...
gi 1036086734 649 PGLPKTRSGKIMRRVLRK 666
Cdd:PLN02860 533 KPFPLTTTGKIRRDEVRR 550
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
90-598 |
1.62e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.55 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVHerKLGDRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 hsivfagfsseslcerimdsqcclliTAdgfyrgdkLINLKLiADEALKKCRDKSFPvekcimlKHLTKEDE-----ASS 244
Cdd:PRK08279 114 --------------------------VA--------LLNTQQ-RGAVLAHSLNLVDA-------KHLIVGEElveafEEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 245 GSLSPPAKRACPDLQQEKQkervrkvrpppqvpwNPEVDMCWHSLIGGASEECePVWCDS---EDPLFILYTSGSTGKPK 321
Cdd:PRK08279 152 RADLARPPRLWVAGGDTLD---------------DPEGYEDLAAAAAGAPTTN-PASRSGvtaKDTAFYIYTSGTTGLPK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 322 GVLHTVSGYMLYTAStFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVL---FEglptypdVSRMWEIVDKY 398
Cdd:PRK08279 216 AAVMSHMRWLKAMGG-FGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 399 HVskfyTAPTAI----RLLMKYgsDPVHKYKRTSLKILgtVGEPINPEAWQWYYNVVGEKRcpvVDTFWqtetgghvmtp 474
Cdd:PRK08279 288 RA----TAFQYIgelcRYLLNQ--PPKPTDRDHRLRLM--IGNGLRPDIWDEFQQRFGIPR---ILEFY----------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 475 lpAATPM---------KPGSATF-PFFGVVPAIL----NESGEELEGPsEGYLVFKQPW-PGVMRTVYGNHLRFE----- 534
Cdd:PRK08279 346 --AASEGnvgfinvfnFDGTVGRvPLWLAHPYAIvkydVDTGEPVRDA-DGRCIKVKPGeVGLLIGRITDRGPFDgytdp 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 535 --------TTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDML-----NVsghllSTAEVESALVEHEAVAEAAVVG 598
Cdd:PRK08279 423 easekkilRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEVENALSGFPGVEEAVVYG 494
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
304-658 |
1.93e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 87.44 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 304 SEDPLFILYTSGSTGKPKGVL--HTVSGYMLYTASTFKMVFDYHSDDVYWCTADIGWIT---------GHSYITYGPLAN 372
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMwrQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVmfpapplmhGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 373 GATSVLFEGLPTYPDvsRMWEIVDKYHVSKFYTAPTAI-RLLMKYGSDPvHKYKRTSLKILGTVGEPINPEawqwyynvV 451
Cdd:cd05924 82 GGQTVVLPDDRFDPE--EVWRTIEKHKVTSMTIVGDAMaRPLIDALRDA-GPYDLSSLFAISSGGALLSPE--------V 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 452 GEKRCP------VVDTFWQTETGghvMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRT 525
Cdd:cd05924 151 KQGLLElvpnitLVDAFGSSETG---FTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARR--GHIPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 526 VYGNHLRFETTYFKKFPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPV 603
Cdd:cd05924 226 GYYGDEAKTAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDER 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1036086734 604 KGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGK 658
Cdd:cd05924 306 WGQEVVAVVQLREG---AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
94-666 |
3.76e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 88.30 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 94 NVHerklGDRVAFYWEGNEPgdeKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSi 172
Cdd:PRK05620 21 TVH----GDTTVTTWGGAEQ---EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 173 vfagfsseSLCERIMDSQCCLLITadgfYRGDKLInlklIADEALKKcrdksfpvEKCIMLKHltkedeassgslsppak 252
Cdd:PRK05620 93 --------PLNKQLMNDQIVHIIN----HAEDEVI----VADPRLAE--------QLGEILKE----------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 253 raCPdlqqekqkeRVRKV---------RPPPQVPWNPEVdMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGV 323
Cdd:PRK05620 132 --CP---------CVRAVvfigpsdadSAAAHMPEGIKV-YSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 324 LHT-----VSGYMLYTASTFKMVFD---------YHSddVYWCTADIGWITGhsyitygplangaTSVLFEGlptyPDVS 389
Cdd:PRK05620 200 VYShrslyLQSLSLRTTDSLAVTHGesflccvpiYHV--LSWGVPLAAFMSG-------------TPLVFPG----PDLS 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 390 --RMWEIVDKYHVSKFYTAPTA-IRLLMKYGSDPVhkyKRTSLKILGTVGEPINP---EAWQWYYNVvgekrcPVVDTFW 463
Cdd:PRK05620 261 apTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPP---ERMSLQEIYVGGSAVPPiliKAWEERYGV------DVVHVWG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 464 QTETG--GHVMTPlPAATpmkPGSATFPFF---GVVPAILN----ESGEELEGP--SEGYLVFKQPW------------- 519
Cdd:PRK05620 332 MTETSpvGTVARP-PSGV---SGEARWAYRvsqGRFPASLEyrivNDGQVMESTdrNEGEIQVRGNWvtasyyhspteeg 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNHLRFETTYFKKfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGR 599
Cdd:PRK05620 408 GGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 600 PHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK05620 487 PDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
305-665 |
3.92e-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: 86.56 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 305 EDPLFILYTSGSTGKPKGVlhTVSGY-MLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEglP 383
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGA--TLTHHnIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPS--P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 384 TYpDVSRMWEIVDKYHVSKFYTAPTA-IRLLMKygsdpvHKYKRTSLKILGT---VGEPINPEAWQWYYNVVGEKRCPVV 459
Cdd:cd05917 78 SF-DPLAVLEAIEKEKCTALHGVPTMfIAELEH------PDFDKFDLSSLRTgimAGAPCPPELMKRVIEVMNMKDVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 460 dtFWQTETG-GHVMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGP-------SEGYlvfkqpwpGVMRTVYGNHL 531
Cdd:cd05917 151 --YGMTETSpVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVgvpgelcIRGY--------SVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 532 RFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCF 611
Cdd:cd05917 221 KTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1036086734 612 VTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:cd05917 299 IRLKEG---AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
284-666 |
8.82e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.11 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 284 MCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTAST--------------FKMVFDYHSDDv 349
Cdd:PRK06018 156 VAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMAnngdalgtsaadtmLPVVPLFHANS- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 yWCTADIGWITGHSYITYGPLANGATsvLFEGLPT-----YPDVSRMWEIVDKYHVSKFYTAPT--------------AI 410
Cdd:PRK06018 235 -WGIAFSAPSMGTKLVMPGAKLDGAS--VYELLDTekvtfTAGVPTVWLMLLQYMEKEGLKLPHlkmvvcggsamprsMI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 411 RLLMKYGSDPVHKYKRTSLKILGTVGEpINPEawqwYYNVVGEKRCPVVdtfwqtetgghvmtplpaatpMKPGsatFPF 490
Cdd:PRK06018 312 KAFEDMGVEVRHAWGMTEMSPLGTLAA-LKPP----FSKLPGDARLDVL---------------------QKQG---YPP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 491 FGVVPAILNESGEEL--EGPSEGYLVFKQPwpgvmrTVYGNHLRFETTYFKKfPGYYVTGDGCRRDKDGYYWITGRIDDM 568
Cdd:PRK06018 363 FGVEMKITDDAGKELpwDGKTFGRLKVRGP------AVAAAYYRVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDV 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQkleAELKKQVREKIGAIATPDYIQNA 648
Cdd:PRK06018 436 IKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR---EEILKYMDGKIAKWWMPDDVAFV 512
|
410
....*....|....*...
gi 1036086734 649 PGLPKTRSGKIMRRVLRK 666
Cdd:PRK06018 513 DAIPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
115-672 |
1.12e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:PRK12316 2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkeDEASSGSLSPPAKRACPDLqqekqkERVRKVRPPP 274
Cdd:PRK12316 2105 LT-------------------------------------------QRHLLERLPLPAGVARLPL------DRDAEWADYP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVpwNPEVDMcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGV--------LHTVSGYMLYTASTFKMVFDYHS 346
Cdd:PRK12316 2136 DT--APAVQL------------------AGENLAYVIYTSGSTGLPKGVavshgalvAHCQAAGERYELSPADCELQFMS 2195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 347 ---DDVYWctadiGWITghsyitygPLANGATSVLFEGlpTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSdpvHK 423
Cdd:PRK12316 2196 fsfDGAHE-----QWFH--------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE---RD 2257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 424 YKRTSLKILGTVGEPINPEAWQWYYNVVGEKRcpVVDTFWQTETgghVMTPLP-AATPMKPGSATFPFFG---------V 493
Cdd:PRK12316 2258 GRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGralgnrrayI 2332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 494 VPAILN----ESGEEL----EGPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGR 564
Cdd:PRK12316 2333 LDADLNllapGMAGELylggEGLARGYL----NRPGLTAE------RFVPDPFSASGErLYRTGDLARYRADGVVEYLGR 2402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 565 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPvKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDY 644
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAH 2478
|
570 580
....*....|....*....|....*...
gi 1036086734 645 IQNAPGLPKTRSGKIMRRVLRKIACNER 672
Cdd:PRK12316 2479 WVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
90-665 |
2.56e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 86.24 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 90 VLDRNVHERKLGDRVAFYwegnEPgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY----AA---DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 170 HSIVFAGFSSESLCERIMDSQCCLLITADGFyrgdklinlkliadealkkcRDKSFPvekcimlkhltkEDEASSGSLSP 249
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDAL--------------------RDRFQP------------SRVAEAAELMS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 250 PAKRACPdlqqekqkervrkvrpppqvpwnpevdmcwhsliggasEECEPVWCDSEdpLFILYTSGSTGKPKGVLHTvsg 329
Cdd:PRK06060 130 EAARVAP--------------------------------------GGYEPMGGDAL--AYATYTSGTTGPPKAAIHR--- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 330 ymlyTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYG-------PLANGATSVLfEGLPTYPDVSRMweIVDKYHVSK 402
Cdd:PRK06060 167 ----HADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAI--LSARFGPSV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 403 FYTAPTAI-RLLMKYGSDPVHkykrtSLKILGTVGEPINPEAWQWYYNVVGEkrCPVVD---------TF-------WQT 465
Cdd:PRK06060 240 LYGVPNFFaRVIDSCSPDSFR-----SLRCVVSAGEALELGLAERLMEFFGG--IPILDgigstevgqTFvsnrvdeWRL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 466 ETGGHVMTPLPAATPMKPGSATFPffGVvpailnESGEELEGPS--EGYLvfkqPWPGVMRTVygnhlrfettyfkkfPG 543
Cdd:PRK06060 313 GTLGRVLPPYEIRVVAPDGTTAGP--GV------EGDLWVRGPAiaKGYW----NRPDSPVAN---------------EG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 544 YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQK 623
Cdd:PRK06060 366 WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGS 445
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1036086734 624 LEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK06060 446 VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
114-664 |
2.62e-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: 85.00 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEkTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:cd17652 9 GDE-TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITadgfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrpp 273
Cdd:cd17652 88 LLT----------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqvpwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVYWCT 353
Cdd:cd17652 91 -----------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQF 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 354 ADIGWITGHSYITYGPLAnGATSVLfegLPTYPDVS--RMWEIVDKYHVSkFYTAPTAIRLLMKYGSDPvhkykrtSLKI 431
Cdd:cd17652 141 ASPSFDASVWELLMALLA-GATLVL---APAEELLPgePLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRT 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 432 LGTVGEPINPE-AWQW-----YYNVVGEKRCPVVDTFWQTETGGhvmTPLPAATPMkPGSATF---------PFfGVVpa 496
Cdd:cd17652 209 LVVAGEACPAElVDRWapgrrMINAYGPTETTVCATMAGPLPGG---GVPPIGRPV-PGTRVYvldarlrpvPP-GVP-- 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 497 ilnesGE-ELEGPS--EGYLvfkqPWPGVMRTvygnhlRFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNV 571
Cdd:cd17652 282 -----GElYIAGAGlaRGYL----NRPGLTAE------RFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKI 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 572 SGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGL 651
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMVPAAFVVLDAL 422
|
570
....*....|...
gi 1036086734 652 PKTRSGKIMRRVL 664
Cdd:cd17652 423 PLTPNGKLDRRAL 435
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
543-668 |
3.90e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.00 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInynQ 622
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA---S 492
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1036086734 623 KLEAELKKQVREKIGAIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 668
Cdd:PRK08162 493 ATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQA 537
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
116-668 |
4.23e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 85.04 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsIVFAGFS---SEsLCERIMDSQCC 192
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFShqrSE-LNAYASQIEPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 193 LLItAD---GFYRGDKLINlKLIADealkkcrdksfpvekCIMLKHLTKEDEASSGSLSppakracpDLQQEKQKERVRK 269
Cdd:PRK10946 123 LLI-ADrqhALFSDDDFLN-TLVAE---------------HSSLRVVLLLNDDGEHSLD--------DAINHPAEDFTAT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 270 VRPPPQVPwnpevdmcwhsliggaseecepvwcdsedplFILYTSGSTGKPKGVLHTVSGYmLYTASTFKMVFDYHSDDV 349
Cdd:PRK10946 178 PSPADEVA-------------------------------FFQLSGGSTGTPKLIPRTHNDY-YYSVRRSVEICGFTPQTR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTADigwiTGHSYITYGPlanGATSVLFEG----LPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPVHKYK 425
Cdd:PRK10946 226 YLCALP----AAHNYPMSSP---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTE----------TGGHVMTPlpAATPMKPGSATFpffgvvp 495
Cdd:PRK10946 299 LASLKLLQVGGARLSETLARRIPAELG---CQLQQVFGMAEglvnytrlddSDERIFTT--QGRPMSPDDEVW------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 496 aILNESGEELEGPSEGYLVFKQPWP--GVMRTVYGNHLRFETTyfkkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSG 573
Cdd:PRK10946 367 -VADADGNPLPQGEVGRLMTRGPYTfrGYYKSPQHNASAFDAN------GFYCSGDLVSIDPDGYITVVGREKDQINRGG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 574 HLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklEAELKKQVREK-IGAIATPDYIQNAPGLP 652
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK-----AVQLRRFLREQgIAEFKLPDRVECVDSLP 514
|
570
....*....|....*.
gi 1036086734 653 KTRSGKIMRRVLRKIA 668
Cdd:PRK10946 515 LTAVGKVDKKQLRQWL 530
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
286-672 |
5.45e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 84.89 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 286 WHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHT-------VSGYMLYTASTFKMVfdyHSDDVYWCTADIGW 358
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLThrnliamVELFVRFEASQYEYP---GSDNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 359 ITGHSYITYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKyGSDPVHKYKRTSLKILGTVGEP 438
Cdd:PLN02574 256 IYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAP 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 439 INPEAWQWYYNVVgekrcPVVDtFWQtetgGHVMTPLPAATPMKPGSATFPFFGVV----PAILN-----ESGEELEGPS 509
Cdd:PLN02574 331 LSGKFIQDFVQTL-----PHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSSVgllaPNMQAkvvdwSTGCLLPPGN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 510 EGYLvfkqpW---PGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALV 586
Cdd:PLN02574 401 CGEL-----WiqgPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 587 EHEAVAEAAVVGRPHPVKGESLYCFVTLNDG--------INYNQKLEAELKKqVREKIgaiatpdYIQNapgLPKTRSGK 658
Cdd:PLN02574 474 SHPEIIDAAVTAVPDKECGEIPVAFVVRRQGstlsqeavINYVAKQVAPYKK-VRKVV-------FVQS---IPKSPAGK 542
|
410
....*....|....
gi 1036086734 659 IMRRVLRKIACNER 672
Cdd:PLN02574 543 ILRRELKRSLTNSV 556
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
118-666 |
7.12e-17 |
|
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: 83.51 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 118 TVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLcERIMD-SQCCLLIT 196
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRtSGATLLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADGfyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracPDlqqekqkervrkvrpppqv 276
Cdd:cd17653 101 TDS--------------------------------------------------------PD------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 pwnpevdmcwhsliggaseecepvwcdseDPLFILYTSGSTGKPKGVLHT---VSGYMLYT------------ASTFKMV 341
Cdd:cd17653 106 -----------------------------DLAYIIFTSGSTGIPKGVMVPhrgVLNYVSQPparldvgpgsrvAQVLSIA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 342 FDYhsddvywCTADIgwitghsyitYGPLANGATSVLFEGLPTYPDVSRmweivdkyHVSKFYTAPTAIRLLmkygsdPV 421
Cdd:cd17653 157 FDA-------CIGEI----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL------SP 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 422 HKYKrtSLKILGTVGEPINP---EAW---QWYYNVVGEKRCPVVDTFWQTETGghvmTPLPAATPMkPGSATFpffgvvp 495
Cdd:cd17653 206 QDFP--NLKTIFLGGEAVPPsllDRWspgRRLYNAYGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY------- 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 496 aILNESGEELEGPSEG--YLVfkqpWPGVMRTVYGNHLRfETTYFKKFPGY-----YVTGDGCRRDKDGYYWITGRIDDM 568
Cdd:cd17653 272 -ILDADLQPVPEGVVGeiCIS----GVQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGREDNQ 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 569 LNVSGHLLSTAEVES-ALVEHEAVAEAAVVgrphpVKGESLYCFVTlNDGINynqklEAELKKQVREKIGAIATPDYIQN 647
Cdd:cd17653 346 VKVRGFRINLEEIEEvVLQSQPEVTQAAAI-----VVNGRLVAFVT-PETVD-----VDGLRSELAKHLPSYAVPDRIIA 414
|
570
....*....|....*....
gi 1036086734 648 APGLPKTRSGKIMRRVLRK 666
Cdd:cd17653 415 LDSFPLTANGKVDRKALRE 433
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
117-666 |
7.37e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 84.26 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLIT 196
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADGFYrgDKLINLKliADEALK-KCRDKsfPVEKCIMLKHLTKEDEASsgslsppakracpdlqqekqkervrkvrpPPQ 275
Cdd:PLN02246 129 QSCYV--DKLKGLA--EDDGVTvVTIDD--PPEGCLHFSELTQADENE-----------------------------LPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 VPWNPEvdmcwhsliggaseecepvwcdseDPLFILYTSGSTGKPKGVLHTVSGymLYTaSTFKMV------FDYHSDDV 349
Cdd:PLN02246 174 VEISPD------------------------DVVALPYSSGTTGLPKGVMLTHKG--LVT-SVAQQVdgenpnLYFHSDDV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 350 YWCTADIGWITGHSYITYGPLANGATSVLfegLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDPVHKYKRTSL 429
Cdd:PLN02246 227 ILCVLPMFHIYSLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVTIAPFVPPIVLAIAK--SPVVEKYDLSSI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 430 KILGTVGEPINPEawqwyynvvgekrcpVVDTFW----QTETG-GHVMT---PLPA--------ATPMKPGSAtfpffGV 493
Cdd:PLN02246 301 RMVLSGAAPLGKE---------------LEDAFRaklpNAVLGqGYGMTeagPVLAmclafakePFPVKSGSC-----GT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 494 VpaILN--------ESGEELEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRI 565
Cdd:PLN02246 361 V--VRNaelkivdpETGASLPRNQPGEICIRGP--QIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 566 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELK----KQV--REKIGAI 639
Cdd:PLN02246 435 KELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKV 511
|
570 580
....*....|....*....|....*..
gi 1036086734 640 ATPDYIqnapglPKTRSGKIMRRVLRK 666
Cdd:PLN02246 512 FFVDSI------PKAPSGKILRKDLRA 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
116-664 |
1.06e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLI 195
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 196 TAdgfyrgdklinlkliadealkkcrdksfpvekcimlKHLTKEdeassgsLSPPAKRACPDLQQEKQkervrkvrpppq 275
Cdd:PRK12467 1677 TQ------------------------------------SHLQAR-------LPLPDGLRSLVLDQEDD------------ 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 vpwnpevdmcWHSligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVL---HTVSGYMLYTASTFKMvfdyhsddvywc 352
Cdd:PRK12467 1702 ----------WLE---GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGnrhGALVNRLCATQEAYQL------------ 1756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 TADIGWITGHSYI-------TYGPLANGAtSVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMkygSDPVHKYK 425
Cdd:PRK12467 1757 SAADVVLQFTSFAfdvsvweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLL---QMDEQVEH 1832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 RTSLKILGTVGEPINPEAWQ-WY--------YNVVGEKRCPVVDTFWQTETG---GHVMTPLpaATPMKPGSATFPFFGV 493
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRpWLerlpdtglFNLYGPTETAVDVTHWTCRRKdleGRDSVPI--GQPIANLSTYILDASL 1910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 494 VPAILNESGEEL---EGPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKFPG-YYVTGDGCRRDKDGYYWITGRIDDML 569
Cdd:PRK12467 1911 NPVPIGVAGELYlggVGLARGYL----NRPALTAE------RFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 570 NVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPvKGESLYCFVT-----LNDGINYNQKLEAELKKQVREKIgaiatPDY 644
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEY 2054
|
570 580
....*....|....*....|....*
gi 1036086734 645 IQNA-----PGLPKTRSGKIMRRVL 664
Cdd:PRK12467 2055 MVPAhlvflARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
305-664 |
1.06e-16 |
|
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: 83.25 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 305 EDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWcTADIGWITGHSYItYGPLANGATSVLFEGLpT 384
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQ-FASIAFDVAAEEI-YVTLLSGATLVLRPEE-M 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 385 YPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGS----DPVHkykrtSLKILGTVGEPINPEAW-QW---------YYNV 450
Cdd:cd17644 183 RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLlstiDLPS-----SLRLVIVGGEAVQPELVrQWqknvgnfiqLINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 451 VGEKRCPVVDTFWQ-TETGGHVMTPLPAATPMkPGSATF---PFFGVVPaiLNESGEEL---EGPSEGYLvfkqPWPGVM 523
Cdd:cd17644 258 YGPTEATIAATVCRlTQLTERNITSVPIGRPI-ANTQVYildENLQPVP--VGVPGELHiggVGLARGYL----NRPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 524 RTVYGNHlRFETTYFKKFpgyYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPV 603
Cdd:cd17644 331 AEKFISH-PFNSSESERL---YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036086734 604 KGESLYCFVTlndGINYNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd17644 407 GNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
30-90 |
1.69e-16 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 73.66 E-value: 1.69e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036086734 30 YKELYIKSVESPEEFWADVAKDFFWKTKYTgKFLDYNFDvtkgeIYIKCMEGATTNICYNV 90
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFD-KVLDGSNG-----PFAKWFVGGKLNVCYNC 55
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
272-665 |
2.06e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 82.35 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 272 PPPQVPWNPEVDMCWHSliGGASEECEPvwcDSEDPLFILYTSGSTGKPKGVLhtVSGYMLytASTFkmvfDYHSDDVYW 351
Cdd:PRK07787 100 APDDPAGLPHVPVRLHA--RSWHRYPEP---DPDAPALIVYTSGTTGPPKGVV--LSRRAI--AADL----DALAEAWQW 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 CTADI-----------GWITGhsyiTYGPLANGATSV-------------------LFEGLPTypdvsrMWEIV--DKYH 399
Cdd:PRK07787 167 TADDVlvhglplfhvhGLVLG----VLGPLRIGNRFVhtgrptpeayaqalseggtLYFGVPT------VWSRIaaDPEA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 400 VSKFYTAptaiRLLMKyGSD--PVHKYKRtslkILGTVGEPinpeawqwyynvvgekrcpVVDTFWQTETgghVMT-PLP 476
Cdd:PRK07787 237 ARALRGA----RLLVS-GSAalPVPVFDR----LAALTGHR-------------------PVERYGMTET---LITlSTR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 AATPMKPGSATFPFFGVVPAILNESGEEL--EGPSEGYLVFKQPwpgvmrTVYGNHL-RFETTYFKKFP-GYYVTGDGCR 552
Cdd:PRK07787 286 ADGERRPGWVGLPLAGVETRLVDEDGGPVphDGETVGELQVRGP------TLFDGYLnRPDATAAAFTAdGWFRTGDVAV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 553 RDKDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklEAELKKQ 631
Cdd:PRK07787 360 VDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-----ADELIDF 434
|
410 420 430
....*....|....*....|....*....|....
gi 1036086734 632 VREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK07787 435 VAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
310-661 |
9.12e-16 |
|
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: 79.08 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 310 ILYTSGSTGKPKGVL--HTVSgymLYTASTFKMVFDYHSDDVYWCTADIgwitghsYITYGPLAnGATSVLFEGLPTYP- 386
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQT---LRAAAAWADCADLTEDDRYLIINPF-------FHTFGYKA-GIVACLLTGATVVPv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 387 ---DVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDPvhKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKRcpVVDTFW 463
Cdd:cd17638 74 avfDVDAILEAIERERITVLPGPPTLFQSLLDHPGRK--KFDLSSLRAAVTGAATVPVELVRRMRSELGFET--VLTAYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 464 QTETGGHVMT-PLPAATPMKPGSATfPFFGVVPAILNESGEELEGPS--EGYLvfKQPwPGVMRTVYGNhlrfettyfkk 540
Cdd:cd17638 150 LTEAGVATMCrPGDDAETVATTCGR-ACPGFEVRIADDGEVLVRGYNvmQGYL--DDP-EATAEAIDAD----------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 541 fpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINY 620
Cdd:cd17638 215 --GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1036086734 621 NqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMR 661
Cdd:cd17638 293 T---EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
272-665 |
1.43e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.14 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 272 PPPQVPWnpevdMCWHSLIGGASEECEpvWcdsedPLF-------ILYTSGSTGKPKGVLHTVSGYMLYT-ASTFKMVFD 343
Cdd:PRK07008 148 PAGSTPL-----LCYETLVGAQDGDYD--W-----PRFdenqassLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 344 YHSDDVY-----------WCTADIGWITGHSYITYGPLANGAtSV--LFE--------GLPTypdvsrMWEIVDKYHVS- 401
Cdd:PRK07008 216 LSARDAVlpvvpmfhvnaWGLPYSAPLTGAKLVLPGPDLDGK-SLyeLIEaervtfsaGVPT------VWLGLLNHMREa 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 402 --KFYT-----------APTAIRLLMK-YGSDPVHKYKRTSLKILGTVgepinpeawqwyynvvgekrCpvvdtfwqTET 467
Cdd:PRK07008 289 glRFSTlrrtviggsacPPAMIRTFEDeYGVEVIHAWGMTEMSPLGTL--------------------C--------KLK 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 468 GGHVMTPLPA--ATPMKPGSAtfpFFGVVPAILNESGEEL--EGPSEGYLVFKQPWpgVMRTvygnhlrfettYFKK--- 540
Cdd:PRK07008 341 WKHSQLPLDEqrKLLEKQGRV---IYGVDMKIVGDDGRELpwDGKAFGDLQVRGPW--VIDR-----------YFRGdas 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 541 --FPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGI 618
Cdd:PRK07008 405 plVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1036086734 619 NYNQKleaELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK07008 485 EVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-666 |
2.66e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.59 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITadgfyrgdklinlkliaDEALkkcrdksfpvekcimLKHLTKEDEASSGSLSPPAKRACpdlqqekqkervrkvrppp 274
Cdd:PRK12467 614 LT-----------------QSHL---------------LAQLPVPAGLRSLCLDEPADLLC------------------- 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qvpwnpevdmcwhsligGASEECEPVWCDSEDPLFILYTSGSTGKPKGVL--H-TVSGYMLYTASTFKMVfdyhSDDVYW 351
Cdd:PRK12467 643 -----------------GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAisHgALANYVCVIAERLQLA----ADDSML 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 CTADIGWITGHSYItYGPLANGATsVLFEGLPTYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYG-SDPVHKYKRTslk 430
Cdd:PRK12467 702 MVSTFAFDLGVTEL-FGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASrVALPRPQRAL--- 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 431 ILGtvGEPINPEAW-QWY--------YNVVGEKRCPVVDTFWQTETGGHVMTPLPAATPMkPGSATF-------PFFGVV 494
Cdd:PRK12467 777 VCG--GEALQVDLLaRVRalgpgarlINHYGPTETTVGVSTYELSDEERDFGNVPIGQPL-ANLGLYildhylnPVPVGV 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 495 PAILNESGEeleGPSEGYLvfkqPWPGVMRTvygnhlRFETTYFKKfPG--YYVTGDGCRRDKDGYYWITGRIDDMLNVS 572
Cdd:PRK12467 854 VGELYIGGA---GLARGYH----RRPALTAE------RFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIR 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 573 GHLLSTAEVESALVEHEAVAEAAVVGRPHpVKGESL--YCFVTLNDGINYNQKLEAELKKQVREKIGAIATPDYIQNAPG 650
Cdd:PRK12467 920 GFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLvaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDS 998
|
570
....*....|....*.
gi 1036086734 651 LPKTRSGKIMRRVLRK 666
Cdd:PRK12467 999 LPLTPNGKLDRKALPK 1014
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
306-657 |
4.08e-15 |
|
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: 76.96 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 306 DPLFILYTSGSTGKPKGVLHTVSGYMlytastfkmvfdYHSddvyWCTADIGWITGHS-YITYGPLANGATsvLFEGLPT 384
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALL------------AQA----LVLAVLQAIDEGTvFLNSGPLFHIGT--LMFTLAT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 385 Y-----------PDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDpvHKYKRTSLKILgtvgepinPEAWQWYYNVvge 453
Cdd:cd17636 63 FhaggtnvfvrrVDAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSS--------PAAPEWNDMA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 454 krcPVVDTFW--------QTETGGhvMTPLPAATPMKPGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWpgVMRT 525
Cdd:cd17636 130 ---TVDTSPWgrkpggygQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT--VMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 526 VYGnhlRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKG 605
Cdd:cd17636 203 YWN---RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWA 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1036086734 606 ESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSG 657
Cdd:cd17636 280 QSVKAIVVLKPG---ASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
303-666 |
5.26e-15 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 78.24 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTVSG-YMLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEg 381
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYSHRAlVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 382 lptYPDVSRMWEIVDKYHVSKFYTAPTAIRLLMKyGSDPVHKYKRTSLKILGTVGEPinPEAWQ-----WYYNVVGEKRC 456
Cdd:cd05915 230 ---RLDPASLVELFDGEGVTFTAGVPTVWLALAD-YLESTGHRLKTLRRLVVGGSAA--PRSLIarferMGVEVRQGYGL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 457 PVV-----DTFWQTEtgghvMTPLPAATPMK-PGSATFPFFGVVPAILNESGEELEGPSEGYLVFKQPWPGVMRTVYGNH 530
Cdd:cd05915 304 TETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 531 LRFETTYFKKfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYC 610
Cdd:cd05915 379 EATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 611 FVTLNDGinynQKLEAELKKQVREKIGAIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05915 457 VVVPRGE----KPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
303-668 |
8.23e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 78.43 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLhtVSGY-MLYTASTFKMVFDYHSDDVywctadigwITG-----HSY----ITYGPLAN 372
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVM--LSHHnILSNIEQISDVFNLRNDDV---------ILSslpffHSFgltvTLWLPLLE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 373 GATSVlFEGLPTypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygSDPVHKYKRTSLKILGTVGEPINPEawqwyynvvg 452
Cdd:PRK08633 849 GIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPE---------- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 453 ekrcpVVDTFWQ------------TETGGHVMTPLPAA--------TPMKPGSATFPFFGVVPAILN-ESGEELEGPSEG 511
Cdd:PRK08633 914 -----VADAFEEkfgirilegygaTETSPVASVNLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 512 YLVFKQPwpGVMRTVYGN-HLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALveHEA 590
Cdd:PRK08633 989 LILIGGP--QVMKGYLGDpEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKA 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 591 VAEA----AVVGRPHPVKGESLYCFVTLNDGInynqklEAELKKQVRE-KIGAIATPDYIQNAPGLPKTRSGKIMRRVLR 665
Cdd:PRK08633 1065 LGGEevvfAVTAVPDEKKGEKLVVLHTCGAED------VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLK 1138
|
...
gi 1036086734 666 KIA 668
Cdd:PRK08633 1139 ELA 1141
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
272-630 |
1.02e-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: 77.51 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 272 PPPQVPWNpevDMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYMlYTASTFKMVFDYHSDDVYW 351
Cdd:cd05932 107 PPPSAANC---QYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRML 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 CTADIGWITGHSYITYGPLANGATSVLFEGLPTYPD------------VSRMW-----EIVDKYHVSK--------FYTA 406
Cdd:cd05932 183 SYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWtkfqqGVQDKIPQQKlnlllkipVVNS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 407 PTAIRLLMKYGSDPVhkykrtslKILGTVGEPINPEAWQWYYNVvgekRCPVVDTFWQTETGGHVMTPLPAATpmKPGSA 486
Cdd:cd05932 263 LVKRKVLKGLGLDQC--------RLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 487 TFPFFGVvpailnesgeELEGPSEGYLVFKQPwpGVMRTVYGNhlrfETTYFKKFP--GYYVTGDGCRRDKDGYYWITGR 564
Cdd:cd05932 329 GNAGPGV----------EVRISEDGEILVRSP--ALMMGYYKD----PEATAEAFTadGFLRTGDKGELDADGNLTITGR 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 565 IDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGR--PHPVKGESLYCFVTLNDGINYNQKLEAELKK 630
Cdd:cd05932 393 VKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRADAFARAELEASLRA 461
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
303-670 |
1.77e-14 |
|
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: 76.43 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVL---HTVSGYMLYTASTFKM-----VFDY--HSDDVywCTADIgwitghsyitYGPLAN 372
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 373 GAT------SVLFEGLPTYpdVSRM---WEIVdkyhvskfytAPTAIRLLmkygsDPVhkyKRTSLKILGTVGEPINP-- 441
Cdd:cd05918 172 GGClcipseEDRLNDLAGF--INRLrvtWAFL----------TPSVARLL-----DPE---DVPSLRTLVLGGEALTQsd 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 442 -EAWQwyynvvgeKRCPVVDTFWQTETggHVMT----PLPAATPMKPGSAtfpfFGVVPAILNESGEE------------ 504
Cdd:cd05918 232 vDTWA--------DRVRLINAYGPAEC--TIAAtvspVVPSTDPRNIGRP----LGATCWVVDPDNHDrlvpigavgell 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 505 LEGP--SEGYL--------VFKQPWPGVMRTVYGNHLRFettyfkkfpgyYVTGDGCRRDKDG--YYwiTGRIDDMLNVS 572
Cdd:cd05918 298 IEGPilARGYLndpektaaAFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQVKIR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 573 GHLLSTAEVESALVEHEAVAEAAVVG--RPHPVKGES-LYCFVTLND---GINYNQKLEAELKKQVREKIGAIAT----- 641
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEvvKPKDGSSSPqLVAFVVLDGsssGSGDGDSLFLEPSDEFRALVAELRSklrqr 444
|
410 420 430
....*....|....*....|....*....|....*
gi 1036086734 642 -PDY-IQNA----PGLPKTRSGKIMRRVLRKIACN 670
Cdd:cd05918 445 lPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
303-661 |
1.45e-13 |
|
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: 73.63 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFdYHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGL 382
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 PT-------------YPDVSRMWEIVDKYHVSKFYTAPTAI---RLLMKYGSDPVHKYKRTSL--------KILGTVGEP 438
Cdd:cd05914 166 PSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVheafggniKEFVIGGAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 439 INPEAWQWYYNVvgekRCPVVDTFWQTETGghvmtPLPAATP---MKPGSATFPFFGVVPAILNESGEelegPSEGYLVF 515
Cdd:cd05914 246 INPDVEEFLRTI----GFPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRIDSPDPA----TGEGEIIV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 516 KQpwPGVMRTVYGNHlrfETTYFKKFP-GYYVTGDGCRRDKDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHEAVAE 593
Cdd:cd05914 313 RG--PNVMKGYYKNP---EATAEAFDKdGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLE 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036086734 594 AAVVGRPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIGAiATPDY-------IQNAPgLPKTRSGKIMR 661
Cdd:cd05914 388 SLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVNQ-KVPNYkkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
102-666 |
1.72e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.47 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYwegnEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivFAGFSSES 181
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 LCERIMD----SQCCLLITADGFYrgdklinlkliadealKKCRDKSFPVekcIMLKHLTKEDEASSGSLSPPAKRACPD 257
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV---IVLGEEKIEGAVNWKELLEAADRAGDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKQKErvrkvrpppqvpwnpeVDMCwhsliggaseecepvwcdsedplFILYTSGSTGKPKGVLHTVSGYMLYTAST 337
Cdd:PLN02330 176 SDNEEILQ----------------TDLC-----------------------ALPFSSGTTGISKGVMLTHRNLVANLCSS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 338 fkmVFDYHSDDvywctadIGWITGHSYITYGPLAnGATSVLFEGLPTYPDVSrmweIVDKYHVSKFYTA----------- 406
Cdd:PLN02330 217 ---LFSVGPEM-------IGQVVTLGLIPFFHIY-GITGICCATLRNKGKVV----VMSRFELRTFLNAlitqevsfapi 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 407 -PTAIRLLMKygsDP-VHKYKRTSLKI--LGTVGEPINPEAWQWYynvvgEKRCP---VVDTFWQTETGGHVMT---PLP 476
Cdd:PLN02330 282 vPPIILNLVK---NPiVEEFDLSKLKLqaIMTAAAPLAPELLTAF-----EAKFPgvqVQEAYGLTEHSCITLThgdPEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 477 AATPMKPGSATFPFFGV-VPAILNESGEELEGPSEGYLVFKQPWpgVMRTVYGNhlRFETTYFKKFPGYYVTGDGCRRDK 555
Cdd:PLN02330 354 GHGIAKKNSVGFILPNLeVKFIDPDTGRSLPKNTPGELCVRSQC--VMQGYYNN--KEETDRTIDEDGWLHTGDIGYIDD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 556 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLN--------DGINYNQKLEAE 627
Cdd:PLN02330 430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINpkakeseeDILNFVAANVAH 509
|
570 580 590
....*....|....*....|....*....|....*....
gi 1036086734 628 LKKqVRekigaiatpdYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PLN02330 510 YKK-VR----------VVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
120-671 |
2.61e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.92 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLcERIMD-SQCCLLITAD 198
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSEL-EYALNqSGCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 GFYRGDKLINLKLIADEaLKKC-----RDKSFPVEKCIMlkHLtkEDEASSGSLSPPAKRAcpdLQQEKQKERVRKVRPp 273
Cdd:PRK08315 124 GFKDSDYVAMLYELAPE-LATCepgqlQSARLPELRRVI--FL--GDEKHPGMLNFDELLA---LGRAVDDAELAARQA- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 pqvpwnpevdmcwhSLiggaseecepvwcDSEDPLFILYTSGSTGKPKGVlhTVS-------GY-----MLYTAStfkmv 341
Cdd:PRK08315 195 --------------TL-------------DPDDPINIQYTSGTTGFPKGA--TLThrnilnnGYfigeaMKLTEE----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 342 fD--------YHsddvywCtadIGWITGhsyiTYGPLANGATSVL----FE-----------------GLPT-------Y 385
Cdd:PRK08315 241 -DrlcipvplYH------C---FGMVLG----NLACVTHGATMVYpgegFDplatlaaveeerctalyGVPTmfiaeldH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 386 PDVSR--------------------MWEIVDKYH---VSKFY----TAP----TAIrllmkygSDPVHKykRTSlkilgT 434
Cdd:PRK08315 307 PDFARfdlsslrtgimagspcpievMKRVIDKMHmseVTIAYgmteTSPvstqTRT-------DDPLEK--RVT-----T 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 435 VGEpINPEAwqwyynvvgEKRcpVVDTfwqtETGGhvmtplpaatpmkpgsatfpffgVVPaiLNESGEELegpSEGYLV 514
Cdd:PRK08315 373 VGR-ALPHL---------EVK--IVDP----ETGE-----------------------TVP--RGEQGELC---TRGYSV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 515 FKqpwpgvmrtvygnhlrfettyfkkfpGYYV----------------TGDGCRRDKDGYYWITGRIDDMLNVSGHLLST 578
Cdd:PRK08315 409 MK--------------------------GYWNdpektaeaidadgwmhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYP 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNqklEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGK 658
Cdd:PRK08315 463 REIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLT---EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
650
....*....|...
gi 1036086734 659 IMRRVLRKIACNE 671
Cdd:PRK08315 540 IQKFKMREMMIEE 552
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
102-664 |
6.07e-13 |
|
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: 71.74 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEgnepgdEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivfagfsses 181
Cdd:cd17656 3 DAVAVVFE------NQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGA------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 lcerimdsqcCLLItadgfyrgdklinlkliadealkkcrDKSFPVEKCIMLKHltkedeaSSGSLSPPAKRACPD-LQQ 260
Cdd:cd17656 65 ----------FVPI--------------------------DPEYPEERRIYIML-------DSGVRVVLTQRHLKSkLSF 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 261 EKQkervrkvrpppqvpwnpEVDMCWHSLIGGASEECEPVWcDSEDPLFILYTSGSTGKPKGV----------LHTVSGY 330
Cdd:cd17656 102 NKS-----------------TILLEDPSISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKGVqlehknmvnlLHFEREK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 331 MLYTASTFKMVFDYHSDDVywCTADIgwitghsyitYGPLANGATSVLFEGlPTYPDVSRMWEIVDKYHVSKFYTAPTAI 410
Cdd:cd17656 164 TNINFSDKVLQFATCSFDV--CYQEI----------FSTLLSGGTLYIIRE-ETKRDVEQLFDLVKRHNIEVVFLPVAFL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 411 RLLM-KYGSDPVHKykrTSLKILGTVGEPInpEAWQWYYNVVGEKRCPVVDTFWQTETggHVMT--------PLPAATPM 481
Cdd:cd17656 231 KFIFsEREFINRFP---TCVKHIITAGEQL--VITNEFKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPI 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 482 -KPGSATFPFfgvvpaILNESGeelegpsegylvfkQPWP-GVMRTVY--------GNHLRFETTYFKKFPG-------Y 544
Cdd:cd17656 304 gKPISNTWIY------ILDQEQ--------------QLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerM 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 545 YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQkl 624
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-- 441
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1036086734 625 eaeLKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd17656 442 ---LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
120-666 |
6.40e-13 |
|
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: 71.69 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLITadg 199
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 fyrgDKLINLKLIADEALKKCRDKSFpvekcimlkhltkedeassgslsppakracpdlqqekqkervrkvrpppqvpwn 279
Cdd:cd05939 82 ----NLLDPLLTQSSTEPPSQDDVNF------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 280 pevdmcwhsliggaseecepvwcdsEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMvFDYHSDDVYWCTADI--- 356
Cdd:cd05939 104 -------------------------RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYA-FGMRPEDVVYDCLPLyhs 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 357 -GWITGHSYItygpLANGATSVLFEGLptypDVSRMWEIVDKYHVskfyTAPTAIRLLMKY--GSDPVHKYKRTSLKILg 433
Cdd:cd05939 158 aGGIMGVGQA----LLHGSTVVIRKKF----SASNFWDDCVKYNC----TIVQYIGEICRYllAQPPSEEEQKHNVRLA- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 434 tVGEPINPEAWQwyyNVVGEKRCPVVDTFW-QTETGGHVMTplpaaTPMKPGSATFpffgvVPAIL-----------NES 501
Cdd:cd05939 225 -VGNGLRPQIWE---QFVRRFGIPQIGEFYgATEGNSSLVN-----IDNHVGACGF-----NSRILpsvypirlikvDED 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 502 GEELEGPSEGYLVFKQPW-PGVM--RTVYGNHLRFETTY--------------FKKFPGYYVTGDGCRRDKDGYYWITGR 564
Cdd:cd05939 291 TGELIRDSDGLCIPCQPGePGLLvgKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDR 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 565 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHP-VKGES-LYCFVTLNDGINYNqKLEAELKKqvreKIGAIATP 642
Cdd:cd05939 371 TGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAgMAAIVDPERKVDLD-RFSAVLAK----SLPPYARP 445
|
570 580
....*....|....*....|....
gi 1036086734 643 DYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05939 446 QFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
98-666 |
1.37e-12 |
|
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: 70.73 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 98 RKLGDRVAFYWEGNEPGDEKTVTYRELLQQVCKFANVLKSQGvKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGF 177
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 178 SSESLcERIMDsqccllITADgfyRGDKLInlkliadealkkcrdksfpvekcimlkhltkedeassgslsppakracpd 257
Cdd:cd05931 83 PGRHA-ERLAA------ILAD---AGPRVV-------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKQKERVRKV---RPPPQVPWNPEVDmcwhSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLhtVS-GYMLY 333
Cdd:cd05931 103 LTTAAALAAVRAFaasRPAAGTPRLLVVD----LLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV--VThRNLLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 334 TASTFKMVFDYHSDD--VYW--CTADIGWITGhsyITyGPLANGATSVLFEglPTY----PdvsRMW-EIVDKYHVSkFY 404
Cdd:cd05931 177 NVRQIRRAYGLDPGDvvVSWlpLYHDMGLIGG---LL-TPLYSGGPSVLMS--PAAflrrP---LRWlRLISRYRAT-IS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 405 TAPT-AIRLLMKYGSDPvhkyKRT-----SLKILGTVGEPINPEAWQWYYN--------------------------VVG 452
Cdd:cd05931 247 AAPNfAYDLCVRRVRDE----DLEgldlsSWRVALNGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGP 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 453 EKRCPVVDTFWQTETGGHVmtplPAATPMKPGSATFPFFG-VVP----AILN-ESGEELE----------GPS--EGYlv 514
Cdd:cd05931 323 PGTGPVVLRVDRDALAGRA----VAVAADDPAARELVSCGrPLPdqevRIVDpETGRELPdgevgeiwvrGPSvaSGY-- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 515 FKQPwPGVMRTvygnhlrFETTYFKKFPGYYVTGD-GCRRdkDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-- 591
Cdd:cd05931 397 WGRP-EATAET-------FGALAATDEGGWLRTGDlGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlr 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 592 -AEAAVVGRPHPVkGESLycFVTLNDGINYNQKLEAELKKQVREKIGA---IATPDYIQNAPG-LPKTRSGKIMRRVLRK 666
Cdd:cd05931 467 pGCVAAFSVPDDG-EERL--VVVAEVERGADPADLAAIAAAIRAAVARehgVAPADVVLVRPGsIPRTSSGKIQRRACRA 543
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
116-666 |
1.70e-12 |
|
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: 70.15 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQ-GVKKGDRVSIYMPMVVELVVAMLACARIGAVHSivfagfsseslcerimdsqccll 194
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPA----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 itadgfyrgdkLINLKLIADealkkcrdksfPVEKCIMLKhltkedeassgslsppakracpdlqqekqkervrkvrppp 274
Cdd:cd05937 60 -----------FINYNLSGD-----------PLIHCLKLS---------------------------------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qvpwnpevdmcwhsliggaseECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSgyMLYTASTF--KMVFDYHSDDVYWC 352
Cdd:cd05937 78 ---------------------GSRFVIVDPDDPAILIYTSGTTGLPKAAAISWR--RTLVTSNLlsHDLNLKNGDRTYTC 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 TAdIGWITGHSYITYGPLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAIRLLMkygSDPVHKYKRTSlKIL 432
Cdd:cd05937 135 MP-LYHGTAAFLGACNCLMSGGTLALSRKF----SASQFWKDVRDSGATIIQYVGELCRYLL---STPPSPYDRDH-KVR 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 433 GTVGEPINPEAWQWY---YNVvgekrcPVVDTFWQTETGGHVMT-----PLPAATPMKPGSATFPFFG---VVPAILNES 501
Cdd:cd05937 206 VAWGNGLRPDIWERFrerFNV------PEIGEFYAATEGVFALTnhnvgDFGAGAIGHHGLIRRWKFEnqvVLVKMDPET 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 502 GEELEGPSEG--------------YLVFKQP---WPGVMRTVYGNHLRFETTYFKKFPGYYVTGDGCRRDKDGYYWITGR 564
Cdd:cd05937 280 DDPIRDPKTGfcvrapvgepgemlGRVPFKNreaFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDR 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 565 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---RPHPVKGESLYCFVTLNDGINYNQKLeAELKKQVREKIGAIAT 641
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAITLEESSAVPTEFTK-SLLASLARKNLPSYAV 438
|
570 580
....*....|....*....|....*
gi 1036086734 642 PDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05937 439 PLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
303-668 |
1.70e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 67.68 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHSDDVYWCTADIGwitgHSYityGpLANGATSVLFEGL 382
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLS-HRNLLANRAQVAARIDFSPEDKVFNALPVF----HSF---G-LTGGLVLPLLSGV 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 383 PTYpdvsrmweivdkyhvskFYTAPTAIRLL--MKYGSDPV----------------HKYKRTSLKILGTVGEPINPEAW 444
Cdd:PRK06814 862 KVF-----------------LYPSPLHYRIIpeLIYDTNATilfgtdtflngyaryaHPYDFRSLRYVFAGAEKVKEETR 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 445 QWYYNVVGEKrcpVVDTFWQTETGghvmtPLPAA-TPM--KPGSATFPFFGV------VPAIlnESGEEL--EGPS--EG 511
Cdd:PRK06814 925 QTWMEKFGIR---ILEGYGVTETA-----PVIALnTPMhnKAGTVGRLLPGIeyrlepVPGI--DEGGRLfvRGPNvmLG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 512 YLvfKQPWPGVMRTVYGnhlrfettyfkkfpGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 591
Cdd:PRK06814 995 YL--RAENPGVLEPPAD--------------GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPD 1058
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036086734 592 AEAAVVGRPHPVKGESLYCFVTLNDGInynqklEAELKKQVREK-IGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK06814 1059 ALHAAVSIPDARKGERIILLTTASDAT------RAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLA 1130
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-664 |
2.54e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLLIT 196
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLS 2291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 197 ADGFYRGdklinLKLIADEALKKCRDKSFPVekcimlkhLTKEDEASSGSLSPPAKRAcpdlqqekqkervrkvrpppqv 276
Cdd:PRK05691 2292 DRALFEA-----LGELPAGVARWCLEDDAAA--------LAAYSDAPLPFLSLPQHQA---------------------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 277 pwnpevdmcwhsliggaseecepvwcdsedplFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMvFDYHSDDvywCTAdi 356
Cdd:PRK05691 2337 --------------------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIER-FGMRADD---CEL-- 2378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 357 gwitgHSY-ITYG--------PLANGATSVL-FEGlptYPDVSRMWEIVDKYHVSKFYTAPTairllmkYGSD----PVH 422
Cdd:PRK05691 2379 -----HFYsINFDaaserllvPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPS-------YGSQlaqwLAG 2443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 423 KYKRTSLKILGTVGEPINPEAWQ---------WYYNVVGEkrcpvvdtfwqTETgghVMTPLPAATP--MKPGSATFPFF 491
Cdd:PRK05691 2444 QGEQLPVRMCITGGEALTGEHLQrirqafapqLFFNAYGP-----------TET---VVMPLACLAPeqLEEGAASVPIG 2509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 492 GVVPA----ILNE---------SGEEL---EGPSEGYlvfkQPWPGVMRTvygnhlRFETTYFKKFPG-YYVTGDGCRRD 554
Cdd:PRK05691 2510 RVVGArvayILDAdlalvpqgaTGELYvggAGLAQGY----HDRPGLTAE------RFVADPFAADGGrLYRTGDLVRLR 2579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 555 KDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPvKGESLYCFVTlNDGINYNQKLEAELKKQVRE 634
Cdd:PRK05691 2580 ADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLV-SAVAGQDDEAQAALREALKA 2657
|
570 580 590
....*....|....*....|....*....|....*
gi 1036086734 635 KIGAiATPDYIQNA-----PGLPKTRSGKIMRRVL 664
Cdd:PRK05691 2658 HLKQ-QLPDYMVPAhlillDSLPLTANGKLDRRAL 2691
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-324 |
2.81e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 66.99 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITAdgfyrgdklinlkliADEALKkcrdksFPvekcimlkhltkeDEASSGSLSPPAKRACPDlqqekqkervrkvrPPP 274
Cdd:PRK10252 560 ITT---------------ADQLPR------FA-------------DVPDLTSLCYNAPLAPQG--------------AAP 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 QVPWNPevdmcwhsliggaseecepvwcdsEDPLFILYTSGSTGKPKGVL 324
Cdd:PRK10252 592 LQLSQP------------------------HHTAYIIFTSGSTGRPKGVM 617
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
543-664 |
5.98e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 543 GYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQ 622
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA 475
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1036086734 623 kleAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:PRK13383 476 ---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
101-395 |
6.65e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 65.55 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 101 GDRVAFYWEGNEPGDE--------------KTVTYRELLQQVCKFANVLKS-QGVKKGDRVSIYMPMVVELVVAMLACAR 165
Cdd:cd17632 36 ADRPALGQRATELVTDpatgrttlrllprfETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 166 IGAVHSIVFAGFSSESLCErIMDSQCCLLITADgfyrGDKLinlkliaDEALKKCRDkSFPVEKCIMLKH---LTKEDEA 242
Cdd:cd17632 116 LGAVSVPLQAGASAAQLAP-ILAETEPRLLAVS----AEHL-------DLAVEAVLE-GGTPPRLVVFDHrpeVDAHRAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 243 SSGSLSPPAKRACPDLQQEKQKERVRKVRPPPQVPWNPevdmcwhsliggaseecepvwcdSEDPL-FILYTSGSTGKPK 321
Cdd:cd17632 183 LESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEP-----------------------DDDPLaLLIYTSGSTGTPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 322 GVLHTVSgymlyTASTFKMVFDYHSDDVYWCTADIGWI-TGHSY---ITYGPLANGAT---------SVLFEGL----PT 384
Cdd:cd17632 240 GAMYTER-----LVATFWLKVSSIQDIRPPASITLNFMpMSHIAgriSLYGTLARGGTayfaaasdmSTLFDDLalvrPT 314
|
330
....*....|..
gi 1036086734 385 -YPDVSRMWEIV 395
Cdd:cd17632 315 eLFLVPRVCDML 326
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
119-672 |
1.31e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.26 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 119 VTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVhsivfagfsseslcerimdsqcclLITAD 198
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI------------------------AVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 199 GFYRGDKLINLKLIADEAlkkcrdKSFPVEKCimlkhltkedEASSGSLsPPAKRACPDLqqekqkeRVRKVRPPPQVPW 278
Cdd:PRK05857 98 GNLPIAAIERFCQITDPA------AALVAPGS----------KMASSAV-PEALHSIPVI-------AVDIAAVTRESEH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 279 NPEVDMCWHSLIGGAseecepvwcdsEDPLFILYTSGSTGKPKGVLhtvsgymlYTASTFKMVFD-YHSDDVYWctadIG 357
Cdd:PRK05857 154 SLDAASLAGNADQGS-----------EDPLAMIFTSGTTGEPKAVL--------LANRTFFAVPDiLQKEGLNW----VT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 358 WITGHSyiTYGPLAngATSV---------LFEG---LPTYPDVSRMWEIVDKYHVSKFYTAPTairLLMKYGSDpvhkyk 425
Cdd:PRK05857 211 WVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPT---LLSKLVSE------ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 426 rtsLKILGTVGEPINPEAWQWYYNVVGEKR------CPVVDTFWQTETGGHVMTpLP----AATPMKPGSATFPFFGVVP 495
Cdd:PRK05857 278 ---LKSANATVPSLRLVGYGGSRAIAADVRfieatgVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVDV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 496 AILNESG------EELEGPSEGYLVFKQPwpGVMRTVYGNHLRFETTYFKkfpGYYVTGDGCRRDKDGYYWITGRIDDML 569
Cdd:PRK05857 354 YLAATDGigptapGAGPSASFGTLWIKSP--ANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 570 NVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGInyNQKLEAELKKQV----REKIGAIATPDYI 645
Cdd:PRK05857 429 ICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL--DESAARALKHTIaarfRRESEPMARPSTI 506
|
570 580
....*....|....*....|....*..
gi 1036086734 646 QNAPGLPKTRSGKIMRRVLRKIACNER 672
Cdd:PRK05857 507 VIVTDIPRTQSGKVMRASLAAAATADK 533
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
303-664 |
5.87e-10 |
|
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: 62.19 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVL---HTVSGYMLYTASTFKMVFDYHSDdVYwctADIGWiTGHSYITYGPLANGATSVLF 379
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMiehHNLVNLCEWHRPYFGVTPADKSL-VY---ASFSF-DASAWEIFPHLTAGAALHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 380 EGLPTYpDVSRMWEIVDKYHVSKFYTAPTAIRLLMKYgsdpvhkyKRTSLKILGTVGEPINPEAWQWY--YNVVGEKRCP 457
Cdd:cd17645 177 PSERRL-DLDALNDYFNQEGITISFLPTGAAEQFMQL--------DNQSLRVLLTGGDKLKKIERKGYklVNNYGPTENT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 458 VVDTFWQTEtgghvmtPLPAATPM-KPGSATFPFfgvvpaILNE---------SGEEL---EGPSEGYLVfkqpwpgvmr 524
Cdd:cd17645 248 VVATSFEID-------KPYANIPIgKPIDNTRVY------ILDEalqlqpigvAGELCiagEGLARGYLN---------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 525 tvygnhlRFETTYfKKF------PG--YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 596
Cdd:cd17645 305 -------RPELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036086734 597 VGRPHPVKGESLYCFVTLNDGINYnQKLEAELKKQVREKIgaiaTPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:cd17645 377 LAKEDADGRKYLVAYVTAPEEIPH-EELREWLKNDLPDYM----IPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
547-679 |
6.43e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 547 TGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINynqklEA 626
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID-----PV 369
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 627 ELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRvlrkiacnERDLGDVST 679
Cdd:PRK08308 370 QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRK--------LLELGEVTA 414
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
542-668 |
7.62e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.55 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 542 PGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYN 621
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL 402
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1036086734 622 QKLEAELKKQ-VREKIgaiatPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK07445 403 EELKTAIKDQlSPFKQ-----PKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
114-371 |
8.81e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.06 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCL 193
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITadgfyrGDKlinlkliadeALKKCRDKSfpvEKCIMLKHLTKEDEASSGSLSPPAKRACPDLQQEKQKERVRKVRP- 272
Cdd:PLN02387 182 VIC------DSK----------QLKKLIDIS---SQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPv 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 273 PPQVPwnpevdmcwhsliggaseecepvwcDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVywc 352
Cdd:PLN02387 243 DPDLP-------------------------SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--- 294
|
250
....*....|....*....
gi 1036086734 353 tadigwitghsYITYGPLA 371
Cdd:PLN02387 295 -----------YLAYLPLA 302
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
115-379 |
2.60e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.38 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 115 DEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIVFAGFSSESLCERIMDSQCCLL 194
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 195 ITadgfyRGDKLINLkliadeaLKKCRDKSFPVEKCIMLkhltkedeassGSLSPPAKRACPDLqqekqkervrkvrppp 274
Cdd:PTZ00216 198 VC-----NGKNVPNL-------LRLMKSGGMPNTTIIYL-----------DSLPASVDTEGCRL---------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 275 qVPWNPEVDMcwhsliGGASEECEPVWC--DSEDPLFILYTSGSTGKPKGVLHT----VSGymlytastfKMVFDYHSDD 348
Cdd:PTZ00216 239 -VAWTDVVAK------GHSAGSHHPLNIpeNNDDLALIMYTSGTTGDPKGVMHThgslTAG---------ILALEDRLND 302
|
250 260 270
....*....|....*....|....*....|....*
gi 1036086734 349 VYWCTADigwitGHSYITYGPLAN----GATSVLF 379
Cdd:PTZ00216 303 LIGPPEE-----DETYCSYLPLAHimefGVTNIFL 332
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
303-664 |
3.24e-09 |
|
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: 59.72 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVL--HT------VSGYMLYTAST---------FKMVFDYHSDDVYwctadIGWITGHSYI 365
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLveHGsvvnlrTSLSERYFGRDngdeavlffSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 366 tygplangatsVLFEGLPTYPDvsRMWEIVDKYHVSKFYTAPTAIRLLmKYGSdpvhkykRTSLKILGTVGEPINPeawQ 445
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLAR-------LPHLKRVDAAGEEFTA---P 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 446 WYYNVVGEKRCPVVDTFWQTETG-GHVMTPLPAATPmKPGSATFPFFGVVPAILNESGE--------EL----EGPSEGY 512
Cdd:cd17648 223 VFEKLRSRFAGLIINAYGPTETTvTNHKRFFPGDQR-FDKSLGRPVRNTKCYVLNDAMKrvpvgavgELylggDGVARGY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 513 LvfkqpwpgvMRTVYGNHlRFETTYFK--------KFPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESA 584
Cdd:cd17648 302 L---------NRPELTAE-RFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 585 LVEHEAVAEAAVVGRPHPVKGES-----LYCFVTLNDGinynQKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKI 659
Cdd:cd17648 372 LASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPG----HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
....*
gi 1036086734 660 MRRVL 664
Cdd:cd17648 448 DVRAL 452
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
304-668 |
3.30e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 304 SEDPLFILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDvywctadigwitghSYITYGPL--ANGATSVLFEG 381
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKS-LLANVEQIKTIADFTPND--------------RFMSALPLfhSFGLTVGLFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 382 LPTYPDVSrmweivdkyhvskFYTAPTAIRLLmkygsdPVHKYKR-------TSlKILGTVGEPINP-EAWQWYYNVVG- 452
Cdd:PRK08043 429 LLTGAEVF-------------LYPSPLHYRIV------PELVYDRnctvlfgTS-TFLGNYARFANPyDFARLRYVVAGa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 453 EKRCPVVDTFWQTETG-----GHVMT---PLPAAT-PM--KPGSATFPFFGV------VPAILNESGEELEGPS--EGYL 513
Cdd:PRK08043 489 EKLQESTKQLWQDKFGlrileGYGVTecaPVVSINvPMaaKPGTVGRILPGMdarllsVPGIEQGGRLQLKGPNimNGYL 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 514 VFKQPwpGVMRTVYGNHLRFETTyfkkfPGYYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 593
Cdd:PRK08043 569 RVEKP--GVLEVPTAENARGEME-----RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQ 641
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036086734 594 AAVVGRPHPVKGESLYCFVTlNDGINYNQkleaeLKKQVREK-IGAIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 668
Cdd:PRK08043 642 HATAIKSDASKGEALVLFTT-DSELTREK-----LQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
304-629 |
3.60e-09 |
|
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: 59.40 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 304 SEDPLFILYTSGSTGKPKGVlhtvsgymLYTASTFKMVFDYHSDDVYWCTADIGWITGHSYITYGPlANGATSVLFEGLP 383
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGV--------VYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 384 TYP---DVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDpvHKYKRTSLKILGTVGEPINPEAWQWYYNVVGEKrCPVVD 460
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKMLSDE-AEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 461 TFWQTET------GGH-VMTPLPAATpmKPGSAT---FPFFGVVPAIL-------NESGEELEGPSE--GYLVFKQpwPG 521
Cdd:cd05910 232 PYGATEAlpvssiGSReLLATTTAAT--SGGAGTcvgRPIPGVRVRIIeiddepiAEWDDTLELPRGeiGEITVTG--PT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 522 VMRTVYGnhlRFETTYFKKFPG-----YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 596
Cdd:cd05910 308 VTPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330 340 350
....*....|....*....|....*....|...
gi 1036086734 597 VGRPHPVKGESLYCFVTLNDGINYNQKLEAELK 629
Cdd:cd05910 385 VGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
542-666 |
5.10e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.52 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 542 PGYYVTGDGCRRDkDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCFVTlndGINYN 621
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV---GDGGP 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1036086734 622 QKLEAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:PRK07824 309 APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
116-666 |
5.12e-09 |
|
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: 58.90 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSivfagfsseslcerimdsqcclli 195
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 196 tadgfyrgdkLINLKLIAdEALKKCRDKSFPvekcimlKHLTKedeassgslsppakracpdlqqekqkervrkvrpppq 275
Cdd:cd05940 57 ----------LINYNLRG-ESLAHCLNVSSA-------KHLVV------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 276 vpwnpevdmcwhsliggaseecepvwcdseDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDVYWC--- 352
Cdd:cd05940 82 ------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTClpl 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 353 ---TADI-GWITGhsyitygpLANGATSVLFEGLptypDVSRMWEIVDKYHVSKFYTAPTAIRLLMKygsDPVHKYKRTS 428
Cdd:cd05940 132 yhsTALIvGWSAC--------LASGATLVIRKKF----SASNFWDDIRKYQATIFQYIGELCRYLLN---QPPKPTERKH 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 429 lKILGTVGEPINPEAWQWYYNVVGekrCPVVDTFWQTETGGHVMTPLPAatpmKPGSAtfpffGVVPAILN--------- 499
Cdd:cd05940 197 -KVRMIFGNGLRPDIWEEFKERFG---VPRIAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLLRkvaplalvk 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 500 ---ESGEELEGPsEGYlVFKQP--WPGVMRTVYGNHLRFE-------------TTYFKKFPGYYVTGDGCRRDKDGYYWI 561
Cdd:cd05940 264 ydlESGEPIRDA-EGR-CIKVPrgEPGLLISRINPLEPFDgytdpaatekkilRDVFKKGDAWFNTGDLMRLDGEGFWYF 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 562 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRPHPVKGESLYCfVTLNDGINYNQKLEAeLKKQVREKIGAIAT 641
Cdd:cd05940 342 VDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGM-AAIVLQPNEEFDLSA-LAAHLEKNLPGYAR 419
|
570 580
....*....|....*....|....*
gi 1036086734 642 PDYIQNAPGLPKTRSGKIMRRVLRK 666
Cdd:cd05940 420 PLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
114-667 |
5.79e-09 |
|
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: 59.22 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 114 GDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACarigavhsiVFAGFSSeslcerimdsqccL 193
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFVP-------------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 194 LITADGFYRgdklinlklIADEALKKcrdksfpvekcimLKHLTKedeassgSLSPPAKRACPDLQQEKQKERVRKVRPP 273
Cdd:cd05906 93 PLTVPPTYD---------EPNARLRK-------------LRHIWQ-------LLGSPVVLTDAELVAEFAGLETLSGLPG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 274 PQVpwnpevdmcwHSLIGGASEECEPVW--CDSEDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMvFDYHSDDVYw 351
Cdd:cd05906 144 IRV----------LSIEELLDTAADHDLpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQH-NGLTPQDVF- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 352 ctadIGWItghsyitygPLANGATSVLFEGLPTY--------------PDVSRMWEIVDKYHVSkfYT-AP----TAIRL 412
Cdd:cd05906 212 ----LNWV---------PLDHVGGLVELHLRAVYlgcqqvhvpteeilADPLRWLDLIDRYRVT--ITwAPnfafALLND 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 413 LMKYGSDPvhKYKRTSLKILGTVGEPINpeawqwyyNVVGE------KRCPVVDT-----FWQTETGGHVMTPLPAATPM 481
Cdd:cd05906 277 LLEEIEDG--TWDLSSLRYLVNAGEAVV--------AKTIRrllrllEPYGLPPDairpaFGMTETCSGVIYSRSFPTYD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 482 KPGSATF-----PFFGVVPAILNESGEELEGPSEGYLVFKQPwpGVMRTVYGNHlrfETT--YFKKfPGYYVTGD-GCRR 553
Cdd:cd05906 347 HSQALEFvslgrPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP--VVTKGYYNNP---EANaeAFTE-DGWFRTGDlGFLD 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 554 DkdGYYWITGRIDDMLNVSGHLLSTAEVESAL-----VEHEAVAEAAVvgRPHPVKGESLYCF----VTLNDGINynqKL 624
Cdd:cd05906 421 N--GNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgVEPSFTAAFAV--RDPGAETEELAIFfvpeYDLQDALS---ET 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1036086734 625 EAELKKQVREKIGaiATPDYI----QNApgLPKTRSGKIMRRVLRKI 667
Cdd:cd05906 494 LRAIRSVVSREVG--VSPAYLiplpKEE--IPKTSLGKIQRSKLKAA 536
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
298-666 |
8.78e-09 |
|
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: 58.27 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 298 EPVWCDSEDPL-FILYTSGSTGKPKGVLHTVSGyMLYTASTFKMVFDYHSDDVY--W--CTADIGWITGHsyitYGPLAN 372
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRIlsWmpLTHDMGLIAFH----LAPLIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 373 GATSVLfegLPTYPDVSR--MW-EIVDKYHVSKFYTAPTAIRLLMK-YGSDPVHKYKRTSLKILGTVGEPINPEAWQWY- 447
Cdd:cd05908 173 GMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYELCHEFl 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 448 -------------YNVVGEKRCPVVDTF------WQTETGGH----VMTPLPAATPMKPGSATFPFFGVVPA-----ILN 499
Cdd:cd05908 250 dhmskyglkrnaiLPVYGLAEASVGASLpkaqspFKTITLGRrhvtHGEPEPEVDKKDSECLTFVEVGKPIDetdirICD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 500 ESGEELEGPSEGYLVFKQpwPGVMRTVYGNHLrfETTYFKKFPGYYVTGD-GCRRdkDGYYWITGRIDDMLNVSGHLLST 578
Cdd:cd05908 330 EDNKILPDGYIGHIQIRG--KNVTPGYYNNPE--ATAKVFTDDGWLKTGDlGFIR--NGRLVITGREKDIIFVNGQNVYP 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 579 AEVESALVEHEAVAEAAVVG---RPHPVKGESLYCFVTLNDGINYNQKLEAELKKQVREKIG-AIATPDYIQNapgLPKT 654
Cdd:cd05908 404 HDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwQINEVLPIRR---IPKT 480
|
410
....*....|..
gi 1036086734 655 RSGKIMRRVLRK 666
Cdd:cd05908 481 TSGKVKRYELAQ 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
545-664 |
1.48e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 545 YVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGRPHPVKGESLYCFVTLNDGINYNQKL 624
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1036086734 625 EAELKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
94-664 |
2.38e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 94 NVHERKLGDRVAFYWEGNepgdekTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIV 173
Cdd:PRK05691 1138 NEQARQTPERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 174 FAGFSSESLCERIMDSQCCLLITADGFYrgDKLINLKLIADEALKKCRDKSFPVekcimlkhltkedeassgslSPPAkr 253
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIALDSLHLDSWPS--------------------QAPG-- 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 254 acpdlqqekqkervrkvrpppqvpwnpeVDMCWHSLIggaseecepvwcdsedplFILYTSGSTGKPKGVLHT---VSGY 330
Cdd:PRK05691 1268 ----------------------------LHLHGDNLA------------------YVIYTSGSTGQPKGVGNThaaLAER 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 331 MLYTASTFKMvfdyHSDDVYWCTADIGWITGhSYITYGPLANGATSVLfEGLPTYPDVSRMWEIVDKYHVSKFYTAPTai 410
Cdd:PRK05691 1302 LQWMQATYAL----DDSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP-- 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 411 rLLMKYGSDPVHKyKRTSLKILGTVGEPINPE----------AWQwYYNVVGEKRCPVVDTFWQTETGGHVMTPL--PAA 478
Cdd:PRK05691 1374 -LLQLFIDEPLAA-ACTSLRRLFSGGEALPAElrnrvlqrlpQVQ-LHNRYGPTETAINVTHWQCQAEDGERSPIgrPLG 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 479 T-----------PMKPGsatfpffgvVPAILNESGEeleGPSEGYLvfKQPWPGVMRTV---YGNhlrfettyfkkfPG- 543
Cdd:PRK05691 1451 NvlcrvldaelnLLPPG---------VAGELCIGGA---GLARGYL--GRPALTAERFVpdpLGE------------DGa 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 544 -YYVTGDGCRRDKDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGRpHPVKGESLYCFVTLNDGinynQ 622
Cdd:PRK05691 1505 rLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAG----Q 1579
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1036086734 623 KLEAE-LKKQVREKIGAIATPDYIQNAPGLPKTRSGKIMRRVL 664
Cdd:PRK05691 1580 EAEAErLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
303-598 |
6.14e-08 |
|
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: 55.83 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 303 DSEDPLFILYTSGSTGKPKGVLHTvSGYMLYTASTFKMVFDYHSDDVYWCTADIgWitgHSY---ITYGPLANGAtSVLF 379
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLT-HANLLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 380 EGLPTYPD------------VSRMWEIVdkyhVSKFYTAPTAirllmkygSDPVHKYKRTSLKILGTVGEPIN-----PE 442
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESL----YSGIQKQVSK--------SSPIKQFLFLFFLSGGIFKFGISgggalPP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 443 AWQWYYNVVGekrCPVVDTFWQTETGGhVMTplpAATPMKP--GSATFPFFGVVPAILN-ESGEELEGPSEGYLVFKQpw 519
Cdd:cd17640 228 HVDTFFEAIG---IEVLNGYGLTETSP-VVS---ARRLKCNvrGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRG-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNHlrfETTyfKKF---PGYYVTGDGCRRDKDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAA 595
Cdd:cd17640 299 PQVMKGYYKNP---EAT--SKVldsDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIM 373
|
...
gi 1036086734 596 VVG 598
Cdd:cd17640 374 VVG 376
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
289-445 |
4.50e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.98 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 289 LIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVlhtvsgymLYTASTFkmvfdyhsddvywcTADIGWITGHSYITYG 368
Cdd:PRK09274 158 LRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGV--------VYTHGMF--------------EAQIEALREDYGIEPG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 369 -------PL------ANGATSVLFEGLPTYP---DVSRMWEIVDKYHVSKFYTAPTAIRLLMKYGSDpvHKYKRTSLKIL 432
Cdd:PRK09274 216 eidlptfPLfalfgpALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLRRV 293
|
170
....*....|...
gi 1036086734 433 GTVGEPINPEAWQ 445
Cdd:PRK09274 294 ISAGAPVPIAVIE 306
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
287-379 |
4.66e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 52.99 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 287 HSLiggASEECEPVWCDS--EDPLFILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHSDDvywctadigwitgHSY 364
Cdd:cd17639 71 HSL---NETECSAIFTDGkpDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRY 134
|
90
....*....|....*....
gi 1036086734 365 ITYGPLAN----GATSVLF 379
Cdd:cd17639 135 LAYLPLAHifelAAENVCL 153
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
584-693 |
1.86e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 47.45 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 584 ALVEHEAVAEAAVVGRPHPVKGESLYCFVTLNDGINYNQkLEAELKKQVREKigaiaTPDYIQNAPGLPKTRSGKIMRRV 663
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFVEAELPADEKS-LRARLAGAKPPK-----PPEHIQPVAALPRDADGTVRDDI 321
|
90 100 110
....*....|....*....|....*....|..
gi 1036086734 664 LRKIACNERDLGD--VSTLADSSVIEHLFENR 693
Cdd:PRK09188 322 LRLIAMNQIDELDdlLREPEIRGLVEAIAAHR 353
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
93-372 |
4.98e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.76 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 93 RNVHERKLGDRVAfywEGNEPGDEKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSI 172
Cdd:PLN02861 55 KYPNNQMLGRRQV---TDSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 173 VFAGFSSESLcERIMDSQCCLLItadgFYRGDKLINLKliadEALKKCRDKsfpvekcimLKHLTkedeaSSGSLSppak 252
Cdd:PLN02861 132 LYDTLGANAV-EFIINHAEVSIA----FVQESKISSIL----SCLPKCSSN---------LKTIV-----SFGDVS---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 253 racpDLQQEKQKERVRKVrpppqvpwnpevdMCWHSLIGGASEECEPVWCDSEDPLFILYTSGSTGKPKGVLHTVSGYML 332
Cdd:PLN02861 185 ----SEQKEEAEELGVSC-------------FSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1036086734 333 YTASTFKMVFDyhSDDVywCTADigwitgHSYITYGPLAN 372
Cdd:PLN02861 248 EVLSTDHLLKV--TDRV--ATEE------DSYFSYLPLAH 277
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
310-414 |
1.47e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 44.90 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 310 ILYTSGSTGKPKGVLHTVSGYMLYTASTFKMVFDYHS---DDVywctadigwitghsYITYGPLANgatsvLFEglptyp 386
Cdd:cd05927 119 ICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKinpTDV--------------YISYLPLAH-----IFE------ 173
|
90 100 110
....*....|....*....|....*....|
gi 1036086734 387 dvsRMWEIVDKYHVSK--FYTAPtaIRLLM 414
Cdd:cd05927 174 ---RVVEALFLYHGAKigFYSGD--IRLLL 198
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
547-685 |
2.22e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 547 TGD-GCRRDkdGYYWITGRIDDMLNVSGHLL------STAEVESALVEHEAVAEAAVvgrphPVKGEslycfvtlnDGIN 619
Cdd:PRK05691 433 TGDlGFLRD--GELFVTGRLKDMLIVRGHNLypqdieKTVEREVEVVRKGRVAAFAV-----NHQGE---------EGIG 496
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036086734 620 YNQKLEAELKKQV--REKIGAI--ATPDYIQNAP---------GLPKTRSGKIMRRvlrkiACNERdlgdvstLADSSV 685
Cdd:PRK05691 497 IAAEISRSVQKILppQALIKSIrqAVAEACQEAPsvvlllnpgALPKTSSGKLQRS-----ACRLR-------LADGSL 563
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
313-653 |
5.27e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.83 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 313 TSGSTGKPKGVLHT---------VSGYMLYTASTfkmvfdyHSDDVYWCTADIGWITGHSYITYGPLANGATSVLFEGLP 383
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdldrwaeLFARSLRAAGV-------RPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 384 TypdvSRMWEIVDKYHVSKFYTAPT-AIRLL---MKYGSDPvhkyKRTSLK--ILGtvGEPInPEAW-QWYYNVVGekrC 456
Cdd:COG1541 164 T----ERQLRLMQDFGPTVLVGTPSyLLYLAevaEEEGIDP----RDLSLKkgIFG--GEPW-SEEMrKEIEERWG---I 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 457 PVVDTFWQTETGGHVMTPLPAATPMKPGSATFpffgvVPAILN-ESGEELEGPSEGYLVFkqpwpgvmrtvygnhlrfeT 535
Cdd:COG1541 230 KAYDIYGLTEVGPGVAYECEAQDGLHIWEDHF-----LVEIIDpETGEPVPEGEEGELVV-------------------T 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 536 TYFKKfpGY----YVTGD---------GCRR-----DKdgyywITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA--A 595
Cdd:COG1541 286 TLTKE--AMplirYRTGDltrllpepcPCGRthpriGR-----ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqI 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036086734 596 VVGRPHPVkgESLYCFVTLNDGINYnQKLEAELKKQVREKIG-----AIATPDYIQNAPGLPK 653
Cdd:COG1541 359 VVDREGGL--DELTVRVELAPGASL-EALAEAIAAALKAVLGlraevELVEPGSLPRSEGKAK 418
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
117-173 |
1.25e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 42.12 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1036086734 117 KTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIV 173
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVI 75
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
117-169 |
1.43e-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: 41.95 E-value: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1036086734 117 KTVTYRELLQQVCKFANVL-KSQGVKKGDRVSIYMPMVVELVVAMLACARIGAV 169
Cdd:cd05905 13 TTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVV 66
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
116-173 |
3.02e-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: 41.20 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1036086734 116 EKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGAVHSIV 173
Cdd:TIGR03443 268 TRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
102-664 |
4.83e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.88 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 102 DRVAFYWEGnepgdeKTVTYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACARIGavHSIVFAGFSSES 181
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 182 lcERIMD----SQCCLLITADGFyrgdklinlkliadealkkcrdksfpvekcimlkhltkedeassgslsPPAKRACPD 257
Cdd:PRK04813 89 --ERIEMiievAKPSLIIATEEL------------------------------------------------PLEILGIPV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 258 LQQEKQKERVRKVRPPPQVPWnpevdmcwhslIGGaseecepvwcdsEDPLFILYTSGSTGKPKGV------LHTVSGYM 331
Cdd:PRK04813 119 ITLDELKDIFATGNPYDFDHA-----------VKG------------DDNYYIIFTSGTTGKPKGVqishdnLVSFTNWM 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 332 LytaSTFKMV------------FDYHSDDVYWCtadigwitghsyitygpLANGATSV------------LFEGLPTYP- 386
Cdd:PRK04813 176 L---EDFALPegpqflnqapysFDLSVMDLYPT-----------------LASGGTLValpkdmtanfkqLFETLPQLPi 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 387 DVsrmWeivdkyhVSkfytAPTAIRL-LMkygsDPvhkykrtslkilgTVGEPINPEAWQWYYnvVGE-----------K 454
Cdd:PRK04813 236 NV---W-------VS----TPSFADMcLL----DP-------------SFNEEHLPNLTHFLF--CGEelphktakkllE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 455 RCP---VVDTFWQTETGGHV------------MTPLPAATPmKPGSATFpffgvvpaILNESGEELEGPSEGYLVFKQpw 519
Cdd:PRK04813 283 RFPsatIYNTYGPTEATVAVtsieitdemldqYKRLPIGYA-KPDSPLL--------IIDEEGTKLPDGEQGEIVISG-- 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 520 PGVMRTVYGNHLRFETTYF--KKFPGYYvTGDGCRRDkDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 597
Cdd:PRK04813 352 PSVSKGYLNNPEKTAEAFFtfDGQPAYH-TGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036086734 598 --GRPHPVkgESLYCFVTLNDGinyNQKLEAELKKQVREKIGAIaTPDYI-------QNApgLPKTRSGKIMRRVL 664
Cdd:PRK04813 430 pyNKDHKV--QYLIAYVVPKEE---DFEREFELTKAIKKELKER-LMEYMiprkfiyRDS--LPLTPNGKIDRKAL 497
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
120-350 |
7.06e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 39.80 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 120 TYRELLQQVCKFANVLKSQGVKKGDRVSIYMPMVVELVVAMLACarigAVHSIVfagfsseslCERIMDSqccLLITADG 199
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEAC----AAHSLI---------CVPLYDT---LGPGAVD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 200 FYRGDKLINLKLIADEALKK-----CRDKSfPVEKCIMLKHLTKE--DEASSGSLSPPAKRACPDLQQEKQKERVrkvrp 272
Cdd:PLN02430 142 YIVDHAEIDFVFVQDKKIKEllepdCKSAK-RLKAIVSFTSVTEEesDKASQIGVKTYSWIDFLHMGKENPSETN----- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036086734 273 PPQvpwnpEVDMCwhsliggaseecepvwcdsedplFILYTSGSTGKPKGVLHTVSGYMLYTAST--FKMVFD--YHSDD 348
Cdd:PLN02430 216 PPK-----PLDIC-----------------------TIMYTSGTSGDPKGVVLTHEAVATFVRGVdlFMEQFEdkMTHDD 267
|
..
gi 1036086734 349 VY 350
Cdd:PLN02430 268 VY 269
|
|
| |
