|
Name |
Accession |
Description |
Interval |
E-value |
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
81-654 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 753.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 81 WYPGAELNVAHNTVDRHAsvdAGTRNHVACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQ 160
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHA---EGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 161 SILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPAD 240
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 241 slswTPRDEWWDDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSD 320
Cdd:COG0365 159 ----MEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 321 IGWMMGPWS-LIGNHAFAGTIVMYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGST 399
Cdd:COG0365 235 IGWATGHSYiVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 400 GEPWDPESWRWFYDHVGggdTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVA 479
Cdd:COG0365 315 GEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 480 RSSSPSMTRRLWSGEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAA 559
Cdd:COG0365 391 KGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 560 VVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTD 639
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGD 550
|
570
....*....|....*
gi 499204776 640 RSSIENPAVLDALRD 654
Cdd:COG0365 551 TSTLEDPEALDEIKE 565
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-646 |
0e+00 |
|
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: 710.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 28 MTAHDIDDVDALRERSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDPQSTAWYPGAELNVAHNTVDRHAsvdAGTRNH 107
Cdd:cd05968 1 MASLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWL---ADTRTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 108 VACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATAT 187
Cdd:cd05968 78 PALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 188 RIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPadsLSWTP-RDEWWDDAVATQSPTFEthS 266
Cdd:cd05968 158 RLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGND---FTPAKgRDLSYDEEKETAGDGAE--R 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 MAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGA 346
Cdd:cd05968 233 TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 347 PDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDTPIINIS 426
Cdd:cd05968 313 PDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDanERGYLVARSSSPSMTRRLWSGEDRYLEAYWSRFE 506
Cdd:cd05968 393 GGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 507 DVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSA 586
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 587 ELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSIENP 646
Cdd:cd05968 551 ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
30-655 |
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: 612.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 30 AHDIDDVDALRERSTTDLDWFWGELPEYLgLEFFEDYDAVRDDADDPqSTAWYPGAELNVAHNTVDRHASVDAgtrNHVA 109
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAREL-LDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARP---DKVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 110 CIWEGED-GTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATR 188
Cdd:TIGR02188 76 IIWEGDEpGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 189 IADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGH-VDHTIVYDRLGIPADSlsWTP-RDEWWDDAVATQSPTFETHS 266
Cdd:TIGR02188 156 INDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVsVEHVLVVRRTGNPVVP--WVEgRDVWWHDLMAKASAYCEPEP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 MAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMYEG 345
Cdd:TIGR02188 234 MDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMFEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 APDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDTPIINI 425
Cdd:TIGR02188 314 VPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 426 SGGTEVFGCFLMPLP-TESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSSSPSMTRRLWSGEDRYLEAYWSR 504
Cdd:TIGR02188 394 WWQTETGGIMITPLPgATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 505 FEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATP 584
Cdd:TIGR02188 474 FPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEP 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 585 SAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGA--DVTDRSSIENPAVLDALRDA 655
Cdd:TIGR02188 554 DDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEaeILGDTSTLEDPSVVEELIEA 626
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
11-655 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 608.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 11 VHEPDPALASSTNVaqfmtahDIDDVDALRERSTTDLDWFWGELPEYLglEFFEDYDAVRDDadDPQSTAWYPGAELNVA 90
Cdd:PRK00174 1 VFPPPAEFAANALI-------DMEQYKALYQESVEDPEGFWAEQAKRL--DWFKPFDTVLDW--NAPFIKWFEDGELNVS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 91 HNTVDRHasVDAGtRNHVACIWEGED-GTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKI 169
Cdd:PRK00174 70 YNCLDRH--LKTR-GDKVAIIWEGDDpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 170 GAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPADslsWTP-RD 248
Cdd:PRK00174 147 GAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDVD---WVEgRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 249 EWWDDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPw 328
Cdd:PRK00174 224 LWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGH- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 329 SLI--GNHAFAGTIVMYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPE 406
Cdd:PRK00174 303 SYIvyGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 407 SWRWFYDHVGGGDTPIINISGGTEVFGCFLMPLP-TESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPS 485
Cdd:PRK00174 383 AWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPgATPLKPGSATRPLPGIQPAVVDEEGNPL-EGGEGGNLVIKDPWPG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRRLWSGEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPD 565
Cdd:PRK00174 462 MMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 566 DTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVT-DRSSIE 644
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEILgDTSTLA 621
|
650
....*....|.
gi 499204776 645 NPAVLDALRDA 655
Cdd:PRK00174 622 DPSVVEKLIEA 632
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
34-645 |
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: 606.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 34 DDVDALRERSTTDLDWFWGELPEYLglEFFEDYDAVRDDADDPQSTAWYPGAELNVAHNTVDRHAsvdAGTRNHVACIWE 113
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKEL--DWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHL---KERGDKVAIIWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 114 GEDGTVRQQ-TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADA 192
Cdd:cd05966 76 GDEPDQSRTiTYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPADslsWTP-RDEWWDDAVATQSPTFETHSMAASD 271
Cdd:cd05966 156 QCKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVP---MTEgRDLWWHDLMAKQSPECEPEWMDSED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 272 PCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMYEGAPDHP 350
Cdd:cd05966 233 PLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGhSYIVYGPLANGATTVMFEGTPTYP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 351 APDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDTPIINISGGTE 430
Cdd:cd05966 313 DPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 431 VFGCFLMPLP-TESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPSMTRRLWSGEDRYLEAYWSRFEDVW 509
Cdd:cd05966 393 TGGIMITPLPgATPLKPGSATRPFFGIEPAILDEEGNEV-EGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 510 NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELR 589
Cdd:cd05966 472 FTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELR 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 590 AELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVT-DRSSIEN 645
Cdd:cd05966 552 KELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELgDTSTLAD 608
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
42-624 |
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: 575.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 42 RSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDPQSTAWYPGAELNVAHNTVDRHASvDAGTRnhVACIWEGEDGT-VR 120
Cdd:cd17634 7 QSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLR-ENGDR--TAIIYEGDDTSqSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 121 QQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTG 200
Cdd:cd17634 84 TISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 201 DGFLRRGDRVTLMDTLNDAIERAG-HVDHTIVYDRLGIPADslsWTP-RDEWWDDAVATQSPTFETHSMAASDPCMLLYS 278
Cdd:cd17634 164 DGGVRAGRSVPLKKNVDDALNPNVtSVEHVIVLKRTGSDID---WQEgRDLWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMYEGAPDHPAPDRFWQ 357
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNWPTPARMWQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 358 LIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDTPIINISGGTEVFGCFLM 437
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMIT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 438 PLP-TESLKPCTLGGPGLGMDIDIVDDDGTSVRDANErGYLVARSSSPSMTRRLWSGEDRYLEAYWSRFEDVWNHGDWAQ 516
Cdd:cd17634 401 PLPgAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 517 MDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHV 596
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWV 559
|
570 580
....*....|....*....|....*...
gi 499204776 597 GDAHGKPFRPREVVFVDDLPKTQSGKLV 624
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
8-654 |
1.59e-142 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 429.99 E-value: 1.59e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 8 GTVVHEPDPALASSTNVAQFM------TAHDIDDVDALRERSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDPQSTaW 81
Cdd:PRK03584 2 GDPLWTPSAERIAASRMTAFIrwlaarRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLAGRRMPGAR-W 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 82 YPGAELNVAHNtVDRHASvdagtRNHVACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQS 161
Cdd:PRK03584 81 FPGARLNYAEN-LLRHRR-----DDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 162 ILYGIFKIGAIavpiFSG----FGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGi 237
Cdd:PRK03584 155 AMLATASLGAI----WSScspdFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 238 PADSLSWTPRDEWWDDAVA---TQSPTFEthSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDR 314
Cdd:PRK03584 230 PAAAAAALPGALLWEDFLApaeAAELEFE--PVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 315 FCWVSDIGWMMGPWsLIGNHAFAGTIVMYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLR 394
Cdd:PRK03584 308 FFWYTTCGWMMWNW-LVSGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 395 ILGSTGEPWDPESWRWFYDHVgGGDTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDanER 474
Cdd:PRK03584 387 TIGSTGSPLPPEGFDWVYEHV-KADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVG--EV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 475 GYLVARSSSPSMTRRLWSGED--RYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDH 552
Cdd:PRK03584 464 GELVCTKPFPSMPLGFWNDPDgsRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEAL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 553 DAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAY 632
Cdd:PRK03584 544 PEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLL 623
|
650 660
....*....|....*....|....*
gi 499204776 633 TGADVTD---RSSIENPAVLDALRD 654
Cdd:PRK03584 624 HGRPVKKavnRDALANPEALDWFAD 648
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
40-652 |
3.45e-136 |
|
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: 412.48 E-value: 3.45e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 40 RERSTTDLDWFWGELPEylGLEFFEDYDAVRDDADDPqSTAWYPGAELNVAHNTVDRHasVDAGTRNHVACIWE-GEDGT 118
Cdd:cd05967 5 YARSIAEPEAFWAEQAR--LIDWFKPPEKILDNSNPP-FTRWFVGGRLNTCYNALDRH--VEAGRGDQIALIYDsPVTGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 119 VRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVF 198
Cdd:cd05967 80 ERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 TGDGFLRRGDRVTLMDTLNDAIERAGH-VDHTIVYDRLGIPADSLSwTPRDEWWDDAVATQSPTfETHSMAASDPCMLLY 277
Cdd:cd05967 160 TASCGIEPGKVVPYKPLLDKALELSGHkPHHVLVLNRPQVPADLTK-PGRDLDWSELLAKAEPV-DCVPVAATDPLYILY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 278 SSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGpwslignHAF-------AG-TIVMYEGAPD- 348
Cdd:cd05967 238 TSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVG-------HSYivygpllHGaTTVLYEGKPVg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPDRFWQLIEDHGITQFGVSPTAIRALR--DHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINIS 426
Cdd:cd05967 311 TPDPGAFWRVIEKYQVNALFTAPTAIRAIRkeDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEV---FGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRdANERGYLV-ARSSSPSMTRRLWSGEDRYLEAYW 502
Cdd:cd05967 388 WQTETgwpITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVG-PNELGNIViKLPLPPGCLLTLWKNDERFKKLYL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 503 SRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAA 582
Cdd:cd05967 467 SKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGV 546
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 583 TPSAE-LRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSIENPAVLDAL 652
Cdd:cd05967 547 KITAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
33-650 |
4.07e-133 |
|
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: 404.73 E-value: 4.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 33 IDDVDALRERSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDPQSTAWYPGAELNVAHNTVDRHASVDAgtrnhvACIW 112
Cdd:cd05943 16 LADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRHADADDP------AAIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 113 EGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADA 192
Cdd:cd05943 90 AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIV--YDRLGIPADsLSWTPRDEWWDDAVAT-QSPTFETHSMAA 269
Cdd:cd05943 170 EPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVvpYTVAAGQPD-LSKIAKALTLEDFLATgAAGELEFEPLPF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 270 SDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWsLIGNHAFAGTIVMYEGAPDH 349
Cdd:cd05943 249 DHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNW-LVSGLAVGATIVLYDGSPFY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVgGGDTPIINISGGT 429
Cdd:cd05943 328 PDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI-KPDVLLASISGGT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 430 EVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDanERGYLVARSSSPSMTRRLWSGED--RYLEAYWSRFED 507
Cdd:cd05943 407 DIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWG--EKGELVCTKPFPSMPVGFWNDPDgsRYRAAYFAKYPG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 508 VWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAE 587
Cdd:cd05943 485 VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE 564
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 588 LRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSIENPAVLD 650
Cdd:cd05943 565 LRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLD 627
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
37-655 |
2.31e-120 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 371.97 E-value: 2.31e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 37 DALRERSTTDLDWFWGELPEYLglEFFEDYDAVRDDaDDPQSTAWYPGAELNVAHNTVDRHASVDAGTRnhvACIW-EGE 115
Cdd:PRK10524 5 SEFYQRSIDDPEAFWAEQARRI--DWQTPFTQVLDY-SNPPFARWFVGGRTNLCHNAVDRHLAKRPEQL---ALIAvSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGDGFLRRGDRVTLMDTLNDAIERAGHV-DHTIVYDRlGIpaDSLSWTP-RDEWW--------DDAVATQSptfeth 265
Cdd:PRK10524 159 LIVSADAGSRGGKVVPYKPLLDEAIALAQHKpRHVLLVDR-GL--APMARVAgRDVDYatlraqhlGARVPVEW------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 266 sMAASDPCMLLYSSGTTGTPKGI---VHTHAGALVQPAKEIhfgFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAG-TIV 341
Cdd:PRK10524 230 -LESNEPSYILYTSGTTGKPKGVqrdTGGYAVALATSMDTI---FGGKAGETFFCASDIGWVVGHSYIVYAPLLAGmATI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 MYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTP 421
Cdd:PRK10524 306 MYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTEVFGCFLMPLPTESLKPCTLGGPGL---GMDIDIVDDDGTSVRDANERGYLVARSSSPS--MTRrLWSGEDR 496
Cdd:PRK10524 383 VIDNYWQTETGWPILAIARGVEDRPTRLGSPGVpmyGYNVKLLNEVTGEPCGPNEKGVLVIEGPLPPgcMQT-VWGDDDR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 497 YLEAYWSRF-EDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAY 575
Cdd:PRK10524 462 FVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 576 VILADAATPS-----AELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSIENPAVLD 650
Cdd:PRK10524 542 VVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQ 621
|
....*
gi 499204776 651 ALRDA 655
Cdd:PRK10524 622 QIRQA 626
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
38-652 |
1.25e-119 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 371.15 E-value: 1.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 38 ALRERSTTDLDWFWGELP-EYLGLEFFEDYDAVRDDAD---DPQSTAWYPGAELNVAHNTVDRHasVDAGTRNHVACIWE 113
Cdd:PLN02654 34 EMYKRSVDDPAGFWSDIAsQFYWKQKWEGDEVCSENLDvrkGPISIEWFKGGKTNICYNCLDRN--VEAGNGDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 114 GED-GTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADA 192
Cdd:PLN02654 112 GNEpGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGH----VDHTIVYD-RLGIPADSLSWTP-RDEWWDDAVATQSPTFETHS 266
Cdd:PLN02654 192 KPKVVITCNAVKRGPKTINLKDIVDAALDESAKngvsVGICLTYEnQLAMKREDTKWQEgRDVWWQDVVPNYPTKCEVEW 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 MAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMYEG 345
Cdd:PLN02654 272 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVFEG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 APDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDTPIINI 425
Cdd:PLN02654 352 APNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 426 SGGTEVFGCFLMPLPTE-SLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPSMTRRLWSGEDRYLEAYWSR 504
Cdd:PLN02654 432 WWQTETGGFMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGKEI-EGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKP 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 505 FEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATP 584
Cdd:PLN02654 511 FAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPY 590
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 585 SAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR---RAVASAYTGaDVTDRSSIENPAVLDAL 652
Cdd:PLN02654 591 SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRrilRKIASRQLD-ELGDTSTLADPGVVDQL 660
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
65-626 |
1.16e-116 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 360.36 E-value: 1.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 65 DYDAVRDD---ADDPQSTAWYPGAELNVAHNTVDRHAsvDAGTRNHVACIWEGEDgTVRQQTYHDLHQQANRVANALAER 141
Cdd:PRK04319 17 DYEETYATfswEEVEKEFSWLETGKVNIAYEAIDRHA--DGGRKDKVALRYLDAS-RKEKYTYKELKELSNKFANVLKEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 142 GIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRgdrvtlmdtlnDAIE 221
Cdd:PRK04319 94 GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLER-----------KPAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 222 RAGHVDHTIVYDrlgipaDSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAK 301
Cdd:PRK04319 163 DLPSLKHVLLVG------EDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-NAMLQHYQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 302 EIHFGFDQRPGDRFCWVSDIGWMMG-------PWsLIGnhafaGTIVMYEGAPDhpaPDRFWQLIEDHGITQFGVSPTAI 374
Cdd:PRK04319 236 TGKYVLDLHEDDVYWCTADPGWVTGtsygifaPW-LNG-----ATNVIDGGRFS---PERWYRILEDYKVTVWYTAPTAI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 375 RALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGL 454
Cdd:PRK04319 307 RMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 455 GMDIDIVDDDGtSVRDANERGYLVARSSSPSMTRRLWSGEDRYlEAYwsrFEDVWN-HGDWAQMDADGD-WFLhGRADDA 532
Cdd:PRK04319 384 GIEAAIVDDQG-NELPPNRMGNLAIKKGWPSMMRGIWNNPEKY-ESY---FAGDWYvSGDSAYMDEDGYfWFQ-GRVDDV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 533 INVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFV 612
Cdd:PRK04319 458 IKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFK 537
|
570
....*....|....
gi 499204776 613 DDLPKTQSGKLVRR 626
Cdd:PRK04319 538 DKLPKTRSGKIMRR 551
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
13-654 |
9.80e-107 |
|
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: 337.24 E-value: 9.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 13 EPDPALASSTNVAQFM----TAH--DIDDVDALRERSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDPQSTaWYPGAE 86
Cdd:TIGR01217 8 QPDAQRIAQARMTRFQawagEHHgaAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVVDDRTMPGAQ-WFPGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 87 LNVAHNTVdRHASVDAgtrnhvACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGI 166
Cdd:TIGR01217 87 LNYAENLL-RAAGTEP------ALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 167 FKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPADSLSWTP 246
Cdd:TIGR01217 160 ASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETEAPKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 247 RDEWWDDAVAT-QSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMM 325
Cdd:TIGR01217 240 GALDLEDFTAAaQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 326 GPWsLIGNHAFAGTIVMYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDP 405
Cdd:TIGR01217 320 WNW-LVSGLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 406 ESWRWFYDHVGGgDTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDanERGYLVARSSSPS 485
Cdd:TIGR01217 399 DGFRWVYDEIKA-DVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTG--EVGELVCTNPMPS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRRLWSGED--RYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGV 563
Cdd:TIGR01217 476 MPIRFWNDPDgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 564 PDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSI 643
Cdd:TIGR01217 556 EQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGAI 635
|
650
....*....|.
gi 499204776 644 ENPAVLDALRD 654
Cdd:TIGR01217 636 DNPELLDLYEE 646
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
123-628 |
1.87e-98 |
|
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: 309.05 E-value: 1.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRRgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsMAASDPCMLLYSSGTT 282
Cdd:cd05969 82 LYER------------------------------------------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGP-WSLIGNHAFAGTIVMYEGAPDhpaPDRFWQLIED 361
Cdd:cd05969 102 GTPKGVLHVHD-AMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTvYGIWAPWLNGVTNVVYEGRFD---AESWYGIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 362 HGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVFGCFLMPLPT 441
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 442 ESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVARSSSPSMTRRLWSGEDRYLEAywsrFEDVWN-HGDWAQMDAD 520
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDENGNELPP-GTKGILALKPGWPSMFRGIWNDEERYKNS----FIDGWYlTGDLAYRDED 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 521 GD-WFLhGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDA 599
Cdd:cd05969 330 GYfWFV-GRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQK 408
|
490 500
....*....|....*....|....*....
gi 499204776 600 HGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd05969 409 LGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
94-632 |
1.87e-95 |
|
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: 301.34 E-value: 1.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 94 VDRHASVDAgtrNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIA 173
Cdd:COG0318 5 LRRAAARHP---DRPALVFGG-----RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 174 VPIFSGFGVEATATRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwdd 253
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 254 avatqsptfethsmaasdpCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVS----DIGWMMGPWS 329
Cdd:COG0318 103 -------------------ALILYTSGTTGRPKGVMLTH-RNLLANAAAIAAALGLTPGDVVLVALplfhVFGLTVGLLA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 330 LIgnhAFAGTIVMyegaPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWR 409
Cdd:COG0318 163 PL---LAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGAPLPPELLE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 410 WFYDHVGggdTPIINISGGTEVFG-CFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVARSssPSMTR 488
Cdd:COG0318 234 RFEERFG---VRIVEGYGLTETSPvVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPP-GEVGEIVVRG--PNVMK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 489 RLWSGEDRYLEAywsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDT 567
Cdd:COG0318 308 GYWNDPEATAEA----FRDGWLRtGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEK 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 568 TGEAAIAYVILADAATPSA-ELRAELRDHVGdAHGkpfRPREVVFVDDLPKTQSGKLVRRAVASAY 632
Cdd:COG0318 384 WGERVVAFVVLRPGAELDAeELRAFLRERLA-RYK---VPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
123-627 |
4.87e-91 |
|
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: 289.24 E-value: 4.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVvftgdg 202
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmdtlndaieraghvdhtIVYDrlgipadslswtprdewwddavatqsptfethsmaASDPCMLLYSSGTT 282
Cdd:cd05972 76 ---------------------------IVTD-----------------------------------AEDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGAL--VQPAKEIHfgfDQRPGDRFCWVSDIGWMMGPWS-LIGNHAFAGTIVMYEGAPDhpAPDRFWQLI 359
Cdd:cd05972 94 GLPKGVLHTHSYPLghIPTAAYWL---GLRPDDIHWNIADPGWAKGAWSsFFGPWLLGATVFVYEGPRF--DAERILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 360 EDHGITQFGVSPTAIRALRDHGDEHvagHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVfGCFLMPL 439
Cdd:cd05972 169 ERYGVTSFCGPPTAYRMLIKQDLSS---YKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTET-GLTVGNF 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 440 PTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPSMTRRLWSGEDRYlEAYWSrfEDVWNHGDWAQMDA 519
Cdd:cd05972 242 PDMPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLGYVGDPEKT-EASIR--GDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 520 DGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDA 599
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKV 397
|
490 500
....*....|....*....|....*...
gi 499204776 600 HGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd05972 398 LAPYKYPREIEFVEELPKTISGKIRRVE 425
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
271-622 |
4.31e-83 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 265.30 E-value: 4.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGapdhP 350
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSH-RNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 351 APDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTE 430
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 431 VFGCFL-MPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVARSssPSMTRRLWsgedRYLEAYWSRFEDVW 509
Cdd:cd04433 151 TGGTVAtGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRG--PSVMKGYW----NNPEATAAVDEDGW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 510 -NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAEl 588
Cdd:cd04433 224 yRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE- 302
|
330 340 350
....*....|....*....|....*....|....
gi 499204776 589 raELRDHVGDAHGKPFRPREVVFVDDLPKTQSGK 622
Cdd:cd04433 303 --ELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
96-628 |
6.07e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 260.12 E-value: 6.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 96 RHASVDAGTRnhVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVP 175
Cdd:PRK06187 13 RHGARKHPDK--EAVYFDG-----RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 176 IfsgfGVEATATRIA----DAECSVVFTGDGFLrrgdrvtlmDTLNDAIERAGHVDHTIVYDrlgiPADSLSWTPRDEWW 251
Cdd:PRK06187 86 I----NIRLKPEEIAyilnDAEDRVVLVDSEFV---------PLLAAILPQLPTVRTVIVEG----DGPAAPLAPEVGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 252 DDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRF----------CWvsdi 321
Cdd:PRK06187 149 EELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHR-NLFLHSLAVCAWLKLSRDDVYlvivpmfhvhAW---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 322 GWMMGPWslignhaFAG-TIVMyegaPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILGSTG 400
Cdd:PRK06187 224 GLPYLAL-------MAGaKQVI----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKA--PRAYFVDFSSLRLVIYGG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 401 EPWDPESWRWFYDHVGGGdtpIINISGGTEV--FGCFLMP---LPTESLKPCTLGGPGLGMDIDIVDDDGTSV-RDANER 474
Cdd:PRK06187 291 AALPPALLREFKEKFGID---LVQGYGMTETspVVSVLPPedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELpPDGGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 475 GYLVARSssPSMTRRLWSGEdrylEAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHD 553
Cdd:PRK06187 368 GEIIVRG--PWLMQGYWNRP----EATAETIDGGWLHtGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHP 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 554 AVTQAAVVGVPDDTTGEAAIAYVILADAATPSA-ELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK06187 442 AVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAkELRAFLRGRL--AKFK--LPKRIAFVDELPRTSVGKILKRVL 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
94-536 |
3.09e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 252.62 E-value: 3.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 94 VDRHAsvdAGTRNHVACiwegEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIA 173
Cdd:pfam00501 1 LERQA---ARTPDKTAL----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 174 VPIFSGFGVEATATRIADAECSVVFTgdgflrrgDRVTLMDTLNDAIERAGHVDHTIVYDRLGIPADslswtprDEWWDD 253
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLIT--------DDALKLEELLEALGKLEVVKLVLVLDRDPVLKE-------EPLPEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 254 AVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGAL---VQPAKEIHFGFDQRPGDRFCWVSDIGWMMG-PWS 329
Cdd:pfam00501 139 AKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlSLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 330 LIGNHAFAGTIVMYEGAPdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAghDLSSLRILGSTGEPWDPESWR 409
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFP-ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 410 WFYDHVGGgdtPIINISGGTE--VFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARssSPSMT 487
Cdd:pfam00501 296 RFRELFGG---ALVNGYGLTEttGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVR--GPGVM 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 RRLWSGEDRYLEAYWsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVA 536
Cdd:pfam00501 371 KGYLNDPELTAEAFD---EDGWYRtGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
116-627 |
2.43e-75 |
|
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: 248.12 E-value: 2.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTgDGflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaASDPCML 275
Cdd:cd05971 81 ALVT-DG------------------------------------------------------------------SDDPALI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHAGALVQ-PAKEIHFGFDQRPGDRFCWVSDIGWMMG------PWSLIGNHAFAGTIVMYEgapd 348
Cdd:cd05971 94 IYTSGTTGPPKGALHAHRVLLGHlPGVQFPFNLFPRDGDLYWTPADWAWIGGlldvllPSLYFGVPVLAHRMTKFD---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 hpaPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGG 428
Cdd:cd05971 170 ---PKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFG---VEVNEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 429 TE---VFG--CFLMPLpteslKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPSMTRRLWSGEdrylEAYWS 503
Cdd:cd05971 242 TEcnlVIGncSALFPI-----KPGSMGKPIPGHRVAIVDDNGTPL-PPGEVGEIAVELPDPVAFLGYWNNP----SATEK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 504 RFEDVW-NHGDWAQMDADGD-WFLhGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADA 581
Cdd:cd05971 312 KMAGDWlLTGDLGRKDSDGYfWYV-GRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499204776 582 ATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd05971 391 ETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
123-625 |
9.56e-74 |
|
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: 243.96 E-value: 9.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTgdg 202
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmdtlnDAIERaghvdhtivyDRLgipadslswtprdewwddavatqsptfethsmaASDPCMLLYSSGTT 282
Cdd:cd05973 79 ---------------DAANR----------HKL---------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHThAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGT-IVMYEGAPdhpAPDRFWQLIED 361
Cdd:cd05973 101 GLPKGVPVP-LRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHpTILLEGGF---SVESTWRVIER 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 362 HGITQFGVSPTAIRALRDHGDEhVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVFgcflMPL-- 439
Cdd:cd05973 177 LGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELG----MVLan 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 440 ---PTESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYL-VARSSSPSMT-RRLWSGEDRYLEAYWSRfedvwnHGDW 514
Cdd:cd05973 249 hhaLEHPVHAGSAGRAMPGWRVAVLDDDGDELGP-GEPGRLaIDIANSPLMWfRGYQLPDTPAIDGGYYL------TGDT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 515 AQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRD 594
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQL 401
|
490 500 510
....*....|....*....|....*....|.
gi 499204776 595 HVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
88-627 |
2.07e-69 |
|
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: 235.47 E-value: 2.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 88 NVAHNTVDRHAsvdAGTRNHVACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIF 167
Cdd:cd05970 17 NFAYDVVDAMA---KEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 168 KIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGflrrgdrVTLMDTLNDAIERAGHVDhtivydRLGIPADSLswtpR 247
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE-------DNIPEEIEKAAPECPSKP------KLVWVGDPV----P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 248 DEW--WDDAVATQSPTFETHSMAAS----DPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEIHfgfDQRPGDRFCWVS 319
Cdd:cd05970 157 EGWidFRKLIKNASPDFERPTANSYpcgeDILLVYFSSGTTGMPKMVEHDFTYPLghIVTAKYWQ---NVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 320 DIGWMMGPWSLIGNHAFAGTIV-MYEGapDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDhgdEHVAGHDLSSLRILGS 398
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVfVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 399 TGEPWDPESWRWFYDHVGggdTPIINISGGTEVFGCfLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLV 478
Cdd:cd05970 309 AGEALNPEVFNTFKEKTG---IKLMEGFGQTETTLT-IATFPWMEPKPGSMGKPAPGYEIDLIDREGRSC-EAGEEGEIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 479 ARSSSP---SMTRRLWSGEDRYLEAYwsrFEDVWNHGDWAQMDADGD-WFLhGRADDAINVAGRKVGPAEVEGALIDHDA 554
Cdd:cd05970 384 IRTSKGkpvGLFGGYYKDAEKTAEVW---HDGYYHTGDAAWMDEDGYlWFV-GRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 555 VTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKlVRRA 627
Cdd:cd05970 460 VLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGK-IRRV 531
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
116-625 |
2.50e-68 |
|
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: 231.49 E-value: 2.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:cd05959 24 IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGDGFLRRgdrvtlmdtLNDAIERAGHVDHTIVYDRlgiPADSLSWTPrdeWWDDAVATQSPTFETHSMAASDPCML 275
Cdd:cd05959 104 VVVVSGELAPV---------LAAALTKSEHTLVVLIVSG---GAGPEAGAL---LLAELVAAEAEQLKPAATHADDPAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHAGalVQPAKEiHFGFD---QRPGDRFCWVSDIGWMMGpwslIGNH-----AFAGTIVMYegaP 347
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHAD--IYWTAE-LYARNvlgIREDDVCFSAAKLFFAYG----LGNSltfplSVGATTVLM---P 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPAPDRFWQLIEDHGITQFGVSPTAIRALRdhGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISG 427
Cdd:cd05959 239 ERPTPAAVFKRIRRYRPTVFFGVPTLYAAML--AAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 428 GTEVFGCFLMPLPtESLKPCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSssPSMTRRLWSGED---RYLEAYWSR 504
Cdd:cd05959 314 STEMLHIFLSNRP-GRVRYGTTGKPVPGYEVELRDEDGGDVADG-EPGELYVRG--PSSATMYWNNRDktrDTFQGEWTR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 505 fedvwnHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATP 584
Cdd:cd05959 390 ------TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYED 463
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499204776 585 SAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd05959 464 SEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
94-623 |
4.22e-68 |
|
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: 229.03 E-value: 4.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 94 VDRHASVDAgtrNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIA 173
Cdd:cd17631 1 LRRRARRHP---DRTALVFGG-----RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 174 VPIfsgfgveatATRIADAECSVVftgdgflrrgdrvtlmdtLNDAieraghvDHTIVYDrlgipadslswtprdewwdd 253
Cdd:cd17631 73 VPL---------NFRLTPPEVAYI------------------LADS-------GAKVLFD-------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 254 avatqsptfethsmaasDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIhFGFDQRPGDRF------CWVSDIGWMMGP 327
Cdd:cd17631 99 -----------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL-AALDLGPDDVLlvvaplFHIGGLGVFTLP 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 328 WSLIGnhafaGTIVMyegaPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWdPES 407
Cdd:cd17631 161 TLLRG-----GTVVI----LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PER 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 408 WRWFYDHVGggdTPIINISGGTEVFGCFLMPLPTESL-KPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssPSM 486
Cdd:cd17631 229 LLRALQARG---VKFVQGYGMTETSPGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREV-PPGEVGEIVVRG--PHV 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 487 TRRLWSGEDRYLEAywsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPD 565
Cdd:cd17631 303 MAGYWNRPEATAAA----FRDGWFHtGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPD 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 566 DTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKL 623
Cdd:cd17631 379 EKWGEAVVAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
106-627 |
1.42e-66 |
|
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: 225.91 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveat 185
Cdd:cd05936 14 DKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 atriadaecSVVFTGDGflrrgdrvtLMDTLNDAIERAGHVDHTivydrlgipadslswtprdewWDDAVATQSPTFETH 265
Cdd:cd05936 80 ---------NPLYTPRE---------LEHILNDSGAKALIVAVS---------------------FTDLLAAGAPLGERV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 266 SMAASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEI--HFGFDQRPGDRFcwvsdigwmMGPWSLIgnHAFAGTIVM- 342
Cdd:cd05936 121 ALTPEDVAVLQYTSGTTGVPKGAMLTH-RNLVANALQIkaWLEDLLEGDDVV---------LAALPLF--HVFGLTVALl 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 343 ---YEGAP----DHPAPDRFWQLIEDHGITQF-GVsPTAIRALRDHgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDH 414
Cdd:cd05936 189 lplALGATivliPRFRPIGVLKEIRKHRVTIFpGV-PTMYIALLNA--PEFKKRDFSSLRLCISGGAPLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 415 VGGgdtPIINISGGTEV--FGCFlMPLPTESlKPCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSssPSMTRrlws 492
Cdd:cd05936 266 TGV---PIVEGYGLTETspVVAV-NPLDGPR-KPGSIGIPLPGTEVKIVDDDGEELPPG-EVGELWVRG--PQVMK---- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 493 gedryleAYWSR-------FEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVP 564
Cdd:cd05936 334 -------GYWNRpeetaeaFVDGWLRtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVP 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499204776 565 DDTTGEAAIAYVILADAATPSA-ELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd05936 407 DPYSGEAVKAFVVLKEGASLTEeEIIAFCREQL--AGYK--VPRQVEFRDELPKSAVGKILRRE 466
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
120-629 |
1.55e-64 |
|
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: 219.66 E-value: 1.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSgfgveatatriadaecsvvf 198
Cdd:cd05958 9 REWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 tgdgFLRRGDRvtlmdtlnDAIERAGHVDHTIVYDRLgipadslswtprdewwddavatqsptfethsMAASDPCMLLYS 278
Cdd:cd05958 69 ----LLRPKEL--------AYILDKARITVALCAHAL-------------------------------TASDDICILAFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHagalvQPAKEIHFGFDQ-----RPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMYEGApdhpAP 352
Cdd:cd05958 106 SGTTGAPKATMHFH-----RDPLASADRYAVnvlrlREDDRFVGSPPLAFTFGlGGVLLFPFGVGASGVLLEEA----TP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 353 DRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVF 432
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 433 GCFLMPLPtESLKPCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSssPSMTRRLWSGEDRyleaywSRFEDVWNH- 511
Cdd:cd05958 252 HIFISARP-GDARPGATGKPVPGYEAKVVDDEGNPVPDG-TIGRLAVRG--PTGCRYLADKRQR------TYVQGGWNIt 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 512 GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAE 591
Cdd:cd05958 322 GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARE 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 499204776 592 LRDHVgDAHGKPF-RPREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:cd05958 402 LQDHA-KAHIAPYkYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
118-623 |
1.71e-64 |
|
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: 220.55 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 118 TVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVV 197
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 198 FT-GDGFlrrgdrvtlmDTLNDAIERAGHVDHTIVY----DRLGIPADSLSWTPRDEWWDDavatqsPTFETHSmaASDP 272
Cdd:cd05911 87 FTdPDGL----------EKVKEAAKELGPKDKIIVLddkpDGVLSIEDLLSPTLGEEDEDL------PPPLKDG--KDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 273 CMLLYSSGTTGTPKGIVHTHAG---ALVQPAKeiHFGFDQRPGDRFCWVSDIGWMMGPWSLIgNHAFAG--TIVMyegap 347
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNliaNLSQVQT--FLYGNDGSNDVILGFLPLYHIYGLFTTL-ASLLNGatVIIM----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPwdpeSWRWFYDHVG--GGDTPIINI 425
Cdd:cd05911 221 PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAP----LSKELQELLAkrFPNATIKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 426 SGGTEVfGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMtrrlWSGedryleaYW--- 502
Cdd:cd05911 295 YGMTET-GGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRG--PQV----MKG-------YYnnp 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 503 -----SRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYV 576
Cdd:cd05911 361 eatkeTFDEDGWLHtGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYV 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499204776 577 ILADAATPSAElraELRDHVGD--AHGKPFRPReVVFVDDLPKTQSGKL 623
Cdd:cd05911 441 VRKPGEKLTEK---EVKDYVAKkvASYKQLRGG-VVFVDEIPKSASGKI 485
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
14-640 |
4.43e-64 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 225.34 E-value: 4.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 14 PDPALASSTNVAQFMTAHD-----------IDDVDALRERSTTDLDWFWGELPEYLGLEFFEDYDAVRDDADDP-QSTAW 81
Cdd:PLN03052 89 PSPEIAKLTNLGRLLEARGkellgskykdpISSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESnPGGQW 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 82 YPGAELNVAHN--TVDRHASVDAgtrnhVACIW--EGEDGT-VRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMV 156
Cdd:PLN03052 169 LPGAVLNVAECclTPKPSKTDDS-----IAIIWrdEGSDDLpVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 157 PEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAieRAGHVdhtIVydrlg 236
Cdd:PLN03052 244 VHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA--KAPKA---IV----- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 237 IPAD--SLSWTPR--DEWWDDAVATQSPTFETHSMAASDPCM-----LLYSSGTTGTPKGIVHTHAGALvQPAKEIHFGF 307
Cdd:PLN03052 314 LPADgkSVRVKLRegDMSWDDFLARANGLRRPDEYKAVEQPVeaftnILFSSGTTGEPKAIPWTQLTPL-RAAADAWAHL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 308 DQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPApdrFWQLIEDHGITQFGVSPTAIRALRDHGdeHVAG 387
Cdd:PLN03052 393 DIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRG---FAKFVQDAKVTMLGTVPSIVKTWKNTN--CMAG 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 388 HDLSSLRILGSTGEPWDPESWRWFYDHvgGGDTPIINISGGTEVFGCFLmplpTES-LKPCTLG---GPGLGMDIDIVDD 463
Cdd:PLN03052 468 LDWSSIRCFGSTGEASSVDDYLWLMSR--AGYKPIIEYCGGTELGGGFV----TGSlLQPQAFAafsTPAMGCKLFILDD 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 464 DGTSV-RDANERGYLVARSSSPSMTRRLWSGeDRYlEAYWSRFEdVWN------HGDWAQMDADGDWFLHGRADDAINVA 536
Cdd:PLN03052 542 SGNPYpDDAPCTGELALFPLMFGASSTLLNA-DHY-KVYFKGMP-VFNgkilrrHGDIFERTSGGYYRAHGRADDTMNLG 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 537 GRKVGPAEVE----GAlidHDAVTQAAVVGVPDDTTG--EAAIAYVILADA-ATPSA-ELRAELRDHVGDAHGKPFRPRE 608
Cdd:PLN03052 619 GIKVSSVEIErvcnAA---DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPgSNPDLnELKKIFNSAIQKKLNPLFKVSA 695
|
650 660 670
....*....|....*....|....*....|..
gi 499204776 609 VVFVDDLPKTQSGKLVRRAVASAYTGADVTDR 640
Cdd:PLN03052 696 VVIVPSFPRTASNKVMRRVLRQQLAQELSRSK 727
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
116-629 |
3.44e-63 |
|
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: 217.57 E-value: 3.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGDGflrrgdrvtlmdTLNDAIERAGHVDHTIVydRLGIPADSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCML 275
Cdd:cd05926 89 LVLTPKG------------ELGPASRAASKLGLAIL--ELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDR-FCwvsdigwMMgPW--------SLIGNHAFAGTIVMyega 346
Cdd:cd05926 155 LHTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRtLV-------VM-PLfhvhglvaSLLSTLAAGGSVVL---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 347 PDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINIS 426
Cdd:cd05926 222 PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPN-PESPPPKLRFIRSCSASLPPAVLEALEATFG---APVLEAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEVfgCFLM---PLPTESLKPCTLGgPGLGMDIDIVDDDGTSVRDANErGYLVARSssPSMTRRLWSGEDRYLEAYws 503
Cdd:cd05926 298 GMTEA--AHQMtsnPLPPGPRKPGSVG-KPVGVEVRILDEDGEILPPGVV-GEICLRG--PNVTRGYLNNPEANAEAA-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 504 rFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAA 582
Cdd:cd05926 370 -FKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499204776 583 TPS-AELRAELRDHVGDahgkpFR-PREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:cd05926 449 SVTeEELRAFCRKHLAA-----FKvPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
120-625 |
3.08e-62 |
|
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: 213.48 E-value: 3.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmAASDPCMLLYSS 279
Cdd:cd05919 89 --------------------------------------------------------------------SADDIAYLLYSS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGALVQP---AKEIhfgFDQRPGDRFCWVSDI--GWMMGPwSLIGNHAFAGTIVMYEGAPDhpaPDR 354
Cdd:cd05919 101 GTTGPPKGVMHAHRDPLLFAdamAREA---LGLTPGDRVFSSAKMffGYGLGN-SLWFPLAVGASAVLNPGWPT---AER 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 355 FWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGgdtPIINISGGTEVFGC 434
Cdd:cd05919 174 VLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFGG---PILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 435 FLMPLPTEsLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssPSMTRRLWsgedRYLEAYWSRFEDVW-NHGD 513
Cdd:cd05919 249 FLSNRPGA-WRLGSTGRPVPGYEIRLVDEEGHTI-PPGEEGDLLVRG--PSAAVGYW----NNPEKSRATFNGGWyRTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 514 WAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELR 593
Cdd:cd05919 321 KFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIH 400
|
490 500 510
....*....|....*....|....*....|..
gi 499204776 594 DHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
153-626 |
4.55e-55 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 195.42 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 153 MPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLndaIERAGHVdhTIVY 232
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKV---VEAAPAK--AIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 233 DRLGIPAdSLSWTPRDEWWDDAVATQSPT-------FETHSMAASDPCMLLYSSGTTGTPKGIVHTHagalVQPAKEIHF 305
Cdd:PLN03051 76 PAAGEPV-AVPLREQDLSWCDFLGVAAAQgsvggneYSPVYAPVESVTNILFSSGTTGEPKAIPWTH----LSPLRCASD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 306 GF---DQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPApdrFWQLIEDHGITQFGVSPTAIRALRDHGD 382
Cdd:PLN03051 151 GWahmDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 383 EHVAGHDLSSLRILGSTGEPWDPESWRWFYDhVGGGDTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVD 462
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDVLWLSS-VRGYYKPVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 463 DDGTSVRDANERGYLVARsSSPSM--TRRLWSGEDR--YLEA---YWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINV 535
Cdd:PLN03051 307 DNGVPYPDDQPCVGEVAL-APPMLgaSDRLLNADHDkvYYKGmpmYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 536 AGRKVGPAEVEGALIDHDA-VTQAAVVGVPDDTTGEAAIAYVILA-------DAATPsAELRAELRDHVGDAHGKPFRPR 607
Cdd:PLN03051 386 GGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGPELLVIFLVLgeekkgfDQARP-EALQKKFQEAIQTNLNPLFKVS 464
|
490
....*....|....*....
gi 499204776 608 EVVFVDDLPKTQSGKLVRR 626
Cdd:PLN03051 465 RVKIVPELPRNASNKLLRR 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
120-627 |
4.06e-54 |
|
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: 193.82 E-value: 4.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIavPIFSGFG------------VEATAT 187
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFALPAhrraeishfaeqSEAVAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 188 RIADAEcsvvftgDGFlrrgDRVTLMDTLNdaiERAGHVDHTIVydrLGIPADSLSWtprDEWWDDAVATQSPTfethsM 267
Cdd:COG1021 127 IIPDRH-------RGF----DYRALARELQ---AEVPSLRHVLV---VGDAGEFTSL---DALLAAPADLSEPR-----P 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 268 AASDPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEIhFGFDqrPGDRFCWVSDIG--WMMGPWSLIGNHAFAGTIVMy 343
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLysVRASAEI-CGLD--ADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVL- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 344 egAPDhPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPESWRWFydhvgggdtpii 423
Cdd:COG1021 258 --APD-PSPDTAFPLIERERVTVTALVPPLALLWLDAAERS--RYDLSSLRVLQVGGAKLSPELARRV------------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 424 nisggTEVFGCFL-----MplpTESLKPCT-LGGP--------GLGM----DIDIVDDDGTSVRDAnERGYLVARS---- 481
Cdd:COG1021 321 -----RPALGCTLqqvfgM---AEGLVNYTrLDDPeevilttqGRPIspddEVRIVDEDGNPVPPG-EVGELLTRGpyti 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 482 ----SSPSMTRRLWSgEDRYleaYWSrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ 557
Cdd:COG1021 392 rgyyRAPEHNARAFT-PDGF---YRT--------GDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 558 AAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHvGDAHGKpfRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:COG1021 460 AAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRER-GLAAFK--LPDRLEFVDALPLTAVGKIDKKA 526
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-626 |
5.37e-53 |
|
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: 187.88 E-value: 5.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 119 VRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVF 198
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 TgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaasDPCMLLYS 278
Cdd:cd05934 81 V-----------------------------------------------------------------------DPASILYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRfCWVSDIGWMMGP--WSLIGNHAFAGTIVMYEGApdhpAPDRFW 356
Cdd:cd05934 90 SGTTGPPKGVVITHANLTFAGYYSARR-FGLGEDDV-YLTVLPLFHINAqaVSVLAALSVGATLVLLPRF----SASRFW 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 357 QLIEDHGITQFGVSPTAIRAL---------RDHgdehvaghdlsSLRILGstGEPWDPESWRWFYDHVGggdTPIINISG 427
Cdd:cd05934 164 SDVRRYGATVTNYLGAMLSYLlaqppspddRAH-----------RLRAAY--GAPNPPELHEEFEERFG---VRLLEGYG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 428 GTEVFGCFLMPLPtESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVARSSSP-SMTRRLWSGEDRYLEAywsrFE 506
Cdd:cd05934 228 MTETIVGVIGPRD-EPRRPGSIGRPAPGYEVRIVDDDGQELPA-GEPGELVIRGLRGwGFFKGYYNMPEATAEA----MR 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 507 DVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPS 585
Cdd:cd05934 302 NGWFHtGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD 381
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499204776 586 -AELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:cd05934 382 pEELFAFCEGQL--AYFK--VPRYIRFVDDLPKTPTEKVAKA 419
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
106-627 |
7.61e-52 |
|
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: 185.42 E-value: 7.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT 185
Cdd:cd05930 2 DAVAVVDGD-----QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSVVFTGdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfeth 265
Cdd:cd05930 77 AYILEDSGAKLVLTD----------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 266 smaASDPCMLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyeg 345
Cdd:cd05930 92 ---PDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVV--- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 APD--HPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaghDLSSLRILGSTGEPWDPESWRWFYDHvgGGDTPII 423
Cdd:cd05930 165 LPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWREL--LPGARLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 424 NISGGTEVFGC---FLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRD--ANE---------RGYLvarsSSPSMTRR 489
Cdd:cd05930 239 NLYGPTEATVDatyYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPgvPGElyiggaglaRGYL----NRPELTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 490 lwsgedryleaywsRFEDVWNH--------GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVV 561
Cdd:cd05930 315 --------------RFVPNPFGpgermyrtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVV 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 562 GVPDDTTGEAAIAYVILADAATPS-AELRAELRDHVgdahgkPF--RPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd05930 381 AREDGDGEKRLVAYVVPDEGGELDeEELRAHLAERL------PDymVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
120-635 |
3.23e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 185.52 E-value: 3.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGflrrgdrvtLMDTLNDAIERAGHVDhTIVYDRLGIPADSLSWTPRDEWwddAVATQSPTFETHsMAASDPCMLLYSS 279
Cdd:PRK08316 115 DPA---------LAPTAEAALALLPVDT-LILSLVLGGREAPGGWLDFADW---AEAGSVAEPDVE-LADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGALVQPAKEIHFGfDQRPGDRF--------CWVSDIgwMMGPWSLIGnhafAGTIVMyegapDHPA 351
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSCIVAG-DMSADDIPlhalplyhCAQLDV--FLGPYLYVG----ATNVIL-----DAPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 352 PDRFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLR--ILGSTGEPWDP-ESWRWFYDHVGggdtpIINISGG 428
Cdd:PRK08316 249 PELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLRkgYYGASIMPVEVlKELRERLPGLR-----FYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 429 TEVfgcflMPL-----PTESL-KPCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSssPSMTRRLWSGEDRYLEAyw 502
Cdd:PRK08316 322 TEI-----APLatvlgPEEHLrRPGSAGRPVLNVETRVVDDDGNDVAPG-EVGEIVHRS--PQLMLGYWDDPEKTAEA-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 503 srFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADA 581
Cdd:PRK08316 392 --FRGGWFHsGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 582 ATPSAElraELRDHVgDAHGKPFR-PREVVFVDDLPKTQSGKLVRRAVASAYTGA 635
Cdd:PRK08316 470 ATVTED---ELIAHC-RARLAGFKvPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
123-623 |
5.22e-51 |
|
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: 182.97 E-value: 5.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FlRRGDRVTLMDtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaasDPCMLLYSSGTT 282
Cdd:cd05903 83 F-RQFDPAAMPD--------------------------------------------------------AVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGALVQPAKEI-HFGFDqrPGDRFcwvsdigWMMGPWSLIGNHAFAGTIVMYEGAPDHPA----PDRFWQ 357
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAeRLGLG--PGDVF-------LVASPMAHQTGFVYGFTLPLLLGAPVVLQdiwdPDKALA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 358 LIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDPESWRWFYDhvgGGDTPIINISGGTEVFGCFLM 437
Cdd:cd05903 177 LMREHGVTFMMGATPFLTDLLNAVEE--AGEPLSRLRTFVCGGATVPRSLARRAAE---LLGAKVCSAYGSTECPGAVTS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 438 PLPTESLKP-CTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssPSM-----TRRLWSGEDryleaywsrFEDVW-N 510
Cdd:cd05903 252 ITPAPEDRRlYTDGRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSVflgylDRPDLTADA---------APEGWfR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 511 HGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRA 590
Cdd:cd05903 320 TGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELV 399
|
490 500 510
....*....|....*....|....*....|...
gi 499204776 591 ELRDHVGDAhgKPFRPREVVFVDDLPKTQSGKL 623
Cdd:cd05903 400 AYLDRQGVA--KQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
106-627 |
9.07e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.95 E-value: 9.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGF-GVEA 184
Cdd:PRK07656 20 DKEAYVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 185 tATRIADAECSVVFTGDGFLrrgdrvtlmDTLNDAIERAGHVDHTIVYDrlgiPADSLSWTPRDEWWDDAVATQSPTFET 264
Cdd:PRK07656 95 -AYILARGDAKALFVLGLFL---------GVDYSATTRLPALEHVVICE----TEEDDPHTEKMKTFTDFLAAGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 265 HSMAASDPCMLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFcwvsdigwmmgpwsLIGN---HAFA---- 337
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHR-QLLSNAADWAEYLGLTEGDRY--------------LAANpffHVFGykag 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 338 --------GTIVMyegapdHP--APDRFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILGStgepwdpes 407
Cdd:PRK07656 226 vnaplmrgATILP------LPvfDPDEVFRLIETERITVLPGPPTMYNSLLQH--PDRSAEDLSSLRLAVT--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 408 wrwfydhvGGGDTPIINIS---------------GGTEV--FGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrD 470
Cdd:PRK07656 289 --------GAASMPVALLErfeselgvdivltgyGLSEAsgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEV-P 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 471 ANERGYLVARSssPSMTRRLWSGEDRYLEAYWSrfeDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGAL 549
Cdd:PRK07656 360 VGEVGELLVRG--PNVMKGYYDDPEATAAAIDA---DGWLHtGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVL 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 550 IDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAE-LRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:PRK07656 435 YEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEeLIAYCREHL--AKYK--VPRSIEFLDELPKNATGKVLKRA 509
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
123-635 |
5.34e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 184.39 E-value: 5.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGaIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLrrgdRVTLMDTLNDAIERAGHVDHTIVYDRLGIPADSLSWTPRDEW---------WDDAVATQSPT--FETHSMAASD 271
Cdd:PRK07529 139 FP----GTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRrkaharildFDAELARQPGDrlFSGRPIGPDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 272 PCMLLYSSGTTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGD-RFCWV------SDIGWMMGPWSLiGNHAFAGTIVmye 344
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLGALLLGLGPGDtVFCGLplfhvnALLVTGLAPLAR-GAHVVLATPQ--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 345 GAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRdhgDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIIN 424
Cdd:PRK07529 290 GYRGPGVIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATG---VRIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 425 ISGGTEVFGCFLMPLPTESLKPCTLGG--PGLGMDIDIVDDDGTSVRDA--NERGYLVArsSSPSmtrrLWSGedrYLEA 500
Cdd:PRK07529 364 GYGLTEATCVSSVNPPDGERRIGSVGLrlPYQRVRVVILDDAGRYLRDCavDEVGVLCI--AGPN----VFSG---YLEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 501 YWSR---FEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYV 576
Cdd:PRK07529 435 AHNKglwLEDGWlNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 577 IL-ADAATPSAELRAELRDHVGD--AHgkpfrPREVVFVDDLPKTQSGK-----LVRRAVASAYTGA 635
Cdd:PRK07529 515 QLkPGASATEAELLAFARDHIAEraAV-----PKHVRILDALPKTAVGKifkpaLRRDAIRRVLRAA 576
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
88-625 |
5.81e-50 |
|
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: 181.58 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 88 NVAHNTVDRhaSVDAGTRNHVACIwegedGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIF 167
Cdd:TIGR02262 4 NAAEDLLDR--NVVEGRGGKTAFI-----DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 168 KIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLrrgdrvtlmDTLNDAIERAGHVDHTIVYDRLGIPADSLSwtpr 247
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGKSPHLEHRVVVGRPEAGEVQLA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 248 dewwdDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGp 327
Cdd:TIGR02262 144 -----ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYG- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 328 wslIGNHAF-----AGTIVMYegaPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRdhGDEHVAGHDLSSLRILGSTGEP 402
Cdd:TIGR02262 218 ---LGNALTfpmsvGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 403 WDPESWRWFYDHVGggdTPIINISGGTEVFGCFLMPLPtESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSS 482
Cdd:TIGR02262 290 LPAEVGQRWQARFG---VDIVDGIGSTEMLHIFLSNLP-GDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 483 SPSM-------TRRLWSGEdryleayWSRfedvwnHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAV 555
Cdd:TIGR02262 366 SATMywnnrakSRDTFQGE-------WTR------SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAV 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 556 TQAAVVGVPDDTTGEAAIAYVILADAATpsaELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:TIGR02262 433 LEAAVVGVADEDGLIKPKAFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
96-627 |
4.16e-48 |
|
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: 176.67 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 96 RHASVDAGTRNHVACiweGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVP 175
Cdd:cd12119 3 EHAARLHGDREIVSR---THEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 176 IFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTlmdtlndaiERAGHVDHTIVY-DRLGIPADSLswtPRDEWWDDA 254
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIA---------PRLPTVEHVVVMtDDAAMPEPAG---VGVLAYEEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 255 VATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTH------AGALVQPakeIHFGFDQrpgdrfcwvSDIGWMMGP- 327
Cdd:cd12119 148 LAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHrslvlhAMAALLT---DGLGLSE---------SDVVLPVVPm 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 328 -----WSLignhAFAGTIVmyeGAP-----DHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILG 397
Cdd:cd12119 216 fhvnaWGL----PYAAAMV---GAKlvlpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEAN--GRDLSSLRRVV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 398 STGEPWDPESWRWFYDHvgggDTPIINISGGTEV--FGCFLMPLPTESLKP--------CTLGGPGLGMDIDIVDDDGTS 467
Cdd:cd12119 287 IGGSAVPRSLIEAFEER----GVRVIHAWGMTETspLGTVARPPSEHSNLSedeqlalrAKQGRPVPGVELRIVDDDGRE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 468 V-RDANERGYLVARSssPSMTRRLWSGEDRyLEAYWsrfEDVWNH-GDWAQMDADGdwFLH--GRADDAINVAGRKVGPA 543
Cdd:cd12119 363 LpWDGKAVGELQVRG--PWVTKSYYKNDEE-SEALT---EDGWLRtGDVATIDEDG--YLTitDRSKDVIKSGGEWISSV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 544 EVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKL 623
Cdd:cd12119 435 ELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKI 511
|
....
gi 499204776 624 VRRA 627
Cdd:cd12119 512 DKKA 515
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
107-628 |
6.40e-48 |
|
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: 175.61 E-value: 6.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 107 HVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATA 186
Cdd:cd17651 11 APALVAEG-----RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 187 TRIADAECSVVFTGDGFLrrgdrvtlmdtlndaieraghvdhtivyDRLGIPADSLSWTPRDEWWDDAVAtqSPTFETHs 266
Cdd:cd17651 86 FMLADAGPVLVLTHPALA----------------------------GELAVELVAVTLLDQPGAAAGADA--EPDPALD- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 maASDPCMLLYSSGTTGTPKGIVHTHAGA--LVQPAKEIhfgFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMye 344
Cdd:cd17651 135 --ADDLAYVIYTSGSTGRPKGVVMPHRSLanLVAWQARA---SSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 345 gAPDH--PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEP--WDPESWRWFYDHVGggdT 420
Cdd:cd17651 208 -PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPL--GVRLAALRYLLTGGEQlvLTEDLREFCAGLPG---L 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 PIINISGGTE---VFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPSM 486
Cdd:cd17651 282 RLHNHYGPTEthvVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPgelyiggaglaRGYL----NRPEL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 487 TRRlwsgedRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDD 566
Cdd:cd17651 358 TAE------RFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 567 TTGEAAIAYVILADAATPS-AELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd17651 432 PGEKRLVAYVVGDPEAPVDaAELRAALATHLPEY----MVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
120-622 |
2.89e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 171.99 E-value: 2.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFlrrGDRVTlmdtlnDAIERAGHVDHTIVydrlgIPADSLSWTPRD-EWWDDAVATQSPT--FETHSmaaSDPCMLL 276
Cdd:PRK07798 107 EREF---APRVA------EVLPRLPKLRTLVV-----VEDGSGNDLLPGaVDYEDALAAGSPErdFGERS---PDDLYLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 277 YSSGTTGTPKGIVHTHA--------------GALVQPAKEIHFGFDQRPGDRFCwvsDIGWMM---GPWSLIGNHAFAGT 339
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQEdifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRF---PAPPLMhgaGQWAAFAALFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 340 IVMYEGapDHPAPDRFWQLIEDHGITQFGVSPTA-----IRALRDHGdehvaGHDLSSLRILGSTGEPWDPESWRWFYDH 414
Cdd:PRK07798 247 VVLLPD--VRFDADEVWRTIEREKVNVITIVGDAmarplLDALEARG-----PYDLSSLFAIASGGALFSPSVKEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 415 VgggdtP---IINISGGTEV-FGCFLMPLPTESlkpcTLGGP--GLGMDIDIVDDDGTSVRDANERGYLVARSSS----- 483
Cdd:PRK07798 320 L-----PnvvLTDSIGSSETgFGGSGTVAKGAV----HTGGPrfTIGPRTVVLDEDGNPVEPGSGEIGWIARRGHiplgy 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 ---PSMTRRLW---SGEdRYLEAywsrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ 557
Cdd:PRK07798 391 ykdPEKTAETFptiDGV-RYAIP-----------GDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 558 AAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVgDAHGKPFR-PREVVFVDDLPKTQSGK 622
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHC-RSSLAGYKvPRAIWFVDEVQRSPAGK 520
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
105-626 |
3.07e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 172.03 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 105 RNHVACIweGEDGTVrqqTYHDLHQQANRVANALAERGIGEGDTVGLympMVPEVQSILYGIFKIGAIAVPIF---SGFG 181
Cdd:PRK07788 63 PDRAALI--DERGTL---TYAELDEQSNALARGLLALGVRAGDGVAV---LARNHRGFVLALYAAGKVGARIIllnTGFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 182 VEATATRIADAECSVVFTGDGFlrrgdrVTLMDTLNDAIERAghvdHTIVYDRLGIPADslswTPRDEWWDDAVATQS-- 259
Cdd:PRK07788 135 GPQLAEVAAREGVKALVYDDEF------TDLLSALPPDLGRL----RAWGGNPDDDEPS----GSTDETLDDLIAGSSta 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 260 --PTFETHSMaasdpcMLLYSSGTTGTPKGIVHTHAGALVQPAKEIhfgfdqrpgDRFCWVSDI----------GWMMGP 327
Cdd:PRK07788 201 plPKPPKPGG------IVILTSGTTGTPKGAPRPEPSPLAPLAGLL---------SRVPFRAGEttllpapmfhATGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 328 WSLIgnHAFAGTIVMYEgapdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPES 407
Cdd:PRK07788 266 LTLA--MALGSTVVLRR----RFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 408 WRWFYDHVGggdtPII-NISGGTEVFGCfLMPLPTE-SLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSPs 485
Cdd:PRK07788 340 ATRALEAFG----PVLyNLYGSTEVAFA-TIATPEDlAEAPGTVGRPPKGVTVKILDENGNEV-PRGVVGRIFVGNGFP- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 mtrrlwsgedryLEAYWS-----RFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAV 560
Cdd:PRK07788 413 ------------FEGYTDgrdkqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 561 VGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK07788 481 IGVDDEEFGQRLRAFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKR 543
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
85-625 |
7.90e-45 |
|
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: 167.64 E-value: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 85 AELNVAHNTVDRHASVD-AGTR-NHVACIWEGEDGTVRQQTYHDLHQQANRVANALAER-GIGEGDTVGLYMPMVPEVQS 161
Cdd:cd05928 3 EYFNFASDVLDQWADKEkAGKRpPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 162 ILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDgflrrgdrvtlmdtlndaiERAGHVDhTIVYDRLGIPADS 241
Cdd:cd05928 83 VNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD-------------------ELAPEVD-SVASECPSLKTKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 242 L-SWTPRDEWWDDAVATQSPTFETHSM--AASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWV 318
Cdd:cd05928 143 LvSEKSRDGWLNFKELLNEASTEHHCVetGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 319 SDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPaPDRFWQLIEDHGITQFGVSPTAIRALRDhgdEHVAGHDLSSLRILGS 398
Cdd:cd05928 223 SDTGWIKSAWSSLFEPWIQGACVFVHHLPRFD-PLVILKTLSSYPITTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 399 TGEPWDP---ESWRwfydHVGGGDtpIINISGGTEVfGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGtSVRDANERG 475
Cdd:cd05928 299 GGEPLNPevlEKWK----AQTGLD--IYEGYGQTET-GLICANFKGMKIKPGSMGKASPPYDVQIIDDNG-NVLPPGTEG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 476 YLVARSSsPSMTRRLWSG-EDRYLEAYWSRFEDVWNHGDWAQMDADGD-WFLhGRADDAINVAGRKVGPAEVEGALIDHD 553
Cdd:cd05928 371 DIGIRVK-PIRPFGLFSGyVDNPEKTAATIRGDFYLTGDRGIMDEDGYfWFM-GRADDVINSSGYRIGPFEVESALIEHP 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 554 AVTQAAVVGVPDDTTGEAAIAYVILADAATPSA--ELRAELRDHVGDAHGkPFR-PREVVFVDDLPKTQSGKLVR 625
Cdd:cd05928 449 AVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDpeQLTKELQQHVKSVTA-PYKyPRKVEFVQELPKTVTGKIQR 522
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
104-627 |
7.31e-43 |
|
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: 161.21 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE-VQSILyGIFKIGAIAVPIFSGFGV 182
Cdd:cd12117 10 TPDAVAVVYGD-----RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPElVVALL-AVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 183 EATATRIADAECSVVFTgDGFLRRGDRVTLMDTLNDAIERAGhvdhtivydrlgiPADSLSwtprdewwddavatqsptf 262
Cdd:cd12117 84 ERLAFMLADAGAKVLLT-DRSLAGRAGGLEVAVVIDEALDAG-------------PAGNPA------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 263 etHSMAASDPCMLLYSSGTTGTPKGIVHTHAG--ALVQPAKEIHFGfdqrPGDRFCWVSDIGW------MMGPWsLIGnh 334
Cdd:cd12117 131 --VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGvvRLVKNTNYVTLG----PDDRVLQTSPLAFdastfeIWGAL-LNG-- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 335 afaGTIVMYEgaPDHPA-PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGhdlssLRILGSTGEPWDPESWRWFYD 413
Cdd:cd12117 202 ---ARLVLAP--KGTLLdPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG-----LRELLTGGEVVSPPHVRRVLA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 414 HVGGGDtpIINISGGTE--VFG-CFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVR-----------DANERGYLva 479
Cdd:cd12117 272 ACPGLR--LVNGYGPTEntTFTtSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPpgvpgelyvggDGLALGYL-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 480 rsSSPSMTRRlwsgedRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAA 559
Cdd:cd12117 348 --NRPALTAE------RFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAV 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 560 VVGVPDDTTGEAAIAYVIlADAATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd12117 420 VVVREDAGGDKRLVAYVV-AEGALDAAELRAFLRERLPAY----MVPAAFVVLDELPLTANGKVDRRA 482
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
109-632 |
6.84e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 158.91 E-value: 6.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 109 ACIWEGEDGTVrqqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATR 188
Cdd:PRK08276 2 AVIMAPSGEVV---TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 189 IADAECSVVFTGDGFLrrgdrvTLMDTLNDAIERAghvdhtiVYDRLGIPADSLSWTPrdewWDDAVATQSPTFETHSMA 268
Cdd:PRK08276 79 VDDSGAKVLIVSAALA------DTAAELAAELPAG-------VPLLLVVAGPVPGFRS----YEEALAAQPDTPIADETA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 269 ASDpcmLLYSSGTTGTPKGI------VHTHAGALVQPAKeIHFGFDQRPGDRFCWVSDIgWMMGPWSLIGN-HAFAGTIV 341
Cdd:PRK08276 142 GAD---MLYSSGTTGRPKGIkrplpgLDPDEAPGMMLAL-LGFGMYGGPDSVYLSPAPL-YHTAPLRFGMSaLALGGTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 MYEgapdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdtP 421
Cdd:PRK08276 217 VME----KFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWG----P 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINIS-GGTEVFGCFLMPlPTESL-KPCTLGGPGLGmDIDIVDDDGTSV-----------RDANERGYLvarsSSPSMTR 488
Cdd:PRK08276 289 IIHEYyASSEGGGVTVIT-SEDWLaHPGSVGKAVLG-EVRILDEDGNELppgeigtvyfeMDGYPFEYH----NDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 489 RLWSGEDryleayWSRFedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTT 568
Cdd:PRK08276 363 AARNPHG------WVTV------GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEM 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 569 GEAAIAYVILADAATPSAELRAELRDHVGD--AHGKpfRPREVVFVDDLPKTQSGKLVRRAVASAY 632
Cdd:PRK08276 431 GERVKAVVQPADGADAGDALAAELIAWLRGrlAHYK--CPRSIDFEDELPRTPTGKLYKRRLRDRY 494
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-622 |
6.89e-42 |
|
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: 158.62 E-value: 6.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVV-- 197
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLfv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 198 ---FTGDGFLRRGDRvtlmdtlndaieraghvdhtivyDRLGIPadslswtPRDEWwddavatqsptfethsmaasDPCM 274
Cdd:cd12118 108 dreFEYEDLLAEGDP-----------------------DFEWIP-------PADEW--------------------DPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALVQP-AKEIHFGFDQRPgdRFCWVSDI----GWMmGPWSLIgnhAFAGTIVMYegapDH 349
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHRGAYLNAlANILEWEMKQHP--VYLWTLPMfhcnGWC-FPWTVA---AVGGTNVCL----RK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 PAPDRFWQLIEDHGITQFGVSPTAIRALRDhgdehvaghdlsslrilgstgepwDPESWRWFYDH-----VGGGDTP--- 421
Cdd:cd12118 208 VDAKAIYDLIEKHKVTHFCGAPTVLNMLAN------------------------APPSDARPLPHrvhvmTAGAPPPaav 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 ----------IINISGGTEVFG----CFLMP----LPTE--SLKPCTLGGPGLGMD-IDIVDDDGT-SV-RDANERGYLV 478
Cdd:cd12118 264 lakmeelgfdVTHVYGLTETYGpatvCAWKPewdeLPTEerARLKARQGVRYVGLEeVDVLDPETMkPVpRDGKTIGEIV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 479 ARSSSpsmtrrLWSGedrYL---EAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDA 554
Cdd:cd12118 344 FRGNI------VMKG---YLknpEATAEAFRGGWFHsGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 555 VTQAAVVGVPDDTTGEAAIAYVILADAATPSA-ELRAELRDHVgdAHGKPfrPREVVFvDDLPKTQSGK 622
Cdd:cd12118 415 VLEAAVVARPDEKWGEVPCAFVELKEGAKVTEeEIIAFCREHL--AGFMV--PKTVVF-GELPKTSTGK 478
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
120-627 |
7.79e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 159.74 E-value: 7.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPevQSIL--YGIFKIGAIAVPIFSGFGVEATATRIADAECSV 196
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSP--QFVIayYAILRANAVVVPVNPMNREEELAHYVTDSGARV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 197 VFTGDgflrrgdrvTLMDTLNDAIERAGhVDHTIVYDRlgipADSLSWTPRD---EW-----------------WDDAVA 256
Cdd:PRK08314 112 AIVGS---------ELAPKVAPAVGNLR-LRHVIVAQY----SDYLPAEPEIavpAWlraepplqalapggvvaWKEALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 257 TQSPTFEtHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRFCWVSD-------IGWMMGPws 329
Cdd:PRK08314 178 AGLAPPP-HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPlfhvtgmVHSMNAP-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 330 lignhAFAG-TIVMYegapdhPAPDR--FWQLIEDHGITQFGVSPTAIRALRdhGDEHVAGHDLSSLRILGSTGEPWdPE 406
Cdd:PRK08314 254 -----IYAGaTVVLM------PRWDReaAARLIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAM-PE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 407 S-WRWFYDHVGggdTPIINISGGTEVFGcFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVArsSSPS 485
Cdd:PRK08314 320 AvAERLKELTG---LDYVEGYGLTETMA-QTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVV--HGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRRLWSGEDRYLEAYWS----RFedvWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVV 561
Cdd:PRK08314 394 VFKGYWNRPEATAEAFIEidgkRF---FRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 562 GVPDDTTGEAAIAYVILADAA--TPSAE-LRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:PRK08314 471 ATPDPRRGETVKAVVVLRPEArgKTTEEeIIAWAREHM--AAYK--YPRIVEFVDSLPKSGSGKILWRQ 535
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
107-628 |
6.54e-41 |
|
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: 155.16 E-value: 6.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 107 HVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATA 186
Cdd:cd17643 3 AVAVVDED-----RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 187 TRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfeths 266
Cdd:cd17643 78 FILADSGPSLLLT------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 mAASDPCMLLYSSGTTGTPKGIVHTHAGAL-VQPAKEIHFGFDqrPGDRFCWVSDIGWMMGPWSLIGNHAFAGT--IVMY 343
Cdd:cd17643 91 -DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQRWFGFN--EDDVWTLFHSYAFDFSVWEIWGALLHGGRlvVVPY 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 344 EGAPDhpaPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLR--ILGstGEPWDPESWRWFYDHVGGGDTP 421
Cdd:cd17643 168 EVARS---PEDFARLLRDEGVTVLNQTPSAFYQLVEAADR--DGRDPLALRyvIFG--GEALEAAMLRPWAGRFGLDRPQ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTE--VFGCFlMPLPTESLKPCT---LGGPGLGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPS 485
Cdd:cd17643 241 LVNMYGITEttVHVTF-RPLDAADLPAAAaspIGRPLPGLRVYVLDADGRPVPPGVVgelyvsgagvaRGYL----GRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MT-RRLWSGE-----DRYleaYWSrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAA 559
Cdd:cd17643 316 LTaERFVANPfggpgSRM---YRT--------GDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAA 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 560 VVGVPDDTTGEAAIAYVILADAATPS-AELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd17643 385 VIVREDEPGDTRLVAYVVADDGAAADiAELRALLKELLPDY----MVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
123-636 |
1.28e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 155.53 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSV-VFTGD 201
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTlIVDPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRGdrvtlmdtlNDAIERAGHVDHTIVYDRLGIPADSLswtprdewwdDAVATQSPTFETHSMAASDPCMLLYSSGT 281
Cdd:PRK06188 119 PFVERA---------LALLARVPSLKHVLTLGPVPDGVDLL----------AAAAKFGPAPLVAAALPPDIAGLAYTGGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 282 TGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDI----GWMMGPWSLIGnhafaGTIVMYEGApdhpAPDRFWQ 357
Cdd:PRK06188 180 TGKPKGVMGTH-RSIATMAQIQLAEWEWPADPRFLMCTPLshagGAFFLPTLLRG-----GTVIVLAKF----DPAEVLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 358 LIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdtPII-NISGGTEVFGCFL 436
Cdd:PRK06188 250 AIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSPVRLAEAIERFG----PIFaQYYGQTEAPMVIT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 437 -------MPLPTESLKPCtlGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssPSMTRRLWSGEDRYLEAywsrFEDVW 509
Cdd:PRK06188 324 ylrkrdhDPDDPKRLTSC--GRPTPGLRVALLDEDGREV-AQGEVGEICVRG--PLVMDGYWNRPEETAEA----FRDGW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 510 NH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAel 588
Cdd:PRK06188 395 LHtGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA-- 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499204776 589 rAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAY-TGAD 636
Cdd:PRK06188 473 -AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYwEGRG 520
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
104-626 |
4.12e-40 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 153.58 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:PRK03640 15 TPDRTAIEFEEK-----KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAECSVVFTGDGFLRR--GDRVTLMDTLNDAIERAGhvdhtivydrlgipadslswTPRDEWWDDAVATqspt 261
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKliPGISVKFAELMNGPKEEA--------------------EIQEEFDLDEVAT---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 262 fethsmaasdpcmLLYSSGTTGTPKGIVHT---HAGALVQPAkeIHFGFDqrpgDRFCW--------VSDIGWMMGpwSL 330
Cdd:PRK03640 146 -------------IMYTSGTTGKPKGVIQTygnHWWSAVGSA--LNLGLT----EDDCWlaavpifhISGLSILMR--SV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 331 IgnhaFAGTIVMYEgapdHPAPDRFWQLIEDHGITQFGVSPTAIRalrdhgdehvaghdlsslRILGSTGEPWDPESWRW 410
Cdd:PRK03640 205 I----YGMRVVLVE----KFDAEKINKLLQTGGVTIISVVSTMLQ------------------RLLERLGEGTYPSSFRC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 411 FYdhVGGG-------------DTPIINISGGTEVFGCFLMPLPTESL-KPCTLGGPGLGMDIDIVDDdgTSVRDANERGY 476
Cdd:PRK03640 259 ML--LGGGpapkplleqckekGIPVYQSYGMTETASQIVTLSPEDALtKLGSAGKPLFPCELKIEKD--GVVVPPFEEGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 477 LVARSssPSMTRRLWSGEDRYLEAywsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAV 555
Cdd:PRK03640 335 IVVKG--PNVTKGYLNREDATRET----FQDGWFKtGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 556 TQAAVVGVPDDTTGEAAIAYVILaDAATPSAELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK03640 409 AEAGVVGVPDDKWGQVPVAFVVK-SGEVTEEELRHFCEEKL--AKYK--VPKRFYFVEELPRNASGKLLRH 474
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
123-626 |
6.82e-40 |
|
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: 153.16 E-value: 6.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAI---AVPIFSgfgVEATATRIADAECSVVFT 199
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVvttANPLST---PAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLRR----GDRVTLMDTlndaieragHVDHTIVYDRLGIPADSLSwTPRDEwwddavatqsptfethsMAASDPCML 275
Cdd:cd05904 111 TAELAEKlaslALPVVLLDS---------AEFDSLSFSDLLFEADEAE-PPVVV-----------------IKQDDVAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDR--------FCWVSDIGWMMgpwsLIGNHAFAGTIVMyegaP 347
Cdd:cd05904 164 LYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGSNSDSEdvflcvlpMFHIYGLSSFA----LGLLRLGATVVVM----P 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPAPDrFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWRWF---YDHVgggdtPIIN 424
Cdd:cd05904 235 RFDLEE-LLAAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPLGKELIEAFrakFPNV-----DLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 425 ISGGTEVFGCFLMPLPTESLkPCTLGGPGL---GMDIDIVDDDGTSVRDANERGYLVARSssPSMTRrlwsGedrYL--- 498
Cdd:cd05904 307 GYGMTESTGVVAMCFAPEKD-RAKYGSVGRlvpNVEAKIVDPETGESLPPNQTGELWIRG--PSIMK----G---YLnnp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 499 EAYWSRF-EDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYV 576
Cdd:cd05904 377 EATAATIdKEGWLHtGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499204776 577 ILADAATPSAElraELRDHVGD--AHGKpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:cd05904 457 VRKPGSSLTED---EIMDFVAKqvAPYK--KVRKVAFVDAIPKSPSGKILRK 503
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
82-635 |
1.32e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 152.54 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 82 YPGaelNVAHNTVDRHASVDAGTRNHVaciwegedgtvrqqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQS 161
Cdd:PRK13391 2 YPG---IHAQTTPDKPAVIMASTGEVV--------------TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 162 ILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGdgflrrgdrVTLMDTLNDAIERAGHVDHTIVYDRLGipaDS 241
Cdd:PRK13391 65 VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITS---------AAKLDVARALLKQCPGVRHRLVLDGDG---EL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 242 LSWTPrdewWDDAVATQSPTFETHSMAASDpcmLLYSSGTTGTPKGIVHTHA-GALVQPAKEIHFG---FDQRPGDRFCW 317
Cdd:PRK13391 133 EGFVG----YAEAVAGLPATPIADESLGTD---MLYSSGTTGRPKGIKRPLPeQPPDTPLPLTAFLqrlWGFRSDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 318 VSDIgWMMGPWSLIGN-HAFAGT-IVMyegapDHPAPDRFWQLIEDHGITQFGVSPTA-IRALRdHGDEHVAGHDLSSLR 394
Cdd:PRK13391 206 PAPL-YHSAPQRAVMLvIRLGGTvIVM-----EHFDAEQYLALIEEYGVTHTQLVPTMfSRMLK-LPEEVRDKYDLSSLE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 395 ILGSTGEPWDPESWRWFYDHVGggdtPIIN-ISGGTEVFGcFLMPLPTESL-KPCTLGGPGLGmDIDIVDDDGTSVRDAN 472
Cdd:PRK13391 279 VAIHAAAPCPPQVKEQMIDWWG----PIIHeYYAATEGLG-FTACDSEEWLaHPGTVGRAMFG-DLHILDDDGAELPPGE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 473 ------ERGYLVARSSSPSMTRrlwsgEDRYLEAYWSRFedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVE 546
Cdd:PRK13391 353 pgtiwfEGGRPFEYLNDPAKTA-----EARHPDGTWSTV------GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 547 GALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGD--AHGKPfrPREVVFVDDLPKTQSGKLV 624
Cdd:PRK13391 422 NLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQrlSRQKC--PRSIDFEDELPRLPTGKLY 499
|
570
....*....|.
gi 499204776 625 RRAVASAYTGA 635
Cdd:PRK13391 500 KRLLRDRYWGN 510
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
123-626 |
2.40e-39 |
|
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: 150.32 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FlrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaaSDPCMLLYSSGTT 282
Cdd:cd05935 83 L------------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGALVQPAKEIHfGFDQRPGD-------RFCWVSDIGWMMGPWslignhAFAGTIVMYEGAPDHPAPDrf 355
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAV-WTGLTPSDvilaclpLFHVTGFVGSLNTAV------YVGGTYVLMARWDRETALE-- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 356 wqLIEDHGITQFGVSPTAIRALRdhGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVfgcf 435
Cdd:cd05935 168 --LIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLTET---- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 436 lMPL----PTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMTRRLWSGEDRYLEAYW----SRFed 507
Cdd:cd05935 237 -MSQthtnPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIeikgRRF-- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 508 vWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILadaaTPSAE 587
Cdd:cd05935 312 -FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVL----RPEYR 386
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499204776 588 LRAELRDHVGDAHGKPF---RPREVVFVDDLPKTQSGKLVRR 626
Cdd:cd05935 387 GKVTEEDIIEWAREQMAaykYPREVEFVDELPRSASGKILWR 428
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
123-629 |
2.85e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 151.17 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAER-GIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveatATRIADAECSVVFTGD 201
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL---------NIRLTENELIFQLKDS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRGDRVTLMDTLNDAIERAGhVDHTIvydRLGIPADSLSWTPRDewwddavatqsptFETHSmaASDPCMLLYSSGT 281
Cdd:PRK06839 100 GTTVLFVEKTFQNMALSMQKVSY-VQRVI---SITSLKEIEDRKIDN-------------FVEKN--ESASFIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 282 TGTPKGIVHTHAGALVQPAKEIhFGFDQRPGDRfCWVSDIGWMMGPWSLIGNHA-FAGTIVMyegAPDHPAPDRFWQLIE 360
Cdd:PRK06839 161 TGKPKGAVLTQENMFWNALNNT-FAIDLTMHDR-SIVLLPLFHIGGIGLFAFPTlFAGGVII---VPRKFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 361 DHGIT-QFGVsPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWRWFYDH---VGGGdtpiiniSGGTEVFGCFL 436
Cdd:PRK06839 236 KHKVTvVMGV-PTIHQALINCSK--FETTNLQSVRWFYNGGAPCPEELMREFIDRgflFGQG-------FGMTETSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 437 MPLPTESL-KPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARssSPSMTRRLWSGEDRYLEAywsrFEDVWNH-GDW 514
Cdd:PRK06839 306 MLSEEDARrKVGSIGKPVLFCDYELIDENKNKV-EVGEVGELLIR--GPNVMKEYWNRPDATEET----IQDGWLCtGDL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 515 AQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRD 594
Cdd:PRK06839 379 ARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEK---DVIE 455
|
490 500 510
....*....|....*....|....*....|....*
gi 499204776 595 HVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:PRK06839 456 HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLV 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-627 |
2.85e-39 |
|
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: 150.90 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDgflrrgdrvTLMDTLNdaieraghvdhtivydrLGIPAdslswTPRDEWWDDAVATQSPTfethSMAASDPCMLLYSS 279
Cdd:cd12116 91 DD---------ALPDRLP-----------------AGLPV-----LLLALAAAAAAPAAPRT----PVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyegAPDHPA--PDRFWQ 357
Cdd:cd12116 136 GSTGRPKGVVVSH-RNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVI---APRETQrdPEALAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 358 LIEDHGITQFGVSPTAIRALRDHGDEhvaghDLSSLRIL-GstGEPWDPESWRWFYDHVGGgdtpIINISGGTEVFGCFL 436
Cdd:cd12116 212 LIEAHSITVMQATPATWRMLLDAGWQ-----GRAGLTALcG--GEALPPDLAARLLSRVGS----LWNLYGPTETTIWST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 437 MPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrdanergylvarssSPSMTRRLWSGEDRYLEAYW-------SRF-EDV 508
Cdd:cd12116 281 AARVTAAAGPIPIGRPLANTQVYVLDAALRPV--------------PPGVPGELYIGGDGVAQGYLgrpaltaERFvPDP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 509 WNH--------GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDttGEAAI-AYVILA 579
Cdd:cd12116 347 FAGpgsrlyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG--GDRRLvAYVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499204776 580 DAATPSA-ELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd12116 425 AGAAPDAaALRAHLRATLPAY----MVPSAFVRLDALPLTANGKLDRKA 469
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
102-632 |
1.01e-38 |
|
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: 150.47 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 102 AGTRNHVACIW-EGEDGTVRQQTYHDLHQQANRVANALAERGiGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIF--- 177
Cdd:cd05931 4 AARPDRPAYTFlDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPppt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 178 SGFGVEATATRIADAECSVVFTGDGFLrrgdrvtlmdtlnDAIERAGHVDhtivydrlgiPADSLSWTPRDEWWDDAVAT 257
Cdd:cd05931 83 PGRHAERLAAILADAGPRVVLTTAAAL-------------AAVRAFAASR----------PAAGTPRLLVVDLLPDTSAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 258 QSPTFEThsmAASDPCMLLYSSGTTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGDRFCwvsdiGWM-----MGpwsLIG 332
Cdd:cd05931 140 DWPPPSP---DPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN-VRQIRRAYGLDPGDVVV-----SWLplyhdMG---LIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 333 nhafaGTIV-MYEGAPD---HPA-----PDRFWQLIEDHGITqFGVSPT-----AIRALRdhgDEHVAGHDLSSLRILGS 398
Cdd:cd05931 208 -----GLLTpLYSGGPSvlmSPAaflrrPLRWLRLISRYRAT-ISAAPNfaydlCVRRVR---DEDLEGLDLSSWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 399 TGEPWDPESWRWFYD--------------------------HVGGGDTPIINISGGTEVFGCFLMPLP----TESLKPCt 448
Cdd:cd05931 279 GAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAAddpaARELVSC- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 449 lGGPGLGMDIDIVDDDGTSVRDANERGYLVARssSPSMTRRLWSGEDRYLEAYWSRFEDVwnHGDWaqMD-------ADG 521
Cdd:cd05931 358 -GRPLPDQEVRIVDPETGRELPDGEVGEIWVR--GPSVASGYWGRPEATAETFGALAATD--EGGW--LRtgdlgflHDG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 522 DWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ---AAVVGVPDDTTGEAAIAYVILADA-ATPSAELRAELRDHVG 597
Cdd:cd05931 431 ELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGAdPADLAAIAAAIRAAVA 510
|
570 580 590
....*....|....*....|....*....|....*..
gi 499204776 598 DAHGkpFRPREVVFV--DDLPKTQSGKLVRRAVASAY 632
Cdd:cd05931 511 REHG--VAPADVVLVrpGSIPRTSSGKIQRRACRAAY 545
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
123-628 |
2.14e-38 |
|
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: 148.81 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAE-CSVVFTGD 201
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRGDRvtlmdtlndaiERAGHVDHTIVYDRLGIPADSlswtprdewwddavatqSPTFETHSMAASDPCMLLYSSGT 281
Cdd:cd05923 110 AQVMDAIF-----------QSGVRVLALSDLVGLGEPESA-----------------GPLIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 282 TGTPKGIVHTHAGALVQPAKEIH-FGFDQRPGDRFCWVSDIGWMMGPWS-LIGNHAFAGTIVMyegaPDHPAPDRFWQLI 359
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTqAGLRHGRHNVVLGLMPLYHVIGFFAvLVAALALDGTYVV----VEEFDPADALKLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 360 EDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGgdtPIINISGGTEVFGCFLMPL 439
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAA--AEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG---EKVNIYGTTEAMNSLYMRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 440 PTESlkpcTLGGPGLGMDIDIVDDDGTSVRDA--NERGYLVARSSSPSMTRRLWsgedRYLEAYWSRFEDVW-NHGDWAQ 516
Cdd:cd05923 313 ARTG----TEMRPGFFSEVRIVRIGGSPDEALanGEEGELIVAAAADAAFTGYL----NQPEATAKKLQDGWyRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 517 MDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHv 596
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRAS- 463
|
490 500 510
....*....|....*....|....*....|..
gi 499204776 597 GDAHGKpfRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd05923 464 ELADFK--RPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
91-627 |
2.57e-38 |
|
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: 148.58 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 91 HNTVDRHAsvdAGTRNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIG 170
Cdd:cd17646 1 HALVAEQA---ARTPDAPAVVDEG-----RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 171 AIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGdrvtlmdtlndaieRAGHVDHTIVYDRLGIPADSLSWTPrdew 250
Cdd:cd17646 73 AAYLPLDPGYPADRLAYMLADAGPAVVLTTADLAARL--------------PAGGDVALLGDEALAAPPATPPLVP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 251 wddavatqsptfethsMAASDPCMLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSL 330
Cdd:cd17646 135 ----------------PRPDNLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWEL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 331 IGNHAFAGTIVMYEgaPD-HPAPDRFWQLIEDHGITQFGVSPTAIRALRdhgdEHVAGHDLSSLRILGSTGEPWDPESWR 409
Cdd:cd17646 198 FWPLVAGARLVVAR--PGgHRDPAYLAALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 410 WFYDHvggGDTPIINISGGTEV------FGCFlmplPTESLKPCTLGGPGLGMDIDIVDDDGTSVRD--ANE-------- 473
Cdd:cd17646 272 RFLAL---PGAELHNLYGPTEAaidvthWPVR----GPAETPSVPIGRPVPNTRLYVLDDALRPVPVgvPGElylggvql 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 474 -RGYLvarsSSPSMTrrlwsgEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDH 552
Cdd:cd17646 345 aRGYL----GRPALT------AERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 553 DAVTQAAVVGVPDDTTGEAAIAYVILADAATPsaELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd17646 415 PAVTHAVVVARAAPAGAARLVGYVVPAAGAAG--PDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAA 487
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
117-623 |
2.74e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 149.43 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 117 GTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSV 196
Cdd:PRK13295 51 GAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 197 VFTGDGFlrRG-DRVTLMDTLNDAIEragHVDHTIVYDrlGIPADS---LSWTPRDEWWDDAVATqsptFETHSMAASDP 272
Cdd:PRK13295 131 LVVPKTF--RGfDHAAMARRLRPELP---ALRHVVVVG--GDGADSfeaLLITPAWEQEPDAPAI----LARLRPGPDDV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 273 CMLLYSSGTTGTPKGIVHTH---AGALVQPAKEIHFGFDqrpgdrfcwvsDIGWMMGPWSLIGNHAFAGTIVMYEGAP-- 347
Cdd:PRK13295 200 TQLIYTSGTTGEPKGVMHTAntlMANIVPYAERLGLGAD-----------DVILMASPMAHQTGFMYGLMMPVMLGATav 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 --DHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDP----ESWRWFydhvgggDTP 421
Cdd:PRK13295 269 lqDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSLRTFLCAGAPIPGalveRARAAL-------GAK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTEVfGCFLMPLPTESLKPC--TLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSSSpsmtrrLWSGEDRYLE 499
Cdd:PRK13295 340 IVSAWGMTEN-GAVTLTKLDDPDERAstTDGCPLPGVEVRVVDADGAPL-PAGQIGRLQVRGCS------NFGGYLKRPQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 500 AYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILA 579
Cdd:PRK13295 412 LNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 499204776 580 DAATPSAELRAELRDHVGDAhgKPFRPREVVFVDDLPKTQSGKL 623
Cdd:PRK13295 492 PGQSLDFEEMVEFLKAQKVA--KQYIPERLVVRDALPRTPSGKI 533
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
107-627 |
4.72e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.04 E-value: 4.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 107 HVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATA 186
Cdd:PRK06178 49 RPAIIFYG-----HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 187 TRIADAECSVVFTGDgflrrgdrvTLMDTLNDAIERAG--HVDHTIVYDRLgiPA-------DSLSWTPR-DEWWDD--- 253
Cdd:PRK06178 124 YELNDAGAEVLLALD---------QLAPVVEQVRAETSlrHVIVTSLADVL--PAeptlplpDSLRAPRLaAAGAIDllp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 254 AVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGN 333
Cdd:PRK06178 193 ALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 334 HAFAGTIVMYEGAPDhpaPDRFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILG--STGEPWDPESWRWF 411
Cdd:PRK06178 273 PLFSGATLVLLARWD---AVAFMAAVERYRVTRTVMLVDNAVELMDH--PRFAEYDLSSLRQVRvvSFVKKLNPDYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 YDHVGggdTPIINIS-GGTEVFGC--FLMPLPTESL----KPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssP 484
Cdd:PRK06178 348 RALTG---SVLAEAAwGMTETHTCdtFTAGFQDDDFdllsQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRT--P 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 485 SMtrrlwsgedryLEAYWSR-------FEDVWNH-GDWAQMDADGdwFLH--GRADDAINVAGRKVGPAEVEGALIDHDA 554
Cdd:PRK06178 423 SL-----------LKGYWNKpeataeaLRDGWLHtGDIGKIDEQG--FLHylGRRKEMLKVNGMSVFPSEVEALLGQHPA 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499204776 555 VTQAAVVGVPDDTTGEAAIAYVILADAATPSAE-LRAELRDHVGdahgkPFRPREVVFVDDLPKTQSGKlVRRA 627
Cdd:PRK06178 490 VLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAaLQAWCRENMA-----VYKVPEIRIVDALPMTATGK-VRKQ 557
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
123-560 |
1.52e-37 |
|
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: 144.72 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPE-VQSILyGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTG 200
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAElVVAIL-AVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 201 DGFLRRGDRVTLMDTLNDAIERAGhvdhtivydrlgipadslswtprdewWDDAVATQSPTFETHsmaASDPCMLLYSSG 280
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDPLELAA--------------------------LDDAPAPPPPDAPSG---PDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 281 TTGTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPAPDRFWQLIE 360
Cdd:TIGR01733 131 STGRPKGVVVTHRSLVNLLAWLARR-YGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 361 DHGITQFGVSPTAIRALRDHGDEhvaghDLSSLRILGSTGE---PWDPESWRWFYdhvggGDTPIINISGGTE---VFGC 434
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEaltPALVDRWRARG-----PGARLINLYGPTEttvWSTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 435 F-LMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANE------------RGYLvarsSSPSMTRrlwsgeDRYLE-A 500
Cdd:TIGR01733 280 TlVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPV-PVGVvgelyiggpgvaRGYL----NRPELTA------ERFVPdP 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 501 YWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAV 560
Cdd:TIGR01733 349 FAGGDGARLYRtGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
81-625 |
2.91e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 147.58 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 81 WYPGAELNVAHNTVDRHASvDAGTRNHVACIWEGE--DGTVRQqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE 158
Cdd:PTZ00237 52 WFKGGELNTCYNVLDIHVK-NPLKRDQDALIYECPylKKTIKL-TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 159 VQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIE----RAGHV-------- 226
Cdd:PTZ00237 130 PLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIElstfKPSNVitlfrndi 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 227 ----DHTIVYDRLGIPaDSLSWTprDEWWDDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKE 302
Cdd:PTZ00237 210 tsesDLKKIETIPTIP-NTLSWY--DEIKKIKENNQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 303 IHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGA---PDHpAPDRFWQLIEDHGITQFGVSPTAIRAL-- 377
Cdd:PTZ00237 287 WRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGiikNKH-IEDDLWNTIEKHKVTHTLTLPKTIRYLik 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 378 RDHGDEHV-AGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGM 456
Cdd:PTZ00237 366 TDPEATIIrSKYDLSNLKEIWCGGEVIEESIPEYIENKLK---IKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 457 DIDIVDDDGTSVRDaNERGYLVAR-SSSPSMTRRLWSGEDRYLEAYwSRFEDVWNHGDWAQMDADGDWFLHGRADDAINV 535
Cdd:PTZ00237 443 KPSILSEDGKELNV-NEIGEVAFKlPMPPSFATTFYKNDEKFKQLF-SKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 536 AGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSA----ELRAELRDHVGDAHGKPFRPREVVF 611
Cdd:PTZ00237 521 SGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIII 600
|
570
....*....|....
gi 499204776 612 VDDLPKTQSGKLVR 625
Cdd:PTZ00237 601 VNQLPKTKTGKIPR 614
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
93-627 |
1.16e-36 |
|
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: 143.62 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 93 TVDRHASVDAGTRNHVACIWEGEdgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAi 172
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGD----RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 173 aVPIFSGFGveatatriadaecsvvftgdgfLRRGDrvtlmdtLNDAIERAGHVDHTIvydrlgipadslswtprdewwD 252
Cdd:cd05920 91 -VPVLALPS----------------------HRRSE-------LSAFCAHAEAVAYIV---------------------P 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 253 DAVATQSPTFETHSMAAS--DPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEIhFGFDQRpgDRFCWVSDIG--WMMG 326
Cdd:cd05920 120 DRHAGFDHRALARELAESipEVALFLLSGGTTGTPKLIPRTHNDYAynVRASAEV-CGLDQD--TVYLAVLPAAhnFPLA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 327 PWSLIGNHAFAGTIVMyegAPDhPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPE 406
Cdd:cd05920 197 CPGVLGTLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 407 SWRwfydhvgggdtPIINISGGT--EVFG------CFLMPLPTESLKPCTLGGPGLGMD-IDIVDDDGTSVRDAnERGYL 477
Cdd:cd05920 271 LAR-----------RVPPVLGCTlqQVFGmaegllNYTRLDDPDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPG-EEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 478 VARS--------SSPSMTRRLWSgEDRYleaYWSrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGAL 549
Cdd:cd05920 339 LTRGpytirgyyRAPEHNARAFT-PDGF---YRT--------GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 550 IDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDhVGDAHGKpfRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd05920 407 LRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRE-RGLAAYK--LPDRIEFVDSLPLTAVGKIDKKA 481
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
120-627 |
2.11e-36 |
|
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: 142.01 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd17652 11 ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmAASDPCMLLYSS 279
Cdd:cd17652 91 --------------------------------------------------------------------TPDNLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyegAPDHP--APDRFWQ 357
Cdd:cd17652 103 GSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLAGATLVL---APAEEllPGEPLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 358 LIEDHGITQFGVSPTAIRALRDHgdehvaghDLSSLRILGSTGEPWDPE-SWRWFYDHVgggdtpIINISGGTEVFGCFL 436
Cdd:cd17652 179 LLREHRITHVTLPPAALAALPPD--------DLPDLRTLVVAGEACPAElVDRWAPGRR------MINAYGPTETTVCAT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 437 MPLPTESLKPCTLGGPGLGMDIDIVDDD---------------GTSVrdanERGYLvarsSSPSMTRrlwsgeDRYL-EA 500
Cdd:cd17652 245 MAGPLPGGGVPPIGRPVPGTRVYVLDARlrpvppgvpgelyiaGAGL----ARGYL----NRPGLTA------ERFVaDP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 501 YWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVgVPDDTTGEAA-IAYVILA 579
Cdd:cd17652 311 FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-VRDDRPGDKRlVAYVVPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499204776 580 DAATPSAelrAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd17652 390 PGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
104-640 |
2.53e-36 |
|
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: 146.54 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE-VQSILyGIFKIGAIAVPIFSGFGV 182
Cdd:COG1020 489 TPDAVAVVFGD-----QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEmVVALL-AVLKAGAAYVPLDPAYPA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 183 EATATRIADAECSVVFTGDGFLRRgdrvtlmdtlndaieraghvdhtivydrlgIPADSLSWTPRDewwDDAVATQSPTF 262
Cdd:COG1020 563 ERLAYMLEDAGARLVLTQSALAAR------------------------------LPELGVPVLALD---ALALAAEPATN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 263 ETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGA--LVQPAKEiHFGFDqrPGDRFCWVSDIGWMMGPWSLIGNHAFAGTI 340
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALvnLLAWMQR-RYGLG--PGDRVLQFASLSFDASVWEIFGALLSGATL 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 341 VMYEGApDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvaghDLSSLRILGSTGEPWDPESWRWFYDHVGGgdT 420
Cdd:COG1020 687 VLAPPE-ARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPG--A 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 PIINISGGTE--VF-GCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRD--ANE---------RGYLvARsssPSM 486
Cdd:COG1020 759 RLVNLYGPTEttVDsTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVgvPGElyiggaglaRGYL-NR---PEL 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 487 TRrlwsgedryleaywSRF-EDVWNH--------GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ 557
Cdd:COG1020 835 TA--------------ERFvADPFGFpgarlyrtGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVRE 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 558 AAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRpreVVFVDDLPKTQSGKLVRRAVASAYTGADV 637
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAA---VVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
...
gi 499204776 638 TDR 640
Cdd:COG1020 978 AAA 980
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
116-628 |
5.66e-36 |
|
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: 140.85 E-value: 5.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:cd05945 11 VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTgdgflrrgdrvtlmdtlndaierAGHvdhtivydrlgipadslswtprdewwddavatqsptfethsmaasDPCML 275
Cdd:cd05945 91 LLIA-----------------------DGD---------------------------------------------DNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHAGALvqpakeiHFG------FDQRPGDRFCWVSDIGW---MMGPW-SLIGnhafAGTIVmyeg 345
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLV-------SFTnwmlsdFPLGPGDVFLNQAPFSFdlsVMDLYpALAS----GATLV---- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 APDHPAPDRFWQL---IEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPW---DPESWRWFYDhvgggD 419
Cdd:cd05945 168 PVPRDATADPKQLfrfLAEHGITVWVSTPSFAAMCLLSPT--FTPESLPSLRHFLFCGEVLphkTARALQQRFP-----D 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 420 TPIINISGGTE----VFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVArsSSPSMTRRLWSGED 495
Cdd:cd05945 241 ARIYNTYGPTEatvaVTYIEVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPV-PPGEKGELVI--SGPSVSKGYLNNPE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 496 RYLEAyWSRFEDVWNH--GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAI 573
Cdd:cd05945 318 KTAAA-FFPDEGQRAYrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELI 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 574 AYVIL--ADAATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd05945 397 AFVVPkpGAEAGLTKAIKAELAERLPPY----MIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
120-627 |
2.79e-35 |
|
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: 138.99 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaASDPCMLLYSS 279
Cdd:cd12115 103 D--------------------------------------------------------------------PDDLAYVIYTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTH--AGALVQPAKEiHFGFDQRPGdrFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGA---PDHPAPDr 354
Cdd:cd12115 115 GSTGRPKGVAIEHrnAAAFLQWAAA-AFSAEELAG--VLASTSICFDLSVFELFGPLATGGKVVLADNVlalPDLPAAA- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 355 fwqliedhGITQFGVSPTAIRALRDHGDEhvaghdLSSLRILGSTGEPWDPESWRWFYDHVGGgdTPIINISGGTE--VF 432
Cdd:cd12115 191 --------EVTLINTVPSAAAELLRHDAL------PASVRVVNLAGEPLPRDLVQRLYARLQV--ERVVNLYGPSEdtTY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 433 GCFLmPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRD--ANE---------RGYLvarsSSPSMTrrlwsgEDRYLEAY 501
Cdd:cd12115 255 STVA-PVPPGASGEVSIGRPLANTQAYVLDRALQPVPLgvPGElyiggagvaRGYL----GRPGLT------AERFLPDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 502 WSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADA 581
Cdd:cd12115 324 FGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499204776 582 ATPsaeLRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd12115 404 AAG---LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-629 |
5.79e-35 |
|
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: 138.34 E-value: 5.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 131 ANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFsgfgVEATATRIADAECSVVFTGDGflrrgdRV 210
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVF----VPLNPTLKESVLRYLVADAGG------RI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 211 TLMDtlndaierAGHVDHtivyDRLGIPA--DSLSWTPRDEWWDDAVATqsptfETHSMAASDPCMLLYSSGTTGTPKGI 288
Cdd:cd05922 73 VLAD--------AGAADR----LRDALPAspDPGTVLDADGIRAARASA-----PAHEVSHEDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 289 VHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyegAPDHPAPDRFWQLIEDHGITQF- 367
Cdd:cd05922 136 RLSHQ-NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVL---TNDGVLDDAFWEDLREHGATGLa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 368 GVSPTAIRALRdhgdehvAGHD---LSSLRILGSTGEPWDPESWRWFYDHVGGGDtpIINISGGTEVFGcFLMPLPTESL 444
Cdd:cd05922 212 GVPSTYAMLTR-------LGFDpakLPSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEATR-RMTYLPPERI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 445 --KPCTLGGPGLGMDIDIVDDDGTSVRdANERGYLVARSssPSMTRRLWSGEDRYLEAywSRFEDVWNHGDWAQMDADGD 522
Cdd:cd05922 282 leKPGSIGLAIPGGEFEILDDDGTPTP-PGEPGEIVHRG--PNVMKGYWNDPPYRRKE--GRGGGVLHTGDLARRDEDGF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 523 WFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDtTGEAAIAYVILADAATPSAelraeLRDHVGDAHGK 602
Cdd:cd05922 357 LFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDPKD-----VLRSLAERLPP 430
|
490 500
....*....|....*....|....*..
gi 499204776 603 PFRPREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
123-626 |
8.77e-35 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 139.12 E-value: 8.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLrrgdrvtlmDTLNDAIERAGHvdhtivydrlgiPADSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCMLLYSSGTT 282
Cdd:PRK13382 150 FS---------ATVDRALADCPQ------------ATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGAlVQPAKEIHfgfdqrpgDRFCWVSD-----IGWMMGPW---SLIGNHAFAGTIVMYEGApdhpAPDR 354
Cdd:PRK13382 209 GTPKGARRSGPGG-IGTLKAIL--------DRTPWRAEeptviVAPMFHAWgfsQLVLAASLACTIVTRRRF----DPEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 355 FWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVfGC 434
Cdd:PRK13382 276 TLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG---DVIYNNYNATEA-GM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 435 FLMPLPTESLK-PCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSSSpsMTRRLWSGEDR-YLEAYWSRfedvwnhG 512
Cdd:PRK13382 352 IATATPADLRAaPDTAGRPAEGTEIRILDQDFREVPTG-EVGTIFVRNDT--QFDGYTSGSTKdFHDGFMAS-------G 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 513 DWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILAD--AATPSaELRA 590
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPgaSATPE-TLKQ 500
|
490 500 510
....*....|....*....|....*....|....*.
gi 499204776 591 ELRDHVgdAHGKPfrPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK13382 501 HVRDNL--ANYKV--PRDIVVLDELPRGATGKILRR 532
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
106-628 |
9.60e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 138.64 E-value: 9.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIWeGEdgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPifsgfgveaT 185
Cdd:PRK07470 22 DRIALVW-GD----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP---------T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSvvftgdgFLRRGDRVTLM-------DTLNDAIERAGHVDHTIVydrLGIPADSLSWtprdewwDDAVATQ 258
Cdd:PRK07470 88 NFRQTPDEVA-------YLAEASGARAMichadfpEHAAAVRAASPDLTHVVA---IGGARAGLDY-------EALVARH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 259 SPT-FETHSMAASDPCMLLYSSGTTGTPKGIVHTHAgalvQPAKEI--HFGfDQRPG----DRFCWVSDIGWMMGPWSLI 331
Cdd:PRK07470 151 LGArVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG----QMAFVItnHLA-DLMPGtteqDASLVVAPLSHGAGIHQLC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 332 GNHAFAGTIVMyegAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILGSTGEPWDPESWRWF 411
Cdd:PRK07470 226 QVARGAATVLL---PSERFDPAEVWALVERHRVTNLFTVPTILKMLVEH--PAVDRYDHSSLRYVIYAGAPMYRADQKRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 YDHVGggdTPIINISGGTEVFGC--FLMPL-------PTESLKPCtlGGPGLGMDIDIVDDDGTSVRdANERGYLVARSS 482
Cdd:PRK07470 301 LAKLG---KVLVQYFGLGEVTGNitVLPPAlhdaedgPDARIGTC--GFERTGMEVQIQDDEGRELP-PGETGEICVIGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 483 SpsmtrrLWSGEDRYLEAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVV 561
Cdd:PRK07470 375 A------VFAGYYNNPEANAKAFRDGWFRtGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 562 GVPDDTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK07470 449 GVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
120-632 |
1.46e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 137.91 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVft 199
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdgflrrgdrVTLMDTLNDAierAGHVDHTI----------VYDRLGIPADSLSWTPRDEWWDDAVATQSPTFEThsmAA 269
Cdd:PRK12406 88 ----------IAHADLLHGL---ASALPAGVtvlsvptppeIAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGP---PV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 270 SDPCMLLYSSGTTGTPKGIVHT-----HAGALVQPAKEIHfgfDQRPGDRfcwvsdiGWMMGPwslignhafagtivMYE 344
Cdd:PRK12406 152 PQPQSMIYTSGTTGHPKGVRRAaptpeQAAAAEQMRALIY---GLKPGIR-------ALLTGP--------------LYH 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 345 GAPDHPA-----------------PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPES 407
Cdd:PRK12406 208 SAPNAYGlragrlggvlvlqprfdPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 408 WRWFYDHVGggdtPIIN-ISGGTEVfGCFLMPLPTESL-KPCTLGGPGLGMDIDIVDDDGTSVRDAnERGYLVARSssPS 485
Cdd:PRK12406 288 KRAMIEWWG----PVIYeYYGSTES-GAVTFATSEDALsHPGTVGKAAPGAELRFVDEDGRPLPQG-EIGEIYSRI--AG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRRLWSGEDRYLEAywSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPD 565
Cdd:PRK12406 360 NPDFTYHNKPEKRAE--IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 566 DTTGEAAIAYVILADAATPSAE-LRAELRDHVGDahgkpFR-PREVVFVDDLPKTQSGKLVRRAVASAY 632
Cdd:PRK12406 438 AEFGEALMAVVEPQPGATLDEAdIRAQLKARLAG-----YKvPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
123-628 |
6.86e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 6.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRRGDrvtlmdtLNDAIERaghvdhtIVYDRLGIpadslswtprdewWDDAVATQSPTFETHsmaASDPCMLLYSSGTT 282
Cdd:PRK12316 618 LGRKLP-------LAAGVQV-------LDLDRPAA-------------WLEGYSEENPGTELN---PENLAYVIYTSGST 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyEGAPDHPAPDRFWQLIEDH 362
Cdd:PRK12316 668 GKPKGAGNRH-RALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVV-AAPGDHRDPAKLVELINRE 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 363 GITQFGVSPTAIRA-LRDHGDEhvaghDLSSLRILGSTGE--PWDP----ESWRW---FYDHVG---------------- 416
Cdd:PRK12316 746 GVDTLHFVPSMLQAfLQDEDVA-----SCTSLRRIVCSGEalPADAqeqvFAKLPqagLYNLYGpteaaidvthwtcvee 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 417 GGDT-----PIINisGGTEVFGCFLMPLPTESLKPCTLGGPGLGmdidivdddgtsvrdaneRGYLvarsSSPSMTrrlw 491
Cdd:PRK12316 821 GGDSvpigrPIAN--LACYILDANLEPVPVGVLGELYLAGRGLA------------------RGYH----GRPGLT---- 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 492 sgEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpddtTGEA 571
Cdd:PRK12316 873 --AERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQ 946
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 572 AIAYVILADAATPSAE-LRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK12316 947 LVGYVVLESEGGDWREaLKAHLAASLPEY----MVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
123-627 |
4.84e-33 |
|
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: 132.49 E-value: 4.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTHHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmdtlndaieraghvdhtivydrlgipaDSLSWtprdewwddavatqsptfethsmaasdpcmLLYSSGTT 282
Cdd:cd17649 94 -------------------------------------RQLAY------------------------------VIYTSGST 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGW------MMGPWslignhaFAGTIVMYEGAPDHPAPDRFW 356
Cdd:cd17649 107 GTPKGVAVSH-GPLAAHCQATAERYGLTPGDRELQFASFNFdgaheqLLPPL-------ICGACVVLRPDELWASADELA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 357 QLIEDHGITQFGVSPTAIRALRDHGDEHVAGhDLSSLRILGSTGEPWDPESW-RWFYDHVGggdtpIINISGGTE----- 430
Cdd:cd17649 179 EMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPELLrRWLKAPVR-----LFNAYGPTEatvtp 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 431 -VFGC--------FLMPLPT-----------ESLKPCTLGGPG---LGmdidivdddGTSVrdanERGYLvarsSSPSMT 487
Cdd:cd17649 253 lVWKCeagaaragASMPIGRplggrsayildADLNPVPVGVTGelyIG---------GEGL----ARGYL----GRPELT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 rrlwsgEDRYLE-AYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDD 566
Cdd:cd17649 316 ------AERFVPdPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 567 tTGEAAIAYVILADAATpSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd17649 390 -GGKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKA 448
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
92-651 |
5.85e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 133.75 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 92 NTVDRHASVDAgtrNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGA 171
Cdd:PRK07786 21 NQLARHALMQP---DAPALRFLG-----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 172 IAVPIFSGFGVEATATRIADAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDHTIVYDrlgipadslswtprdewW 251
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG-----------------Y 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 252 DDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIH-FGFDQRPGDRFCWV-----SDIGwMM 325
Cdd:PRK07786 156 EDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRtNGADINSDVGFVGVplfhiAGIG-SM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 326 GPWSLIGnhafaGTIVMYE-GAPDhpaPDRFWQLIEDHGITQFGVSPTAIRALRDhgDEHVAGHDLSsLRILGSTGEPWD 404
Cdd:PRK07786 235 LPGLLLG-----APTVIYPlGAFD---PGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDLA-LRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 405 PESWRWFYDHVGggDTPIINISGGTEVFGCFLMPLPTESL-KPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSss 483
Cdd:PRK07786 304 DTLLRQMAATFP--EAQILAAFGQTEMSPVTCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDV-PVGEVGEIVYRA-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 PSMTRRLWSGEDRYLEAywsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVG 562
Cdd:PRK07786 379 PTLMSGYWNNPEATAEA----FAGGWFHsGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 563 VPDDTTGEAAIAYVILADaatPSAELR-AELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRS 641
Cdd:PRK07786 455 RADEKWGEVPVAVAAVRN---DDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERR 531
|
570
....*....|
gi 499204776 642 SIENPAVLDA 651
Cdd:PRK07786 532 SASAGFTERR 541
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
106-628 |
6.95e-33 |
|
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: 131.82 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIwegeDGTvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT 185
Cdd:cd17650 2 DAIAVS----DAT-RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqSPTfeth 265
Cdd:cd17650 77 QYMLEDSGAKLLLT-----------------------------------------------------------QPE---- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 266 smaasDPCMLLYSSGTTGTPKGIVHTHAG-ALVQPAKEIHFGFDQRPgDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMye 344
Cdd:cd17650 94 -----DLAYVIYTSGTTGKPKGVMVEHRNvAHAAHAWRREYELDSFP-VRLLQMASFSFDVFAGDFARSLLNGGTLVI-- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 345 gAPDHPA--PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRIL--GSTGEPwdPESWRWFYDHVGGGdT 420
Cdd:cd17650 166 -CPDEVKldPAALYDLILKSRITLMESTPALIRPVMAYVYRN--GLDLSAMRLLivGSDGCK--AQDFKTLAARFGQG-M 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 PIINISGGTE------VFGCFLMPLPTESLKPctLGGPGLGMDIDIVD--DDGTSVRDANE---------RGYLvarsSS 483
Cdd:cd17650 240 RIINSYGVTEatidstYYEEGRDPLGDSANVP--IGRPLPNTAMYVLDerLQPQPVGVAGElyiggagvaRGYL----NR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 PSMTrrlwsgEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVgV 563
Cdd:cd17650 314 PELT------AERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-V 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 564 PDDTTGEAAIAYVILADAATPSAELRAELRDHVGDahgkPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd17650 387 REDKGGEARLCAYVVAAATLNTAELRAFLAKELPS----YMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
120-628 |
2.08e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.43 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAV---PIFSGFGVEAtatRIADAECSV 196
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAHELEH---PFEDHGARV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 197 VFTGD---GFLRRGDRVTLMDT-----LNDAIERaghvdHTIVYDRLGIPA-----DSLSWTPRD-EWWDDAVATQSP-- 260
Cdd:PRK05605 133 AIVWDkvaPTVERLRRTTPLETivsvnMIAAMPL-----LQRLALRLPIPAlrkarAALTGPAPGtVPWETLVDAAIGgd 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 -TFETH-SMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHfgfdqrpgdrfcWVSDIGwmMGPWSLIGN----H 334
Cdd:PRK05605 208 gSDVSHpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKA------------WVPGLG--DGPERVLAAlpmfH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 335 AFA----GTIVMYEGA-----PdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDP 405
Cdd:PRK05605 274 AYGltlcLTLAVSIGGelvllP-APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEER--GVDLSGVRNAFSGAMALPV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 406 ESWRWFYDHVGGGdtpIINISGGTE----VFGcflMPLpTESLKPCTLGGPGLGMDIDIVD-DDGTSVRDANERGYLVAR 480
Cdd:PRK05605 351 STVELWEKLTGGL---LVEGYGLTEtspiIVG---NPM-SDDRRPGYVGVPFPDTEVRIVDpEDPDETMPDGEEGELLVR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 481 SssPSMTRRLWSGEDRYLEAywsrFEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAA 559
Cdd:PRK05605 424 G--PQVFKGYWNRPEETAKS----FLDGWfRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 560 VVGVPDDTTGEAAIAYVILADAATPSAE-LRAELRDHVgdAHGKPfrPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK05605 498 VVGLPREDGSEEVVAAVVLEPGAALDPEgLRAYCREHL--TRYKV--PRRFYHVDELPRDQLGKVRRREV 563
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
125-628 |
2.48e-32 |
|
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: 130.58 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 125 HDLHQQANRVANALAERGIGEGDTVGLYMPmvpevqsilygifkigaiavPIFSGFGVEATATRIADAECSVVFTgdgfl 204
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLI--------------------NSILTVFAAAAAWKCGACPAYKSSR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 205 rrgdrvtlmdTLNDAIERAGHVDHTIVYDrlGIPADslsWTPRDEWWDDAVATQ-SPtfETHSMAASDPCMLLYSSGTTG 283
Cdd:cd05929 76 ----------APRAEACAIIEIKAAALVC--GLFTG---GGALDGLEDYEAAEGgSP--ETPIEDEAAGWKMLYSGGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 284 TPKGI------VHTHAGALVQPAKEIHFGFDQR---PGDRFCWVSDIGWMMGpwslignHAFAGTIVMYEgapdHPAPDR 354
Cdd:cd05929 139 RPKGIkrglpgGPPDNDTLMAAALGFGPGADSVylsPAPLYHAAPFRWSMTA-------LFMGGTLVLME----KFDPEE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 355 FWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEP---WDPESW-RWfydhvggGDTPIINISGGTE 430
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppWVKEQWiDW-------GGPIIWEYYGGTE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 431 VFG-CFLMPlpTESLK-PCTLGGPGLGmDIDIVDDDGTSVrDANERGYLVARSSSPSMTRRlwsgedRYLEAYWSRFEDV 508
Cdd:cd05929 281 GQGlTIING--EEWLThPGSVGRAVLG-KVHILDEDGNEV-PPGEIGEVYFANGPGFEYTN------DPEKTAAARNEGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 509 WNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAE 587
Cdd:cd05929 351 WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499204776 588 LRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
106-626 |
3.07e-32 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 130.96 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT 185
Cdd:PRK08008 22 HKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREES 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSVVFTGDGFLrrgdrvtlmdTLNDAIERAGH--VDHtIVYDRLGIPADSLSWTprdewWDDAVATQSPTFE 263
Cdd:PRK08008 102 AWILQNSQASLLVTSAQFY----------PMYRQIQQEDAtpLRH-ICLTRVALPADDGVSS-----FTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 TH-SMAASDPCMLLYSSGTTGTPKGIVHTHA------------GAL--------VQPAKEIHFGfdqrpgdrfCWVSDIG 322
Cdd:PRK08008 166 YApPLSTDDTAEILFTSGTTSRPKGVVITHYnlrfagyysawqCALrdddvyltVMPAFHIDCQ---------CTAAMAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 323 WMMGpwslignhafaGTIVMYEGApdhpAPDRFWQLIEDHGITQFGVSPTAIRAL---------RDHGDEHVaghdLSSL 393
Cdd:PRK08008 237 FSAG-----------ATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLmvqppsandRQHCLREV----MFYL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 394 RIlgSTGEPWDPESwRWfydhvgggDTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANE 473
Cdd:PRK08008 298 NL--SDQEKDAFEE-RF--------GVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPL-PAGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 474 RGYLVARS-----------SSPSMTRRLwsgedryLEAywsrfeDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVG 541
Cdd:PRK08008 366 IGEICIKGvpgktifkeyyLDPKATAKV-------LEA------DGWLHtGDTGYVDEEGFFYFVDRRCNMIKRGGENVS 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 542 PAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVgDAHGKPFR-PREVVFVDDLPKTQS 620
Cdd:PRK08008 433 CVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFC-EQNMAKFKvPSYLEIRKDLPRNCS 508
|
....*.
gi 499204776 621 GKLVRR 626
Cdd:PRK08008 509 GKIIKK 514
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-623 |
3.46e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 131.43 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FlRRGDRVTLMDTL----------NDAIERAGHVDHTIVYDrlgiPADSLSWTPRDEWWD--DAVATQSPTFETHSMAAS 270
Cdd:PRK12583 127 F-KTSDYHAMLQELlpglaegqpgALACERLPELRGVVSLA----PAPPPGFLAWHELQArgETVSREALAERQASLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHA-----GALVqpAKEIHFGfdqrPGDRFCwvsdigwmmGPWSLIgnHAF----AGTIV 341
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHnilnnGYFV--AESLGLT----EHDRLC---------VPVPLY--HCFgmvlANLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 MYEGAP-----DHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEPWDPESWRWFYDHVG 416
Cdd:PRK12583 265 MTVGAClvypnEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEVMRRVMDEMH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 417 GGDTPIIniSGGTEVFGCFLMPLPTESL--KPCTLGGPGLGMDIDIVDDDGTSVR--DANE---RGYLVARSsspsmtrr 489
Cdd:PRK12583 343 MAEVQIA--YGMTETSPVSLQTTAADDLerRVETVGRTQPHLEVKVVDPDGATVPrgEIGElctRGYSVMKG-------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 490 LWSGEDRYLEAYwsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTT 568
Cdd:PRK12583 413 YWNNPEATAESI---DEDGWMHtGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 569 GEAAIAYVIL-ADAATPSAELRAELRDHVgdAHGKPfrPREVVFVDDLPKTQSGKL 623
Cdd:PRK12583 490 GEEIVAWVRLhPGHAASEEELREFCKARI--AHFKV--PRYFRFVDEFPMTVTGKV 541
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
120-631 |
4.00e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 131.22 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK08162 42 RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGF---------LRRGDRVTLMDTLNDAIERAGHVdHTIVYDRL---GIPADSLSWtPRDEWwdDAVAtqsptfethsm 267
Cdd:PRK08162 122 DTEFaevarealaLLPGPKPLVIDVDDPEYPGGRFI-GALDYEAFlasGDPDFAWTL-PADEW--DAIA----------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 268 aasdpcmLLYSSGTTGTPKGIVHTHAGA-LVQPAKEIHFGFDQRPgdRFCWVSDI----GWMMgPWSLIgnhAFAGTIVM 342
Cdd:PRK08162 187 -------LNYTSGTTGNPKGVVYHHRGAyLNALSNILAWGMPKHP--VYLWTLPMfhcnGWCF-PWTVA---ARAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 343 YEGApdhpAPDRFWQLIEDHGITQFGVSPTAIRALRDHgdehvaghdlsslrilgstgepwdPESWRWFYDH-----VGG 417
Cdd:PRK08162 254 LRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINA------------------------PAEWRAGIDHpvhamVAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 418 GDTPIINISGG-------TEVFGCflmplpTESLKPCTLggpglgmdidIVDDDGTSVRDANERGYLVARSSSP------ 484
Cdd:PRK08162 306 AAPPAAVIAKMeeigfdlTHVYGL------TETYGPATV----------CAWQPEWDALPLDERAQLKARQGVRyplqeg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 485 -------SMTRRLWSGEDR-------------YL---EAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKV 540
Cdd:PRK08162 370 vtvldpdTMQPVPADGETIgeimfrgnivmkgYLknpKATEEAFAGGWFHtGDLAVLHPDGYIKIKDRSKDIIISGGENI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 541 GPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPS-AELRAELRDHVgdAHGKpfRPREVVFvDDLPKTQ 619
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATeEEIIAHCREHL--AGFK--VPKAVVF-GELPKTS 524
|
570
....*....|....*.
gi 499204776 620 SGKL----VRRAVASA 631
Cdd:PRK08162 525 TGKIqkfvLREQAKSL 540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
123-628 |
5.32e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.54 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLrrgdrvtlmdtlndaieraghvdhtivyDRLGIPAD--SLSWTPRDEWWDdaVATQSPTFEThsmAASDPCMLLYSSG 280
Cdd:PRK12316 2110 LL----------------------------ERLPLPAGvaRLPLDRDAEWAD--YPDTAPAVQL---AGENLAYVIYTSG 2156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 281 TTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDR------FCW-VSDIGWMmgpWSLIgnhafAGTIVMYEGApDHPAPD 353
Cdd:PRK12316 2157 STGLPKGVAVSH-GALVAHCQAAGERYELSPADCelqfmsFSFdGAHEQWF---HPLL-----NGARVLIRDD-ELWDPE 2226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 354 RFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSsLRILGSTGEPWDPESWRWFYDHVGGGDtpIINISGGTEVF- 432
Cdd:PRK12316 2227 QLYDEMERHGVTILDFPPVYLQQLAEH--AERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEAVv 2301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 433 -------------GCFLMPLPT-----------ESLKPCTLGGPG---LGmdidivdddGTSVrdanERGYLvarsSSPS 485
Cdd:PRK12316 2302 tpllwkcrpqdpcGAAYVPIGRalgnrrayildADLNLLAPGMAGelyLG---------GEGL----ARGYL----NRPG 2364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTrrlwsgEDRYL-EAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVp 564
Cdd:PRK12316 2365 LT------AERFVpDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ- 2437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499204776 565 DDTTGEAAIAYVILADAATpsaELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK12316 2438 DGASGKQLVAYVVPDDAAE---DLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
121-623 |
2.47e-31 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 128.32 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 121 QQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTG 200
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 201 DGFLRRGDR-VTLMDTLNDAieraghvdhtivydrlgiPADSLSWtprdEWWDDAVATQSPTFE-THSMAASDPCMLLYS 278
Cdd:cd05915 104 PNLLPLVEAiRGELKTVQHF------------------VVMDEKA----PEGYLAYEEALGEEAdPVRVPERAACGMAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHAGA-LVQPAKEIHFGFDQRPGDRF-CWVSDI---GWMMgPWSLIgnhAFAGTIVMYEGAPDHpapD 353
Cdd:cd05915 162 TGTTGLPKGVVYSHRALvLHSLAASLVDGTALSEKDVVlPVVPMFhvnAWCL-PYAAT---LVGAKQVLPGPRLDP---A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 354 RFWQLIEDHGITQFGVSPTAIRALRDHGDehvaghdlsSLRilgstgepwdpESWRWFYDHVGGGDTP------------ 421
Cdd:cd05915 235 SLVELFDGEGVTFTAGVPTVWLALADYLE---------STG-----------HRLKTLRRLVVGGSAAprsliarfermg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 --IINISGGTEVFG----CFLMP----LPTES-------------------LKPCTLGGPGLGMDIDIVDDDGTSVRDan 472
Cdd:cd05915 295 veVRQGYGLTETSPvvvqNFVKShlesLSEEEkltlkaktglpiplvrlrvADEEGRPVPKDGKALGEVQLKGPWITG-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 473 erGYLVARSSSPSMT-RRLWsgedryleaYWSRfedvwnhgDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALID 551
Cdd:cd05915 373 --GYYGNEEATRSALtPDGF---------FRTG--------DIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMG 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 552 HDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHgkpFRPREVVFVDDLPKTQSGKL 623
Cdd:cd05915 434 HPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKW---QLPDAYVFAEEIPRTSAGKF 502
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
120-630 |
3.06e-31 |
|
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: 127.02 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVF 198
Cdd:cd05941 10 DSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 tgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaasDPCMLLYS 278
Cdd:cd05941 90 ------------------------------------------------------------------------DPALILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHA--GALVQP-AKEIHFgfdqRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDhpaPDRF 355
Cdd:cd05941 98 SGTTGRPKGVVLTHAnlAANVRAlVDAWRW----TEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFD---PKEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 356 WQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSS------LRIL--GSTGEPWDP-ESWRWFYDHVgggdtpIINIS 426
Cdd:cd05941 171 AISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARaaaaerLRLMvsGSAALPVPTlEEWEAITGHT------LLERY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEvfgcFLM----PLPTESlKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMTRRLWSGEDRYLEAYw 502
Cdd:cd05941 245 GMTE----IGMalsnPLDGER-RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRG--PSVFKEYWNKPEATKEEF- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 503 srFEDVW-NHGDWAQMDADGDWFLHGR-ADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILAD 580
Cdd:cd05941 317 --TDDGWfKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499204776 581 AATPSAElrAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:cd05941 395 GAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
123-626 |
8.04e-31 |
|
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: 125.15 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveatATRIADAEcsvvftgdg 202
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL---------NTRLTPNE--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmdtLNDAIERAGhvdhtIVYDrlgipadslswtprdewwddAVATqsptfethsmaasdpcmLLYSSGTT 282
Cdd:cd05912 65 -------------LAFQLKDSD-----VKLD--------------------DIAT-----------------IMYTSGTT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHT---HAGALVqpAKEIHFGFDqrpgDRFCW--------VSDIGWMMGpwSLIgnhaFAGTIVMYegapDHPA 351
Cdd:cd05912 90 GKPKGVQQTfgnHWWSAI--GSALNLGLT----EDDNWlcalplfhISGLSILMR--SVI----YGMTVYLV----DKFD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 352 PDRFWQLIEDHGITQFGVSPTAIRalrdhgdehvaghdlsslRILGSTGEPWdPESWRWFYdhVGGG------------- 418
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQ------------------RLLEILGEGY-PNNLRCIL--LGGGpapkplleqckek 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 419 DTPIINISGGTEVFGCFLMPLPTESL-KPCTLGGPGLGMDIDIVDDDGtsvrDANERGYLVARSssPSMTRRLWSGEDRY 497
Cdd:cd05912 213 GIPVYQSYGMTETCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDDGQ----PPYEVGEILLKG--PNVTKGYLNRPDAT 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 498 LEAywsrFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYV 576
Cdd:cd05912 287 EES----FENGWFKtGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499204776 577 IlADAATPSAELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:cd05912 363 V-SERPISEEELIAYCSEKL--AKYK--VPKKIYFVDELPRTASGKLLRH 407
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
82-625 |
8.44e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 126.66 E-value: 8.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 82 YPGAELNVAHntvDRHASVDAGTrnhvaciweGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQS 161
Cdd:PRK13390 2 YPGTHAQIAP---DRPAVIVAET---------GE-----QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 162 ILYGIFKigaiavpifSGFGVEATATRIADAECSVVfTGDGflrrGDRVTLMDTLNDAI--ERAGHVDHTIVYdrlGIPA 239
Cdd:PRK13390 65 VLWAALR---------SGLYITAINHHLTAPEADYI-VGDS----GARVLVASAALDGLaaKVGADLPLRLSF---GGEI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 240 DSLSWtprdewWDDAVATQSPTFethsmaASDPC--MLLYSSGTTGTPKGIVHThagalvQPAKEIhfgfDQrPGDRFCW 317
Cdd:PRK13390 128 DGFGS------FEAALAGAGPRL------TEQPCgaVMLYSSGTTGFPKGIQPD------LPGRDV----DA-PGDPIVA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 318 V---------SDIGWMMGP--------W-SLIgnHAFAGTIVMyegAPDHPAPDRFwQLIEDHGITQFGVSPTAIRALRD 379
Cdd:PRK13390 185 IarafydiseSDIYYSSAPiyhaaplrWcSMV--HALGGTVVL---AKRFDAQATL-GHVERYRITVTQMVPTMFVRLLK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 380 HGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdtPII-NISGGTEVFGCFLMPLPTESLKPCTLGGPGLGmDI 458
Cdd:PRK13390 259 LDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG----PIVyEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLG-DL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 459 DIVDDDGTSV-----------RDANERGYLvarsSSPSMTrrlwSGEDRYLEAYWSRFedvwnhGDWAQMDADGDWFLHG 527
Cdd:PRK13390 334 HICDDDGNELpagrigtvyfeRDRLPFRYL----NDPEKT----AAAQHPAHPFWTTV------GDLGSVDEDGYLYLAD 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 528 RADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGD--AHGKPfr 605
Cdd:PRK13390 400 RKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSriAHYKA-- 477
|
570 580
....*....|....*....|
gi 499204776 606 PREVVFVDDLPKTQSGKLVR 625
Cdd:PRK13390 478 PRSVEFVDELPRTPTGKLVK 497
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
271-625 |
9.15e-31 |
|
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: 123.15 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRFCWVSDIGWMMG-PWSLIGNHAFAGTIVMyegapDH 349
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHA-MGLTEADVYLNMLPLFHIAGlNLALATFHAGGANVVM-----EK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRilgstgepwdpeswrwfydHVGGGDTPIINIS--- 426
Cdd:cd17637 75 FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKS--GVDLSSLR-------------------HVLGLDAPETIQRfee 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 ----------GGTEVFGCFLMPLPTEslKPCTLGGPGLGMDIDIVDDDGTSVRdANERGYLVARssSPSMTRRLWSGEDr 496
Cdd:cd17637 134 ttgatfwslyGQTETSGLVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVP-AGETGEIVVR--GPLVFQGYWNLPE- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 497 yLEAYwsRFEDVWNH-GDWAQMDADGDWFLHGR--ADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAI 573
Cdd:cd17637 208 -LTAY--TFRNGWHHtGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIK 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499204776 574 AYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd17637 285 AVCVLKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
77-644 |
2.11e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.74 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 77 QSTAWYPGAELnvAHNTVDRHAsvdAGTRNHVACIWeGEdgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMV 156
Cdd:PRK12467 1565 ATHTGYPLARL--VHQLIEDQA---AATPEAVALVF-GE----QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 157 PEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdHTIVYDRLG 236
Cdd:PRK12467 1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT----------------------------QSHLQARLP 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 237 IPA--DSLSWTPRDEWwddaVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDr 314
Cdd:PRK12467 1687 LPDglRSLVLDQEDDW----LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRH-GALVNRLCATQEAYQLSAAD- 1760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 315 fCW---------VSDIGWMmgpWSLIGnhafAGTIVMyegAPD--HPAPDRFWQLIEDHGITQFGVSPTAIRALRDHgDE 383
Cdd:PRK12467 1761 -VVlqftsfafdVSVWELF---WPLIN----GARLVI---APPgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DE 1828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 384 HVAGhdLSSLRILGSTGEPWDPESWRWFYDHVGggDTPIINISGGTEVfgcflmpLPTESLKPCTLGGPGLGMDIDI--- 460
Cdd:PRK12467 1829 QVEH--PLSLRRVVCGGEALEVEALRPWLERLP--DTGLFNLYGPTET-------AVDVTHWTCRRKDLEGRDSVPIgqp 1897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 461 VDDDGTSVRDAN-------------------ERGYLvarsSSPSMTrrlwsgEDRYLEAYWSRF-EDVWNHGDWAQMDAD 520
Cdd:PRK12467 1898 IANLSTYILDASlnpvpigvagelylggvglARGYL----NRPALT------AERFVADPFGTVgSRLYRTGDLARYRAD 1967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 521 GDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpDDTTGEAAIAYVILADAATPSAE-----LRAELRDH 595
Cdd:PRK12467 1968 GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDeaqvaLRAILKNH 2046
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 499204776 596 VGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV----ASAYTGADVTDRSSIE 644
Cdd:PRK12467 2047 LKASLPEYMVPAHLVFLARMPLTPNGKLDRKALpapdASELQQAYVAPQSELE 2099
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
94-622 |
8.04e-30 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 123.95 E-value: 8.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 94 VDRHASVDAgtrnhVACIwEGEdgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIA 173
Cdd:PRK10946 31 LTRHAASDA-----IAVI-CGE----RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 174 V-PIFSGFGVEATA--------TRIADAECSVvFTGDGFLrrgdrvtlmDTLndaieRAGHVDHTIVYDRLGIPADSLsw 244
Cdd:PRK10946 101 VnALFSHQRSELNAyasqiepaLLIADRQHAL-FSDDDFL---------NTL-----VAEHSSLRVVLLLNDDGEHSL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 245 tprdewwDDAVATQSPTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEI-HFGFDQR----------- 310
Cdd:PRK10946 164 -------DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYysVRRSVEIcGFTPQTRylcalpaahny 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 311 PgdrfcwvsdigwMMGPWSLIGNHAfAGTIVMyegAPDhPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDL 390
Cdd:PRK10946 237 P------------MSSPGALGVFLA-GGTVVL---APD-PSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 391 SSLRILgstgepwdpeswrwfydHVGGGDTPIINISGGTEVFGC-----FLMplpTESLKP------------CTLGGPG 453
Cdd:PRK10946 300 ASLKLL-----------------QVGGARLSETLARRIPAELGCqlqqvFGM---AEGLVNytrlddsderifTTQGRPM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 454 LGMD-IDIVDDDGTSVRDaNERGYLVARS--------SSPSMTRRLWSGEDRYLEaywsrfedvwnhGDWAQMDADGDWF 524
Cdd:PRK10946 360 SPDDeVWVADADGNPLPQ-GEVGRLMTRGpytfrgyyKSPQHNASAFDANGFYCS------------GDLVSIDPDGYIT 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 525 LHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAeLRAELRDHvGDAHGKpf 604
Cdd:PRK10946 427 VVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ-LRRFLREQ-GIAEFK-- 502
|
570
....*....|....*...
gi 499204776 605 RPREVVFVDDLPKTQSGK 622
Cdd:PRK10946 503 LPDRVECVDSLPLTAVGK 520
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
123-627 |
9.55e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.43 E-value: 9.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRRGDRVTlmdtlndaieraghvdhtivydrlGIPADSLSwTPRDEWWDDAVATQSPTFETHSMAasdpcMLLYSSGTT 282
Cdd:PRK12467 619 LLAQLPVPA------------------------GLRSLCLD-EPADLLCGYSGHNPEVALDPDNLA-----YVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVM--YEGAPDhpaPDRFWQLIE 360
Cdd:PRK12467 669 GQPKGVAISH-GALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLlpPDCARD---AEAFAALMA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 361 DHGITQFGVSPTAIRALRDhgDEHVAGhdLSSLRILGSTGE--PWD-PESWRWFYDHVGggdtpIINISGGTE------V 431
Cdd:PRK12467 745 DQGVTVLKIVPSHLQALLQ--ASRVAL--PRPQRALVCGGEalQVDlLARVRALGPGAR-----LINHYGPTEttvgvsT 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 432 FGCFLMPLPTESLkpcTLGGPGLGMDIDIVDDDGTSVR-----------DANERGYLvarsSSPSMTrrlwsgEDRYL-E 499
Cdd:PRK12467 816 YELSDEERDFGNV---PIGQPLANLGLYILDHYLNPVPvgvvgelyiggAGLARGYH----RRPALT------AERFVpD 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 500 AYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDtTGEAAIAYVI-- 577
Cdd:PRK12467 883 PFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVpa 961
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 578 -LADAATPSA---ELRAELR----DHVGDAHgkpfrpreVVFVDDLPKTQSGKLVRRA 627
Cdd:PRK12467 962 aVADGAEHQAtrdELKAQLRqvlpDYMVPAH--------LLLLDSLPLTPNGKLDRKA 1011
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
123-628 |
1.38e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 123.60 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAV---PIFSGFGVEataTRIADAECSVVFT 199
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTERELE---YQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLrrgDRVTlmdtlndAIERAGHVDHTIVY---DRLGIPADSL---------------SWTPRDEWWDDAVATQSPT 261
Cdd:PRK06710 128 LDLVF---PRVT-------NVQSATKIEHVIVTriaDFLPFPKNLLypfvqkkqsnlvvkvSESETIHLWNSVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 262 FETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFcwvsdigwMMGPWSLIgnHAFAGTIV 341
Cdd:PRK06710 198 VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEV--------VLGVLPFF--HVYGMTAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 M----YEGAPDHPAPD----RFWQLIEDHGITQFGVSPTAIRALRDhgDEHVAGHDLSSLRILGSTGEPWDPESWRWFYD 413
Cdd:PRK06710 268 MnlsiMQGYKMVLIPKfdmkMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 414 HVGGgdtPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMTRRLWSG 493
Cdd:PRK06710 346 VTGG---KLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKG--PQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 494 EdrylEAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAA 572
Cdd:PRK06710 421 P----EETAAVLQDGWLHtGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 573 IAYVILADAATPSAElraELrDHVGDAHGKPFR-PREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK06710 497 KAFVVLKEGTECSEE---EL-NQFARKYLAAYKvPKVYEFRDELPKTTVGKILRRVL 549
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
123-625 |
1.67e-29 |
|
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: 121.52 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPifsgfgveatATRIADAecsvvftgdg 202
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP----------ATTLLTP---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmDTLNDAIERAGHVdhtivydrlgipadslswtprdewwddaVATQSPTfeTHsmaASDPCMLLYSSGTT 282
Cdd:cd05974 62 -----------DDLRDRVDRGGAV----------------------------YAAVDEN--TH---ADDPMLLYFTSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGALVQPAKEIHFgFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPApDRFWQLIEDH 362
Cdd:cd05974 98 SKPKLVEHTHRSYPVGHLSTMYW-IGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDA-KRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 363 GITQFGVSPTAIRALRDhgdEHVAGHDLSSLRILGStGEPWDPE-------SW-RWFYDhvGGGDTPIINISGGTevfgc 434
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEvieqvrrAWgLTIRD--GYGQTETTALVGNS----- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 435 flmplPTESLKPCTLGGPGLGMDIDIVDDDGTSVR---------DANERGYLVARSSSPSMTRRLWSGedryleAYWSRf 505
Cdd:cd05974 245 -----PGQPVKAGSMGRPLPGYRVALLDPDGAPATegevaldlgDTRPVGLMKGYAGDPDKTAHAMRG------GYYRT- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 506 edvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPS 585
Cdd:cd05974 313 ------GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPS 386
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499204776 586 AELRAELRDHVGDAHGKPFRPREVVFVdDLPKTQSGKLVR 625
Cdd:cd05974 387 PETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
123-628 |
2.56e-29 |
|
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: 121.99 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfGVEATATRI----ADAECSVVF 198
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV----DIDQPAARReailADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 TGDGflrrgdrvtlmdtlndaieraghvdhtivydrlgiPADSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCMLLYS 278
Cdd:cd12114 90 TDGP-----------------------------------DAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHAGAL--VQPAKEiHFGFDqrPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDhPAPDRFW 356
Cdd:cd12114 135 SGSTGTPKGVMISHRAALntILDINR-RFAVG--PDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR-RDPAHWA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 357 QLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLRILGSTGEpWDPEswrwfydhvgggDTP--IINISGGTEVFgc 434
Cdd:cd12114 211 ELIERHGVTLWNSVPALLEMLLDVLEA--AQALLPSLRLVLLSGD-WIPL------------DLParLRALAPDARLI-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 435 flmplpteslkpcTLGGPGLG------MDIDIVDDDGTSV----RDANERGYLVARSSSPS---MTRRLWSGEDRYLEAY 501
Cdd:cd12114 274 -------------SLGGATEAsiwsiyHPIDEVPPDWRSIpygrPLANQRYRVLDPRGRDCpdwVPGELWIGGRGVALGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 502 W-------SRFEDVWNH------GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpDDTT 568
Cdd:cd12114 341 LgdpeltaARFVTHPDGerlyrtGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPG 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 569 GEAAIAYVILADAATP--SAELRAELRDHVGDAHgkpfRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd12114 420 GKRLAAFVVPDNDGTPiaPDALRAFLAQTLPAYM----IPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
123-625 |
2.75e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.55 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGvEATATRIADAECSVVFTGDG 202
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR-EAELVWVLNKCQAKMFFAPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRRGDRVTLMDTLndaIERAGHVDHTIVYDRLG--IPADSLSwtprdewwddAVATQSPTFETHSMAASDP-CMLLYSS 279
Cdd:PRK06087 130 LFKQTRPVDLILPL---QNQLPQLQQIVGVDKLApaTSSLSLS----------QIIADYEPLTTAITTHGDElAAVLFTS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGALvqpakeihfgFDQRPgdrFCWVSDIGW---MMGPWSLigNHA---FAGTIV-MYEGAP----D 348
Cdd:PRK06087 197 GTEGLPKGVMLTHNNIL----------ASERA---YCARLNLTWqdvFMMPAPL--GHAtgfLHGVTApFLIGARsvllD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPDRFWQLIEDHGIT-QFGVSPTaIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPESWRWFYDHvgggDTPIINISG 427
Cdd:PRK06087 262 IFTPDACLALLEQQRCTcMLGATPF-IYDLLNLLEKQ--PADLSALRFFLCGGTTIPKKVARECQQR----GIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 428 GTEVFGCFLMPL--PTEsLKPCTLGGPGLGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPSMTrrlwsge 494
Cdd:PRK06087 335 STESSPHAVVNLddPLS-RFMHTDGYAAAGVEIKVVDEARKTLPPGCEgeeasrgpnvfMGYL----DEPELT------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 495 DRYLEaywsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAI 573
Cdd:PRK06087 403 ARALD------EEGWYYsGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 574 AYVILADA-ATPS-AELRAEL-RDHVgdahGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:PRK06087 477 AYVVLKAPhHSLTlEEVVAFFsRKRV----AKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
123-629 |
4.76e-29 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 121.92 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAecsvvftgdg 202
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAA---------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrGDRVTLMDTLNDAIERAGHVDHTIVYDRLGipADSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCMLLYSSGTT 282
Cdd:PRK05852 115 ----GARVVLIDADGPHDRAEPTTRWWPLTVNVG--GDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFCWVSDI----GWMMgpwSLIGNHAFAGTIVMyegapdhPAPDRF--- 355
Cdd:PRK05852 189 GLPKMVPWTHAN-IASSVRAIITGYRLSPRDATVAVMPLyhghGLIA---ALLATLASGGAVLL-------PARGRFsah 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 356 --WQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGgdtPIINISGGTE--- 430
Cdd:PRK05852 258 tfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEath 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 431 ------VFGCFLMPLPTESLKPCtlgGPGLGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPSMTRrlwsg 493
Cdd:PRK05852 335 qvtttqIEGIGQTENPVVSTGLV---GRSTGAQIRIVGSDGLPLPAGAVgevwlrgttvvRGYL----GDPTITA----- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 494 edryleaywSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAA 572
Cdd:PRK05852 403 ---------ANFTDGWLRtGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAV 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 573 IAYVILADAATPSA-ELRAELRDHVGdahgkPFR-PREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:PRK05852 474 AAVIVPRESAPPTAeELVQFCRERLA-----AFEiPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
77-644 |
1.02e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.53 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 77 QSTAWYPgAELNVaHNTVDRHAsvdAGTRNHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMV 156
Cdd:PRK12316 4542 RTDAGYP-ATRCV-HQLVAERA---RMTPDAVAVVFDE-----EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERS 4611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 157 PEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdHTIVYDRLG 236
Cdd:PRK12316 4612 AEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT----------------------------QSHLLQRLP 4663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 237 IPA--DSLSWTPRDEWwdDAVATQSPTFETHsmaASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDR 314
Cdd:PRK12316 4664 IPDglASLALDRDEDW--EGFPAHDPAVRLH---PDNLAYVIYTSGSTGRPKGVAVSH-GSLVNHLHATGERYELTPDDR 4737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 315 FCWVSDIGWMMGPWSLIGNHAFAGTIVMyeGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvagHDLSSLR 394
Cdd:PRK12316 4738 VLQFMSFSFDGSHEGLYHPLINGASVVI--RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD---GEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 395 ILGSTGEPWDPESWR--WFYDHVGGgdtpIINISGGTEVfgcflmplpteSLKPCTLGGPGLGMDIDIVDDDGTSVrdAN 472
Cdd:PRK12316 4813 VYCFGGEAVAQASYDlaWRALKPVY----LFNGYGPTET-----------TVTVLLWKARDGDACGAAYMPIGTPL--GN 4875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 473 ERGYLVARSSSP---SMTRRLWSGEDRYLEAYWSR------------FED----VWNHGDWAQMDADGDWFLHGRADDAI 533
Cdd:PRK12316 4876 RSGYVLDGQLNPlpvGVAGELYLGGEGVARGYLERpaltaerfvpdpFGApggrLYRTGDLARYRADGVIDYLGRVDHQV 4955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 534 NVAGRKVGPAEVEGALIDHDAVTQAAVVGVpDDTTGEAAIAYVI-----LADAATPSAELRAELRDHVGDAHGKPFRPRE 608
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAH 5034
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 499204776 609 VVFVDDLPKTQSGKLVRRAV----ASAYTGADVTDRSSIE 644
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALpqpdASLLQQAYVAPRSELE 5074
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-622 |
1.04e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 117.87 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGF-----DQRPGDRFCWVSDIGWMMGP--------WSLIGNHAFAGTIV 341
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTgeftpSEDAHKAAAAAAGTVMFPAPplmhgtgsWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 MYEGAPDhpaPDRFWQLIEDHGITQFGVSPTA-----IRALRDHGDehvagHDLSSLRILGSTGEPWDPESWRWFYDHVG 416
Cdd:cd05924 88 LPDDRFD---PEEVWRTIEKHKVTSMTIVGDAmarplIDALRDAGP-----YDLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 417 ggDTPIINISGGTEV-FGCFLMPLPT-ESLKPCTLGGPGLGmdidIVDDDGTSVRDANERGYLVARS--------SSPSM 486
Cdd:cd05924 160 --NITLVDAFGSSETgFTGSGHSAGSgPETGPFTRANPDTV----VLDDDGRVVPPGSGGVGWIARRghiplgyyGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 487 TRRLWSGED--RYLEAywsrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVP 564
Cdd:cd05924 234 TAETFPEVDgvRYAVP-----------GDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 565 DDTTGEAAIAYVILADAATPSaelRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGK 622
Cdd:cd05924 303 DERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
277-622 |
1.91e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 117.20 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 277 YSSGTTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDHPAP---D 353
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPglfD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 354 RFWQLIEDHGITQFGVSPTAIRALRDHGDehvaGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEVFG 433
Cdd:cd05944 88 NFWKLVERYRITSLSTVPTVYAALLQVPV----NADISSLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 434 CFLMPLPTESLKPCTLGG--PGLGMDIDIVDDDGTSVRDA--NERGYLVARSsspsmtRRLWSGEDRYLEAYWSRFEDVW 509
Cdd:cd05944 161 LVAVNPPDGPKRPGSVGLrlPYARVRIKVLDGVGRLLRDCapDEVGEICVAG------PGVFGGYLYTEGNKNAFVADGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 510 -NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPS-AE 587
Cdd:cd05944 235 lNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEeEE 314
|
330 340 350
....*....|....*....|....*....|....*
gi 499204776 588 LRAELRDHVgdaHGKPFRPREVVFVDDLPKTQSGK 622
Cdd:cd05944 315 LLAWARDHV---PERAAVPKHIEVLEELPVTAVGK 346
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
106-632 |
7.35e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 118.66 E-value: 7.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVAcIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT 185
Cdd:COG1022 26 DRVA-LREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSVVFTGDGFLRrgdrvtlmDTLNDAIERAGHVDHTIVYDRLGIPADS--LSWtprDEWWDDAVATQSPTFE 263
Cdd:COG1022 105 AYILNDSGAKVLFVEDQEQL--------DKLLEVRDELPSLRHIVVLDPRGLRDDPrlLSL---DELLALGREVADPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 THSMAA---SDPCMLLYSSGTTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGDRF-CWVsdigwmmgPWSlignHAFA-- 337
Cdd:COG1022 174 EARRAAvkpDDLATIIYTSGTTGRPKGVMLTHRNLLSN-ARALLERLPLGPGDRTlSFL--------PLA----HVFErt 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 338 -GTIVMYEGA-------PDHPAPD-------------RFW--------QLIEDHGITQFGVSPTAIRALRDHGDEHVAGH 388
Cdd:COG1022 241 vSYYALAAGAtvafaesPDTLAEDlrevkptfmlavpRVWekvyagiqAKAEEAGGLKRKLFRWALAVGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 389 DLSS------------------------LRILGSTGEPWDPESWRWFYDhVGggdtpiINIsggTEVFGCflmplpTESL 444
Cdd:COG1022 321 SPSLllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LG------IPV---LEGYGL------TETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 445 KPCTLGGPGlgmDIDIvdD------DGTSVRDAnERGYLVARssSPSMTRRLWSGEDRYLEAYwsrFEDVWNH-GDWAQM 517
Cdd:COG1022 385 PVITVNRPG---DNRI--GtvgpplPGVEVKIA-EDGEILVR--GPNVMKGYYKNPEATAEAF---DADGWLHtGDIGEL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 518 DADGDWFLHGRADDAINVA-GRKVGPAEVEGALIDHDAVTQAAVVG----------VPD-DTTGEAA----IAYVILADA 581
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDfEALGEWAeengLPYTSYAEL 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 582 ATpSAELRAELRDHVgDAHGKPFRPREVV--FVdDLPK---------TQSGKLVRRAVASAY 632
Cdd:COG1022 534 AQ-DPEVRALIQEEV-DRANAGLSRAEQIkrFR-LLPKeftiengelTPTLKLKRKVILEKY 592
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
120-623 |
7.91e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.60 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPI---FSGFGVEATatrIADAECSV 196
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSASELDAL---LQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 197 VFTGDGFLRRGDRVTLMDTLNDAIERAGhvdhtivydrlgiPADslswtprdewwddavatqsptfeTHSMAASDPCMLL 276
Cdd:PRK09088 98 LLGDDAVAAGRTDVEDLAAFIASADALE-------------PAD-----------------------TPSIPPERVSLIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 277 YSSGTTGTPKGIVHTHAgALVQPAkeIHFGFDQRPGDRFCWVSDIGwMMGPWSLIGN----HAFAGTIVMYEGApdHPAP 352
Cdd:PRK09088 142 FTSGTSGQPKGVMLSER-NLQQTA--HNFGVLGRVDAHSSFLCDAP-MFHIIGLITSvrpvLAVGGSILVSNGF--EPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 353 DRFWQLIEDHGITQFGVSPTAIRALRDHGDehVAGHDLSSLRILGSTGEPWDPESWRWFYDHvgggDTPIINISGGTEVF 432
Cdd:PRK09088 216 TLGRLGDPALGITHYFCVPQMAQAFRAQPG--FDAAALRHLTALFTGGAPHAAEDILGWLDD----GIPMVDGFGMSEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 433 GCFLMPLPTESL--KPCTLGGPGLGMDIDIVDDDGTSVRdANERGYLVARSssPSMTRRLWSGEDRYLEAYwsrFEDVW- 509
Cdd:PRK09088 290 TVFGMSVDCDVIraKAGAAGIPTPTVQTRVVDDQGNDCP-AGVPGELLLRG--PNLSPGYWRRPQATARAF---TGDGWf 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 510 NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElr 589
Cdd:PRK09088 364 RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE-- 441
|
490 500 510
....*....|....*....|....*....|....
gi 499204776 590 aELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKL 623
Cdd:PRK09088 442 -RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
123-634 |
1.35e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.91 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAecsvvftgdg 202
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDA---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrGDRVTLMDTLNDAIerAGHVDHTIVYDrlgipADSLSWTPRdewwddAVATQSPTFETHSMAASDPCMLLYSSGTT 282
Cdd:PRK06145 99 ----GAKLLLVDEEFDAI--VALETPKIVID-----AAAQADSRR------LAQGGLEIPPQAAVAPTDLVRLMYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHAGALVQPAKEIhFGFDQRPGDRFCWVsdigwmmGPWSLIGNHAFAGTIVMYEGA----PDHPAPDRFWQL 358
Cdd:PRK06145 162 DRPKGVMHSYGNLHWKSIDHV-IALGLTASERLLVV-------GPLYHVGAFDLPGIAVLWVGGtlriHREFDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 359 IEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGDtpIINISGGTE-VFGCFLM 437
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEKTPESRIRDFTRVFTRAR--YIDAYGLTEtCSGDTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 438 PLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssPSMTRRLWSGEDRYLEAYwsrFEDVWNHGDWAQM 517
Cdd:PRK06145 310 EAGREIEKIGSTGRALAHVEIRIADGAGRWL-PPNMKGEICMRG--PKVTKGYWKDPEKTAEAF---YGDWFRSGDVGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 518 DADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVG 597
Cdd:PRK06145 384 DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCR 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 499204776 598 DAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTG 634
Cdd:PRK06145 461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
120-644 |
1.89e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.11 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLRRGDRVtlmdtlndaieragHVDHTIVYDRLgipadslswtprdEWWDDAVATQSPTFETHSMAasdpcMLLYSS 279
Cdd:PRK12467 3199 QAHLLEQLPAP--------------AGDTALTLDRL-------------DLNGYSENNPSTRVMGENLA-----YVIYTS 3246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGapDHPAPDRFWQLI 359
Cdd:PRK12467 3247 GSTGKPKGVGVRH-GALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDN--DLWDPEELWQAI 3323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 360 EDHGITQFGVSPTAIRALRDHGDehvaGHDLSSLRILGSTGEPWDPESWRWFYDHVGggDTPIINISGGTE------VFG 433
Cdd:PRK12467 3324 HAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFEQVKRKLK--PRGLTNGYGPTEavvtvtLWK 3397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 434 CFLMPLPTESLKPctLGGPGLGMDIDIVDDDG--TSVRDANER---GYLVARS--SSPSMTrrlwsgEDRYL-EAYWSRF 505
Cdd:PRK12467 3398 CGGDAVCEAPYAP--IGRPVAGRSIYVLDGQLnpVPVGVAGELyigGVGLARGyhQRPSLT------AERFVaDPFSGSG 3469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 506 EDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpDDTTGEAAIAYVILADaatPS 585
Cdd:PRK12467 3470 GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD---PQ 3545
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 586 AELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYT---GADVTDRSSIE 644
Cdd:PRK12467 3546 GDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAkgsREYVAPRSEVE 3607
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
271-629 |
2.02e-27 |
|
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: 113.19 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDrfCWVSDIgwmmgPWSLIGNHAFAgTIVMYEGAPDHP 350
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAA-NLLASAAGLHSRLGFGGGD--SWLLSL-----PLYHVGGLAIL-VRSLLAGAELVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 351 aPDRFWQLIEDH---GITQFGVSPTAI-RALRDHGdehvAGHDLSSLRILGSTGEPWDPESWRWFYDHvgggDTPIINIS 426
Cdd:cd17630 72 -LERNQALAEDLappGVTHVSLVPTQLqRLLDSGQ----GPAALKSLRAVLLGGAPIPPELLERAADR----GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEVFGC-FLMPLPTESLKpcTLGGPGLGMDIDIVDDDgtsvrdanergylvarssspsmtrRLWSGEDRYLEAYWSR- 504
Cdd:cd17630 143 GMTETASQvATKRPDGFGRG--GVGVLLPGRELRIVEDG------------------------EIWVGGASLAMGYLRGq 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 505 -----FEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVIL 578
Cdd:cd17630 197 lvpefNEDGWFTtKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499204776 579 ADAATPsaelrAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVA 629
Cdd:cd17630 277 RGPADP-----AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
104-627 |
2.02e-27 |
|
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: 116.27 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:cd17655 10 TPDHTAVVFEDQ-----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAECSVVFTgdgflrrgdrvtlmdtlndaierAGHVDHTIVYDRLGIPADslswtprdewwDDAVATQSPTFE 263
Cdd:cd17655 85 RIQYILEDSGADILLT-----------------------QSHLQPPIAFIGLIDLLD-----------EDTIYHEESENL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 THSMAASDPCMLLYSSGTTGTPKGIVHTHAGaLVQpakeIHFGFDQR----PGDRFCWVSDIGWMMGPWSLIGNHAFAGT 339
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG-VVN----LVEWANKViyqgEHLRVALFASISFDASVTEIFASLLSGNT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 340 IVMYEGAPDHPAPdRFWQLIEDHGITQFGVSPTAIRALrdhgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGGD 419
Cdd:cd17655 206 LYIVRKETVLDGQ-ALTQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 420 TpIINISGGTE-VFGCFLMPLPTESLKPCT--LGGPGLGMDIDIVDDDG--TSVRDANE---------RGYLvarsSSPS 485
Cdd:cd17655 280 T-ITNAYGPTEtTVDASIYQYEPETDQQVSvpIGKPLGNTRIYILDQYGrpQPVGVAGElyiggegvaRGYL----NRPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTrrlwsgEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPD 565
Cdd:cd17655 355 LT------AEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKD 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 566 DTTGEAAIAYVIlADAATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd17655 429 EQGQNYLCAYIV-SEKELPVAQLREFLARELPDY----MIPSYFIKLDEIPLTPNGKVDRKA 485
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
115-630 |
6.19e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 115.09 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 115 EDGTVrqqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAEC 194
Cdd:PRK13383 57 DDGAL---SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 195 SVVFTGDGFLrrgDRVtlmdtlndaierAGHVDHTIVYDRLGIPADSLSWTPRdewwddavatqsptfethsMAASDPCM 274
Cdd:PRK13383 134 STVVADNEFA---ERI------------AGADDAVAVIDPATAGAEESGGRPA-------------------VAAPGRIV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLySSGTTGTPKGI-----VHTHAGALVQPAKEIHFgfdqRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEgapdH 349
Cdd:PRK13383 180 LL-TSGTTGKPKGVprapqLRSAVGVWVTILDRTRL----RTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHR----H 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGT 429
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYG---DILYNGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 430 EVfGCFLMPLPTESLK-PCTLGGPGLGMDIDIVDDDGtsvrdanergylvaRSSSPSMTRRLWSG----EDRYLEAYWSR 504
Cdd:PRK13383 328 EV-GIGALATPADLRDaPETVGKPVAGCPVRILDRNN--------------RPVGPRVTGRIFVGgelaGTRYTDGGGKA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 505 FED-VWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAAT 583
Cdd:PRK13383 393 VVDgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499204776 584 PSAelrAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:PRK13383 473 VDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-622 |
9.71e-27 |
|
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: 111.99 E-value: 9.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGpwSLIGNHAFA--GTIVMYEGAPD 348
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHN-IVNNGYFIGERLGLTEQDRLCIPVPLFHCFG--SVLGVLACLthGATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPdrFWQLIEDHGITQ-FGVsPTAIRALRDHGDehVAGHDLSSLR--ILGstGEPWDPESWRWFYDHVGGGDTPIIni 425
Cdd:cd05917 80 DPLA--VLEAIEKEKCTAlHGV-PTMFIAELEHPD--FDKFDLSSLRtgIMA--GAPCPPELMKRVIEVMNMKDVTIA-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 426 SGGTEVFGCFLMPLPTESL--KPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSSSpsMTRRLWSGEDRYLEAYws 503
Cdd:cd05917 151 YGMTETSPVSTQTRTDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYS--VMKGYWNDPEKTAEAI-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 504 rFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAA 582
Cdd:cd05917 227 -DGDGWLHtGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499204776 583 TPSAE-LRAELRDHVgdAHGKPfrPREVVFVDDLPKTQSGK 622
Cdd:cd05917 306 ELTEEdIKAYCKGKI--AHYKV--PRYVFFVDEFPLTVSGK 342
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
544-622 |
3.49e-26 |
|
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: 101.85 E-value: 3.49e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 544 EVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPsaeLRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGK 622
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
123-628 |
4.71e-26 |
|
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: 112.62 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGL--------YMPMvpevqsiLYGIFkIGAIAVPIFSGFGVEATATRIADAEC 194
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVcsenslqfFLPV-------IAGLF-IGVGVAPTNDIYNERELDHSLNISKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 195 SVVFTGDGFLrrgDRVTLMDTLNDAIERAGHVDhtIVYDRLGIPADSLSWTPRDEWWDDAVATQSPTFETHSMAAsdpcM 274
Cdd:cd17642 118 TIVFCSKKGL---QKVLNVQKKLKIIKTIIILD--SKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVA----L 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALVQ--PAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPDhpap 352
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIVARfsHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEE---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 353 DRFWQLIEDHGITQFGVSPTAIRALRDHgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGG-TEV 431
Cdd:cd17642 265 ELFLRSLQDYKVQSALLVPTLFAFFAKS--TLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFK---LPGIRQGYGlTET 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 432 FGCFLMPlPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSSspsMTRRLWSGEDRYLEAYWSrfEDVWNH 511
Cdd:cd17642 340 TSAILIT-PEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGP---MIMKGYVNNPEATKALID--KDGWLH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 512 -GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElra 590
Cdd:cd17642 414 sGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEK--- 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 499204776 591 ELRDHVGDAHGKPFRPR-EVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd17642 491 EVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKI 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
270-625 |
5.14e-26 |
|
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: 109.66 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 270 SDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDqrpgdrfcWVS-DIGWMMGPWSLIGNHAFAGTIVMYEGA-- 346
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN--------WVVgDVTYLPLPATHIGGLWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 347 --PDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAghDLSSLRILGSTGEPW---DPESWRWFydhvggGDTP 421
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANA--TVPSLRLIGYGGSRAiaaDVRFIEAT------GLTN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANErGYLVARSssPSMTRRLWSGEDRYLEAY 501
Cdd:cd17635 145 TAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASF-GTIWIKS--PANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 502 wsrFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADA 581
Cdd:cd17635 222 ---IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499204776 582 ATPSAeLRAeLRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd17635 299 LDENA-IRA-LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
271-625 |
7.12e-26 |
|
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: 108.65 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTH---AGALVQPAKEIHFGFDQRpgdrfcwvsdigwMMGPWSLIGNHAFAGTI-VMYEGA 346
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErswIESFVCNEDLFNISGEDA-------------ILAPGPLSHSLFLYGAIsALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 347 PDH----PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaghdlSSLRILGSTGEPWDPESWRWFYDhvGGGDTPI 422
Cdd:cd17633 68 TFIgqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE------SKIKSIFSSGQKLFESTKKKLKN--IFPKANL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 423 INISGGTEV-FGCFLmpLPTESLKPCTLGGPGLGMDIDIVDDDGtsvrdaNERGYLVARSSspsmtrRLWSGedrYLEAY 501
Cdd:cd17633 140 IEFYGTSELsFITYN--FNQESRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSE------MVFSG---YVRGG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 502 WSRfEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAyVILAD 580
Cdd:cd17633 203 FSN-PDGWmSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499204776 581 AATPSAeLRAELRDHVgdahGKPFRPREVVFVDDLPKTQSGKLVR 625
Cdd:cd17633 281 KLTYKQ-LKRFLKQKL----SRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
120-640 |
9.24e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 108.69 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveATATRIADAEcsvvft 199
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI-------NTALRGPQLE------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdGFLRR-GDRVTLMD-TLNDAIEraghvdhtivydrlGIPADSLswtPRDEWW--DDAVATQSPT-FETHSMAAS---- 270
Cdd:PRK06155 112 --HILRNsGARLLVVEaALLAALE--------------AADPGDL---PLPAVWllDAPASVSVPAgWSTAPLPPLdapa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 --------DPCMLLYSSGTTGTPKGIVHTHA-----GALVQPAKEIhfgfdqRPGDRFCwvsdigwmmGPWSLIGNHAFA 337
Cdd:PRK06155 173 paaavqpgDTAAILYTSGTTGPSKGVCCPHAqfywwGRNSAEDLEI------GADDVLY---------TTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 338 GTI-VMYEGAPDHPAP----DRFWQLIEDHGITQF-----GVSPTAIRALRDHGDEHvaghdlsSLRILGSTGEPwdPES 407
Cdd:PRK06155 238 AFFqALLAGATYVLEPrfsaSGFWPAVRRHGATVTyllgaMVSILLSQPARESDRAH-------RVRVALGPGVP--AAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 408 WRWFYDHVGggdTPIINISGGTEVfgCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDaNERGYLVARSSSPSMt 487
Cdd:PRK06155 309 HAAFRERFG---VDLLDGYGSTET--NFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD-GEPGELLLRADEPFA- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 rrLWSGEDRYLEAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDD 566
Cdd:PRK06155 382 --FATGYFGMPEKTVEAWRNLWFHtGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 567 TTGEAAIAYVILAD--AATPSAELRaelrdhvgdaHGKP----FR-PREVVFVDDLPKTQSGKLVRRAVASAYTGADVTD 639
Cdd:PRK06155 460 LGEDEVMAAVVLRDgtALEPVALVR----------HCEPrlayFAvPRYVEFVAALPKTENGKVQKFVLREQGVTADTWD 529
|
.
gi 499204776 640 R 640
Cdd:PRK06155 530 R 530
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
120-600 |
9.87e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 108.83 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 -----------GDGFLRRGDRVTlmdtlndaieraghvdhtiVYDRLGIPADSLSWTPRDewwddavaTQSPTFETHSMA 268
Cdd:PRK09274 120 ipkahlarrlfGWGKPSVRRLVT-------------------VGGRLLWGGTTLATLLRD--------GAAAPFPMADLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 269 ASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRfcwvsDIGwMMGPWSLIgNHAFAGTIVMYEGAPD 348
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTH-GMFEAQIEALREDYGIEPGEI-----DLP-TFPLFALF-GPALGMTSVIPDMDPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPA---PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPESW----RWFYDhvgggDTP 421
Cdd:PRK09274 245 RPAtvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEAN--GIKLPSLRRVISAGAPVPIAVIerfrAMLPP-----DAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTEVfgcflMPLPT----ESLKPCT----------LGGPGLGMD---IDIVDD-----DGTSVRDANERGYLVA 479
Cdd:PRK09274 318 ILTPYGATEA-----LPISSiesrEILFATRaatdngagicVGRPVDGVEvriIAISDApipewDDALRLATGEIGEIVV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 480 rsSSPSMTRR-LWSGEDRYLEAYWSRFEDVWnH--GDWAQMDADGD-WFLhGRADDAINVAGRKVGPAEVEGALIDHDAV 555
Cdd:PRK09274 393 --AGPMVTRSyYNRPEATRLAKIPDGQGDVW-HrmGDLGYLDAQGRlWFC-GRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499204776 556 TQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHvGDAH 600
Cdd:PRK09274 469 KRSALVGVGVPGAQRPVLCVELEPGVACSKSALYQELRAL-AAAH 512
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
109-626 |
2.65e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.37 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 109 ACIWEGEDGTVRqqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE-VQSILyGIFKIGAI---AVPIFSGFGVE- 183
Cdd:PLN02246 40 PCLIDGATGRVY--TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEfVLAFL-GASRRGAVtttANPFYTPAEIAk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ---ATATRIADAECSVVFTGDGFLRRGDrVTLMdTLNDAIERAGHVDHTIVYDRLGIPADSLSwtPrdewwDDAVAtqsp 260
Cdd:PLN02246 117 qakASGAKLIITQSCYVDKLKGLAEDDG-VTVV-TIDDPPEGCLHFSELTQADENELPEVEIS--P-----DDVVA---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 tfethsmaasdpcmLLYSSGTTGTPKGIVHTHAGALVQPAKEI-----HFGFdqRPGDRFCWVSDigwMMGPWSL----- 330
Cdd:PLN02246 184 --------------LPYSSGTTGLPKGVMLTHKGLVTSVAQQVdgenpNLYF--HSDDVILCVLP---MFHIYSLnsvll 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 331 IGNHAFAGTIVM--YEGApdhpapdRFWQLIEDHGITQFGVSPTAIRALRDhgDEHVAGHDLSSLRILGSTGEPWDPESW 408
Cdd:PLN02246 245 CGLRVGAAILIMpkFEIG-------ALLELIQRHKVTIAPFVPPIVLAIAK--SPVVEKYDLSSIRMVLSGAAPLGKELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 409 RWFYDHV-----GGGdtpiiniSGGTEVFGCFLM-------PLPTeslKPCTLGGPGLGMDIDIVD-DDGTSVR--DANE 473
Cdd:PLN02246 316 DAFRAKLpnavlGQG-------YGMTEAGPVLAMclafakePFPV---KSGSCGTVVRNAELKIVDpETGASLPrnQPGE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 474 ---------RGYLvarsSSPSMTRRLWSgedryleaywsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPA 543
Cdd:PLN02246 386 icirgpqimKGYL----NDPEATANTID-------------KDGWLHtGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 544 EVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGD--AHGKpfRPREVVFVDDLPKTQSG 621
Cdd:PLN02246 449 ELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED---EIKQFVAKqvVFYK--RIHKVFFVDSIPKAPSG 523
|
....*
gi 499204776 622 KLVRR 626
Cdd:PLN02246 524 KILRK 528
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
123-626 |
1.00e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 105.49 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAV---PIFSGFGVEAtatRIADAECSVVFT 199
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTPRELEH---QLKDSGAEAIVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLRrgdrvtlmdTLNDAIERAGhVDHTIVY---DRLG----------------IPADSLswtPRDEWWDDAVAT-QS 259
Cdd:PRK07059 127 LENFAT---------TVQQVLAKTA-VKHVVVAsmgDLLGfkghivnfvvrrvkkmVPAWSL---PGHVRFNDALAEgAR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 260 PTFETHSMAASDPCMLLYSSGTTGTPKGIVHTHA---------GALVQPAkeihfgFDQRPG-DRFCWVSdigwmmgpwS 329
Cdd:PRK07059 194 QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRnivanvlqmEAWLQPA------FEKKPRpDQLNFVC---------A 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 330 LIGNHAFAGT----IVMYEGAPDH--PAPDRFWQLIEDHGITQFGVSP---TAIRALRDHGDehVAGHDLSSLRI-LGST 399
Cdd:PRK07059 259 LPLYHIFALTvcglLGMRTGGRNIliPNPRDIPGFIKELKKYQVHIFPavnTLYNALLNNPD--FDKLDFSKLIVaNGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 400 GEPWDPESWRWFydHVGGgdTPII--------------NISGGTEVFGCFLMPLPteslkpctlggpglGMDIDIVDDDG 465
Cdd:PRK07059 337 MAVQRPVAERWL--EMTG--CPITegyglsetspvatcNPVDATEFSGTIGLPLP--------------STEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 466 TSVrDANERGYLVARSssPSMtrrlwsgedryLEAYWSRFEDV---------WNHGDWAQMDADGDWFLHGRADDAINVA 536
Cdd:PRK07059 399 NDL-PLGEPGEICIRG--PQV-----------MAGYWNRPDETakvmtadgfFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 537 GRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHgkpfRPREVVFVDDLP 616
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYK----RPKFVEFRTELP 540
|
570
....*....|
gi 499204776 617 KTQSGKLVRR 626
Cdd:PRK07059 541 KTNVGKILRR 550
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
275-625 |
1.26e-23 |
|
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: 102.19 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGfDQRPGDRFcwvsdigwmmgpwsLIGN---HAF---AGTIV-MYEGAP 347
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA-DLTEDDRY--------------LIINpffHTFgykAGIVAcLLTGAT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPA----PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAghDLSSLRiLGSTGEPWDPESWRWFYDHVGGGDTpII 423
Cdd:cd17638 70 VVPVavfdVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKF--DLSSLR-AAVTGAATVPVELVRRMRSELGFET-VL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 424 NISGGTEVfGCFLMPLPTES--LKPCTLGGPGLGMDIDIVDDDGTSVRDAN-ERGYLvarsSSPSMTRRLWSgedrylea 500
Cdd:cd17638 146 TAYGLTEA-GVATMCRPGDDaeTVATTCGRACPGFEVRIADDGEVLVRGYNvMQGYL----DDPEATAEAID-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 501 ywsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILA 579
Cdd:cd17638 213 -----ADGWLHtGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 499204776 580 DAATPSAE-LRAELRDHVGDahgkpFR-PREVVFVDDLPKTQSGKLVR 625
Cdd:cd17638 288 PGVTLTEEdVIAWCRERLAN-----YKvPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
110-632 |
1.32e-23 |
|
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: 105.06 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 110 CIWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfGVEATATRI 189
Cdd:cd05906 28 ITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 190 ADAECSvvftgdgfLRR-----GDRVTLMDT-LNDAIERAGHVDHTIvyDRLGIPADSLSWTPRDEWWddavatqsptfe 263
Cdd:cd05906 104 NARLRK--------LRHiwqllGSPVVLTDAeLVAEFAGLETLSGLP--GIRVLSIEELLDTAADHDL------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 tHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALV-QPAKEIHFGFDqrPGDRFcwvsdIGWMmgPWSLIGNHAFAGTIVM 342
Cdd:cd05906 162 -PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILArSAGKIQHNGLT--PQDVF-----LNWV--PLDHVGGLVELHLRAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 343 YEG------APDH--PAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGH-DLSSLRILGSTGEPWDPESWRWFYD 413
Cdd:cd05906 232 YLGcqqvhvPTEEilADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAKTIRRLLR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 414 HV---GGGDTPIINISGGTEVF-GC-----FLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssP 484
Cdd:cd05906 312 LLepyGLPPDAIRPAFGMTETCsGViysrsFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLL-PEGEVGRLQVRG--P 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 485 SMTRRLWSGEDRYLEAYwsrFEDVW-NHGDWAQMDaDGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAV----TQAA 559
Cdd:cd05906 389 VVTKGYYNNPEANAEAF---TEDGWfRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsfTAAF 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 560 VVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGkpFRPREVVFV--DDLPKTQSGKLVRRAVASAY 632
Cdd:cd05906 465 AVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
123-628 |
1.83e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.58 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FlrrgdrvtlmdtlndaieRAGHVDHTIVYDRLGIPADSLSWTPRDEWWDDAVAtqsptfethsmaasdpcMLLYSSGTT 282
Cdd:PRK12316 3164 L------------------RLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLA-----------------YVIYTSGST 3208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAfAGTIVMYEGAPDHPAPDRFWQLIEDH 362
Cdd:PRK12316 3209 GKPKGVGIRH-SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLM-SGARVVLAGPEDWRDPALLVELINSE 3286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 363 GITQFGVSPTAIRALRdhgdEHVAGHDLSSLRILGSTGEPWDPE-SWRWFydhvggGDTPIINISGGTE-VFGCFLMPLP 440
Cdd:PRK12316 3287 GVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADlQQQVF------AGLPLYNLYGPTEaTITVTHWQCV 3356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 441 TESLKPCTLGGPGLGMDIDIVDDDGTSVRDAN-ERGYLVARSSSPSMTRRLWSGEDRYLEAYWSRFEDVWNHGDWAQMDA 519
Cdd:PRK12316 3357 EEGKDAVPIGRPIANRACYILDGSLEPVPVGAlGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRA 3436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 520 DGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpddtTGEAAIAYVILADaatPSAELRAELRDHVGDA 599
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPED---EAGDLREALKAHLKAS 3509
|
490 500
....*....|....*....|....*....
gi 499204776 600 HGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK12316 3510 LPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
123-650 |
4.81e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 104.34 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRRGDRVTLMDtlndaieraghvdhtivydrlgiPADSLSWTPRDEWWD-DAVATQSPTFEThsmaasdpcmllYSSGT 281
Cdd:PRK06060 112 LRDRFQPSRVAE-----------------------AAELMSEAARVAPGGyEPMGGDALAYAT------------YTSGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 282 TGTPKGIVHTHAGALVQPAKEIHFGFDQRPGD------RFCWVSDIG---WMmgPWSLIGNHAFAGTIVMYEGAPDHPAp 352
Cdd:PRK06060 157 TGPPKAAIHRHADPLTFVDAMCRKALRLTPEDtglcsaRMYFAYGLGnsvWF--PLATGGSAVINSAPVTPEAAAILSA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 353 dRFWQLIEdHGITQF------GVSPTAIRalrdhgdehvaghdlsSLRILGSTGEPWDPESWRWFYDHVGGgdTPIINIS 426
Cdd:PRK06060 234 -RFGPSVL-YGVPNFfarvidSCSPDSFR----------------SLRCVVSAGEALELGLAERLMEFFGG--IPILDGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEVFGCFLMPlPTESLKPCTLGGPGLGMDIDIVDDDGTSvrdanergylvarsSSPSMTRRLWSGEDRYLEAYWSRFE 506
Cdd:PRK06060 294 GSTEVGQTFVSN-RVDEWRLGTLGRVLPPYEIRVVAPDGTT--------------AGPGVEGDLWVRGPAIAKGYWNRPD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 507 DVWNHGDW------AQMDADGdWFLHG-RADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILA 579
Cdd:PRK06060 359 SPVANEGWldtrdrVCIDSDG-WVTYRcRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVAT 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 580 DAATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGADVTDRSSIEN----PAVLD 650
Cdd:PRK06060 438 SGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPgsgvRAQRD 512
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
115-626 |
7.46e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 102.75 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 115 EDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEvqsilYGIFKIGAIAVP-IFSGFGVEATATRIA-DA 192
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAE-----YGIVALGIMAAGgVFSGANPTALESEIKkQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ECSvvftgdgflrrGDRVTLMDTLNdaieraghvdhtivYDR---LGIP---------ADSLSWTPRDEWWDDAvatqSP 260
Cdd:PLN02330 124 EAA-----------GAKLIVTNDTN--------------YGKvkgLGLPvivlgeekiEGAVNWKELLEAADRA----GD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 TFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIhfgFDQRPGdrfcwvsdigwMMGPWSLIG----NHAF 336
Cdd:PLN02330 175 TSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL---FSVGPE-----------MIGQVVTLGlipfFHIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 337 AGTIVMYEGAPDHP---APDRFWQLIEDHGITQFGVS-----PTAIRALRDhgDEHVAGHDLSSLRI--LGSTGEPWDPE 406
Cdd:PLN02330 241 GITGICCATLRNKGkvvVMSRFELRTFLNALITQEVSfapivPPIILNLVK--NPIVEEFDLSKLKLqaIMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 407 SWRWFYDHVgggdtPIINISggtEVFGcflmpLPTESLKPCTLGGPGLG---------------MDIDIVDDDGTSVRDA 471
Cdd:PLN02330 319 LLTAFEAKF-----PGVQVQ---EAYG-----LTEHSCITLTHGDPEKGhgiakknsvgfilpnLEVKFIDPDTGRSLPK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 472 NERGYLVARSSSpSMTRRLWSGE--DRYLEaywsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGA 548
Cdd:PLN02330 386 NTPGELCVRSQC-VMQGYYNNKEetDRTID------EDGWLHtGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 549 LIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGD--AHGKpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:PLN02330 459 LLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE---DILNFVAAnvAHYK--KVRVVQFVDSIPKSLSGKIMRR 533
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
122-631 |
4.01e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 100.86 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 122 QTYhdlhQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGD 201
Cdd:PLN03102 44 QTY----DRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRGDRVTLMdtlndaieraghvdhtivydrlgIPADSLSWTPRDEWWDDAVATQSPTFE-------------THSMA 268
Cdd:PLN03102 120 SFEPLAREVLHL-----------------------LSSEDSNLNLPVIFIHEIDFPKRPSSEeldyecliqrgepTPSLV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 269 AS--------DPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIhFGFDQRPGDRFCWVSDI----GWMMgPWSLIgnhAF 336
Cdd:PLN03102 177 ARmfriqdehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI-IGWEMGTCPVYLWTLPMfhcnGWTF-TWGTA---AR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 337 AGTIVMYEgapdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDhGDEHVAGHDLSSLRILgsTGEPWDPESWRWFYDHVG 416
Cdd:PLN03102 252 GGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL--TGGSPPPAALVKKVQRLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 417 ggdTPIINISGGTEVFGCFL----------MPLPTESLKPCTLGGPGLGM-DIDIVDDDG--TSVRDANERGYLVARSSS 483
Cdd:PLN03102 325 ---FQVMHAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGVSILGLaDVDVKNKETqeSVPRDGKTMGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 psmtrrLWSGEDRYLEAYWSRFEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVG 562
Cdd:PLN03102 402 ------IMKGYLKNPKATSEAFKHGWlNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 563 VPDDTTGEAAIAYVILADAATPSAELRAELRDHVGD-----AHGKP--FRPREVVFVDDLPKTQSGKLVR---RAVASA 631
Cdd:PLN03102 476 MPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDlieycRENLPhfMCPRKVVFLQELPKNGNGKILKpklRDIAKG 554
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
123-622 |
6.04e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 100.27 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveATATRIAD-------AECS 195
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI-------NPAYRLSEleyalnqSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGDGFlRRGDRVTLMDTL----------NDAIERAGHVDHTIvydRLG--IPADSLSWtprDEWWDDAVATQSPTFE 263
Cdd:PRK08315 118 ALIAADGF-KDSDYVAMLYELapelatcepgQLQSARLPELRRVI---FLGdeKHPGMLNF---DELLALGRAVDDAELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 TH--SMAASDPCMLLYSSGTTGTPKGIVHTHA-----GALVqpAKEIHFGfdqrPGDRFCwvsdI--------GWMMGPW 328
Cdd:PRK08315 191 ARqaTLDPDDPINIQYTSGTTGFPKGATLTHRnilnnGYFI--GEAMKLT----EEDRLC----IpvplyhcfGMVLGNL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 329 SLIgNHAfaGTIVMyegapdhPApDRF-----WQLIEDHGITQ-FGVsPTAIRALRDHGDehVAGHDLSSLRilgsTGep 402
Cdd:PRK08315 261 ACV-THG--ATMVY-------PG-EGFdplatLAAVEEERCTAlYGV-PTMFIAELDHPD--FARFDLSSLR----TG-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 403 wdpeswrwfydhVGGGDT-PI------INISGGTEVFGCFLM----PLPTESL------KPC-TLGGPGLGMDIDIVDDD 464
Cdd:PRK08315 321 ------------IMAGSPcPIevmkrvIDKMHMSEVTIAYGMtetsPVSTQTRtddpleKRVtTVGRALPHLEVKIVDPE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 465 GTSVRDANERGYLVARSSS--------PSMTRRlwsgedryleaywSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINV 535
Cdd:PRK08315 389 TGETVPRGEQGELCTRGYSvmkgywndPEKTAE-------------AIDADGWMHtGDLAVMDEEGYVNIVGRIKDMIIR 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 536 AGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAE-LRAELRDHVgdAHGKPfrPREVVFVDD 614
Cdd:PRK08315 456 GGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEdVRDFCRGKI--AHYKI--PRYIRFVDE 531
|
....*...
gi 499204776 615 LPKTQSGK 622
Cdd:PRK08315 532 FPMTVTGK 539
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
116-628 |
9.84e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 99.44 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:PRK06018 34 EGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGDGFlrrgdrVTLMDTLNDAIEragHVDHTIVY-DRLGIPADSLswtPRDEWWDDAVATQSPTFETHSMAASDPCM 274
Cdd:PRK06018 114 VVITDLTF------VPILEKIADKLP---SVERYVVLtDAAHMPQTTL---KNAVAYEEWIAEADGDFAWKTFDENTAAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALvqpakeIHFGFDQRPGDRFCWVSDIGWMMGP------WSLIGNHAFAGTIVMYEGAPD 348
Cdd:PRK06018 182 MCYTSGTTGDPKGVLYSHRSNV------LHALMANNGDALGTSAADTMLPVVPlfhansWGIAFSAPSMGTKLVMPGAKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPdrFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAG-HDLSSLRILGSTGepwdPESW-RWFYDHvgggDTPIINIS 426
Cdd:PRK06018 256 DGAS--VYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKlPHLKMVVCGGSAM----PRSMiKAFEDM----GVEVRHAW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 427 GGTEvfgcfLMPLPT-ESLKP--------------CTLGGPGLGMDIDIVDDDGTSV-RDANERGYLVARSssPSMTRRL 490
Cdd:PRK06018 326 GMTE-----MSPLGTlAALKPpfsklpgdarldvlQKQGYPPFGVEMKITDDAGKELpWDGKTFGRLKVRG--PAVAAAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 491 WSGEDRYLEAywsrfEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGE 570
Cdd:PRK06018 399 YRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 571 AAIAYVILADAATPSaelRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK06018 474 RPLLIVQLKPGETAT---REEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
104-628 |
1.14e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.01 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:PRK05691 1144 TPERIALVWDGG-----SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAE 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAEcsvvftgdgflrrgdrVTLMDTLNDAIERAGHVDHTIVydrlgIPADSLSWtprDEWwddavATQSPTFE 263
Cdd:PRK05691 1219 RLAYMLADSG----------------VELLLTQSHLLERLPQAEGVSA-----IALDSLHL---DSW-----PSQAPGLH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 THsmaASDPCMLLYSSGTTGTPKGIVHTHAgALvqpakeihfgfdqrpGDRFCWV--------SDIGWMMGP-------- 327
Cdd:PRK05691 1270 LH---GDNLAYVIYTSGSTGQPKGVGNTHA-AL---------------AERLQWMqatyalddSDVLMQKAPisfdvsvw 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 328 ---WSLIgnhafAGTIVMYEGAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRdhgDEHVAGhDLSSLRILGSTGEPWD 404
Cdd:PRK05691 1331 ecfWPLI-----TGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI---DEPLAA-ACTSLRRLFSGGEALP 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 405 PESWR--------------------------WFYDHVGGGDTPIINISGGT--EVFGCFLMPLPTESLKPCTLGGPGLGm 456
Cdd:PRK05691 1402 AELRNrvlqrlpqvqlhnrygptetainvthWQCQAEDGERSPIGRPLGNVlcRVLDAELNLLPPGVAGELCIGGAGLA- 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 457 didivdddgtsvrdaneRGYLvarsSSPSMTrrlwsgEDRYL-EAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINV 535
Cdd:PRK05691 1481 -----------------RGYL----GRPALT------AERFVpDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKL 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 536 AGRKVGPAEVEGALIDHDAVTQAAVVgVPDDTTGEAAIAYVILADAATPSAE-----LRAELRDHVgdahgkpfRPREVV 610
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAErlkaaLAAELPEYM--------VPAQLI 1604
|
570
....*....|....*...
gi 499204776 611 FVDDLPKTQSGKLVRRAV 628
Cdd:PRK05691 1605 RLDQMPLGPSGKLDRRAL 1622
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
120-616 |
1.72e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 97.92 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAEcsvvft 199
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLrrgdrvtlmdtlndaieraghvdhtivydrlGIPAdslswtprdewwddavatqsptfethsmaASDPCMLLYSS 279
Cdd:cd05910 75 PDAFI-------------------------------GIPK-----------------------------ADEPAAILFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDR----FCWVSDIGWMMGPWSLIGNhafagtivMYEGAPDHPAPDRF 355
Cdd:cd05910 95 GSTGTPKGVVYRH-GTFAAQIDALRQLYGIRPGEVdlatFPLFALFGPALGLTSVIPD--------MDPTRPARADPQKL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 356 WQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDLSSLRILGSTGEPWDPESWRWFYDHVgGGDTPIINISGGTEVfgcf 435
Cdd:cd05910 166 VGAIRQYGVSIVFGSPALLERVARYCAQH--GITLPSLRRVLSAGAPVPIALAARLRKML-SDEAEILTPYGATEA---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 436 lMPL--------------PTESLKPCTLGGPGLGMDIDIV--DD------DGTSVRDANERGYLVArsSSPSMTRRLWSG 493
Cdd:cd05910 239 -LPVssigsrellatttaATSGGAGTCVGRPIPGVRVRIIeiDDepiaewDDTLELPRGEIGEITV--TGPTVTPTYVNR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 494 EDR-YLEAYWSRFEDVWNH-GDWAQMDADGD-WFLhGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGE 570
Cdd:cd05910 316 PVAtALAKIDDNSEGFWHRmGDLGYLDDEGRlWFC-GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQL 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499204776 571 AAIAYVILADAATPSAELRAELRDhVGDAHGKPFRPREVVFVDDLP 616
Cdd:cd05910 395 PVLCVEPLPGTITPRARLEQELRA-LAKDYPHTQRIGRFLIHPSFP 439
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
116-623 |
1.85e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 98.63 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGL-----YMPMvpevqSILYGIFKIGAIAVPIFSGFGVEATATRIA 190
Cdd:PRK07008 34 EGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTlawngYRHL-----EAYYGVSGSGAVCHTINPRLFPEQIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 191 DAECSVVFTGDGFLrrgdrvTLMDTLNDaieRAGHVDHTIVY-DRLGIPADSLSWTPRDEWwddaVATQSPTFETHSMAA 269
Cdd:PRK07008 109 HAEDRYVLFDLTFL------PLVDALAP---QCPNVKGWVAMtDAAHLPAGSTPLLCYETL----VGAQDGDYDWPRFDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 270 SDPCMLLYSSGTTGTPKGIVHTH--------AGALvqpakeihfgfdqrPGDRFCWVSDIGWMMGP------WSLIGNHA 335
Cdd:PRK07008 176 NQASSLCYTSGTTGNPKGALYSHrstvlhayGAAL--------------PDAMGLSARDAVLPVVPmfhvnaWGLPYSAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 336 FAGTIVMYEGapdhPAPD--RFWQLIEDHGITQFGVSPTAIRALRDHGDEhvAGHDLSSLR--ILGSTGEPwdPESWRWF 411
Cdd:PRK07008 242 LTGAKLVLPG----PDLDgkSLYELIEAERVTFSAGVPTVWLGLLNHMRE--AGLRFSTLRrtVIGGSACP--PAMIRTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 YDHVGggdTPIINISGGTEvfgcfLMPLPTEslkpCTL-------------------GGPGLGMDIDIVDDDGTSVR-DA 471
Cdd:PRK07008 314 EDEYG---VEVIHAWGMTE-----MSPLGTL----CKLkwkhsqlpldeqrkllekqGRVIYGVDMKIVGDDGRELPwDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 472 NERGYLVARSssPSMTRRLWSGEDRYLEAYWsrfedvWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALID 551
Cdd:PRK07008 382 KAFGDLQVRG--PWVIDRYFRGDASPLVDGW------FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 552 HDAVTQAAVVGVPDDTTGEAAIAYVILadaaTPSAEL-RAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKL 623
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVK----RPGAEVtREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
113-630 |
2.20e-21 |
|
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: 97.38 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 113 EGEDGTVrqqTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveatatriada 192
Cdd:cd17653 17 ESLGGSL---TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ecsvvftgDGFLRRGDRVTLMDTLNDAIeraghvdhtIVYDRlgipadslswtprdewwddavatqsptfethsmAASDP 272
Cdd:cd17653 78 --------DAKLPSARIQAILRTSGATL---------LLTTD---------------------------------SPDDL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 273 CMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMyegaPDHPAP 352
Cdd:cd17653 108 AYIIFTSGSTGIPKGVMVPH-RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL----ADPSDP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 353 drFWQLIEDhgITQFGVSPTAIRALRDhgdehvagHDLSSLRILGSTGEPWDP---ESWrwfydhvgGGDTPIINISGGT 429
Cdd:cd17653 183 --FAHVART--VDALMSTPSILSTLSP--------QDFPNLKTIFLGGEAVPPsllDRW--------SPGRRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 430 EVFGCFLMPLpTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPSMTRRlwsgedRYL 498
Cdd:cd17653 243 ECTISSTMTE-LLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVgeicisgvqvaRGYL----GNPALTAS------KFV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 499 EAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDA-VTQAAVVGVpddttGEAAIAYVI 577
Cdd:cd17653 312 PDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIVV-----NGRLVAFVT 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499204776 578 LADAATpsAELRAELRDHVGDAHgkpfRPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:cd17653 387 PETVDV--DGLRSELAKHLPSYA----VPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
104-627 |
2.31e-21 |
|
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: 97.51 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:cd17644 13 TPDAVAVVFEDQ-----QLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAECSVVFTgdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfE 263
Cdd:cd17644 88 RLTYILEDAQISVLLT---------------------------------------------------------------Q 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 THSMAasdpcMLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMY 343
Cdd:cd17644 105 PENLA-----YVIYTSGSTGKPKGVMIEHQ-SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 344 EGAPdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDlSSLRILGSTGEPWDPESWR-WFydHVGGGDTPI 422
Cdd:cd17644 179 PEEM-RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRqWQ--KNVGNFIQL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 423 INISGGTE----VFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDD------GT-------SVRDAneRGYLvarsSSPS 485
Cdd:cd17644 255 INVYGPTEatiaATVCRLTQLTERNITSVPIGRPIANTQVYILDENlqpvpvGVpgelhigGVGLA--RGYL----NRPE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRrlwsgeDRYLEA--YWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGV 563
Cdd:cd17644 329 LTA------EKFISHpfNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVR 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 564 PDDTTGEAAIAYVILADAATPS-AELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:cd17644 403 EDQPGNKRLVAYIVPHYEESPStVELRQFLKAKLPDY----MIPSAFVVLEELPLTPNGKIDRRA 463
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
269-630 |
2.36e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 97.75 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 269 ASDPCMLLYSSGTTGTPKGIVhthagalvQPAKEIHFGFDQRpGDRFCWVSDI------------GWMMGpwsLIGNHAF 336
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVV--------LSRRAIAADLDAL-AEAWQWTADDvlvhglplfhvhGLVLG---VLGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 337 AGTIVmyegapdH---PAPDRFWQLIEDHGITQFGVsPTAIRALRDHGDEHVAghdLSSLRIL--GSTGEPwDPESWRwF 411
Cdd:PRK07787 195 GNRFV-------HtgrPTPEAYAQALSEGGTLYFGV-PTVWSRIAADPEAARA---LRGARLLvsGSAALP-VPVFDR-L 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 YDHVGggdTPIINISGGTEVfgcfLMPLPTES---LKPCTLGGPGLGMDIDIVDDDGTSV-RDANERGYLVARSSSpsmt 487
Cdd:PRK07787 262 AALTG---HRPVERYGMTET----LITLSTRAdgeRRPGWVGLPLAGVETRLVDEDGGPVpHDGETVGELQVRGPT---- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 rrLWSGedrYL---EAYWSRF-EDVWNH-GDWAQMDADGDWFLHGR-ADDAINVAGRKVGPAEVEGALIDHDAVTQAAVV 561
Cdd:PRK07787 331 --LFDG---YLnrpDATAAAFtADGWFRtGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVV 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 562 GVPDDTTGEAAIAYVILADAATPSaelraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:PRK07787 406 GVPDDDLGQRIVAYVVGADDVAAD-----ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
115-623 |
4.22e-21 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 97.02 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 115 EDGTVRQQTYHDLHQQANRVANALaERGIGEGDTVGLYMPmvPEVQSIL--YGIFKIGAIAVPIFSGFGVEATATRIADA 192
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLP--PSAGGALanFALALSGKVPVMLNYTAGLRELRACIKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 193 ECSVVFTGDGFLRRGDRVTLMDTLNDAieraghvdhTIVY--DRLGipadSLSW----------TPRDEWWDD--AVATQ 258
Cdd:cd05909 78 GIKTVLTSKQFIEKLKLHHLFDVEYDA---------RIVYleDLRA----KISKadkckaflagKFPPKWLLRifGVAPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 259 SPtfethsmaaSDPCMLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRfcwvsdigwMMGPWSLIGNHAFAG 338
Cdd:cd05909 145 QP---------DDPAVILFTSGSEGLPKGVVLSHKN-LLANVEQITAIFDPNPEDV---------VFGALPFFHSFGLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 339 TIVM--YEGAPD--HPAPDRFWQ---LIEDHGITQFGVSPTAIRA-LRDHGDEhvaghDLSSLRILGSTGEPWDPESWRW 410
Cdd:cd05909 206 CLWLplLSGIKVvfHPNPLDYKKipeLIYDKKATILLGTPTFLRGyARAAHPE-----DFSSLRLVVAGAEKLKDTLRQE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 411 FYDHVGggdTPIINISGGTEVFGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARssSPSMTRRL 490
Cdd:cd05909 281 FQEKFG---IRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVR--GPNVMLGY 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 491 WSGEDRYLEAYwsrfEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAV-TQAAVVGVPDDTT 568
Cdd:cd05909 356 LNEPELTSFAF----GDGWyDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRK 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 569 GEAAIAYViladaaTPSAELRAELRDHVgDAHGKP--FRPREVVFVDDLPKTQSGKL 623
Cdd:cd05909 432 GEKIVLLT------TTTDTDPSSLNDIL-KNAGISnlAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
94-621 |
5.97e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 96.74 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 94 VDRHASVDAGtrnHVACIWEGedgtvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIA 173
Cdd:PRK06164 16 LDAHARARPD---AVALIDED-----RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 174 VPIFSGFGVEATATRIADAECSVVFTGDGFlrRGDrvtlmdtlnDAIERAGHVDHTIVYDRLGIPA--DSLSWTPRDEWW 251
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVWPGF--KGI---------DFAAILAAVPPDALPPLRAIAVvdDAADATPAPAPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 252 DDAVATQSPTFETHSMAAS-----DPCMLLYS-SGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMM 325
Cdd:PRK06164 157 ARVQLFALPDPAPPAAAGEraadpDAGALLFTtSGTTSGPKLVLHRQA-TLLRHARAIARAYGYDPGAVLLAALPFCGVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 326 GPWSLIGNHAFAGTIVM---YEGApdhpapdRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvagHDLSSLRILG-STGE 401
Cdd:PRK06164 236 GFSTLLGALAGGAPLVCepvFDAA-------RTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFGfASFA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 402 PWDPESWRWFYDHvgggDTPIINISGGTEVFGCFLMPLPTESLKPCTLGGpGLGMD----IDIVDDDGTSVRDANERGYL 477
Cdd:PRK06164 306 PALGELAALARAR----GVPLTGLYGSSEVQALVALQPATDPVSVRIEGG-GRPASpearVRARDPQDGALLPDGESGEI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 478 VARSssPSMTRRLWSGEDRYLEAYWSrfeDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVT 556
Cdd:PRK06164 381 EIRA--PSLMRGYLDNPDATARALTD---DGYfRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVA 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 557 QAAVVGVPDDTTGEAAiAYVILADAATP-SAELRAELRDHVGdahgkPFR-PREVVFVDDLPKTQSG 621
Cdd:PRK06164 456 AAQVVGATRDGKTVPV-AFVIPTDGASPdEAGLMAACREALA-----GFKvPARVQVVEAFPVTESA 516
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
271-621 |
9.43e-21 |
|
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: 93.91 E-value: 9.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHAGALVQpakEIHFGFDQRPGDRFCWVSD-----IGWMMGpwsLIGNHAFAGTIVMYEG 345
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQ---ALVLAVLQAIDEGTVFLNSgplfhIGTLMF---TLATFHAGGTNVFVRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 ApdhpAPDRFWQLIEDHGITQ-FGVSPT--AIRALRDHGdehvaGHDLSSLRILGSTGEPWD---PESWRWFYdHVGGgd 419
Cdd:cd17636 75 V----DAEEVLELIEAERCTHaFLLPPTidQIVELNADG-----LYDLSSLRSSPAAPEWNDmatVDTSPWGR-KPGG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 420 tpiiniSGGTEVFGCFLMPlpteslkpcTLGGPGLG--------MDIDIVDDDGTSVRDAnERGYLVARSssPSMTRRLW 491
Cdd:cd17636 143 ------YGQTEVMGLATFA---------ALGGGAIGgagrpsplVQVRILDEDGREVPDG-EVGEIVARG--PTVMAGYW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 492 SGEDryLEAywSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGE 570
Cdd:cd17636 205 NRPE--VNA--RRTRGGWHHtNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499204776 571 AAIAYVILADAATPSAelrAELRDHVGDAHGKPFRPREVVFVDDLPKTQSG 621
Cdd:cd17636 281 SVKAIVVLKPGASVTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
120-628 |
1.31e-20 |
|
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: 94.97 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethsmaASDPCMLLYSS 279
Cdd:cd05907 84 ED-------------------------------------------------------------------PDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFcwVSdigwmMGPWSlignHAFAGTIVMYegAP-DHPAPDRFWQL 358
Cdd:cd05907 97 GTTGRPKGVMLSHRN-ILSNALALAERLPATEGDRH--LS-----FLPLA----HVFERRAGLY--VPlLAGARIYFASS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 359 IEDHGITQFGVSPT----AIRALRDH--GDEHVAGHDL----------SSLRILGSTGEPWDPESWRWFYdHVGggdTPI 422
Cdd:cd05907 163 AETLLDDLSEVRPTvflaVPRVWEKVyaAIKVKAVPGLkrklfdlavgGRLRFAASGGAPLPAELLHFFR-ALG---IPV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 423 INISGGTEVFGCFLMPLPtESLKPCTLGGPGLGMDIDIVDDdgtsvrdanerGYLVARssSPSMTRRLWSGEDRYLEAYw 502
Cdd:cd05907 239 YEGYGLTETSAVVTLNPP-GDNRIGTVGKPLPGVEVRIADD-----------GEILVR--GPNVMLGYYKNPEATAEAL- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 503 srFEDVWNH-GDWAQMDADGdwFLH--GRADD-AINVAGRKVGPAEVEGALIDHDAVTQAAVVG----------VPDDTT 568
Cdd:cd05907 304 --DADGWLHtGDLGEIDEDG--FLHitGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEA 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499204776 569 GEA-----AIAYVILADAATpSAELRAELRDHVGDAHG--------KPFRPREVVF-VDDLPKTQSGKLVRRAV 628
Cdd:cd05907 380 LEAwaeehGIAYTDVAELAA-NPAVRAEIEAAVEAANArlsryeqiKKFLLLPEPFtIENGELTPTLKLKRPVI 452
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
123-626 |
2.68e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.91 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAER-GIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGd 201
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 gflrrgdrvtlmdtlNDAIERAGhvdhtivydRLGIPADSLSwtprDEWWDDAVATQSPTFETHSMAASDPCM------- 274
Cdd:PLN02574 147 ---------------PENVEKLS---------PLGVPVIGVP----ENYDFDSKRIEFPKFYELIKEDFDFVPkpvikqd 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 ----LLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQ--RPGDRFCWVSDIGwMMGPWSL----IGNHAFAGTIVMYE 344
Cdd:PLN02574 199 dvaaIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeYPGSDNVYLAALP-MFHIYGLslfvVGLLSLGSTIVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 345 gapdhpapdRF-----WQLIEDHGITQFGVSPTAIRALRdHGDEHVAGHDLSSLRILGSTGEPWDPESWRWF---YDHVG 416
Cdd:PLN02574 278 ---------RFdasdmVKVIDRFKVTHFPVVPPILMALT-KKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvqtLPHVD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 417 ggdtpIINISGGTEVFGCFLMPLPTESLKP-CTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMTRRLWSGEd 495
Cdd:PLN02574 348 -----FIQGYGMTESTAVGTRGFNTEKLSKySSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQG--PGVMKGYLNNP- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 496 rylEAYWSRF-EDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAI 573
Cdd:PLN02574 420 ---KATQSTIdKDGWLRtGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 499204776 574 AYVILADAATPSAElraELRDHVGDaHGKPFRP-REVVFVDDLPKTQSGKLVRR 626
Cdd:PLN02574 497 AFVVRRQGSTLSQE---AVINYVAK-QVAPYKKvRKVVFVQSIPKSPAGKILRR 546
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
106-632 |
5.59e-20 |
|
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: 93.38 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVA-CIWEGedgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE-VQSILyGIFKIGAIAVPIfsgfGVE 183
Cdd:cd05918 14 DAPAvCAWDG------SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWaVVAML-AVLKAGGAFVPL----DPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATR----IADAECSVVFTGDgflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqs 259
Cdd:cd05918 83 HPLQRlqeiLQDTGAKVVLTSS---------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 260 ptfethsmaASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCW-------VSdIGWMMGPWslig 332
Cdd:cd05918 105 ---------PSDAAYVIFTSGSTGKPKGVVIEH-RALSTSALAHGRALGLTSESRVLQfasytfdVS-ILEIFTTL---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 333 nhAFAGTIVMyegAPDHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHgdehvaghDLSSLRILGSTGEPWDPESW-RWf 411
Cdd:cd05918 170 --AAGGCLCI---PSEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPE--------DVPSLRTLVLGGEALTQSDVdTW- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 ydhvgGGDTPIINISGGTEVFGCFLMPLPTESLKPCTLGgPGLGMDIDIVD-DDGTSVRDANE------------RGYL- 477
Cdd:cd05918 236 -----ADRVRLINAYGPAECTIAATVSPVVPSTDPRNIG-RPLGATCWVVDpDNHDRLVPIGAvgelliegpilaRGYLn 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 478 ----VARS--SSPSMTRRLWSGEDRYLeaYWSrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALID 551
Cdd:cd05918 310 dpekTAAAfiEDPAWLKQEGSGRGRRL--YRT--------GDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 552 HDAVTQAAVVGV--PDDTTGEAAIAYVILADAATPS--------AELRAELRDHVGDAHGK------PF-RPREVVFVDD 614
Cdd:cd05918 380 SLPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGSSSGsgdgdslfLEPSDEFRALVAELRSKlrqrlpSYmVPSVFLPLSH 459
|
570
....*....|....*...
gi 499204776 615 LPKTQSGKLVRRAVASAY 632
Cdd:cd05918 460 LPLTASGKIDRRALRELA 477
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
448-626 |
5.92e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.97 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 448 TLGGPGLGMDIDIVDDDGTSVrDANERGylvarssspsmtrRLWSGEDRYLEAYWSRFE-------DVWNH-GDWAQMDA 519
Cdd:PRK08974 379 SIGLPVPSTEIKLVDDDGNEV-PPGEPG-------------ELWVKGPQVMLGYWQRPEatdevikDGWLAtGDIAVMDE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 520 DGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGda 599
Cdd:PRK08974 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLT-- 522
|
170 180
....*....|....*....|....*..
gi 499204776 600 hGKPFrPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK08974 523 -GYKV-PKLVEFRDELPKSNVGKILRR 547
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
116-601 |
3.55e-19 |
|
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: 90.99 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECS 195
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 VVFTGdgflrrgdrvtlmdTLNDAIERAGHVDHTIVydrlGIPADSLSWTPRDEWWDDAVATQSPTFETHSMAASDPCML 275
Cdd:cd05932 81 ALFVG--------------KLDDWKAMAPGVPEGLI----SISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 276 LYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDR------FCWVSDIGWMMGPWsLIGnhafaGTIVMYEGAPDH 349
Cdd:cd05932 143 IYTSGTTGQPKGVMLTF-GSFAWAAQAGIEHIGTEENDRmlsylpLAHVTERVFVEGGS-LYG-----GVLVAFAESLDT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 PAPD-------------RFWQLIEDHGITQFGVSP-------TAIRALRDHgdEHVAGHDLSSLRILGSTGEPWDPESWR 409
Cdd:cd05932 216 FVEDvqrarptlffsvpRLWTKFQQGVQDKIPQQKlnlllkiPVVNSLVKR--KVLKGLGLDQCRLAGCGSAPVPPALLE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 410 WfYDHVGggdTPIINISGGTEVFGCFLMPLPTESlKPCTLGGPGLGMDIDIVDDDGTSVRdanERGYLVARSSSPSMTRR 489
Cdd:cd05932 294 W-YRSLG---LNILEAYGMTENFAYSHLNYPGRD-KIGTVGNAGPGVEVRISEDGEILVR---SPALMMGYYKDPEATAE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 490 LWSgedryleaywsrfEDVWNH-GDWAQMDADGDWFLHGRADDAINVA-GRKVGPAEVEGALIDHDAVTQAAVVGvpddT 567
Cdd:cd05932 366 AFT-------------ADGFLRtGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG----S 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499204776 568 TGEAAIAYVILADAATPSA------ELRAELRDHVGDAHG 601
Cdd:cd05932 429 GLPAPLALVVLSEEARLRAdafaraELEASLRAHLARVNS 468
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
120-631 |
5.19e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.01 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGlympmVPEVQSILY-----GIFKIGAIAVPIFSGFGVEATATRIADAEC 194
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVA-----IAALNSDLYlewllAVACAGGIVAPLNYRWSFEEAKSAMLLVRP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 195 SVVFTGDGFLRRGDRVTlmdtlNDAIERAG-HVDHTIVYDRLGIPADSLSWTprDEWWDDAVATQSPTFethSMAASDPC 273
Cdd:PLN02860 106 VMLVTDETCSSWYEELQ-----NDRLPSLMwQVFLESPSSSVFIFLNSFLTT--EMLKQRALGTTELDY---AWAPDDAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 274 MLLYSSGTTGTPKGIVHTHAGALVQPAKEIHF-GFDQrpgdrfcwvSDIGWMMGPWSLIGNHAFAGTIVMYEGA----PD 348
Cdd:PLN02860 176 LICFTSGTTGRPKGVTISHSALIVQSLAKIAIvGYGE---------DDVYLHTAPLCHIGGLSSALAMLMVGAChvllPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPDRFwQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLR-ILGstgepwdpeswrwfydhvGGGDTPIINISG 427
Cdd:PLN02860 247 FDAKAAL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRkILN------------------GGGSLSSRLLPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 428 GTEVFGCF----------------LMPL--PTESLKPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSSSPSMTRR 489
Cdd:PLN02860 308 AKKLFPNAklfsaygmteacssltFMTLhdPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVGR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 490 LWSGEDRYLEAYW--------SRFEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAV 560
Cdd:PLN02860 388 ILTRGPHVMLGYWgqnsetasVLSNDGWlDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 561 VGVPDDTTGEAAIAYV------ILADAATPSAE-----LRAELRDHVGDAHGKPFR-PRE-VVFVDDLPKTQSGKL---- 623
Cdd:PLN02860 468 VGVPDSRLTEMVVACVrlrdgwIWSDNEKENAKknltlSSETLRHHCREKNLSRFKiPKLfVQWRKPFPLTTTGKIrrde 547
|
....*...
gi 499204776 624 VRRAVASA 631
Cdd:PLN02860 548 VRREVLSH 555
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
106-630 |
6.85e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 90.22 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVAcIWEGEdgtvRQQTYHDLHQQANRVANALAERGiGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT 185
Cdd:PRK07638 16 NKIA-IKEND----RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ATRIADAECSVVFTGDGFLRRGD----RVTLMDTLNDAIERAghvdhtivydrlgipadslswtprdewwddavatqSPT 261
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPdeegRVIEIDEWKRMIEKY-----------------------------------LPT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 262 FETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEihfGFDQRPGDRfcwvsdigwMMGPWSLIGNHAFAGT 339
Cdd:PRK07638 135 YAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLhsFDCNVH---DFHMKREDS---------VLIAGTLVHSLFLYGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 340 I-VMYEGAPDH------PAPDRFWQLIEDHGITqFGVsPTAIRAL------RDHgdehvaghdlsSLRILgSTGEPWDPE 406
Cdd:PRK07638 203 IsTLYVGQTVHlmrkfiPNQVLDKLETENISVM-YTV-PTMLESLykenrvIEN-----------KMKII-SSGAKWEAE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 407 S-----WRW----FYDHVGGGDtpiinISggtevFGCFLMPLPTEsLKPCTLGGPGLGMDIDIVDDDGTSVRdANERGYL 477
Cdd:PRK07638 269 AkekikNIFpyakLYEFYGASE-----LS-----FVTALVDEESE-RRPNSVGRPFHNVQVRICNEAGEEVQ-KGEIGTV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 478 VARSSSPSMTRRLWSGEDRYLEAywSRFEDVwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ 557
Cdd:PRK07638 337 YVKSPQFFMGYIIGGVLARELNA--DGWMTV---RDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDE 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499204776 558 AAVVGVPDDTTGEAAIAYVilaDAATPSAELRAELRDHVGdahgkPF-RPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:PRK07638 412 IVVIGVPDSYWGEKPVAII---KGSATKQQLKSFCLQRLS-----SFkIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
527-635 |
9.35e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 88.18 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 527 GRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRP 606
Cdd:PRK07824 253 GRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE---ALRAHVARTLDRTAAP 329
|
90 100
....*....|....*....|....*....
gi 499204776 607 REVVFVDDLPKTQSGKLVRRAVASAYTGA 635
Cdd:PRK07824 330 RELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
114-633 |
1.43e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.67 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 114 GEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGA-------------IAVpifsgf 180
Cdd:PRK07768 22 GEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAsltmlhqptprtdLAV------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 181 GVEATATRIADAECSVVFTGDGFlrrgdrvtlmDTLNDAIERAGHVDHTIvydrlgipadslswtprDEWWDDAVATQSP 260
Cdd:PRK07768 96 WAEDTLRVIGMIGAKAVVVGEPF----------LAAAPVLEEKGIRVLTV-----------------ADLLAADPIDPVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 TFEthsmaaSDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFG--FDQRPGDRFCWVS---DIGwMMGpwslignha 335
Cdd:PRK07768 149 TGE------DDLALMQLTSGSTGSPKAVQITH-GNLYANAEAMFVAaeFDVETDVMVSWLPlfhDMG-MVG--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 336 fAGTIVMYEGAPD-HPAPDRF------W-QLIEDHGIT-----QFGVSPTAiRALRDHGDEhvAGHDLSSLRILGSTGEP 402
Cdd:PRK07768 212 -FLTVPMYFGAELvKVTPMDFlrdpllWaELISKYRGTmtaapNFAYALLA-RRLRRQAKP--GAFDLSSLRFALNGAEP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 403 WDPESWRWFYD---HVGGGDTPIINISGGTEV-----FGCFLMPLPTESLKP--------------------CTLGGPGL 454
Cdd:PRK07768 288 IDPADVEDLLDagaRFGLRPEAILPAYGMAEAtlavsFSPCGAGLVVDEVDAdllaalrravpatkgntrrlATLGPPLP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 455 GMDIDIVDDDGTsVRDANERGYLVARSssPSMTRRlWSGEDRYLEAywsRFEDVW-NHGDWAQMDADGDWFLHGRADDAI 533
Cdd:PRK07768 368 GLEVRVVDEDGQ-VLPPRGVGVIELRG--ESVTPG-YLTMDGFIPA---QDADGWlDTGDLGYLTEEGEVVVCGRVKDVI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 534 NVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDT-TGEAAIAYVILADAATPSAELR-------AELRDHVGdahgkpFR 605
Cdd:PRK07768 441 IMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAgHSREGFAVAVESNAFEDPAEVRrirhqvaHEVVAEVG------VR 514
|
570 580 590
....*....|....*....|....*....|
gi 499204776 606 PREVVFVD--DLPKTQSGKLVRRAVASAYT 633
Cdd:PRK07768 515 PRNVVVLGpgSIPKTPSGKLRRANAAELVT 544
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
123-631 |
3.69e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.40 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVAN-ALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGD 201
Cdd:PRK08751 52 TYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRrgdrvTLMDTLNDAIERagHVDHTIVYDRLGIPADSL--------------SWTPRDEWWDDAVATQSP-TFETHS 266
Cdd:PRK08751 132 NFGT-----TVQQVIADTPVK--QVITTGLGDMLGFPKAALvnfvvkyvkklvpeYRINGAIRFREALALGRKhSMPTLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 MAASDPCMLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHfgfdqrpgdrfCWVSDIGWMM-GPWSLIGN----HAFA---- 337
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRN-LVANMQQAH-----------QWLAGTGKLEeGCEVVITAlplyHIFAltan 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 338 GTIVMYEGAPDH--PAPDRFWQLIEDHGITQF----GVSPTAIRALRDHGDEHVaghDLSSLRI-LGSTGEPWDPESWRW 410
Cdd:PRK08751 273 GLVFMKIGGCNHliSNPRDMPGFVKELKKTRFtaftGVNTLFNGLLNTPGFDQI---DFSSLKMtLGGGMAVQRSVAERW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 411 fyDHVGGgdTPIINISGGTEVFgcflmplPTESLKPCTL-------GGPGLGMDIDIVDDDGTSVrDANERGYLVARSss 483
Cdd:PRK08751 350 --KQVTG--LTLVEAYGLTETS-------PAACINPLTLkeyngsiGLPIPSTDACIKDDAGTVL-AIGEIGELCIKG-- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 PSMTRRLWSGEDRYLEAYWSrfeDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVG 562
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVMDA---DGWLHtGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 563 VPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHgkpfRPREVVFVDDLPKTQSGKLVRRAVASA 631
Cdd:PRK08751 493 VPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYK----QPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
104-628 |
4.00e-18 |
|
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: 87.53 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:cd17656 1 TPDAVAVVFENQ-----KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAECSVVFTgdgflrrgdRVTLMDTLNDAIEraghvdhTIVYDrlgipadslswtprdewwDDAVATQSPTFE 263
Cdd:cd17656 76 RRIYIMLDSGVRVVLT---------QRHLKSKLSFNKS-------TILLE------------------DPSISQEDTSNI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 THSMAASDPCMLLYSSGTTGTPKGIVHTHAGAlvqpAKEIHFGFDQRPGDRFCWVSDIGWMM---------------GPW 328
Cdd:cd17656 122 DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM----VNLLHFEREKTNINFSDKVLQFATCSfdvcyqeifstllsgGTL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 329 SLIGNHAFAGTIVMYEGAPDHPA-----PDRFWQLIE-------------DHGIT---QFGVSPTAIRALRDHGDEhvag 387
Cdd:cd17656 198 YIIREETKRDVEQLFDLVKRHNIevvflPVAFLKFIFserefinrfptcvKHIITageQLVITNEFKEMLHEHNVH---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 388 hdlsslrilgstgepwdpeswrwFYDHVGGGDTPIinisggteVFGCFLMPLPTESLKPcTLGGPGLGMDIDIVDDDGT- 466
Cdd:cd17656 274 -----------------------LHNHYGPSETHV--------VTTYTINPEAEIPELP-PIGKPISNTWIYILDQEQQl 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 467 ---------SVRDAN-ERGYLvarsSSPSMTrrlwsgEDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVA 536
Cdd:cd17656 322 qpqgivgelYISGASvARGYL----NRQELT------AEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 537 GRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSaelraELRDHVGDAHGKPFRPREVVFVDDLP 616
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNIS-----QLREYLAKQLPEYMIPSFFVPLDQLP 466
|
570
....*....|..
gi 499204776 617 KTQSGKLVRRAV 628
Cdd:cd17656 467 LTPNGKVDRKAL 478
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
120-623 |
4.67e-18 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 87.98 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLRR------------------------GDRVTLMDTLNDAIERAGhvdhtIVYDRL---GIPAdsLSWT-PRDEWw 251
Cdd:PLN02479 124 DQEFFTLaeealkilaekkkssfkpplliviGDPTCDPKSLQYALGKGA-----IEYEKFletGDPE--FAWKpPADEW- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 252 ddavatqsptfetHSMAasdpcmLLYSSGTTGTPKGIVHTHAGA-LVQPAKEIHFGFDQrpGDRFCWVSDI----GWMMg 326
Cdd:PLN02479 196 -------------QSIA------LGYTSGTTASPKGVVLHHRGAyLMALSNALIWGMNE--GAVYLWTLPMfhcnGWCF- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 327 PWSLIgnhAFAGTIVMYEgapdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDE----------HV--AGHD----- 389
Cdd:PLN02479 254 TWTLA---ALCGTNICLR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSetilplprvvHVmtAGAApppsv 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 390 LSSLRILG---------------STGEPWDPEswrwfYDHVGGGDTPIINISGGTEVFGC-FLMPLPTESLKPctlggpg 453
Cdd:PLN02479 327 LFAMSEKGfrvthtyglsetygpSTVCAWKPE-----WDSLPPEEQARLNARQGVRYIGLeGLDVVDTKTMKP------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 454 lgmdidiVDDDGTSVRDANERGYLVARSsspsmtrrlwsgedrYL---EAYWSRFEDVWNH-GDWAQMDADGDWFLHGRA 529
Cdd:PLN02479 395 -------VPADGKTMGEIVMRGNMVMKG---------------YLknpKANEEAFANGWFHsGDLGVKHPDGYIEIKDRS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 530 DDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAE--LRAELRDHVGDAHGKPFRPR 607
Cdd:PLN02479 453 KDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPK 532
|
570
....*....|....*.
gi 499204776 608 EVVFvDDLPKTQSGKL 623
Cdd:PLN02479 533 SVVF-GPLPKTATGKI 547
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
120-595 |
8.20e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 87.24 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSG---------FGVEATATRIA 190
Cdd:PRK08279 61 QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQqrgavlahsLNLVDAKHLIV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 191 DAECSVVFTGDGFLRRGDRVTLMDTLNDAIERAGHVDhtivydrlgipADSLSWTPRDewwDDAVATQSPTfethsmaAS 270
Cdd:PRK08279 141 GEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYED-----------LAAAAAGAPT---TNPASRSGVT-------AK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DPCMLLYSSGTTGTPKGIVHTHAgalvqpakeihfgfdqRpgdrfcWVSDIGWMMGPWSLIGN----------HAFAGTI 340
Cdd:PRK08279 200 DTAFYIYTSGTTGLPKAAVMSHM----------------R------WLKAMGGFGGLLRLTPDdvlycclplyHNTGGTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 341 ----VMYEGAP----DHPAPDRFWQLIEDHGITQFG-------------VSPTAiralRDHGDEHVAGHDLSslrilgst 399
Cdd:PRK08279 258 awssVLAAGATlalrRKFSASRFWDDVRRYRATAFQyigelcryllnqpPKPTD----RDHRLRLMIGNGLR-------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 400 gepwdPESWRWFYDHVGGGDtpIINISGGTE-------VFGcflmplpteslKPCTLG-GPGLGMD-IDIVD---DDGTS 467
Cdd:PRK08279 326 -----PDIWDEFQQRFGIPR--ILEFYAASEgnvgfinVFN-----------FDGTVGrVPLWLAHpYAIVKydvDTGEP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 468 VRDAN---------ERGYLVARSS---------SPSMTrrlwsgEDRYLeaywsR--FE--DVW-NHGDWaqMDADGDWF 524
Cdd:PRK08279 388 VRDADgrcikvkpgEVGLLIGRITdrgpfdgytDPEAS------EKKIL-----RdvFKkgDAWfNTGDL--MRDDGFGH 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 525 LH--GRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVP-DDTTGEAAIAYVILADAATPS-AELRAELRDH 595
Cdd:PRK08279 455 AQfvDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADGAEFDlAALAAHLYER 529
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
261-626 |
9.67e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.13 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 TFETHSMAASDPCMLLYSSGTTGTPKGIVHTHA-------------GALVQPAKEI--------HFgfdqrpgdrFCWVS 319
Cdd:PRK05677 198 PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcralmGSNLNEGCEIliaplplyHI---------YAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 320 DIGWMMgpwsLIGNHafagTIVMyegapdhPAPDRFWQLIEDHGITQF----GVSpTAIRALRDhgDEHVAGHDLSSLRI 395
Cdd:PRK05677 269 HCMAMM----LIGNH----NILI-------SNPRDLPAMVKELGKWKFsgfvGLN-TLFVALCN--NEAFRKLDFSALKL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 396 LGSTG---EPWDPESWRwfydHVGGgdTPIINISGGTEVfgcflMPL----PTESLKPCTLGGPGLGMDIDIVDDDGTSV 468
Cdd:PRK05677 331 TLSGGmalQLATAERWK----EVTG--CAICEGYGMTET-----SPVvsvnPSQAIQVGTIGIPVPSTLCKVIDDDGNEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 469 rDANERGYLVARSssPSMTRRLWSGEDRYLEAYWSrfeDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEG 547
Cdd:PRK05677 400 -PLGEVGELCVKG--PQVMKGYWQRPEATDEILDS---DGWlKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELED 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 548 ALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAElraELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK05677 474 VLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRR 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
265-626 |
1.19e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 86.80 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 265 HSMAASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIHFGFDQ-RPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMY 343
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTH-GNLVANMLQVRACLSQlGPDGQPLMKEGQEVMIAPLPLYHIYAFTANCMCM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 344 EGAPDHPA----PDRFWQLIEDHGITQF----GVSpTAIRALRDHGDehVAGHDLSSLRILGSTGEPW---DPESWRwfy 412
Cdd:PRK12492 281 MVSGNHNVlitnPRDIPGFIKELGKWRFsallGLN-TLFVALMDHPG--FKDLDFSALKLTNSGGTALvkaTAERWE--- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 413 dhvgggdtpiiNISGGTEVFGCFLMPL-PTESLKPC-------TLGGPGLGMDIDIVDDDGTSVrDANERGYLVARSssP 484
Cdd:PRK12492 355 -----------QLTGCTIVEGYGLTETsPVASTNPYgelarlgTVGIPVPGTALKVIDDDGNEL-PLGERGELCIKG--P 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 485 SMTRRLWSGEDRYLEAYWSrfEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVP 564
Cdd:PRK12492 421 QVMKGYWQQPEATAEALDA--EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVP 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 565 DDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHgkpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:PRK12492 499 DERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYK----VPKHIVLRDSLPMTPVGKILRR 556
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
116-635 |
1.19e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.60 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 116 DGTvRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVpIFSGFGVEATATRIADaecs 195
Cdd:PRK05857 37 DGT-SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV-MADGNLPIAAIERFCQ---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 196 vvftgdgflrrgdrvtLMDTLNDAIERAGHVDHTIVYDRL-GIPADSLSWTPRDEWWDDAVATQSPTFETHSmAASDPCM 274
Cdd:PRK05857 111 ----------------ITDPAAALVAPGSKMASSAVPEALhSIPVIAVDIAAVTRESEHSLDAASLAGNADQ-GSEDPLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 275 LLYSSGTTGTPKGIVHTHAGALVQPakeihfgfDQRPGDRFCWVSdigWMMG-------PWSLIGNHAFAGTIVMYEG-- 345
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAVP--------DILQKEGLNWVT---WVVGettysplPATHIGGLWWILTCLMHGGlc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 346 --APDHPAPDRfwQLIEDHGITQFGVSPTAIRALRDhgDEHVAGHDLSSLRILGSTGEpwdpeswrwfydHVGGGDTPII 423
Cdd:PRK05857 243 vtGGENTTSLL--EILTTNAVATTCLVPTLLSKLVS--ELKSANATVPSLRLVGYGGS------------RAIAADVRFI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 424 NISG-------GTEVFGCFLMPLPTES-----LKPCTLGGPGLGMDIDIVDDDG---TSVRDANERGYLVARSSSPSMTR 488
Cdd:PRK05857 307 EATGvrtaqvyGLSETGCTALCLPTDDgsivkIEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSASFGTLWIKSPANML 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 489 RLWSGEDRYLEAywsrFEDVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDT 567
Cdd:PRK05857 387 GYWNNPERTAEV----LIDGWvNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499204776 568 TGeAAIAYVILADA---ATPSAELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAYTGA 635
Cdd:PRK05857 463 FG-ALVGLAVVASAeldESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATAD 532
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
120-627 |
2.19e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 86.64 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 GDGFLRRGDrvtlmdtlndaieraghvdhtivydrlGIPaDSLSWTPRDEWWDDAVATQSPTfethsmAASDPCMLLYSS 279
Cdd:PRK10252 562 TADQLPRFA---------------------------DVP-DLTSLCYNAPLAPQGAAPLQLS------QPHHTAYIIFTS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEgaPD-HPAPDRFWQL 358
Cdd:PRK10252 608 GSTGRPKGVMVGQT-AIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAE--PEaHRDPLAMQQF 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 359 IEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGggdTPIINISGGTEV------- 431
Cdd:PRK10252 685 FAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTG---APLHNLYGPTEAavdvswy 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 432 --FGCFLMPLPTESLKpctLGGPGLGMDIDIVDDDG-------------TSVRDAneRGYLvarsSSPSMTrrlwsgEDR 496
Cdd:PRK10252 762 paFGEELAAVRGSSVP---IGYPVWNTGLRILDARMrpvppgvagdlylTGIQLA--QGYL----GRPDLT------ASR 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 497 YLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGV----PDDTTGEAA 572
Cdd:PRK10252 827 FIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGGDAR 906
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 573 --IAYVILADAATPSAE-LRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:PRK10252 907 qlVGYLVSQSGLPLDTSaLQAQLRERLPPH----MVPVVLLQLDQLPLSANGKLDRKA 960
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
119-635 |
4.10e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.06 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 119 VRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVP--IFSGFG-----VEATATRIAD 191
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGgresyIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 192 AECSVVFTGDGFLrrgdrvtlmDTLNDAIERAGHVdHTIVYDRLGIPADSlswtprdewwDDAVATQSPTfethsmaasD 271
Cdd:PRK09192 127 AQPAAIITPDELL---------PWVNEATHGNPLL-HVLSHAWFKALPEA----------DVALPRPTPD---------D 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 272 PCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRfCwvsdIGWMmgPW----SLIGnhaFAGTIVMYEGAP 347
Cdd:PRK09192 178 IAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDR-C----VSWL--PFyhdmGLVG---FLLTPVATQLSV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPAPDRF------W-QLIEDHGITqFGVSPT---AIRALRDHGDEHvAGHDLSSLRILGSTGEPWDPESWRWFYDH--- 414
Cdd:PRK09192 248 DYLPTRDFarrplqWlDLISRNRGT-ISYSPPfgyELCARRVNSKDL-AELDLSCWRVAGIGADMIRPDVLHQFAEAfap 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 415 VGGGDTPIINISGGTEV-FGCFLMPL-------------------------PTESLKPCTLGGPGL-GMDIDIVDDDGTS 467
Cdd:PRK09192 326 AGFDDKAFMPSYGLAEAtLAVSFSPLgsgivveevdrdrleyqgkavapgaETRRVRTFVNCGKALpGHEIEIRNEAGMP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 468 VrdaNER--GYLVARSSSpsmtrrLWSGEDRYLEAYWSRFEDVW-NHGDWAQMdADGDWFLHGRADDAINVAGRKVGPAE 544
Cdd:PRK09192 406 L---PERvvGHICVRGPS------LMSGYFRDEESQDVLAADGWlDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 545 VEGALIDHDAVTQ--AAVVGVPDDttGEAAIAYVILADAATPSA--ELRAELRDHVGDAHGKPFRPrEVVFVDDLPKTQS 620
Cdd:PRK09192 476 IEWIAEQEPELRSgdAAAFSIAQE--NGEKIVLLVQCRISDEERrgQLIHALAALVRSEFGVEAAV-ELVPPHSLPRTSS 552
|
570
....*....|....*.
gi 499204776 621 GKLVRRAVASAY-TGA 635
Cdd:PRK09192 553 GKLSRAKAKKRYlSGA 568
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
123-633 |
9.90e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 83.39 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQsILY-GIFKIGAIAVPIFSGFgveaTATRIA----DAECSVV 197
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEAL-ALYlATLRAGAVFLPLNTAY----TLAELDyfigDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 198 FTGDGflRRGDRVTLMDTLNdaierAGHVDhTIVYDRLGipadSLSwtprdewwdDAVATQSPTFETHSMAASDPCMLLY 277
Cdd:PRK07514 105 VCDPA--NFAWLSKIAAAAG-----APHVE-TLDADGTG----SLL---------EAAAAAPDDFETVPRGADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 278 SSGTTGTPKGIVHTH------AGALVQpakeiHFGFdqRPGDRfcwvsdigwmmgpwsLIgnHAF----------AGTIV 341
Cdd:PRK07514 164 TSGTTGRSKGAMLSHgnllsnALTLVD-----YWRF--TPDDV---------------LI--HALpifhthglfvATNVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 MYEGAP-------DhpaPDRFWQLIEDhgITQF-GVsPT-AIRALRDHG-DEHVAGHdlssLRILGSTGEPWDPESWRWF 411
Cdd:PRK07514 220 LLAGASmiflpkfD---PDAVLALMPR--ATVMmGV-PTfYTRLLQEPRlTREAAAH----MRLFISGSAPLLAETHREF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 412 YDHVGggdTPIINISGGTEVfgcfLM----PLPTESLkPCTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARSssPSMT 487
Cdd:PRK07514 290 QERTG---HAILERYGMTET----NMntsnPYDGERR-AGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKG--PNVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 RRLWsgedRYLEAYWSRF-EDVW-NHGDWAQMDADGdwFLH--GRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGV 563
Cdd:PRK07514 360 KGYW----RMPEKTAEEFrADGFfITGDLGKIDERG--YVHivGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499204776 564 PDDTTGEAAIAYVILADAATPS-AELRAELRDHVgdAHGKpfRPREVVFVDDLPKTQSGK----LVRRAVASAYT 633
Cdd:PRK07514 434 PHPDFGEGVTAVVVPKPGAALDeAAILAALKGRL--ARFK--QPKRVFFVDELPRNTMGKvqknLLREQYADLFA 504
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
123-639 |
6.13e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 81.27 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAER-GIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGD 201
Cdd:PRK07867 30 SWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTES 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLrrgdrvtlmDTLNDAIERAGHVDhtivydrlgipADSLSWTprdewwdDAVATQSPTFETHSMA-ASDPCMLLYSSG 280
Cdd:PRK07867 110 AHA---------ELLDGLDPGVRVIN-----------VDSPAWA-------DELAAHRDAEPPFRVAdPDDLFMLIFTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 281 TTGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDrFCWVS----DIGWMMGPWSlIGNHAFAGTIVmyegapdhpaPDRFW 356
Cdd:PRK07867 163 TSGDPKAVRCTH-RKVASAGVMLAQRFGLGPDD-VCYVSmplfHSNAVMAGWA-VALAAGASIAL----------RRKFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 357 --QLIEDhgITQFGVS-------PTA-IRALRDHGDEHVaghdlSSLRIL-GSTGEPWDPESW-RWFYDHV--GGGDTpi 422
Cdd:PRK07867 230 asGFLPD--VRRYGATyanyvgkPLSyVLATPERPDDAD-----NPLRIVyGNEGAPGDIARFaRRFGCVVvdGFGST-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 423 iniSGGTEVFgcflmplPTESLKPCTLGGpgLGMDIDIVDDD-----GTSVRDANER-------GYLVaRSSSPSMTRRL 490
Cdd:PRK07867 301 ---EGGVAIT-------RTPDTPPGALGP--LPPGVAIVDPDtgtecPPAEDADGRLlnadeaiGELV-NTAGPGGFEGY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 491 WSGEdrylEAYWSRFEDVWNH-GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTG 569
Cdd:PRK07867 368 YNDP----EADAERMRGGVYWsGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 570 EAAIAYVILADAATPSAELRAELRDHVGDAhGKPFRPREVVFVDDLPKTQSGKLVRRAVASayTGADVTD 639
Cdd:PRK07867 444 DQVMAALVLAPGAKFDPDAFAEFLAAQPDL-GPKQWPSYVRVCAELPRTATFKVLKRQLSA--EGVDCAD 510
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
104-628 |
1.05e-15 |
|
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: 79.91 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 104 TRNHVACIWEGEdgtvrQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVE 183
Cdd:cd17645 11 TPDHVAVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 184 ATATRIADAECSVVFTGdgflrrgdrvtlmdtlndaieraghvdhtivydrlgipADSLSWtprdewwddavatqsptfe 263
Cdd:cd17645 86 RIAYMLADSSAKILLTN--------------------------------------PDDLAY------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 264 thsmaasdpcmLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIgNHAFAGTIVMY 343
Cdd:cd17645 109 -----------VIYTSGSTGLPKGVMIEHH-NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIF-PHLTAGAALHV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 344 EGAPDHPAPDRFWQLIEDHGITqfgvsptaIRALRDHGDEHVAGHDLSSLRILgstgepwdpeswrwfydhVGGGDT--- 420
Cdd:cd17645 176 VPSERRLDLDALNDYFNQEGIT--------ISFLPTGAAEQFMQLDNQSLRVL------------------LTGGDKlkk 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 ------PIINISGGTEvfgCFLMPLPTESLKP---CTLGGPGLGMDIDIVDDD------GTS-----VRDANERGYLvar 480
Cdd:cd17645 230 ierkgyKLVNNYGPTE---NTVVATSFEIDKPyanIPIGKPIDNTRVYILDEAlqlqpiGVAgelciAGEGLARGYL--- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 481 sSSPSMTRrlwsgeDRYLEAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAV 560
Cdd:cd17645 304 -NRPELTA------EKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 561 VGVPDDTTGEAAIAYVIlADAATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:cd17645 377 LAKEDADGRKYLVAYVT-APEEIPHEELREWLKNDLPDY----MIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
112-622 |
1.54e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.21 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 112 WEGEDgtVRQQTYHDLHQQANRVANALAER-GIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFG--------- 181
Cdd:PRK05620 31 WGGAE--QEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMndqivhiin 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 182 -----VEATATRIAD------AEC----SVVFTGDGFLRRGdrvtlmdtlndAIERAGHVdHTIVYDRL--GIPADSlsw 244
Cdd:PRK05620 109 haedeVIVADPRLAEqlgeilKECpcvrAVVFIGPSDADSA-----------AAHMPEGI-KVYSYEALldGRSTVY--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 245 tprdEWwddavatqsPTFETHSMAAsdpcmLLYSSGTTGTPKGIVHTHAGALVQpakeihfGFDQRPGDRFCWVSDIGWM 324
Cdd:PRK05620 174 ----DW---------PELDETTAAA-----ICYSTGTTGAPKGVVYSHRSLYLQ-------SLSLRTTDSLAVTHGESFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 325 MG-------PWSLIGNHAFAGTIVMYEGApdHPAPDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAghDLSSLRILG 397
Cdd:PRK05620 229 CCvpiyhvlSWGVPLAAFMSGTPLVFPGP--DLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPP--ERMSLQEIY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 398 STGEPWDP---ESWRWFYdhvgGGDtpIINISGGTEVfgcflMPLPTESLKPCTLGGPG------------LGMDIDIVD 462
Cdd:PRK05620 305 VGGSAVPPiliKAWEERY----GVD--VVHVWGMTET-----SPVGTVARPPSGVSGEArwayrvsqgrfpASLEYRIVN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 463 DDGT-SVRDANE-----RGYLVARS--SSPSMTRRLWSGE--DRYLEAYWSRF-EDVW-NHGDWAQMDADGDWFLHGRAD 530
Cdd:PRK05620 374 DGQVmESTDRNEgeiqvRGNWVTASyyHSPTEEGGGAASTfrGEDVEDANDRFtADGWlRTGDVGSVTRDGFLTIHDRAR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 531 DAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGKPFRPREVV 610
Cdd:PRK05620 454 DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWT 533
|
570
....*....|..
gi 499204776 611 FVDDLPKTQSGK 622
Cdd:PRK05620 534 FVDEIDKTSVGK 545
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
106-626 |
2.28e-15 |
|
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: 78.98 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 106 NHVACIwegeDGTVRQqTYHDLHQQANRVANALAERGIGEGDT-VGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFgvea 184
Cdd:cd17648 2 DRVAVV----YGDKRL-TYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 185 tatriadaecsvvftgdgflrRGDRVTLMdtLNDAIERAghvdhtivydrlgipadslswtprdewwddaVATQSptfet 264
Cdd:cd17648 73 ---------------------PDERIQFI--LEDTGARV-------------------------------VITNS----- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 265 hsmaaSDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFDQRPGDRFC-----WVSDIGWMMGPWSLIGNHAFAgt 339
Cdd:cd17648 94 -----TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVlffsnYVFDFFVEQMTLALLNGQKLV-- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 340 IVMYEGAPDhpaPDRFWQLIEDHGITQFGVSPTAIralrdhgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHVGGgd 419
Cdd:cd17648 167 VPPDEMRFD---PDRFYAYINREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 420 tPIINISGGTEV-FGCFLMPLPTESLKPCTLGGPGLGMDIDIVDDDGTSVR-----------DANERGYLvarsSSPSMT 487
Cdd:cd17648 234 -LIINAYGPTETtVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPvgavgelylggDGVARGYL----NRPELT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 488 RrlwsgeDRYL--------EAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAA 559
Cdd:cd17648 309 A------ERFLpnpfqteqERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECA 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499204776 560 VVGVPDDTTGEAAI-----AYVILADAATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKL-VRR 626
Cdd:cd17648 383 VVAKEDASQAQSRIqkylvGYYLPEPGHVPESDLLSFLRAKLPRY----MVPARLVRLEGIPVTINGKLdVRA 451
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
123-628 |
6.94e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.06 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADaecsvvfTGDG 202
Cdd:PRK05691 2215 SYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIED-------SGIG 2287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 FLRrGDRVtLMDTLNDaieraghvdhtivydrlgIPADSLSWTPRDewwDDAVATQSPTFETHSMAASD-PCMLLYSSGT 281
Cdd:PRK05691 2288 LLL-SDRA-LFEALGE------------------LPAGVARWCLED---DAAALAAYSDAPLPFLSLPQhQAYLIYTSGS 2344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 282 TGTPKGIVHTHaGALVQPAKEIHFGFDQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYegAPDHPAPDRFWQLIED 361
Cdd:PRK05691 2345 TGKPKGVVVSH-GEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLR--AQGQWGAEEICQLIRE 2421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 362 HGITQFGVSPTAIRALRdhgdEHVAGHD-LSSLRILGSTGEPWDPESWRwfydHVGGGDTP--IINISGGTEVFgcfLMP 438
Cdd:PRK05691 2422 QQVSILGFTPSYGSQLA----QWLAGQGeQLPVRMCITGGEALTGEHLQ----RIRQAFAPqlFFNAYGPTETV---VMP 2490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 439 LPteSLKPCTL----GGPGLGMDID-----IVDDDGTSV-RDANERGYLVARSSSPSMTRRLWSGEDRYL-EAYWSRFED 507
Cdd:PRK05691 2491 LA--CLAPEQLeegaASVPIGRVVGarvayILDADLALVpQGATGELYVGGAGLAQGYHDRPGLTAERFVaDPFAADGGR 2568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 508 VWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVpDDTTGEAAIAYVILADAATPS-- 585
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDea 2647
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 499204776 586 -AELRAELRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK05691 2648 qAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-627 |
8.17e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.67 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 114 GEDGTVRQQTYHDLHQQANRVANALAERGiGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGV-----EATATR 188
Cdd:PRK05691 33 DDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 189 IADAECSVVFTGDGflrrgdrvtlmdtLNDAIERAGHVDHTIVYDRLGIpaDSLSWTPRDEWwddavatQSPTfethsMA 268
Cdd:PRK05691 112 IADAEPRLLLTVAD-------------LRDSLLQMEELAAANAPELLCV--DTLDPALAEAW-------QEPA-----LQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 269 ASDPCMLLYSSGTTGTPKGIVHTHaGALVQPAKEIH--FGFDQRPGDRFcwvsdIGWM-----MGpwsLIG---NHAFAG 338
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSH-GNLVANEQLIRhgFGIDLNPDDVI-----VSWLplyhdMG---LIGgllQPIFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 339 T--IVMyegAPDH--PAPDRFWQLIEDHGITQFGVSPTAIRALRDH-GDEHVAGHDLSSLRILGSTGEPWDPESWRWFYD 413
Cdd:PRK05691 236 VpcVLM---SPAYflERPLRWLEAISEYGGTISGGPDFAYRLCSERvSESALERLDLSRWRVAYSGSEPIRQDSLERFAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 414 HVGG-GDTP------------IINISGGTEVFGCFLMPLPTESLK-------------PCTLGGPGLGmdIDIVDDDGTS 467
Cdd:PRK05691 313 KFAAcGFDPdsffasyglaeaTLFVSGGRRGQGIPALELDAEALArnraepgtgsvlmSCGRSQPGHA--VLIVDPQSLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 468 VRDANERGYLVArsSSPSMTRRLWSGEDRYLEAYWSRFEDVW-NHGDWAQMdADGDWFLHGRADDAINVAGRKVGPAEVE 546
Cdd:PRK05691 391 VLGDNRVGEIWA--SGPSIAHGYWRNPEASAKTFVEHDGRTWlRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 547 GALIDHDAVT---QAAVVGVPDDttGEAAIAyvILAD------AATPSAELRAELRDHVGDAHGKPfrPREVVFVDD--L 615
Cdd:PRK05691 468 KTVEREVEVVrkgRVAAFAVNHQ--GEEGIG--IAAEisrsvqKILPPQALIKSIRQAVAEACQEA--PSVVLLLNPgaL 541
|
570
....*....|..
gi 499204776 616 PKTQSGKLVRRA 627
Cdd:PRK05691 542 PKTSSGKLQRSA 553
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
501-633 |
1.74e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 73.10 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 501 YWSRFED---VWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVI 577
Cdd:PRK07445 315 YYPQILDsqgIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499204776 578 LADAATPSAELRAELRDHVGdahgkPFR-PREVVFVDDLPKTQSGKLVRRAVASAYT 633
Cdd:PRK07445 395 PKDPSISLEELKTAIKDQLS-----PFKqPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
120-579 |
1.75e-13 |
|
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: 73.16 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIfsgfgveatatriadaecsvvft 199
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdGFLRRGDrvTLMDTLNdaIERAGHVdhtIVydrlgipadslswtprdewwddavatqsptfethsmaasDPCMLLYSS 279
Cdd:cd05940 59 --NYNLRGE--SLAHCLN--VSSAKHL---VV---------------------------------------DAALYIYTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTH-----AGALVQpakeihFGFDQRPGDRF-----CWVSDiGWMMGPWSLIGNhafAGTIVMYEGApdh 349
Cdd:cd05940 91 GTTGLPKAAIISHrrawrGGAFFA------GSGGALPSDVLytclpLYHST-ALIVGWSACLAS---GATLVIRKKF--- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 350 pAPDRFWQLIEDHGITQFGVSPTAIRAL---------RDHGDEHVAGHDLSslrilgstgepwdPESWRWFYDHVGGGDt 420
Cdd:cd05940 158 -SASNFWDDIRKYQATIFQYIGELCRYLlnqppkpteRKHKVRMIFGNGLR-------------PDIWEEFKERFGVPR- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 pIINISGGTE-VFGCFLMPlptesLKPCTLG----GPGLGMDIDIVDDD---GTSVRDAN---------ERGYLVARSSs 483
Cdd:cd05940 223 -IAEFYAATEgNSGFINFF-----GKPGAIGrnpsLLRKVAPLALVKYDlesGEPIRDAEgrcikvprgEPGLLISRIN- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 484 psmtrRLWSGeDRYLEAYWSR-------FE--DVW-NHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHD 553
Cdd:cd05940 296 -----PLEPF-DGYTDPAATEkkilrdvFKkgDAWfNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFP 369
|
490 500
....*....|....*....|....*..
gi 499204776 554 AVTQAAVVGVP-DDTTGEAAIAYVILA 579
Cdd:cd05940 370 GVEEANVYGVQvPGTDGRAGMAAIVLQ 396
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
501-627 |
6.87e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 71.60 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 501 YWSrfedvwnhGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILAD 580
Cdd:PRK13388 382 YWS--------GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499204776 581 AATPSAELRAELRDHVGDAhGKPFRPREVVFVDDLPKTQSGKLVRRA 627
Cdd:PRK13388 454 GATFDPDAFAAFLAAQPDL-GTKAWPRYVRIAADLPSTATNKVLKRE 499
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
113-562 |
8.65e-13 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 71.30 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 113 EGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEvqsILYGIFK---IGAIAVPIFSGFGVEATATRI 189
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPE---WVWAELAaqaIGALSLGIYQDSMAEEVAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 190 ADAECSVVFTGDGflrrgDRVTLMDTLNDAIEragHVDHTIVYDRLGIPA---DSLSWTPRDEWWDDAVATQSPTFETHS 266
Cdd:cd17641 80 NYTGARVVIAEDE-----EQVDKLLEIADRIP---SVRYVIYCDPRGMRKyddPRLISFEDVVALGRALDRRDPGLYERE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 267 MAASDP---CMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHFGFdQRPGDRFCWVSDIGWMMGPWSLIGNHAFAGTIV-- 341
Cdd:cd17641 152 VAAGKGedvAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP-LGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 342 ----------MYEGAPDHP-APDRFW------------------QLIEDHGI--------TQFGVSPTAI---------- 374
Cdd:cd17641 231 peepetmmedLREIGPTFVlLPPRVWegiaadvrarmmdatpfkRFMFELGMklglraldRGKRGRPVSLwlrlaswlad 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 375 ----RALRDH-GdehvaghdLSSLRILGSTGEPWDPESWRwFYDHVGggdTPIINISGGTEVFGCFLMPlPTESLKPCTL 449
Cdd:cd17641 311 allfRPLRDRlG--------FSRLRSAATGGAALGPDTFR-FFHAIG---VPLKQLYGQTELAGAYTVH-RDGDVDPDTV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 450 GGPGlgmdidivddDGTSVRDANErGYLVARssSPSMTRRLWSGEDRYLEAYwsrFEDVWNH-GDWAQMDADGDWFLHGR 528
Cdd:cd17641 378 GVPF----------PGTEVRIDEV-GEILVR--SPGVFVGYYKNPEATAEDF---DEDGWLHtGDAGYFKENGHLVVIDR 441
|
490 500 510
....*....|....*....|....*....|....*
gi 499204776 529 ADDAINVA-GRKVGPAEVEGALIDHDAVTQAAVVG 562
Cdd:cd17641 442 AKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
37-92 |
9.19e-13 |
|
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: 63.26 E-value: 9.19e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 37 DALRERSTTDLDWFWGELPEYLglEFFEDYDAVRDDADDPqSTAWYPGAELNVAHN 92
Cdd:pfam16177 2 EALYRRSIEDPEGFWGEVAKEL--DWFKPFDKVLDGSNGP-FAKWFVGGKLNVCYN 54
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
512-626 |
2.08e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.29 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 512 GDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVIlADAATPSAELRAE 591
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPVQLREW 374
|
90 100 110
....*....|....*....|....*....|....*
gi 499204776 592 LRDHVGdAHGKPFrprEVVFVDDLPKTQSGKLVRR 626
Cdd:PRK08308 375 CIQHLA-PYQVPH---EIESVTEIPKNANGKVSRK 405
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
120-628 |
1.09e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.66 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGF---------GVEATATRIA 190
Cdd:PRK05691 3744 QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLpaqrlqriiELSRTPVLVC 3823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 191 DAECsvvftgdgflrRGDRVTLMDTLNDAIEraghvdhtivydrlgipadslswtPRDEWWDDAVATQSPTFETHSMAAS 270
Cdd:PRK05691 3824 SAAC-----------REQARALLDELGCANR------------------------PRLLVWEEVQAGEVASHNPGIYSGP 3868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 271 DP-CMLLYSSGTTGTPKGIVHTHAGALV-QPAKEIHFGFDQRpgDRFCWVSDIGWMMGPWSLIGNHAFAGTIVMYEGAPD 348
Cdd:PRK05691 3869 DNlAYVIYTSGSTGLPKGVMVEQRGMLNnQLSKVPYLALSEA--DVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIA 3946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPaPDRFWQLIEDHGITQFGVSPTAIRALRdhGDEHVAghdLSSLRILGSTGEPWDPE---SWRWFYDHVGggdtpIINI 425
Cdd:PRK05691 3947 HD-PQGLLAHVQAQGITVLESVPSLIQGML--AEDRQA---LDGLRWMLPTGEAMPPElarQWLQRYPQIG-----LVNA 4015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 426 SGGTEvfgC----FLMPLPTESLKPCTL--GGPGLGMDIDIVDDD---------------GTSVrdanERGYLvarsSSP 484
Cdd:PRK05691 4016 YGPAE---CsddvAFFRVDLASTRGSYLpiGSPTDNNRLYLLDEAlelvplgavgelcvaGTGV----GRGYV----GDP 4084
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 485 SMTRRLWSGEdryleAYWSRFEDVWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAvVGVP 564
Cdd:PRK05691 4085 LRTALAFVPH-----PFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQ 4158
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 565 DDTTGEAAIAYVILADAATPSAE--------LRAELRDHVGDAHgkpfrpreVVFVDDLPKTQSGKLVRRAV 628
Cdd:PRK05691 4159 EGVNGKHLVGYLVPHQTVLAQGAllerikqrLRAELPDYMVPLH--------WLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
111-637 |
2.38e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.71 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 111 IWEGEDGTVRQQTYHDLHQQANRVANALAERGigEGDTVGLY-MPMVPEVQSILyGIFKIGAiAVPIFSGF--------G 181
Cdd:PRK05851 21 VLDRESGLWRRHPWPEVHGRAENVAARLLDRD--RPGAVGLVgEPTVELVAAIQ-GAWLAGA-AVSILPGPvrgaddgrW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 182 VEATATRIADAECSVVFTGDGFLRR----GDRVTLMDtlndaIERAGHvdhtivydrlgipadslswTPRDewwddavAT 257
Cdd:PRK05851 97 ADATLTRFAGIGVRTVLSHGSHLERlravDSSVTVHD-----LATAAH-------------------TNRS-------AS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 258 QSPTfethsmAASDPCMLLYSSGTTGTPK------GIVHTHAGALVQpakeiHFGFDqRPGDRFCwvsdiGWM-----MG 326
Cdd:PRK05851 146 LTPP------DSGGPAVLQGTAGSTGTPRtailspGAVLSNLRGLNA-----RVGLD-AATDVGC-----SWLplyhdMG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 327 PWSLIGNhAFAGTIVMYegAPD---HPAPDRFWQLIEDHGITqFGVSPTAIRALRDHGDEHVAGHDLSSLRILGSTGEPW 403
Cdd:PRK05851 209 LAFLLTA-ALAGAPLWL--APTtafSASPFRWLSWLSDSRAT-LTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 404 DPESWRWFYDHVG--GGDTPIINISGGTEVFGCFL-MPLPTESL--------------KPCTLGGPGLGMDIDIVDDDGT 466
Cdd:PRK05851 285 DCDGFERFATAMApfGFDAGAAAPSYGLAESTCAVtVPVPGIGLrvdevttddgsgarRHAVLGNPIPGMEVRISPGDGA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 467 SVRDANERGYLVARSSSpsmtrrLWSGedrYLEaywsrfEDVWNHGDW-AQMD----ADGDWFLHGRADDAINVAGRKVG 541
Cdd:PRK05851 365 AGVAGREIGEIEIRGAS------MMSG---YLG------QAPIDPDDWfPTGDlgylVDGGLVVCGRAKELITVAGRNIF 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 542 PAEVEGALIDHDAVTQAAVVGVpddTTGEAAI--AYVILADAATPS-AELRAELRDHVGDAHGkpFRPREVVFVD--DLP 616
Cdd:PRK05851 430 PTEIERVAAQVRGVREGAVVAV---GTGEGSArpGLVIAAEFRGPDeAGARSEVVQRVASECG--VVPSDVVFVApgSLP 504
|
570 580
....*....|....*....|.
gi 499204776 617 KTQSGKLVRRAVASAYTGADV 637
Cdd:PRK05851 505 RTSSGKLRRLAVKRSLEAADG 525
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
255-623 |
2.77e-11 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 65.96 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 255 VATQSPTFETHSMAASDP---CMLLYSSGTTGTPKgIVH----------THAGALVQPAKE-IHFG-----FDQRPGDRF 315
Cdd:cd17654 100 NAPLSFTPEHRHFNIRTDeclAYVIHTSGTTGTPK-IVAvphkcilpniQHFRSLFNITSEdILFLtspltFDPSVVEIF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 316 CWVSDIGWMmgpwsLIGNHAfagtivmYEGAPDHPAPDRFwqliEDHGITQFGVSPTAIRALrdhGDEHVAGHDLS---S 392
Cdd:cd17654 179 LSLSSGATL-----LIVPTS-------VKVLPSKLADILF----KRHRITVLQATPTLFRRF---GSQSIKSTVLSatsS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 393 LRILGSTGEPWdP-----ESWRwfydHVGGGdTPIINISGGTEVfGCF--LMPLPTESLkPCTLGGPGLGMDIDIVDDDG 465
Cdd:cd17654 240 LRVLALGGEPF-PslvilSSWR----GKGNR-TRIFNIYGITEV-SCWalAYKVPEEDS-PVQLGSPLLGTVIEVRDQNG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 466 TSVRdANERGYLVARSSspsmtrrlwsgedrYLEAYWSRFEDVWNH-GDWAQMDaDGDWFLHGRADDAINVAGRKVGPAE 544
Cdd:cd17654 312 SEGT-GQVFLGGLNRVC--------------ILDDEVTVPKGTMRAtGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDL 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499204776 545 VEGALIDHDAVtQAAVVGVPDDttgEAAIAYVILADAatpSAELRAELRDHVGDAHGKPFRpreVVFVDDLPKTQSGKL 623
Cdd:cd17654 376 IQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESS---SSRIHKELQLTLLSSHAIPDT---FVQIDKLPLTSHGKV 444
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
274-634 |
5.27e-11 |
|
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: 65.59 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 274 MLLYSSGTTGTPKGIVHTHAGaLVQPAKEIHFGFDQRPGDRFcwvsdIGWM-----MGpwsLIGNHafagTIVMYEGAPD 348
Cdd:cd05908 110 FIQFSSGSTGDPKGVMLTHEN-LVHNMFAILNSTEWKTKDRI-----LSWMplthdMG---LIAFH----LAPLIAGMNQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 349 HPAPDR-------FW-QLIEDHGITQ-----FGvSPTAIRALRDhgdEHVAGHDLSSLRILGSTGEPWDPESWRWFYDHV 415
Cdd:cd05908 177 YLMPTRlfirrpiLWlKKASEHKATIvsspnFG-YKYFLKTLKP---EKANDWDLSSIRMILNGAEPIDYELCHEFLDHM 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 416 ---GGGDTPIINISGGTE--VFGCFlmPLPTESLKPCTLGGPGL--GMDIDIVDD---------------DGTSVRDANE 473
Cdd:cd05908 253 skyGLKRNAILPVYGLAEasVGASL--PKAQSPFKTITLGRRHVthGEPEPEVDKkdsecltfvevgkpiDETDIRICDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 474 R---------GYLVARSSS--------PSMTRRLWSgedryleaywsrfEDVW-NHGDWAQMdADGDWFLHGRADDAINV 535
Cdd:cd05908 331 DnkilpdgyiGHIQIRGKNvtpgyynnPEATAKVFT-------------DDGWlKTGDLGFI-RNGRLVITGREKDIIFV 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 536 AGRKVGPAEVEGALIDHDAVT--QAAVVGVPD-DTTGEAAIAYVILADAATPSAELRAELRDHVGDAHGkpFRPREVVFV 612
Cdd:cd05908 397 NGQNVYPHDIERIAEELEGVElgRVVACGVNNsNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGG--WQINEVLPI 474
|
410 420
....*....|....*....|..
gi 499204776 613 DDLPKTQSGKLVRRAVASAYTG 634
Cdd:cd05908 475 RRIPKTTSGKVKRYELAQRYQS 496
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
121-562 |
5.74e-11 |
|
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: 65.07 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 121 QQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFtg 200
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 201 dgflrrgdrvtlmdtlndaIERAGhvdhtivydrlgipadslswtprdewwdDAVATqsptfethsmaasdpcmLLYSSG 280
Cdd:cd17640 83 -------------------VENDS----------------------------DDLAT-----------------IIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 281 TTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGDRFcwVSdigwMMGPWslignHAF----------AGTIVMYEGAPDHP 350
Cdd:cd17640 99 TTGNPKGVMLTHANLLHQ-IRSLSDIVPPQPGDRF--LS----ILPIW-----HSYersaeyfifaCGCSQAYTSIRTLK 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 351 A------PD------RFWQLIEDHGITQFGVSPTAIRALrdhgdehvAGHDLSSLRI-LGSTGEPWDPESWRWFYDHVGg 417
Cdd:cd17640 167 DdlkrvkPHyivsvpRLWESLYSGIQKQVSKSSPIKQFL--------FLFFLSGGIFkFGISGGGALPPHVDTFFEAIG- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 418 gdTPIINISGGTE---VFGCFLMPLPTESlkpcTLGGPGLGMDIDIVDDDGTSVRDANERGYLVARS--------SSPSM 486
Cdd:cd17640 238 --IEVLNGYGLTEtspVVSARRLKCNVRG----SVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGpqvmkgyyKNPEA 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499204776 487 TRRLWSgedryleaywsrfEDVW-NHGDWAQMDADGDWFLHGRADDAINVA-GRKVGPAEVEGALIDHDAVTQAAVVG 562
Cdd:cd17640 312 TSKVLD-------------SDGWfNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
123-298 |
2.34e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.84 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDG 202
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flRRGDRVTLMdtlndaieRAGHVDHT-IVY-DRLGIPADS-----LSWTprdewwdDAVATQSPTFETHSMAASDPC-- 273
Cdd:PTZ00216 203 --NVPNLLRLM--------KSGGMPNTtIIYlDSLPASVDTegcrlVAWT-------DVVAKGHSAGSHHPLNIPENNdd 265
|
170 180
....*....|....*....|....*..
gi 499204776 274 --MLLYSSGTTGTPKGIVHTHaGALVQ 298
Cdd:PTZ00216 266 laLIMYTSGTTGDPKGVMHTH-GSLTA 291
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
120-626 |
2.81e-10 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 62.83 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFT 199
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 200 gdgflrrgdrvTLMDTLNDAIEraghvdhtivydrlgipadslswtprdewwddavaTQSPTfeTHSMAASDPCMLLYSS 279
Cdd:cd05939 82 -----------NLLDPLLTQSS-----------------------------------TEPPS--QDDVNFRDKLFYIYTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 280 GTTGTPKGIVHTHAGALvQPAKEIHFGFDQRPGDRFcWVS-----DIGWMMGPWSLIgnhAFAGTIVMYEGApdhpAPDR 354
Cdd:cd05939 114 GTTGLPKAAVIVHSRYY-RIAAGAYYAFGMRPEDVV-YDClplyhSAGGIMGVGQAL---LHGSTVVIRKKF----SASN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 355 FWQLIEDHGITQFGVSPTAIRAL-----RDHGDEHvaghdlsSLRIL---GSTGEPWDPESWRWFYDHVG------GGDT 420
Cdd:cd05939 185 FWDDCVKYNCTIVQYIGEICRYLlaqppSEEEQKH-------NVRLAvgnGLRPQIWEQFVRRFGIPQIGefygatEGNS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 PIINISGgtEVFGCFLMPLPTESLKPCTLggpglgmdIDIVDDDGTSVRDAN---------ERGYLVARSSSPSMTRRLw 491
Cdd:cd05939 258 SLVNIDN--HVGACGFNSRILPSVYPIRL--------IKVDEDTGELIRDSDglcipcqpgEPGLLVGKIIQNDPLRRF- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 492 sgeDRYLEAYWSR---FEDVWNHGDWA-------QMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVV 561
Cdd:cd05939 327 ---DGYVNEGATNkkiARDVFKKGDSAflsgdvlVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 562 GVP-DDTTGEAAIAYVIL----ADAATPSAELRAELRDHVgdahgkpfRPREVVFVDDLPKTQSGKLVRR 626
Cdd:cd05939 404 GVEvPGVEGRAGMAAIVDperkVDLDRFSAVLAKSLPPYA--------RPQFIRLLPEVDKTGTFKLQKT 465
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
438-630 |
1.99e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.29 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 438 PLPTESLKPctlggpglGMDIDIVDDDGTSVRDANE-----------RGYLvarsSSPSMTRRLWSGEDRYlEAYWSrfe 506
Cdd:PRK04813 317 RLPIGYAKP--------DSPLLIIDEEGTKLPDGEQgeivisgpsvsKGYL----NNPEKTAEAFFTFDGQ-PAYHT--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 507 dvwnhGDWAQMDaDGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAYVILAD-----A 581
Cdd:PRK04813 381 -----GDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEedferE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499204776 582 ATPSAELRAELRDHVGDAhgkpFRPREVVFVDDLPKTQSGKLVRRAVAS 630
Cdd:PRK04813 455 FELTKAIKKELKERLMEY----MIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
122-292 |
3.49e-09 |
|
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: 59.54 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 122 QTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTgd 201
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 gflrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwddavatqsptfethSMAASDPCMLLYSSGT 281
Cdd:cd17639 84 ----------------------------------------------------------------DGKPDDLACIMYTSGS 99
|
170
....*....|.
gi 499204776 282 TGTPKGIVHTH 292
Cdd:cd17639 100 TGNPKGVMLTH 110
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
123-293 |
3.67e-09 |
|
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: 59.54 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGI--GEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTG 200
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 201 DGFlrrgdRVTLMDTLNDaIERAGHVDHTIvydrlgipadslswtprdewwddavatqsPTFEthsmaasDPCMLLYSSG 280
Cdd:cd05927 87 AGV-----KVYSLEEFEK-LGKKNKVPPPP-----------------------------PKPE-------DLATICYTSG 124
|
170
....*....|...
gi 499204776 281 TTGTPKGIVHTHA 293
Cdd:cd05927 125 TTGNPKGVMLTHG 137
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
97-622 |
5.60e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.59 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 97 HASVDAGTRNHVAciwegEDGTVRQQTYHDLHQQANrVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPI 176
Cdd:PRK06814 639 EAAKIHGFKKLAV-----EDPVNGPLTYRKLLTGAF-VLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 177 -FSGfgveATATRIAD---AECSVVFTGDGFLRRGDrvtlMDTLNDAIERaghvDHTIVY--D-RLGI-PADSL-----S 243
Cdd:PRK06814 713 nFSA----GIANILSAckaAQVKTVLTSRAFIEKAR----LGPLIEALEF----GIRIIYleDvRAQIgLADKIkgllaG 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 244 WTPRdewwddavatqsptFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALV---QPAKEIHFGfdqrPGDR-FCwvs 319
Cdd:PRK06814 781 RFPL--------------VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLAnraQVAARIDFS----PEDKvFN--- 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 320 digwmmgpwSLIGNHAF---AGTIV-MYEGAPD--HPAPDRFW---QLIEDHGIT-QFGVsptairalrdhgDEHVAGH- 388
Cdd:PRK06814 840 ---------ALPVFHSFgltGGLVLpLLSGVKVflYPSPLHYRiipELIYDTNATiLFGT------------DTFLNGYa 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 389 ------DLSSLRILGSTGEPWDPESWRWFYDHVG-----G-GDT---PIINISggTEVFGCF-----LMPLPTESLKPCt 448
Cdd:PRK06814 899 ryahpyDFRSLRYVFAGAEKVKEETRQTWMEKFGirileGyGVTetaPVIALN--TPMHNKAgtvgrLLPGIEYRLEPV- 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 449 lggPGlgmdidiVDDDGT-SVRDAN-ERGYLvaRSSSPSMTRRLWSGedryleayWsrfedvWNHGDWAQMDADGDWFLH 526
Cdd:PRK06814 976 ---PG-------IDEGGRlFVRGPNvMLGYL--RAENPGVLEPPADG--------W------YDTGDIVTIDEEGFITIK 1029
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 527 GRADDAINVAGRKVGPAEVEG--ALIDHDAvtQAAVVGVPDDTTGEAAIayvILADAATPSaelRAELRDHVgDAHGKP- 603
Cdd:PRK06814 1030 GRAKRFAKIAGEMISLAAVEElaAELWPDA--LHAAVSIPDARKGERII---LLTTASDAT---RAAFLAHA-KAAGASe 1100
|
570 580
....*....|....*....|
gi 499204776 604 -FRPREVVFVDDLPKTQSGK 622
Cdd:PRK06814 1101 lMVPAEIITIDEIPLLGTGK 1120
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
120-634 |
6.72e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 58.60 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAiaVPIFSGFGVeatatriadaecsvvf 198
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGA--APAFINYNL---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 199 TGDGFLR--RGDRVTLmdtlndaieraghvdhtIVYDrlgipadslswtprdewwDDavatqsptfethsmaasDPCMLL 276
Cdd:cd05937 66 SGDPLIHclKLSGSRF-----------------VIVD------------------PD-----------------DPAILI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 277 YSSGTTGTPKGIVHTHAGALVQpAKEIHFGFDQRPGDRfcWVSDIGWMMGPWSLIGNHAF---AGTIVMyegAPDHPApD 353
Cdd:cd05937 94 YTSGTTGLPKAAAISWRRTLVT-SNLLSHDLNLKNGDR--TYTCMPLYHGTAAFLGACNClmsGGTLAL---SRKFSA-S 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 354 RFWQLIEDHGITQFGVSPTAIRAL---------RDHGDEHVAGHDLSslrilgstgepwdPESWRWFYDHVGggdTPII- 423
Cdd:cd05937 167 QFWKDVRDSGATIIQYVGELCRYLlstppspydRDHKVRVAWGNGLR-------------PDIWERFRERFN---VPEIg 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 424 NISGGTEVFGCFLmplpTESLKPCTLGGPG---------LGMDIDIVD---DDGTSVRD----------ANERGYLVARS 481
Cdd:cd05937 231 EFYAATEGVFALT----NHNVGDFGAGAIGhhglirrwkFENQVVLVKmdpETDDPIRDpktgfcvrapVGEPGEMLGRV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 482 ssPSMTRRLWSGEDRYLEAYWSRF-EDVWNHGDWAQ-------MDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHD 553
Cdd:cd05937 307 --PFKNREAFQGYLHNEDATESKLvRDVFRKGDIYFrtgdllrQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHP 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 554 AVTQAAVVGV--PDDtTGEAAIAYVILADAATPSAELR-AELRDHVgdahgkpfrprevvfVDDLPKTQSGKLVRRAVAS 630
Cdd:cd05937 385 DIAEANVYGVkvPGH-DGRAGCAAITLEESSAVPTEFTkSLLASLA---------------RKNLPSYAVPLFLRLTEEV 448
|
....
gi 499204776 631 AYTG 634
Cdd:cd05937 449 ATTD 452
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
107-622 |
1.69e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.80 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 107 HVACIwegEDGTVRQQTYHDLHQQANRVANALaERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATA 186
Cdd:PRK08043 220 GKPCI---EDVNFTPDSYRKLLKKTLFVGRIL-EKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 187 TRIADAECSVVFTGDGFLRRGD-----------RVTLMDTLNDAIERAghvdhtivyDRLGIPADSLswTPRDewwddAV 255
Cdd:PRK08043 296 SAITAAEIKTIFTSRQFLDKGKlwhlpeqltqvRWVYLEDLKDDVTTA---------DKLWIFAHLL--MPRL-----AQ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 256 ATQSPTfethsmaasDPCMLLYSSGTTGTPKGIVHTHAgALVQPAKEIHFGFDQRPGDRFcwvsdigwmMGPWSLIgnHA 335
Cdd:PRK08043 360 VKQQPE---------DAALILFTSGSEGHPKGVVHSHK-SLLANVEQIKTIADFTPNDRF---------MSALPLF--HS 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 336 FAGTIVMYE----GAPD--HPAPDRFW---QLIEDHGIT-QFGVSptairALRDHGDEHVAGHDLSSLRILGSTGEPWDP 405
Cdd:PRK08043 419 FGLTVGLFTplltGAEVflYPSPLHYRivpELVYDRNCTvLFGTS-----TFLGNYARFANPYDFARLRYVVAGAEKLQE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 406 ESWRWFYDHVGggdtpiINISGGTEVFGCflmpLPTESL------KPCTLGGPGLGMDIDIVDDDGTS------VRDAN- 472
Cdd:PRK08043 494 STKQLWQDKFG------LRILEGYGVTEC----APVVSInvpmaaKPGTVGRILPGMDARLLSVPGIEqggrlqLKGPNi 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 473 ERGYLvaRSSSPSM----TRRLWSGEdryLEAYWsrfedvWNHGDWAQMDADGDWFLHGRADDAINVAGRKVGPAEVEGA 548
Cdd:PRK08043 564 MNGYL--RVEKPGVlevpTAENARGE---MERGW------YDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 549 LIDHDAVTQAAVVGVPDDTTGEAAIAYviladaaTPSAELRAELRDHVGDAHGKP--FRPREVVFVDDLPKTQSGK 622
Cdd:PRK08043 633 ALGVSPDKQHATAIKSDASKGEALVLF-------TTDSELTREKLQQYAREHGVPelAVPRDIRYLKQLPLLGSGK 701
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
123-625 |
1.95e-08 |
|
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: 57.07 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGDg 202
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 203 flrrgdrvtlmdtlndaieraghvdhtivydrlgipadslswtprdewwDDAVAtqsptfethsmaasdpcMLLYSSGTT 282
Cdd:cd05914 88 -------------------------------------------------EDDVA-----------------LINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 283 GTPKGIVHTH--------AGALVQPAKEihfgfdqrpGDRFcwVSdigwmMGPWSLIGNHAFAGTIVMYEGAP----DHP 350
Cdd:cd05914 102 GNSKGVMLTYrnivsnvdGVKEVVLLGK---------GDKI--LS-----ILPLHHIYPLTFTLLLPLLNGAHvvflDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 351 APDRFWQLIEDHGITQFGVS-------------------------------PTAIR-ALRDHGDEHVAGHdlssLRILGS 398
Cdd:cd05914 166 PSAKIIALAFAQVTPTLGVPvplviekifkmdiipkltlkkfkfklakkinNRKIRkLAFKKVHEAFGGN----IKEFVI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 399 TGEPWDPESWRWFYD-----HVGGGDT---PIINISggtevfgcflmplPTESLKPCTLGGPGLGMDIDIVDDDgtsvrD 470
Cdd:cd05914 242 GGAKINPDVEEFLRTigfpyTIGYGMTetaPIISYS-------------PPNRIRLGSAGKVIDGVEVRIDSPD-----P 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 471 ANERGYLVARssSPSMTRRLWSGEDRYLEAYwsrFEDVWNH-GDWAQMDADGDWFLHGRADDAI-NVAGRKVGPAEVEGA 548
Cdd:cd05914 304 ATGEGEIIVR--GPNVMKGYYKNPEATAEAF---DKDGWFHtGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAK 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 549 LIDHDAVTQAAVVGVPDDttgEAAIAYvILADAATPSAELRAELRDHVGDAHGKPF--------RPREVVFV-DDLPKTQ 619
Cdd:cd05914 379 INNMPFVLESLVVVQEKK---LVALAY-IDPDFLDVKALKQRNIIDAIKWEVRDKVnqkvpnykKISKVKIVkEEFEKTP 454
|
....*.
gi 499204776 620 SGKLVR 625
Cdd:cd05914 455 KGKIKR 460
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
113-400 |
2.38e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.98 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 113 EGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVglympMVPEVQSI-----LYGIFKIGAIAVPIFSGFGVEAT-- 185
Cdd:PRK12582 72 EPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPV-----MILSGNSIehalmTLAAMQAGVPAAPVSPAYSLMSHdh 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 186 ------ATRIADAecsVVFTGDGflrrgdrvtlmDTLNDAIERAGHVDHTIVYdrLGIPADSLSWTPRDEWwddavATQS 259
Cdd:PRK12582 147 aklkhlFDLVKPR---VVFAQSG-----------APFARALAALDLLDVTVVH--VTGPGEGIASIAFADL-----AATP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 260 PTFETH-SMAASDPCM---LLYSSGTTGTPKGIVHTH---AGALVQPAKEIHFGFDQRPGDRfcwvsdIGWMmgPWSLI- 331
Cdd:PRK12582 206 PTAAVAaAIAAITPDTvakYLFTSGSTGMPKAVINTQrmmCANIAMQEQLRPREPDPPPPVS------LDWM--PWNHTm 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 332 -GNHAFAGtiVMYEGA-----PDHPAPDRFWQLIED-HGI--TQFGVSPTAIRALRDH--GDEHVAGHDLSSLRILGSTG 400
Cdd:PRK12582 278 gGNANFNG--LLWGGGtlyidDGKPLPGMFEETIRNlREIspTVYGNVPAGYAMLAEAmeKDDALRRSFFKNLRLMAYGG 355
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
122-298 |
1.30e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.85 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 122 QTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGD 201
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRGDRVTLMDTLN-DAIERAGHVDHTIVY--DRLGIPADSlswtprdewWDDAVATQSPTFETHSMAASDPCMLLYS 278
Cdd:PLN02861 158 SKISSILSCLPKCSSNlKTIVSFGDVSSEQKEeaEELGVSCFS---------WEEFSLMGSLDCELPPKQKTDICTIMYT 228
|
170 180
....*....|....*....|
gi 499204776 279 SGTTGTPKGIVHTHAGALVQ 298
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAE 248
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
261-623 |
4.91e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 53.39 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 261 TFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGAL--VQPAKEIhFGFDQRpgDRfcwvsdigwMMGpwSLIGNHAFAG 338
Cdd:PRK08633 773 RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILsnIEQISDV-FNLRND--DV---------ILS--SLPFFHSFGL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 339 TIVMY----EGAPD--HPAP-DRFW--QLIEDHGITQFGVSPTAIRA-LRDhgdEHVAGHDLSSLRILGSTGEPWDPESW 408
Cdd:PRK08633 839 TVTLWlpllEGIKVvyHPDPtDALGiaKLVAKHRATILLGTPTFLRLyLRN---KKLHPLMFASLRLVVAGAEKLKPEVA 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 409 RWFYDHVGggdTPIINISGGTEvfgcfLMPLPTESL--------------KPCTLGGPGLGMDIDIVDDDGTSVRDANER 474
Cdd:PRK08633 916 DAFEEKFG---IRILEGYGATE-----TSPVASVNLpdvlaadfkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGED 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 475 GYLVARSssPSMTRRLWSGEDRYLEAYWSRFEDVW-NHGDWAQMDADGdwFLH--GRADDAINVAGRKVGPAEVEGAL-- 549
Cdd:PRK08633 988 GLILIGG--PQVMKGYLGDPEKTAEVIKDIDGIGWyVTGDKGHLDEDG--FLTitDRYSRFAKIGGEMVPLGAVEEELak 1063
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499204776 550 IDHDAVTQAAVVGVPDDTTGEAaIAYVIladaaTPSAELRAELRDHVGDAhGKP--FRPREVVFVDDLPKTQSGKL 623
Cdd:PRK08633 1064 ALGGEEVVFAVTAVPDEKKGEK-LVVLH-----TCGAEDVEELKRAIKES-GLPnlWKPSRYFKVEALPLLGSGKL 1132
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
111-305 |
5.17e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 52.72 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 111 IWEGEDGTVRQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIA 190
Cdd:PLN02614 69 IVDGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIIS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 191 DAECSVVFTGDGFLRRgdrvtLMDTLNDAIEraghvdhtivYDRLGIPADSLSWTPRDEW---------WDDAVAT-QSP 260
Cdd:PLN02614 149 HSEVSIVFVEEKKISE-----LFKTCPNSTE----------YMKTVVSFGGVSREQKEEAetfglviyaWDEFLKLgEGK 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499204776 261 TFETHSMAASDPCMLLYSSGTTGTPKGIVHTHAGALVQPAKEIHF 305
Cdd:PLN02614 214 QYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRL 258
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
278-625 |
1.06e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 51.30 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 278 SSGTTGTPKGIVHT----------HAGALVqpakeiHFGFdqRPGDRFCwvsdIGWMMGPWSlIGNHAFAGTIVMyeGAP 347
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdldrwaelFARSLR------AAGV--RPGDRVQ----NAFGYGLFT-GGLGLHYGAERL--GAT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPA----PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHvaGHDL--SSLRILGSTGEPWdPESWR-WFYDHVGggdT 420
Cdd:COG1541 156 VIPAgggnTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEE--GIDPrdLSLKKGIFGGEPW-SEEMRkEIEERWG---I 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 421 PIINISGGTEVfgcflmplpteslkpctlgGPGLGMD---------------IDIVDDD-GTSVRDAnERGYLV----AR 480
Cdd:COG1541 230 KAYDIYGLTEV-------------------GPGVAYEceaqdglhiwedhflVEIIDPEtGEPVPEG-EEGELVvttlTK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 481 SSSPsMTRrlwsgedryleaYWSrfedvwnhGDWAQMDAD-----------GDWFlhGRADDAINVAGRKVGPAEVEGAL 549
Cdd:COG1541 290 EAMP-LIR------------YRT--------GDLTRLLPEpcpcgrthpriGRIL--GRADDMLIIRGVNVFPSQIEEVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 550 IDHDAVTQAAVVGVPDDTTGEAAIAYVILADAATPSA---ELRAELRDHVGdahgkpFRPR-EVVFVDDLPKTQsGKLVR 625
Cdd:COG1541 347 LRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEAlaeAIAAALKAVLG------LRAEvELVEPGSLPRSE-GKAKR 419
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
115-292 |
2.26e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 50.75 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 115 EDGTVrqqTYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPEVQSILYGIFKIGaiavpifsgfgveatatriadae 193
Cdd:cd05938 2 EGETY---TYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 194 CSVVFTGDG---------FLRRGDRVTLMDT-LNDAIER--------------AGHVDHTIVYDRLGIPADSLSwtprde 249
Cdd:cd05938 56 CPVAFLNTNirsksllhcFRCCGAKVLVVAPeLQEAVEEvlpalradgvsvwyLSHTSNTEGVISLLDKVDAAS------ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499204776 250 wwDDAVATQSPTFEThsmaASDPCMLLYSSGTTGTPKGIVHTH 292
Cdd:cd05938 130 --DEPVPASLRAHVT----IKSPALYIYTSGTTGLPKAARISH 166
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
352-620 |
3.29e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 50.49 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 352 PDRFWQLIEDHGITQFGVSPTAIRALRDhgDEHVAGHDLSSLRILGSTGEP---WDPESWRWFYDHV------GGGDTPI 422
Cdd:PRK07868 683 PDRFVQEVRQYGVTVVSYTWAMLREVVD--DPAFVLHGNHPVRLFIGSGMPtglWERVVEAFAPAHVveffatTDGQAVL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 423 INISGGTevFGCFLMPLPTESlkPCTLGGpglgMDID---IVDDDGTSVRDA--NERGYLVARSSSP-----SMTRRLWS 492
Cdd:PRK07868 761 ANVSGAK--IGSKGRPLPGAG--RVELAA----YDPEhdlILEDDRGFVRRAevNEVGVLLARARGPidptaSVKRGVFA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 493 GEDRyleayWSRFEDVWnhgdwaQMDADGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAA 572
Cdd:PRK07868 833 PADT-----WISTEYLF------RRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAV 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499204776 573 IAYVILADAATPSAELRAELRD-HVGdahgkpFRPREVVFVDDLPKTQS 620
Cdd:PRK07868 902 AAVTLRPGAAITAADLTEALASlPVG------LGPDIVHVVPEIPLSAT 944
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
123-293 |
5.52e-06 |
|
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: 49.38 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANAL-AERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVftgd 201
Cdd:cd17632 69 TYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 gflrrgdrVTLMDTLNDAIERA-------------GHVDHTIVYDRLGIPADSLSWTPRDEWWDDAVATQSPTFETHSMA 268
Cdd:cd17632 145 --------AVSAEHLDLAVEAVleggtpprlvvfdHRPEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLF 216
|
170 180 190
....*....|....*....|....*....|
gi 499204776 269 ASDP-----CMLLYSSGTTGTPKGIVHTHA 293
Cdd:cd17632 217 RPEPdddplALLIYTSGSTGTPKGAMYTER 246
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
278-625 |
1.18e-05 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 48.00 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 278 SSGTTGTPKGIVHTHAG----ALVQpAKEIH-FGFdqRPGDRFcwvsdigwMMGPwsliGNHAFAGTIVMYEGA-----P 347
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDldvwAELV-ARCLDaAGV--TPGDRV--------QNAY----GYGLFTGGLGFHYGAerlgaL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 348 DHPA----PDRFWQLIEDHGITQFGVSPTAIRALRDHGDEHVAGHDLSSLR--ILGstGEPWDPESWRWFYDHVGGGdtp 421
Cdd:cd05913 151 VIPAgggnTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKvgIFG--AEPWTEEMRKRIERRLGIK--- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 422 IINISGGTEVfgcflmplpteslkpctlGGPGLGMD---------------IDIVDD-DGTSVRDAnERGYLVArsssPS 485
Cdd:cd05913 226 AYDIYGLTEI------------------IGPGVAFEceekdglhiwedhfiPEIIDPeTGEPVPPG-EVGELVF----TT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 486 MTRrlwsgEDRYLEAYWSRfeD----VWNHGDWAQ----MDAdgdwfLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQ 557
Cdd:cd05913 283 LTK-----EAMPLIRYRTR--DitrlLPGPCPCGRthrrIDR-----ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGP 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499204776 558 AA--VVGVPDDT-TGEAAIAYVILADAATPSAELRAELRDHVGDAHGkpFRPR-EVVFVDDLPKTQsGKLVR 625
Cdd:cd05913 351 HYqlILTRQEHLdELTIKVEVRPEADDDEKLEALKQRLERHIKSVLG--VTVEvELVEPGSLPRSE-GKAKR 419
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
122-293 |
2.10e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.80 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 122 QTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEATATRIADAECSVVFTGD 201
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 GFLRRgdrvtlmdtLNDAIERAGHVDHTIVYDRLGIPADSL-----SWTPRDEWWDDAVATQSPTfETHSMAASDPCMLL 276
Cdd:PLN02387 187 KQLKK---------LIDISSQLETVKRVIYMDDEGVDSDSSlsgssNWTVSSFSEVEKLGKENPV-DPDLPSPNDIAVIM 256
|
170
....*....|....*..
gi 499204776 277 YSSGTTGTPKGIVHTHA 293
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHG 273
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
123-298 |
4.31e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.50 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 123 TYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPE-VQSILYGIFKiGAIAVPIFSGFGVEATATRIADAECSVVFTgd 201
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEwFIAAVGAIFA-GGIAVGIYTTNSPEACQYVAETSEANILVV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 202 gflrrgDRVTLMDTLNDAIERAGHVDHTIVYdRLGIP---ADSLSWTPRDEWWDDAVATQSPTFEThSMAASDPCMLLYS 278
Cdd:cd05933 87 ------ENQKQLQKILQIQDKLPHLKAIIQY-KEPLKekePNLYSWDEFMELGRSIPDEQLDAIIS-SQKPNQCCTLIYT 158
|
170 180
....*....|....*....|....*.
gi 499204776 279 SGTTGTPKGIVHTH------AGALVQ 298
Cdd:cd05933 159 SGTTGMPKGVMLSHdnitwtAKAASQ 184
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
120-373 |
6.81e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 42.80 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 120 RQQTYHDLHQQANRVANALAERGIGEGDTVGLYMPMVPEVQSILYGIFKIGAIAVPIFSGFGVEAT-ATRIADA----EC 194
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQdLAKLKHLfellKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 195 SVVFTGDGflrrgdrvtlmDTLNDAIERAGHVDHTIVYDRLGIPAdslswtpRDEWWDDAVATQSPTFET-HSMAASDP- 272
Cdd:cd05921 104 GLVFAQDA-----------APFARALAAIFPLGTPLVVSRNAVAG-------RGAISFAELAATPPTAAVdAAFAAVGPd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 273 --CMLLYSSGTTGTPKGIVHTHAG-ALVQPAKEIHFGFdqrPGDRFCWVSDigWMmgPWSLI--GNHAFAgtIVMYEGAP 347
Cdd:cd05921 166 tvAKFLFTSGSTGLPKAVINTQRMlCANQAMLEQTYPF---FGEEPPVLVD--WL--PWNHTfgGNHNFN--LVLYNGGT 236
|
250 260 270
....*....|....*....|....*....|.
gi 499204776 348 DH-----PAPDRFWQLIEDhgitQFGVSPTA 373
Cdd:cd05921 237 LYiddgkPMPGGFEETLRN----LREISPTV 263
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
506-594 |
6.91e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 42.55 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 506 EDVWNH----GDWAqmdaDGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVGVPDDTTGEAAIAyVILADA 581
Cdd:PRK09029 330 DEGWFAtrdrGEWQ----NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESDS 404
|
90
....*....|...
gi 499204776 582 ATPSAELRAELRD 594
Cdd:PRK09029 405 EAAVVNLAEWLQD 417
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
520-632 |
2.82e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.88 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499204776 520 DGDWFLHGRADDAINVAGRKVGPAEVEGALIDHDAVTQAAVVG---VPddttGEAAIAYVILADAATPSAelRAE----- 591
Cdd:PRK12476 488 DGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTaftVP----AEDNERLVIVAERAAGTS--RADpapai 561
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 499204776 592 --LRDHVGDAHGKPFRPREVVFVDDLPKTQSGKLVRRAVASAY 632
Cdd:PRK12476 562 daIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQY 604
|
|
| |
