|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-553 |
0e+00 |
|
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: 1019.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 48 IPEYFNFAKDVLDQWTNMEKAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMK 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 208 YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 288 QGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 368 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLR 447
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 448 GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSH 527
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500
....*....|....*....|....*.
gi 568949898 528 DQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKV 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-553 |
0e+00 |
|
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: 592.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 DtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSsFGL 248
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 329 QNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENG 408
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 409 ATLPPGQEGDIALQVlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 488
Cdd:cd05972 268 RELPPGEEGDIAIKL---PPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949898 489 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREI 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
45-553 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 570.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 45 KIEIPEYFNFAKDVLDQWtnmekAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKI 124
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIV---- 191
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 192 SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSD 271
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 272 TGWAKSAWSSVFSPWTQGACVFAhylprFESTS-------ILQTLSKFPITVFCSAPTAYRMLVQND---MSSYKFNSLK 341
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVL-----YEGRPdfpdpgrLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 342 HCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIA 420
Cdd:COG0365 310 LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 421 LQvlpeRPF-GLFTHYVDNPSKTASTLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 496
Cdd:COG0365 390 IK----GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568949898 497 IAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREI 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
37-553 |
0e+00 |
|
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: 557.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 37 YESMKQDFKIEIPEYFNFAKDVLDQWTNMEKagkrlSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTeACSLQRGDR 116
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYP-----DKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD--DTLAPAVDAVAAKCENLHSKLIVSQH 194
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 195 SREGWGNLKEMMKYASDS----HTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIASDVMWNTS 270
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 271 DTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPI 350
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 351 NPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPFG 430
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 431 LFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 510
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568949898 511 GEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05970 474 GQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIV 514
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
28-551 |
1.57e-139 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 416.99 E-value: 1.57e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 28 TATPQNFSNYESMKQDFKI-EIPEYF--------NFAKDVLDQWTNMEKAGKrlsnPAFWWIDGNGEElRWSFEELGLLS 98
Cdd:PRK04319 9 IKGEPNLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 99 RKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVdaV 178
Cdd:PRK04319 84 NKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--P 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 179 AAKCENLHSKLIVSQHSREGWG--NLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRF 256
Cdd:PRK04319 161 ADDLPSLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 257 WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA--CVFAhylPRFESTSILQTLSKFPITVFCSAPTAYRMLvqndMSS 334
Cdd:PRK04319 240 VLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRML----MGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 335 -------YKFNSLKHCVSAGEPINPEVMeQWRKKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKIL 404
Cdd:PRK04319 313 gddlvkkYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 405 DENGATLPPGQEGDIALQvlPERPfGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 484
Cdd:PRK04319 391 DDQGNELPPNRMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949898 485 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPR 551
Cdd:PRK04319 468 FEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPR 532
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-553 |
7.17e-136 |
|
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: 402.72 E-value: 7.17e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAkciitdd 169
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 tlapavdAVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05974 74 -------VYAAVDENTHA---------------------------------DDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 250 lSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ 329
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 330 NDMSSYKFnSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGA 409
Cdd:cd05974 193 QDLASFDV-KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 410 tlpPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVES 489
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949898 490 ALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRL 410
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-553 |
3.50e-123 |
|
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: 370.68 E-value: 3.50e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 DTLAPAVDAvaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgL 248
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 329 QND---MSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKI 403
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 404 LDENGATLPPGQEGDIALQvlPERPfGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 483
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 484 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP--SDELKEEIINFVRQKLGAHVAPREI 418
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
88-553 |
2.52e-112 |
|
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: 342.49 E-value: 2.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DDTLAPAVdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemmaIYFTSGTTGPPKMIGHTHSsFG 247
Cdd:cd05971 85 DGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHAHR-VL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLSVNGRFWLDLI--ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05971 114 LGHLPGVQFPFNLFprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 326 ML-VQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPAFDVKI 403
Cdd:cd05971 194 MMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 404 LDENGATLPPGQEGDIALqvlpERPFGL-FTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRI 482
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAV----ELPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949898 483 GPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
85-553 |
1.19e-109 |
|
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: 336.01 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemMAIYFTSGTTGPPKMIGHTHS 244
Cdd:COG0318 100 LVT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SFgLGLSVNGRFWLDLIASDVMWNTS----DTGWaksaWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSA 320
Cdd:COG0318 124 NL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 321 PTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSP 397
Cdd:COG0318 197 PTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 398 AFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILS 477
Cdd:COG0318 277 GVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 478 SGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVkkttAPYKYPRKV 553
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAFLRERL----ARYKVPRRV 422
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-553 |
4.69e-98 |
|
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: 305.60 E-value: 4.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 tlapavdavAAKCENLHSKLIVsqhsregwgnlkemmkyasdshtcvdtkhdeMMaiyFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05973 80 ---------AANRHKLDSDPFV-------------------------------MM---FTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG-ACVFAHylPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 329 QNDMSSYKF--NSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIL 404
Cdd:cd05973 194 AAGAEVPARpkGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 405 DENGATLPPGQEGDIALQVlPERPFGLFTHYVDNPSKTAStlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 484
Cdd:cd05973 274 DDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 485 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTI 416
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-553 |
7.85e-96 |
|
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: 302.37 E-value: 7.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 50 EYFNFAKDVLDQwtnmeKAGKRLSNPAFwwIDGNGEelrWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWL 129
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSRE--GWGNLKEMMK 207
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 208 YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 288 QGACVFahYLP-RFESTSILQTLSKFPITVFCSAPTAYR-MLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD 365
Cdd:cd05959 230 VGATTV--LMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 366 IYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDiaLQVlpeRPFGLFTHYVDNPSKTAS 444
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGE--LYV---RGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 445 TLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 524
Cdd:cd05959 382 TFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500
....*....|....*....|....*....
gi 568949898 525 KshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05959 462 E--DSEALEEELKEFVKDRLAPYKYPRWI 488
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
226-553 |
9.79e-95 |
|
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: 293.42 E-value: 9.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFAHylPRFESTSI 305
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 306 LQTLSKFPITVFCSAPTAYRMLVQNDMSS-YKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--VLICGNF 382
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 383 KGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDED 462
Cdd:cd04433 161 DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-----RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 463 GYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKK 542
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRAHVRE 310
|
330
....*....|.
gi 568949898 543 TTAPYKYPRKV 553
Cdd:cd04433 311 RLAPYKVPRRV 321
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
66-553 |
7.01e-94 |
|
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: 296.01 E-value: 7.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 66 EKAGKRLSN-PAFWWIDgngeeLRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05936 6 EEAARRFPDkTALIFMG-----RKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 TTQLTQKDILYRLQSSKAKCIITDDTLApavdavaakcenlhsKLIVSQHSREGWgnlkemmkyasdshtCVDTKHDeMM 224
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------DLLAAGAPLGER---------------VALTPED-VA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 225 AIYFTSGTTGPPKMIGHTHSSfglgLSVNgrfwldliASDVMWNTSDTGWAKS------------AWS-SVFSPWTQGAC 291
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRN----LVAN--------ALQIKAWLEDLLEGDDvvlaalplfhvfGLTvALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 292 VFahYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGY 370
Cdd:cd05936 197 IV--LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTASTL 446
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVrgpQV--------MKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyks 526
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---- 422
|
490 500
....*....|....*....|....*..
gi 568949898 527 hDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05936 423 -GASLTEEEIIAFCREQLAGYKVPRQV 448
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-553 |
4.76e-87 |
|
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: 277.05 E-value: 4.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaKCI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLAPAVDAVaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd05958 84 ITVALCAHALTAS------------------------------------------DDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 246 FGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFESTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 326 -MLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIL 404
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 405 DENGATLPPGQEGDIALQvlpeRPFGLftHYVDNPSKtASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 484
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 485 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAI 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-553 |
2.22e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 264.74 E-value: 2.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAVAAKCENLHSKLIVSQHSREG----WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIG 240
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 241 HTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWAksawssvFSPWTQGACVFahYLPRFESTSILQTLSKFPI 314
Cdd:PRK06187 187 LSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGAKQV--IPRRFDPENLLDLIETERV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 315 TVFCSAPTAYRMLVQNDMSS-YKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNF-----KGMKI 387
Cdd:PRK06187 257 TFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 388 KPGSMGKPSPAFDVKILDENGATLPP--GQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYF 465
Cdd:PRK06187 337 KRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIV-----RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 466 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVkkttA 545
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAKELRAFLRGRL----A 486
|
....*...
gi 568949898 546 PYKYPRKV 553
Cdd:PRK06187 487 KFKLPKRI 494
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
78-553 |
4.78e-78 |
|
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: 259.10 E-value: 4.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 78 WWIDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDIL 154
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 155 YRLQSSKAKCIITDDT---------LAPAVDAVAAKCENLHSKLIVSQH----------SREGWGNlkEMMKYASDSHTC 215
Cdd:TIGR02188 154 DRINDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRtgnpvvpwveGRDVWWH--DLMAKASAYCEP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 216 VDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAH 295
Cdd:TIGR02188 232 EPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 296 Y-LPRFESTS-ILQTLSKFPITVFCSAPTAYRMLVQ---NDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD---IY 367
Cdd:TIGR02188 312 EgVPTYPDPGrFWEIIEKHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 368 EGYGQTET--VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLP-PGQEGDIAL-QVLPERPFGLF---THYVDNPS 440
Cdd:TIGR02188 392 DTWWQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIkQPWPGMLRTIYgdhERFVDTYF 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 441 KTAStlrgSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 520
Cdd:TIGR02188 472 SPFP----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTL 547
|
490 500 510
....*....|....*....|....*....|...
gi 568949898 521 NPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:TIGR02188 548 KDGYEPDD--ELRKELRKHVRKEIGPIAKPDKI 578
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-478 |
4.97e-78 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 253.00 E-value: 4.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 82 GNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 162 AKCIITDDTL-APAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSH-TCVDTKHDEMMAIYFTSGTTGPPKMI 239
Cdd:pfam00501 94 AKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTH---SSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 391
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGApKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 392 MGKPSPAFDVKILDEN-GATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVA 469
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV-----RGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 568949898 470 RSDDIILSS 478
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-555 |
1.17e-76 |
|
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: 250.07 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 tlapavDAVAakcenlhsklivsqhsregwgnlkemmkYASdshtcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05919 91 ------DDIA----------------------------YLL-----------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFEStsILQTLSKFPITVFCSAPTAY-RML 327
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWPTAER--VLATLARFRPTVLYGVPTFYaNLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 328 VQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDEN 407
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 408 GATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 487
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 488 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKVGV 555
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAF 418
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-553 |
2.73e-76 |
|
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: 254.02 E-value: 2.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 53 NFAKDVLDQwtNMEKAGKRlsnPAFWWiDGN--GEELRWSFEELglLSR--KFANILTEAcSLQRGDRVMVILPKIPEWW 128
Cdd:cd05966 53 NISYNCLDR--HLKERGDK---VAIIW-EGDepDQSRTITYREL--LREvcRFANVLKSL-GVKKGDRVAIYMPMIPELV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 129 LANVACLRTG---TVLIPGttqLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHsKLIVSQHS- 195
Cdd:cd05966 124 IAMLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTg 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 196 --------REGWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMW 267
Cdd:cd05966 200 gevpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 268 NTSDTGWAKSAWSSVFSPWTQGACVFAhylprFEST----------SILQtlsKFPITVFCSAPTAYRMLVQ---NDMSS 334
Cdd:cd05966 278 CTADIGWITGHSYIVYGPLANGATTVM-----FEGTptypdpgrywDIVE---KHKVTIFYTAPTAIRALMKfgdEWVKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 335 YKFNSLKHCVSAGEPINPEVMEQWRKKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDVKILDE 406
Cdd:cd05966 350 HDLSSLRVLGSVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 407 NGATLPPGQEGDIALqvlpERPFglfthyvdnPSkTASTLRGS--------------FYITGDRGYMDEDGYFWFVARSD 472
Cdd:cd05966 427 EGNEVEGEVEGYLVI----KRPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 473 DIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRK 552
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDK 570
|
.
gi 568949898 553 V 553
Cdd:cd05966 571 I 571
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-558 |
7.76e-74 |
|
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: 246.72 E-value: 7.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 53 NFAKDVLDQwtNMEKAGKRLsnpAFWWIDGNGEELR-WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLAN 131
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 132 VACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVD-AVAAKCENLHSKLIVSqhsREG--- 198
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDdALNPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 199 ------WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 273 GWAKSAWSSVFSPWTQGACVFAHY-LPRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQND---MSSYKFNSLKHCVSAG 347
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWPTPARMwQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 348 EPINPEVMEQWRKKTGLD---IYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQ 422
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 423 V-LPERPFGLFThyvDNPSKTASTLR--GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:cd17634 444 DpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 500 SAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKVGVPGT 558
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDS 577
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
88-553 |
1.21e-73 |
|
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: 242.13 E-value: 1.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIt 167
Cdd:cd17631 20 SLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 ddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17631 98 -----------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLSVNGRFWLDLIASDV------MWNTSDTGwaksawssVFSPWT--QGACVfaHYLPRFESTSILQTLSKFPITVFCS 319
Cdd:cd17631 124 LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTllRGGTV--VILRKFDPETVLDLIERHRVTSFFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 320 APTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGKPS 396
Cdd:cd17631 194 VPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 397 PAFDVKILDENGATLPPGQEGDIAL---QVLPErpfglfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDD 473
Cdd:cd17631 273 FFVEVRIVDPDGREVPPGEVGEIVVrgpHVMAG--------YWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 474 IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd17631 345 MIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP-----GAELDEDELIAHCRERLARYKIPKSV 419
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-551 |
4.40e-73 |
|
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: 242.44 E-value: 4.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 50 EYFNFAKDVLDqwTNMEKAgkRLSNPAFwwIDGNGeelRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWL 129
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVEG--RGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSkLIVSQHSREGWGNLKEMMKYA 209
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 210 SDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 290 ACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYR-MLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYE 368
Cdd:TIGR02262 230 ATTVL-MGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 369 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRG 448
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 449 SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShd 528
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500
....*....|....*....|...
gi 568949898 529 qeqLKKEIQEHVKKTTAPYKYPR 551
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPR 481
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
85-553 |
1.54e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 230.56 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPK--M 238
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKgaM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 239 IGHTHSsfglgLSvNGRFW---LDLIASD---------------VMWNTsdtgwaksawssvfsPWTQGACVFAHylPRF 300
Cdd:PRK07656 186 LTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA---------------PLMRGATILPL--PVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 301 ESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY-EGYGQTE---T 375
Cdd:PRK07656 243 DPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEasgV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLR--GSFYiT 453
Cdd:PRK07656 323 TTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGYYDDPEATAAAIDadGWLH-T 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 454 GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLK 533
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-AELTEEELI 475
|
490 500
....*....|....*....|
gi 568949898 534 KEIQEHVkkttAPYKYPRKV 553
Cdd:PRK07656 476 AYCREHL----AKYKVPRSI 491
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
89-548 |
5.22e-68 |
|
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: 228.64 E-value: 5.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 DTLAPAVDAvAAKCENLHSKLIVSQHSREGWGNLKEMMK---YASDSH--TCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05911 90 PDGLEKVKE-AAKELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSFGLGL-SVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWtQGACVfaHYLPRFESTSILQTLSKFPITVFCSAPT 322
Cdd:cd05911 169 RNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATV--IIMPKFDSELFLDLIEKYKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 323 AYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFD 400
Cdd:cd05911 246 IAAALAKSPLlDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 401 VKILDENG-ATLPPGQEGDIAL---QVLPErpfglfthYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDII 475
Cdd:cd05911 326 AKIVDDDGkDSLGPNEPGEICVrgpQVMKG--------YYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949898 476 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqlkKEIQEHVKKTTAPYK 548
Cdd:cd05911 398 KYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYK 465
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
84-553 |
4.73e-67 |
|
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: 229.51 E-value: 4.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIPG---TTQLTQkdilyRLQ 158
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfaAKELAS-----RID 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 159 SSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIVSQHSR--------EGWGNLKEMMKYASdSHTCVDTKHD 221
Cdd:cd05967 152 DAKPKLIVTAScgiepgkvvPYKPLLDKALELSGHKPHHVLVLNRPQvpadltkpGRDLDWSELLAKAE-PVDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 222 EMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGAcvfahylprfe 301
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGA----------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 302 sTSIL---------------QTLSKFPITVFCSAPTAYRMLVQND-----MSSYKFNSLKHCVSAGEPINPEVMEQWRKK 361
Cdd:cd05967 300 -TTVLyegkpvgtpdpgafwRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 362 TGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvLPERPFGLFTHYVD 437
Cdd:cd05967 379 LGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTLWKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 438 NPSKTASTLRGS--FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 515
Cdd:cd05967 458 DERFKKLYLSKFpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPL 537
|
490 500 510
....*....|....*....|....*....|....*...
gi 568949898 516 AFIVLNPDYKShDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05967 538 GLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLV 574
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-553 |
1.84e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 225.99 E-value: 1.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 62 WTNMEKAGKRLSNPAFWWIDGNgeelRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVL 141
Cdd:PRK08314 13 FHNLEVSARRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 142 IPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAV------------------DAVAAKCENLHSKLIVSQHSRE-----G 198
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEIAVPAWLRAEPPLQalapgG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 199 WGNLKEMMK--YASDSHTcvdTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSD----T 272
Cdd:PRK08314 169 VVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 273 GWAKSAWSSVFSpwtqGACVFahYLPRFESTSILQTLSKFPITVFCSAPTayrMLV----QNDMSSYKFNSLKHCVSAGE 348
Cdd:PRK08314 245 GMVHSMNAPIYA----GATVV--LMPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 349 PINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIAL---QV 423
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVhgpQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 lperpfglFTHYVDNPSKTAS---TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:PRK08314 395 --------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568949898 500 SAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK08314 467 ACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIV 517
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-553 |
4.80e-66 |
|
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: 221.97 E-value: 4.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITdd 169
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 tlapavdavaakcenlHSKLivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ 329
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 330 N-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILD-EN 407
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 408 GATLPPGQEGDIALQVlPErpfgLFTHYVDNPSKTAS---TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 483
Cdd:cd05935 270 GRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 484 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREV 411
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
100-553 |
6.04e-66 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 226.95 E-value: 6.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 100 KFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKAKCIITDD------- 169
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 --TLAPAVDAVAAKCENLHSKLIVS--------QHSREGWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMI 239
Cdd:PRK00174 186 piPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHY-LPRFESTS-ILQTLSKFPITVF 317
Cdd:PRK00174 264 LHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEgVPNYPDPGrFWEVIDKHKVTIF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 318 CSAPTAYRMLVQ---NDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD---IYEGYGQTET--VLIC---GnfkGMK 386
Cdd:PRK00174 344 YTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGErcpIVDTWWQTETggIMITplpG---ATP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 387 IKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL------QVL-----PERpfglfthYVdnpsKTA-STLRGSfYITG 454
Cdd:PRK00174 421 LKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIkdpwpgMMRtiygdHER-------FV----KTYfSTFKGM-YFTG 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 455 DRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKK 534
Cdd:PRK00174 489 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRK 566
|
490
....*....|....*....
gi 568949898 535 EIQEHVKKTTAPYKYPRKV 553
Cdd:PRK00174 567 ELRNWVRKEIGPIAKPDVI 585
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-553 |
3.47e-64 |
|
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: 217.16 E-value: 3.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYrlqsskakcIIT 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY---------VIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyaSDSHTCVDtkhdeMMAIYFTSGTTGPPKMIGHTHSSfg 247
Cdd:cd05941 82 D-----------------------------------------SEPSLVLD-----PALILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 lglsvngrfwldlIASDVMWNTSDTGWAKS--------------AWSSVFSP-WTQGACVFahyLPRFESTSILQTLSKF 312
Cdd:cd05941 114 -------------LAANVRALVDAWRWTEDdvllhvlplhhvhgLVNALLCPlFAGASVEF---LPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 313 PITVFCSAPTAYRMLVQ--NDMSSYKFNSLKHC-------VSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGN-F 382
Cdd:cd05941 178 SITVFMGVPTIYTRLLQyyEAHFTDPQFARAAAaerlrlmVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 383 KGmKIKPGSMGKPSPAFDVKILDENGA-TLPPGQEGDIalQVlpeRPFGLFTHYVDNPSKTASTLRG-SFYITGDRGYMD 460
Cdd:cd05941 258 DG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEI--QV---RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 461 EDGYFWFVAR-SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLKkeiqEH 539
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EW 407
|
490
....*....|....
gi 568949898 540 VKKTTAPYKYPRKV 553
Cdd:cd05941 408 AKQRLAPYKRPRRL 421
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-553 |
4.87e-63 |
|
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: 213.69 E-value: 4.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd05934 1 GRRWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDdtlaPAvdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemmAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd05934 80 VVD----PA--------------------------------------------------SILYTSGTTGPPKgvVITHAN 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSFGLGLSVNgrfWLDLIASDVMW--------NTSDTGWAkSAWSSvfspwtQGACVFahyLPRFESTSILQTLSKFPIT 315
Cdd:cd05934 106 LTFAGYYSAR---RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRML-VQNDMSSYKFNSLKHCVSAgePINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGK 394
Cdd:cd05934 173 VTNYLGAMLSYLlAQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 395 PSPAFDVKILDENGATLPPGQEGDIALQvlPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDI 474
Cdd:cd05934 251 PAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDM 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 475 ILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK-SHDqeqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05934 329 IRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE------ELFAFCEGQLAYFKVPRYI 402
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
66-553 |
2.81e-60 |
|
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: 208.63 E-value: 2.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 66 EKAGKRLSNPAFwwIDG-NGEELrwSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05904 13 LFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 TTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGwgnlkemMKYASDSHTC-VDTKHDEM 223
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDL-------LFEADEAEPPvVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 224 MAIYFTSGTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDLIASDVMwntsdtGWAKSAWSSVFSpwtqGACV 292
Cdd:cd05904 161 AALLYSSGTTGRSKgvMLTHrnliamvaqFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 293 FAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGY 370
Cdd:cd05904 231 VV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIvDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL 446
Cdd:cd05904 309 GMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RG-SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyk 525
Cdd:cd05904 384 DKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG-- 461
|
490 500
....*....|....*....|....*...
gi 568949898 526 SHDQEQlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05904 462 SSLTED---EIMDFVAKQVAPYKKVRKV 486
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-551 |
1.37e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.96 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAV--AAKCENL-----------------------HSKLIV---SQHSREGWGNLKEMMKYASDshTCVDTKHD 221
Cdd:PRK06710 130 LVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVkvsESETIHLWNSVEKEVNTGVE--VPCDPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 222 eMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLdliasdvmWNTSDTGWAKSAWSSVFSPWTQGAC----VFAHY- 296
Cdd:PRK06710 208 -LALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVmnlsIMQGYk 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 297 ---LPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQ 372
Cdd:PRK06710 278 mvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 373 TETVLIC-GNFKGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALQVlPErpfgLFTHYVDNPSKTASTLRGSF 450
Cdd:PRK06710 358 TESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG-PQ----IMKGYWNKPEETAAVLQDGW 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 451 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyksHDQE 530
Cdd:PRK06710 433 LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK-----EGTE 507
|
490 500
....*....|....*....|.
gi 568949898 531 QLKKEIQEHVKKTTAPYKYPR 551
Cdd:PRK06710 508 CSEEELNQFARKYLAAYKVPK 528
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
53-540 |
1.85e-59 |
|
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: 208.88 E-value: 1.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 53 NFAKDVLDQWTnmekaGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANV 132
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 133 ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLhSKLIVSQHSregwGNLK 203
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTV-EKVVVVRHL----GNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 204 EMMKYASDSHTCVDTKH----------DEMMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTG 273
Cdd:cd05968 210 TPAKGRDLSYDEEKETAgdgaerteseDPLMIIY-TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 274 WAKSAWSsVFSPWTQGACVFAHY-LPRFESTSIL-QTLSKFPITVFCSAPTAYRMLV---QNDMSSYKFNSLKHCVSAGE 348
Cdd:cd05968 289 WMMGPWL-IFGGLILGATMVLYDgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 349 PINPEVMeQWRKKTGLD----IYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPgQEGDIALqv 423
Cdd:cd05968 368 PWNPEPW-NWLFETVGKgrnpIINYSGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVL-- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 lpERPF-GLFTHYVDNPSKTASTLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:cd05968 444 --LAPWpGMTRGFWRDEDRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 568949898 500 SAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHV 540
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERV 560
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
89-553 |
2.84e-57 |
|
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: 200.23 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 -DTLAPAVDAvAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKH---DEMMAIYFTSGTTGPPKMIGHTHs 244
Cdd:cd05926 94 kGELGPASRA-ASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVplpDDLALILHTSGTTGRPKGVPLTH- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 sfgLGLSVNGRFwldlIASDVMWNTSDT-----------GWAKSAWSSVFSpwtQGACVFAhylPRFESTSILQTLSKFP 313
Cdd:cd05926 172 ---RNLAASATN----ITNTYKLTPDDRtlvvmplfhvhGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 314 ITVFCSAPTAYRMLVQNDMSSY--KFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV--LICGNFKGMKIKP 389
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 390 GSMGKPSPAfDVKILDENGATLPPGQEGDIALQ---VlperpfglfTH-YVDNPSKTA-STLRGSFYITGDRGYMDEDGY 464
Cdd:cd05926 319 GSVGKPVGV-EVRILDEDGEILPPGVVGEICLRgpnV---------TRgYLNNPEANAeAAFKDGWFRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 465 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdqeqLKKEIQEHVKKTT 544
Cdd:cd05926 389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-----TEEELRAFCRKHL 463
|
....*....
gi 568949898 545 APYKYPRKV 553
Cdd:cd05926 464 AAFKVPKKV 472
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
84-553 |
1.20e-56 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 198.56 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLAPAVDAVAAKCENLHskliVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPK--M--- 238
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlsh 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 239 ---------------------------IGHTHssfGLGLSVNGRfwldLIAsdvmwntsdtgwaksawssvfspwtqGAC 291
Cdd:PRK07514 179 gnllsnaltlvdywrftpddvlihalpIFHTH---GLFVATNVA----LLA--------------------------GAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 292 VFahYLPRFESTSILQTLSKfpITVFCSAPTAY-RMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGY 370
Cdd:PRK07514 226 MI--FLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTETVLICGN-FKGMKIkPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIalQVlpeRPFGLFTHYVDNPSKTASTLRG 448
Cdd:PRK07514 302 GMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMI--EV---KGPNVFKGYWRMPEKTAEEFRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 449 -SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSH 527
Cdd:PRK07514 376 dGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AAL 454
|
490 500
....*....|....*....|....*.
gi 568949898 528 DQEQLKKEIQEHVkkttAPYKYPRKV 553
Cdd:PRK07514 455 DEAAILAALKGRL----ARFKQPKRV 476
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
85-553 |
6.08e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 191.68 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAVAAKCENLHSKLIVS---QHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 242 THSSFgLGLSVNGRFWLDLIASDVMWNtsdtgwA----KSAWSSVF-SPWTQ-GACVfaHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSaGEPINP-EVMEQWRKK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 387
Cdd:PRK08316 263 SFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 388 KPGSMGKPSPAFDVKILDENGATLPPGQEGDIAlqvlpERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWF 467
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 468 VARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPY 547
Cdd:PRK08316 414 VDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA-----GATVTEDELIAHCRARLAGF 488
|
....*.
gi 568949898 548 KYPRKV 553
Cdd:PRK08316 489 KVPKRV 494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-553 |
9.42e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 190.89 E-value: 9.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGEElrWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 160 SKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMaiyFTSGTTGPPKMI 239
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 ------GHTHSSFGLGLSVNGRFwldliasdvMWNTSDTGWAKSA--WSSVFSPWTQGACVFAH---YLPRFESTSILQT 308
Cdd:PRK08276 159 krplpgLDPDEAPGMMLALLGFG---------MYGGPDSVYLSPAplYHTAPLRFGMSALALGGtvvVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 309 LSKFPITVFCSAPTAY-RML-----VQNdmsSYKFNSLKHCVSAGEPINPEVMEQ----WrkktGLDIYEGYGQTE---- 374
Cdd:PRK08276 230 IERYRVTHSQLVPTMFvRMLklpeeVRA---RYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEgggv 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 375 TVLICGNFKGmkiKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALQvLPERPFglftHYVDNPSKTASTLRGSFYIT- 453
Cdd:PRK08276 303 TVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVTv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 454 GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLK 533
Cdd:PRK08276 374 GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDALA 451
|
490 500
....*....|....*....|
gi 568949898 534 KEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK08276 452 AELIAWLRGRLAHYKCPRSI 471
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
90-550 |
2.47e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 188.33 E-value: 2.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK06178 60 TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCEnLHSKLIVSQH--------------------SREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFT 229
Cdd:PRK06178 139 QLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 230 SGTTGPPKMIGHTHSsfglglsvngrfwlDLIasdvmwntsDTGWAKSAWSSVFSPWTqgacVFAHYLPRF----ESTSI 305
Cdd:PRK06178 218 GGTTGMPKGCEHTQR--------------DMV---------YTAAAAYAVAVVGGEDS----VFLSFLPEFwiagENFGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 306 LqtlskFPI----TV----------FCSAPTAYR-----MLVQN--------DMSSYKFNSLKH--CVSAGEPINPEVME 356
Cdd:PRK06178 271 L-----FPLfsgaTLvllarwdavaFMAAVERYRvtrtvMLVDNavelmdhpRFAEYDLSSLRQvrVVSFVKKLNPDYRQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 357 QWRKKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpe 426
Cdd:PRK06178 346 RWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVV----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 427 RPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 506
Cdd:PRK06178 420 RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRP 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 568949898 507 DPIRGEVVKAFIVLNPDyksHDQEQlkKEIQEHVKKTTAPYKYP 550
Cdd:PRK06178 500 DPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP 538
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-522 |
3.36e-50 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 181.88 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKemMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 242 THSSFglglsvngrFW--------LDLIASDVMWNTSDTgWAKSAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFP 313
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 314 ITVFCSAPTAYRMLV-QNDMSSYKFNSLKHCVSAGEPinPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 392
Cdd:PRK06155 269 ATVTYLLGAMVSILLsQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 GKPSPAFDVKILDENGATLPPGQEGDIALQVlpERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSD 472
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568949898 473 DIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 522
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRD 473
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-553 |
1.78e-49 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 178.90 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLAPAVDAVAAKCENLHSKLIVSqhsregwgnLKEMMKYASDShtCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSFGLGlSVNGRFWLDLIASDV------MWNTSDTGWAksawssVFSPWTQGACVFahyLP-RFESTSILQTLSKFPITV 316
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVII---VPrKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 317 FCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTET-----VLICGNFKGmkiKPG 390
Cdd:PRK06839 242 VMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 391 SMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVAR 470
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLI-----RGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS-----SSVLIEKDVIEHCRLFLAKYKIP 467
|
...
gi 568949898 551 RKV 553
Cdd:PRK06839 468 KEI 470
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
70-553 |
2.88e-48 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 178.22 E-value: 2.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 70 KRLSNPAFWWIDGN-GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPG- 144
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 -TTQLTQkdilyRLQSSKAKCIITDDTLA---------PAVDAVAAKCENLHSK-LIVSQhsregwgNLKEMMK------ 207
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHvLLVDR-------GLAPMARvagrdv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 208 -YAS------DSHT-CVDTKHDEMMAIYFTSGTTGPPKMI-----GHThssFGLGLSVNGRFwlDLIASDVMWNTSDTGW 274
Cdd:PRK10524 212 dYATlraqhlGARVpVEWLESNEPSYILYTSGTTGKPKGVqrdtgGYA---VALATSMDTIF--GGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 275 AKSAWSSVFSPWTQG-ACVFAHYLPRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQND---MSSYKFNSLKHCVSAGEP 349
Cdd:PRK10524 287 VVGHSYIVYAPLLAGmATIMYEGLPTRPDAGIWwRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 350 INpEVMEQWRKKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKILDEN-GATLPPGQEGDIALQV 423
Cdd:PRK10524 367 LD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 -LPerPFGLFTHYVDNpSKTASTLRGSF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIA 498
Cdd:PRK10524 446 pLP--PGCMQTVWGDD-DRFVKTYWSLFgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 499 ESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQ---LKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK10524 523 EVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARV 580
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
57-553 |
5.22e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 176.34 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 57 DVLDQwtNMEKAGKRlsnPAFWWIdgnGEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK05605 36 DLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 137 TGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAP---------------AVD------------------AVAAKCE 183
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNmiaampllqrlalrlpipALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 184 NLHSKL-------IVSQHSREGWGNLkemmkyasDSHTCVdTKHDEMMaIYFTSGTTGPPKMIGHTHSsfglGLSVN--- 253
Cdd:PRK05605 185 ALTGPApgtvpweTLVDAAIGGDGSD--------VSHPRP-TPDDVAL-ILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 254 GRFWLDLIASD----------------VMWNTsdtgwaksawssvFSPWTQGACVFahyLPRFESTSILQTLSKFPITVF 317
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 318 CSAPTAYRMLVQ----NDMSsykFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSM 392
Cdd:PRK05605 315 PGVPPLYEKIAEaaeeRGVD---LSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 GKPSPAFDVKILD-EN-GATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWF 467
Cdd:PRK05605 392 GVPFPDTEVRIVDpEDpDETMPDGEEGELLVrgpQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 468 VARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKkeiqEHVKKTTAPY 547
Cdd:PRK05605 464 VDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGLR----AYCREHLTRY 538
|
....*.
gi 568949898 548 KYPRKV 553
Cdd:PRK05605 539 KVPRRF 544
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-553 |
1.19e-47 |
|
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: 171.76 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEEL----GLLSRKFANILTeacslQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05912 2 YTFAELfeevSRLAEHLAALGV-----RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 iitddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHT-- 242
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 243 -H------SSFGLGLSVNGRfWLDLIAsdvMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFESTSILQTLSKFPIT 315
Cdd:cd05912 101 nHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQNDMSSYKfNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 393
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 394 KPSPAFDVKILDENGatlPPGQEGDIALQ---VLPErpfglfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVAR 470
Cdd:cd05912 246 KPLFPVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDR 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQLKKEIQEHVKKttapYKYP 550
Cdd:cd05912 315 RSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKVP 387
|
...
gi 568949898 551 RKV 553
Cdd:cd05912 388 KKI 390
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-553 |
5.00e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 172.92 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 65 MEKAGKRLSN-PAFWWidgnGEElRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP 143
Cdd:PRK07470 13 LRQAARRFPDrIALVW----GDR-SWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 144 GTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKL-IVSQHSREGWGNLkeMMKYASDSHTCVDTKHDE 222
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVaIGGARAGLDYEAL--VARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 223 MMAIYFTSGTTGPPKMIGHTHSSfgLGLSVNGRFwldliaSDVMWNTSDTGWaksawSSVFSPWTQGACVfaHYL----- 297
Cdd:PRK07470 165 PCWFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL------ADLMPGTTEQDA-----SLVVAPLSHGAGI--HQLcqvar 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 298 ---------PRFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY 367
Cdd:PRK07470 230 gaatvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 368 EGYGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPerpfgLFTHYVDNP 439
Cdd:PRK07470 310 QYFGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFAGYYNNP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 519
Cdd:PRK07470 385 EANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCV 464
|
490 500 510
....*....|....*....|....*....|....
gi 568949898 520 LNpDYKSHDQEqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07470 465 AR-DGAPVDEA----ELLAWLDGKVARYKLPKRF 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
84-555 |
4.40e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 170.34 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSfeELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSfglglsVNGRFwLDLIASDVMWNTSDTGWAKS------AWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPIT-V 316
Cdd:PRK07786 197 AN------LTGQA-MTCLRTNGADINSDVGFVGVplfhiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 317 FCsAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTE----TVLICGNFKGMKIkpGS 391
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEmspvTCMLLGEDAIRKL--GS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 392 MGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARS 471
Cdd:PRK07786 347 VGKVIPTVAARVVDENMNDVPVGEVGEIVY-----RAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 472 DDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLKKEIQEHVkkttAPYKYPR 551
Cdd:PRK07786 422 KDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----ARYKHPK 497
|
....
gi 568949898 552 KVGV 555
Cdd:PRK07786 498 ALEI 501
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
297-553 |
1.48e-45 |
|
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: 163.98 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 297 LPRFESTSILQTLSKFPITVFCS-APTAYRMLVQNDMSSYKFNSLKHcVSAGEpiNPEVMEQWRKKTGLDIYEGYGQTET 375
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 ---VLICGNFKgmkiKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYI 452
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 453 TGDRGYMDEDGYFWFVARS--DDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQE 530
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP-----GAT 294
|
250 260
....*....|....*....|...
gi 568949898 531 QLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd17637 295 LTADELIEFVGSRIARYKKPRYV 317
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-553 |
1.54e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 168.63 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 73 SNPAFWWIDGngeelRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIP-GTTQl 148
Cdd:PRK06188 27 DRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 149 tqkDILYRLQSSKAKCIITDDtlAPAVD---AVAAKCENLHSKLIVSQhSREGWGNLKEMMKYASDSHTCVDTkHDEMMA 225
Cdd:PRK06188 100 ---DHAYVLEDAGISTLIVDP--APFVEralALLARVPSLKHVLTLGP-VPDGVDLLAAAAKFGPAPLVAAAL-PPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF----------AH 295
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRS---------------IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFflptllrggtVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 296 YLPRFESTSILQTLSKFPITVFCSAPTA-YRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE 374
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTMiYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 375 -----TVLICGNFKGMKIKP-GSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRG 448
Cdd:PRK06188 318 apmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 449 SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHD 528
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVD 471
|
490 500
....*....|....*....|....*
gi 568949898 529 QEqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK06188 472 AA----ELQAHVKERKGSVHAPKQV 492
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-551 |
7.71e-45 |
|
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: 165.01 E-value: 7.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGeelRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05930 7 VDGDQ---SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 160 SKAKCIITDdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkHDEMMAIYFTSGTTGPPKMI 239
Cdd:cd05930 83 SGAKLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPRFESTS---ILQTLSKF 312
Cdd:cd05930 112 MVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPEEVRKDpeaLADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 313 PITVFCSAPTAYRMLVQnDMSSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICGNF--KGMKIKP 389
Cdd:cd05930 184 GITVLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYrvPPDDEED 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 390 GSM--GKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTAStlrgSF-----------YITGDR 456
Cdd:cd05930 263 GRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI-----GGAGLARGYLNRPELTAE----RFvpnpfgpgermYRTGDL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 457 GYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEI 536
Cdd:cd05930 334 VRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEEL 408
|
490
....*....|....*
gi 568949898 537 QEHVKKTTAPYKYPR 551
Cdd:cd05930 409 RAHLAERLPDYMVPS 423
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
85-553 |
1.10e-44 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 165.52 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLApavdavaakcenlhSKLIVSQHSRegwgnLKEMMKYASDSHTCVDTKH-DEMMAIYFTSGTTGPPKMI---- 239
Cdd:PRK03640 103 LITDDDFE--------------AKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKGViqty 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 -GHTHSSFG----LGLSVNGRfWLdliASDVMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFESTSILQTLSKFPI 314
Cdd:PRK03640 164 gNHWWSAVGsalnLGLTEDDC-WL---AAVPIFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 315 TVFCSAPTAY-RMLVQNDMSSYKfNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 391
Cdd:PRK03640 231 TIISVVSTMLqRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 392 MGKPSPAFDVKILDeNGATLPPGQEGDIALQ---VLPerpfGlfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFV 468
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKgpnVTK----G----YLNREDATRETFQDGWFKTGDIGYLDEEGFLYVL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 469 ARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyKSHDQEQLKKEIQEHVkkttAPYK 548
Cdd:PRK03640 380 DRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRHFCEEKL----AKYK 452
|
....*
gi 568949898 549 YPRKV 553
Cdd:PRK03640 453 VPKRF 457
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-553 |
1.85e-44 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 166.35 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCE--------------------NL---HSKLIVSQHSREGWGNLKEMMKY-ASDSHTCVDTKHDEMMA 225
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvasmgdllgfkghivNFvvrRVKKMVPAWSLPGHVRFNDALAEgARQTFKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSdtgWAKSAWSSvfsPWTQGACVFAHYLP------- 298
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRN---------------IVANVLQMEA---WLQPAFEK---KPRPDQLNFVCALPlyhifal 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 299 --------RFESTSIL-----------QTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQW 358
Cdd:PRK07059 268 tvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 359 RKKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLPerpfglft 433
Cdd:PRK07059 348 LEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIrgpQVMA-------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 434 HYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGE 512
Cdd:PRK07059 419 GYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 568949898 513 VVKAFIVlnpdykSHDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07059 499 AVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
88-522 |
2.57e-44 |
|
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: 163.32 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKipeWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPN---WWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTlapavdavaakcenlhsklivsqhsregWGNlkemMKYASDShtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSAP 321
Cdd:cd05903 117 T----LSASIRQYAERLGlgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 322 T-AYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNfkgmkIKPG-------SMG 393
Cdd:cd05903 191 PfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrlyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 394 KPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDD 473
Cdd:cd05903 266 RPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKD 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 568949898 474 IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 522
Cdd:cd05903 341 IIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS 389
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-559 |
2.70e-44 |
|
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: 164.39 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLApavdavaakcenlHSKLIVSQHSREGWgnlkemmKYASDSHtcvdtkhdEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12118 106 FVDREFE-------------YEDLLAEGDPDFEW-------IPPADEW--------DPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 246 FglglsvngrfWLDLIASDVMWNTSD-------------TGWAksawssvfSPWTQGACVFAHY-LPRFESTSILQTLSK 311
Cdd:cd12118 158 A----------YLNALANILEWEMKQhpvylwtlpmfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 312 FPITVFCSAPTAYRMLVqNDMSSYKfNSLKHCVS---AGEPINPEVMEQwRKKTGLDIYEGYGQTET---VLICG----- 380
Cdd:cd12118 220 HKVTHFCGAPTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwkpew 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 381 -----------------NFKGMK----IKPGSMgKPSPAfdvkildeNGATLppgqeGDIALqvlpeRPFGLFTHYVDNP 439
Cdd:cd12118 297 delpteerarlkarqgvRYVGLEevdvLDPETM-KPVPR--------DGKTI-----GEIVF-----RGNIVMKGYLKNP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 519
Cdd:cd12118 358 EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568949898 520 LNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV---GVPGTS 559
Cdd:cd12118 438 LKEGAKVTEE-----EIIAFCREHLAGFMVPKTVvfgELPKTS 475
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-553 |
3.44e-44 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 165.15 E-value: 3.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 66 EKAGKRLSNPAFwwIDG-NGEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGaTGRVY--TYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 TTQLTQKDILYRLQSSKAKCIITddtLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMM 224
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 225 AIYFTSGTTGPPKMIGHTHSsfGLGLSV---------NgrfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAh 295
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 296 yLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY-EGYGQT 373
Cdd:PLN02246 256 -MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVvEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 E--TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL- 446
Cdd:PLN02246 335 EagPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTId 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdyKS 526
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV-----RS 484
|
490 500
....*....|....*....|....*..
gi 568949898 527 HDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PLN02246 485 NGSEITEDEIKQFVAKQVVFYKRIHKV 511
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
66-550 |
3.55e-44 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 164.86 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 66 EKAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANiLTEACSLQRGDRVMVILPKIPEW---WLAnVACLrtGTVLI 142
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 143 PGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSqhsREGWGNLKEMMKYAS--DSHTCVDTKH 220
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT---RVALPADDGVSSFTQlkAQQPATLCYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 -----DEMMAIYFTSGTTGPPKMIGHTHSsfglglsvNGRF------W-LDLIASDVMWNTSDTGWAKSAWSSVFSPWTQ 288
Cdd:PRK08008 168 pplstDDTAEILFTSGTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 289 GACVFAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNslkHCVSagepinpEVM----------EQW 358
Cdd:PRK08008 240 GATFVL--LEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ---HCLR-------EVMfylnlsdqekDAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 359 RKKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPfgLFTHYVD 437
Cdd:PRK08008 308 EERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 438 NPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 516
Cdd:PRK08008 386 DPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
|
490 500 510
....*....|....*....|....*....|....*
gi 568949898 517 FIVLNPDykshdqEQLKKE-IQEHVKKTTAPYKYP 550
Cdd:PRK08008 466 FVVLNEG------ETLSEEeFFAFCEQNMAKFKVP 494
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
85-551 |
1.19e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 164.18 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDD------------TLAPAV---DAVAAKCENL-HSKLIVSQHSRE-----GWGNLKEMMKYASDSHTCVDT---KH 220
Cdd:PRK12583 121 VICADafktsdyhamlqELLPGLaegQPGALACERLpELRGVVSLAPAPppgflAWHELQARGETVSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 DEMMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRF---WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahyL 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV---Y 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 298 PR--FESTSILQTLSKFPITVFCSAPTAY-RMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-DIYEGYGQT 373
Cdd:PRK12583 274 PNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ET---VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSF 450
Cdd:PRK12583 354 ETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT-----RGYSVMKGYWNNPEATAESIDEDG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 451 YI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 529
Cdd:PRK12583 429 WMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE 508
|
490 500
....*....|....*....|..
gi 568949898 530 eqlkkEIQEHVKKTTAPYKYPR 551
Cdd:PRK12583 509 -----ELREFCKARIAHFKVPR 525
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-502 |
1.45e-43 |
|
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: 160.51 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 162
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 163 KCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSRegwgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHT 242
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 243 HSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF----AHYLPRFESTSILqtLSKFPITVFC 318
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVvppeDEERDDAALLAAL--IAEHPVTVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 319 SAPTAYRMLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKKTG-LDIYEGYGQTETVLICGnfkgMKIKPGSM----- 392
Cdd:TIGR01733 218 LTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDapres 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 ----GKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTA---------STLRGSFYITGDRGYM 459
Cdd:TIGR01733 292 pvpiGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRY 366
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568949898 460 DEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 502
Cdd:TIGR01733 367 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
85-540 |
6.32e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 163.20 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELglLSR--KFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVlIPGTTQLTQKDILYRLQSSKA 162
Cdd:PRK07529 55 RPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 163 KCIIT-----DDTLAPAVDAVAAKCENLhsKLIVSQHSREGWGNLK--------------------EMMKYASDSHTCVD 217
Cdd:PRK07529 131 KVLVTlgpfpGTDIWQKVAEVLAALPEL--RTVVEVDLARYLPGPKrlavplirrkaharildfdaELARQPGDRLFSGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 218 TKHDEMMAIYF-TSGTTGPPKMIGHTHSsfglGLSVNGrfWLdlIASDVMWNTSDTGWA-------KSAWSSVFSPWTQG 289
Cdd:PRK07529 209 PIGPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WL--GALLLGLGPGDTVFCglplfhvNALLVTGLAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 290 A-CVFA--------HYLPRFesTSILQtlsKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRK 360
Cdd:PRK07529 281 AhVVLAtpqgyrgpGVIANF--WKIVE---RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 361 KTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKI--LDENGATL---PPGQEGDIALQvlpeRPfGLFTH 434
Cdd:PRK07529 356 ATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIA----GP-NVFSG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 435 YVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 514
Cdd:PRK07529 431 YLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELP 510
|
490 500
....*....|....*....|....*.
gi 568949898 515 KAFIVLNPDyKSHDQEQLKKEIQEHV 540
Cdd:PRK07529 511 VAYVQLKPG-ASATEAELLAFARDHI 535
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-553 |
1.57e-42 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 160.99 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCENLHSKL--IVSQHSReGWGNL--------KEMM-KY---ASDSHTCV------------DTKHDEM 223
Cdd:PRK08974 130 NFAHTLEKVVFKTPVKHVILtrMGDQLST-AKGTLvnfvvkyiKRLVpKYhlpDAISFRSAlhkgrrmqyvkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 224 MAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWntsdtgwAKSAWSSVFSPwtqGACVFAHYLPRFE-- 301
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN---------------MLANLEQ-------AKAAYGPLLHP---GKELVVTALPLYHif 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 302 -------------STSILQT-----------LSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVME 356
Cdd:PRK08974 264 altvncllfielgGQNLLITnprdipgfvkeLKKYPFTAITGVNTLFNALLNNeEFQELDFSSLKLSVGGGMAVQQAVAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 357 QWRKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDiaLQVL-PERPFGlfth 434
Cdd:PRK08974 344 RWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGE--LWVKgPQVMLG---- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 435 YVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 514
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510
....*....|....*....|....*....|....*....
gi 568949898 515 KAFIVLNpdykshDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK08974 498 KIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLV 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
75-553 |
9.38e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 157.93 E-value: 9.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 75 PAFWwIDGNGEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIL 154
Cdd:PRK13391 14 PAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 155 YRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQH-SREGWGNLKEMMKYASDSHTCVDTKHDEMMaiyFTSGTT 233
Cdd:PRK13391 90 YIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLDGDgELEGFVGYAEAVAGLPATPIADESLGTDML---YSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 234 GPPKMIGHTHSSFGLGLSVNgrfWLDLIASdvMWN-TSDTGW---------AKSAWSSVfspwTQ--GACVFAhyLPRFE 301
Cdd:PRK13391 167 GRPKGIKRPLPEQPPDTPLP---LTAFLQR--LWGfRSDMVYlspaplyhsAPQRAVML----VIrlGGTVIV--MEHFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 302 STSILQTLSKFPITVFCSAPTAY-RMLV--QNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLI 378
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 379 CG-NFKGMKIKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALQvlPERPFglftHYVDNPSKTASTL--RGSFYITGD 455
Cdd:PRK13391 316 TAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 456 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKE 535
Cdd:PRK13391 389 IGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGP--ALAAE 466
|
490
....*....|....*...
gi 568949898 536 IQEHVKKTTAPYKYPRKV 553
Cdd:PRK13391 467 LIAFCRQRLSRQKCPRSI 484
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
84-553 |
1.13e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 154.78 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK13390 22 GEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITddtlAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvdtKHDEMMAIYFTSGTTGPPKMI---- 239
Cdd:PRK13390 99 VLVA----SAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT----EQPCGAVMLYSSGTTGFPKGIqpdl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 -GHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKS-AWSSVFSPwTQGACVFAHylpRFESTSILQTLSKFPITVF 317
Cdd:PRK13390 171 pGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 318 CSAPTAY-RMLVQND--MSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE----TVLICGNFKGmkiKPG 390
Cdd:PRK13390 247 QMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 391 SMGKpSPAFDVKILDENGATLPPGQEGDIALQ--VLPERpfglfthYVDNPSKTASTLRGS--FYIT-GDRGYMDEDGYF 465
Cdd:PRK13390 324 SVGR-SVLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 466 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTA 545
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELARELIDYTRSRIA 473
|
....*...
gi 568949898 546 PYKYPRKV 553
Cdd:PRK13390 474 HYKAPRSV 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
90-553 |
1.45e-40 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 155.42 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCE---------------------NL---HSKLIVSQHSREGWGNLKEMMKYASdSHTC--VDTKHDEM 223
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 224 MAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRfWLD-----------LIASDVMWNTsdtgWAKSAWSSVFSPWtqGACV 292
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAgtgkleegcevVITALPLYHI----FALTANGLVFMKI--GGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 293 FAHYLPRfESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG 371
Cdd:PRK08751 284 HLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 372 QTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLperpfglfTHYVDNPSKTASTLR 447
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIkgpQVM--------KGYWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 448 GSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdykS 526
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------K 508
|
490 500
....*....|....*....|....*..
gi 568949898 527 HDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK08751 509 KDPALTAEDVKAHARANLTGYKQPRII 535
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
88-550 |
5.49e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 153.36 E-value: 5.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 D-------------------DTLAP--AVDAVAAKcenlHSKLIVSQhsregwgnlkEMMKYASDSHTCvDTKHDEMMAI 226
Cdd:PRK06087 128 PtlfkqtrpvdlilplqnqlPQLQQivGVDKLAPA----TSSLSLSQ----------IIADYEPLTTAI-TTHGDELAAV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFESTSI 305
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDAC 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 306 LQTLSKFPITVFCSA-PTAYRMLVQNDMSSYKFNSLKHCVSAGEPInPEVMEQWRKKTGLDIYEGYGQTETV--LICGNF 382
Cdd:PRK06087 269 LALLEQQRCTCMLGAtPFIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNLD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 383 KGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAlqvlpERPFGLFTHYVDNPSKTASTL--RGSFYiTGDRGYMD 460
Cdd:PRK06087 348 DPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRMD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 461 EDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEqlkkEIQEHV 540
Cdd:PRK06087 422 EAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLE----EVVAFF 497
|
490
....*....|.
gi 568949898 541 -KKTTAPYKYP 550
Cdd:PRK06087 498 sRKRVAKYKYP 508
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
82-558 |
1.66e-39 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 153.51 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 82 GNGEE--LRWSFEELGL-LSRKFANILTEACSL---------QRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLT 149
Cdd:PLN02654 101 GNGDKiaIYWEGNEPGFdASLTYSELLDRVCQLanylkdvgvKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 150 QKDILYRLQSSKAKCIITDDT---------LAPAVDAVAAKCENLHSKLIV-------SQHSREG--WGNLKEMM----- 206
Cdd:PLN02654 181 AESLAQRIVDCKPKVVITCNAvkrgpktinLKDIVDAALDESAKNGVSVGIcltyenqLAMKREDtkWQEGRDVWwqdvv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 207 -KYASDSHTCVDTKHDEMMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSP 285
Cdd:PLN02654 261 pNYPTKCEVEWVDAEDPLFLLY-TSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 286 WTQGACVFA-HYLPRF-ESTSILQTLSKFPITVFCSAPTAYRMLVQND---MSSYKFNSLKHCVSAGEPINPEVmeqWR- 359
Cdd:PLN02654 340 MLNGATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRw 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 360 -----KKTGLDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKILDENGATLppgqEGDIA--LQVLPE 426
Cdd:PLN02654 417 ffnvvGDSRCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGKEI----EGECSgyLCVKKS 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 427 RPFGLFTHYVDNPSKTASTLR--GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVS 504
Cdd:PLN02654 489 WPGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVG 568
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 505 SPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV----GVPGT 558
Cdd:PLN02654 569 IEHEVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIhwapGLPKT 624
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-553 |
1.93e-39 |
|
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: 147.81 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 DEMMAIYFTSGTTGPPKMIGHTHSSFglglsVNGRFwldlIASDVMWNTSDT------------GWAKSAWSSVfspwTQ 288
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI-----VNNGY----FIGERLGLTEQDrlcipvplfhcfGSVLGVLACL----TH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 289 GA-CVFAHylPRFESTSILQTLSKFPITVFCSAPTAY-RMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-D 365
Cdd:cd05917 69 GAtMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 366 IYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNP 439
Cdd:cd05917 147 VTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCI-----RGYSVMKGYWNDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 518
Cdd:cd05917 220 EKTAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299
|
330 340 350
....*....|....*....|....*....|....*
gi 568949898 519 VLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05917 300 RLKEGAELTEE-----DIKAYCKGKIAHYKVPRYV 329
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
84-555 |
2.00e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 150.81 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK06145 25 DQEI--SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLapavDAVAAKcenLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvdTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06145 102 LLLVDEEF----DAIVAL---ETPKIVIDAAAQADSRRLAQGGLEIPPQAA---VAPTDLVRLMYTSGTTDRPKGVMHSY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSF---------GLGLSVNGRFW----------LDLIASDVMWntsdtgwaksawssvfspwtQGACVFAHYlpRFESTS 304
Cdd:PRK06145 172 GNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------VGGTLRIHR--EFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 305 ILQTLSKFPITVFCSAPTAY-RMLVQNDMSSYKFNSLKHCVSAGEPiNPE--VMEQWRKKTGLDIYEGYGQTETvliCGN 381
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 382 FKGMKI-----KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGSFYITGDR 456
Cdd:PRK06145 306 DTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG----YWKDPEKTAEAFYGDWFRSGDV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 457 GYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEI 536
Cdd:PRK06145 381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP-----GATLTLEAL 455
|
490
....*....|....*....
gi 568949898 537 QEHVKKTTAPYKYPRKVGV 555
Cdd:PRK06145 456 DRHCRQRLASFKVPRQLKV 474
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
81-555 |
2.41e-39 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 151.74 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 81 DGNGEELRWSFEELGLLSRKFANILTEaCSLQRGDrvmVILPKIPEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 158 QSSKAKCIItddtlAPAV----DAvAAKCENLHSKLIVSQH----SREGWGNLKEMM-----KYASDSHTCVDTKH---D 221
Cdd:PRK13295 124 KHAESKVLV-----VPKTfrgfDH-AAMARRLRPELPALRHvvvvGGDGADSFEALLitpawEQEPDAPAILARLRpgpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 222 EMMAIYFTSGTTGPPKMIGHTHSS-FGLGLSVNGRfwLDLIASDVMWNTS----DTGWAKSAwssvFSPWTQGACVFahY 296
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 297 LPRFESTSILQTLSKFPITvFCSAPTAYRM-LVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE 374
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVT-FTMASTPFLTdLTRAvKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 375 TVLICGnfkgmkIKPG--------SMGKPSPAFDVKILDENGATLPPGQEGdiALQVlpeRPFGLFTHYVDNPSKTASTL 446
Cdd:PRK13295 349 NGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIG--RLQV---RGCSNFGGYLKRPQLNGTDA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGSFYiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKS 526
Cdd:PRK13295 418 DGWFD-TGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QS 495
|
490 500
....*....|....*....|....*....
gi 568949898 527 HDQEQLKKEIQEHvkKTTAPYkYPRKVGV 555
Cdd:PRK13295 496 LDFEEMVEFLKAQ--KVAKQY-IPERLVV 521
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
75-552 |
3.88e-39 |
|
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: 149.32 E-value: 3.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 75 PAFWWidgngEELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIL 154
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 155 YRLQSSKAKCIITDDtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTG 234
Cdd:cd05945 82 EILDAAKPALLIADG---------------------------------------------------DDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 235 PPKMIGHTHS---SFGLGLsvNGRFwlDLIASDVMWNTSDtgwaksaWS---SVFS---PWTQGACVFAhyLPRFESTSI 305
Cdd:cd05945 111 RPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 306 LQ---TLSKFPITVFCSAPTAYRMLvqndMSSYKFN-----SLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETV 376
Cdd:cd05945 178 KQlfrFLAEHGITVWVSTPSFAAMC----LLSPTFTpeslpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEAT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 377 LICgnfKGMKIKPGSM--------GKPSPAFDVKILDENGATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTAST 445
Cdd:cd05945 254 VAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVIsgpSV--------SKGYLNNPEKTAAA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 446 LRGSF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:cd05945 323 FFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK 402
|
490 500 510
....*....|....*....|....*....|.
gi 568949898 522 PdyksHDQEQLKKEIQEHVKKTTAPYKYPRK 552
Cdd:cd05945 403 P----GAEAGLTKAIKAELAERLPPYMIPRR 429
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-553 |
9.88e-39 |
|
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: 148.36 E-value: 9.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENlh 186
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 187 SKLIVSQhsrEGWgnlkemmKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRfwLDLIASDV 265
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 266 MWNTSDTGWAkSAWSSVFSPWTQGACVFAHYLPRFESTsILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVS 345
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 346 AGEPINPEVMEQWRKK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFDVKILDENGATLPPGQE 416
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 417 GDIAlqvlPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 496
Cdd:cd05922 313 GEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568949898 497 IAESAVVSSPDPIrGEVVKAFIVLNPDYKSHDqeqlkkeIQEHVKKTTAPYKYPRKV 553
Cdd:cd05922 389 IIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATV 437
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
226-555 |
1.04e-38 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 149.52 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKmiGHTHSSFGlGLSVngrfwldliASDVMwntSDTGWAKSAWSSVFSP----WTQGACVFAHYLP--- 298
Cdd:PRK13382 201 ILLTSGTTGTPK--GARRSGPG-GIGT---------LKAIL---DRTPWRAEEPTVIVAPmfhaWGFSQLVLAASLActi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 299 ----RFESTSILQTLSKFPITVFCSAPTAYRM---LVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG 371
Cdd:PRK13382 266 vtrrRFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 372 QTETVLIC-GNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVdnPSKTASTLRGsF 450
Cdd:PRK13382 346 ATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-F 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 451 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQE 530
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE 496
|
330 340
....*....|....*....|....*
gi 568949898 531 QLKkeiqEHVKKTTAPYKYPRKVGV 555
Cdd:PRK13382 497 TLK----QHVRDNLANYKVPRDIVV 517
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-559 |
1.21e-38 |
|
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: 148.93 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 81 DGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILpkipeW--------WLAnVAClrTGTVLIPGTTQLTQKD 152
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA-----WnthrhlelYYA-VPG--MGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 153 ILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSR------EGWGNLKEMMKYASDSHTCVDTKHDEMMAI 226
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRFWLDLIASDV------MWNTSdtgwaksAWSSVFSPWTQGACvfaHYLP- 298
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAK---LVLPg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 299 -RFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTET- 375
Cdd:cd12119 239 pYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 -VLICGnfkgmKIKPG--------------SMGKPSPAFDVKILDENGATLP--PGQEGDiaLQVlpeR-PFgLFTHYVD 437
Cdd:cd12119 318 pLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGE--LQV---RgPW-VTKSYYK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 438 NPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAF 517
Cdd:cd12119 387 NDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAV 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568949898 518 IVLNPdykshDQEQLKKEIQEHVKKTTAPYKYPRKV----GVPGTS 559
Cdd:cd12119 467 VVLKE-----GATVTAEELLEFLADKVAKWWLPDDVvfvdEIPKTS 507
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-542 |
1.89e-38 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 149.87 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 74 NPAFWWIDgNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDI 153
Cdd:COG1022 27 RVALREKE-DGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 154 LYRLQSSKAKCIIT-DDTLAPAVDAVAAKCENLhsKLIVSQHSREGWG-----NLKEMMKYASDSHT-------CVDTKH 220
Cdd:COG1022 105 AYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelearRAAVKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 DEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWaksawsSVFSpWTQGACVfa 294
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAAGATV-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 295 HYLPRFEStsILQTLSKFPITVFCSAP--------------------------------TAYRMLVQNDMSSYKFNSLKH 342
Cdd:COG1022 253 AFAESPDT--LAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalavgRRYARARLAGKSPSLLLRLKH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 343 ---------------------CVSAGEPINPEVMEQWRKkTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMGKPSPAFD 400
Cdd:COG1022 331 aladklvfsklrealggrlrfAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLPGVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 401 VKIlDENGatlppgqEgdiaLQVlpeR-PfGLFTHYVDNPSKTASTLR--GSFYiTGDRGYMDEDGYFWFVARSDDII-L 476
Cdd:COG1022 409 VKI-AEDG-------E----ILV---RgP-NVMKGYYKNPEATAEAFDadGWLH-TGDIGELDEDGFLRITGRKKDLIvT 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 477 SSGYRIGPFEVESALIEHPSIAESAVVsspdpirGE----VVkAFIVLNPD------------YKSHDQ----EQLKKEI 536
Cdd:COG1022 472 SGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEalgewaeenglpYTSYAElaqdPEVRALI 543
|
....*.
gi 568949898 537 QEHVKK 542
Cdd:COG1022 544 QEEVDR 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-551 |
1.96e-38 |
|
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: 148.83 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLAPAVDAVAAKceNLHSKLIVSQHSREGWGNLKEMMKYASD---------SHTCVDTKHDEMMA-IYFTSGTTGP 235
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTFITQnlppgfneyDFKPPSFDRDEQVAlIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 236 PKMIGHTHSSFGLGLSVngrfwldliASDVMWntsdtGWAKSAWSSVFS--PWTQG---------ACVFAH--YLPRFES 302
Cdd:cd17642 199 PKGVQLTHKNIVARFSH---------ARDPIF-----GNQIIPDTAILTviPFHHGfgmfttlgyLICGFRvvLMYKFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 303 TSILQTLSKFPITVFCSAPTAYRMLVQNDM-SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTET---VL 377
Cdd:cd17642 265 ELFLRSLQDYKVQSALLVPTLFAFFAKSTLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 378 ICGNfkgMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKT-ASTLRGSFYITGD 455
Cdd:cd17642 345 ITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCV-----KGPMIMKGYVNNPEATkALIDKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 456 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdykSHDQEQLKKE 535
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKE 491
|
490
....*....|....*.
gi 568949898 536 IQEHVKKTTAPYKYPR 551
Cdd:cd17642 492 VMDYVASQVSTAKRLR 507
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-553 |
2.04e-38 |
|
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: 147.52 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 225 AIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIasdvmwntsdtGWakSAWSSVFSPWT------QGACVFAHYL- 297
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLP-GGPPDNDTLMAAALGF-----------GP--GADSVYLSPAPlyhaapFRWSMTALFMg 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 298 ------PRFESTSILQTLSKFPITVFCSAPTAY-RM--LVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYE 368
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 369 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALqvlpeRPFGLFThYVDNPSKTA-STL 446
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYF-----ANGPGFE-YTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAfiVLNPDYKS 526
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340
....*....|....*....|....*..
gi 568949898 527 HDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSI 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-545 |
3.32e-38 |
|
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: 144.55 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 220 HDEMMAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRFWLDliasDVMWNTSDTGWAKSAWSSVFSPWTQGACVF--- 293
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEvynAWMLALNSLFDPD----DVLLCGLPLFHVNGSVVTLLTPLASGAHVVlag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 -AHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ----NDMSSykfnsLKHCVSAGEPINPEVMEQWRKKTGLDIYE 368
Cdd:cd05944 77 pAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQvpvnADISS-----LRFAMSGAAPLPVELRARFEDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 369 GYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLP-----PGQEGDIALQvlpeRPfGLFTHYVDNPSKT 442
Cdd:cd05944 152 GYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLlrdcaPDEVGEICVA----GP-GVFGGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 443 ASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 522
Cdd:cd05944 227 NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340
....*....|....*....|...
gi 568949898 523 DYKShDQEQLKKEIQEHVKKTTA 545
Cdd:cd05944 307 GAVV-EEEELLAWARDHVPERAA 328
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-553 |
7.36e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 145.90 E-value: 7.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKmighthssfGLGLSVNGrfwldlIASDVmwntsdTGWAKsAWSsvfspWTqGACVFAHYLP------- 298
Cdd:PRK07787 133 IVYTSGTTGPPK---------GVVLSRRA------IAADL------DALAE-AWQ-----WT-ADDVLVHGLPlfhvhgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 299 ------------------RFESTSILQTLSkFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRK 360
Cdd:PRK07787 185 vlgvlgplrignrfvhtgRPTPEAYAQALS-EGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 361 KTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlpeRPFGLFTHYVDNPS 440
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 441 KTASTLRG-SFYITGDRGYMDEDGYFWFVAR-SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 518
Cdd:PRK07787 341 ATAAAFTAdGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV 420
|
330 340 350
....*....|....*....|....*....|....*
gi 568949898 519 VLNPDYKShdqeqlkKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07787 421 VGADDVAA-------DELIDFVAQQLSVHKRPREV 448
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
80-553 |
8.89e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 147.00 E-value: 8.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGEelrWSFEELGLLSRKFANILTEAcSLQRGDRVMViLPKIPEWW-LANVACLRTGTVLI-----PGTTQLtqKDI 153
Cdd:PRK07788 69 IDERGT---LTYAELDEQSNALARGLLAL-GVRAGDGVAV-LARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 154 LYRLqssKAKCIITDDTLAPAVDAVAAKCENLHSkLIVS----QHSREGWGNLKEMMKYASDSHTCVDTKHDEMmaIYFT 229
Cdd:PRK07788 142 AARE---GVKALVYDDEFTDLLSALPPDLGRLRA-WGGNpdddEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 230 SGTTGPPKMIGHTHSSfglGLSVNGRFwLDLI---ASDVMWNTS----DTGWAKSAWSsvfspWTQGACVFAHYlpRFES 302
Cdd:PRK07788 216 SGTTGTPKGAPRPEPS---PLAPLAGL-LSRVpfrAGETTLLPApmfhATGWAHLTLA-----MALGSTVVLRR--RFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 303 TSILQTLSKFPITVFCSAPTAY-RML--VQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE----T 375
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLsRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VlicGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKtaSTLRGsFYITGD 455
Cdd:PRK07788 365 I---ATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 456 RGYMDEDGYfWFVA-RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQL-K 533
Cdd:PRK07788 434 VGYFDEDGL-LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG------AALdE 506
|
490 500
....*....|....*....|
gi 568949898 534 KEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPRDV 526
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-553 |
1.61e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 146.45 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 53 NFAKDV----------LDQWTNM----EKAGKRLSN-PAFWWIdgnGEELRWSfeELGLLSRKFANILTEACSLQRGDRV 117
Cdd:PRK05677 4 NFWKDKypagiaaeinPDEYPNIqavlKQSCQRFADkPAFSNL---GKTLTYG--ELYKLSGAFAAWLQQHTDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 118 MVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCE----------NLHS 187
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGvkhvivtevaDMLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 188 ---------------KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsfglglsv 252
Cdd:PRK05677 159 plkrllinavvkhvkKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 253 ngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSP--------WTQGaCVF-----AHYL----PRfESTSILQTLSKFPIT 315
Cdd:PRK05677 231 ------NLVANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFH-CMAmmligNHNIlisnPR-DLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMG 393
Cdd:PRK05677 303 GFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 394 KPSPAFDVKILDENGATLPPGQEGDIAL---QVLperpfglfTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVA 469
Cdd:PRK05677 382 IPVPSTLCKVIDDDGNELPLGEVGELCVkgpQVM--------KGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 470 RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQLKKE-IQEHVKKTTAPYK 548
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYK 527
|
....*
gi 568949898 549 YPRKV 553
Cdd:PRK05677 528 VPKAV 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
111-553 |
3.04e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 144.84 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT-DDTLAPAVDAVAAKCENLH--- 186
Cdd:PRK12406 33 VRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLLHGLASALPAGVTVLSvpt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 187 -----SKLIVSQHSR---------EGWgnLKEMMKYASDshtcvdTKHDEMMAIYfTSGTTGPPK--------------- 237
Cdd:PRK12406 113 ppeiaAAYRISPALLtppagaidwEGW--LAQQEPYDGP------PVPQPQSMIY-TSGTTGHPKgvrraaptpeqaaaa 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 238 --MIGHTHssfglGLSVNGRfwldLIASDVMWNTSDTGWAKSAWSsvfspwtqgacvFAHYL---PRFESTSILQTLSKF 312
Cdd:PRK12406 184 eqMRALIY-----GLKPGIR----ALLTGPLYHSAPNAYGLRAGR------------LGGVLvlqPRFDPEELLQLIERH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 313 PITVFCSAPTAY-RMLVQND--MSSYKFNSLKHCVSAGEPINPEV----MEQWrkktGLDIYEGYGQTET--VLICGNFK 383
Cdd:PRK12406 243 RITHMHMVPTMFiRLLKLPEevRAKYDVSSLRHVIHAAAPCPADVkramIEWW----GPVIYEYYGSTESgaVTFATSED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 384 GMKiKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPfgLFThYVDNPSKTASTLRGSFYITGDRGYMDEDG 463
Cdd:PRK12406 319 ALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI-AGNP--DFT-YHNKPEKRAEIDRGGFITSGDVGYLDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 464 YFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlkkEIQEHVKKT 543
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEA----DIRAQLKAR 468
|
490
....*....|
gi 568949898 544 TAPYKYPRKV 553
Cdd:PRK12406 469 LAGYKVPKHI 478
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
89-542 |
7.91e-37 |
|
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: 142.73 E-value: 7.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 DTlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgl 248
Cdd:cd05907 85 DP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 249 gLSVngrfwldLIASDVMWNTSDTGW-----------AKSAWSSVfsPWTQGACVFahYLPRFEStsILQTLSKFPITVF 317
Cdd:cd05907 113 -LSN-------ALALAERLPATEGDRhlsflplahvfERRAGLYV--PLLAGARIY--FASSAET--LLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 318 CSAPTAYRML----VQNDMSSYK--------FNSLKHCVSAGEPINPEVMEQWRKkTGLDIYEGYGQTETV-LICGNFKG 384
Cdd:cd05907 179 LAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 385 mKIKPGSMGKPSPAFDVKIldengatlppGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL--RGSFYiTGDRGYMDED 462
Cdd:cd05907 258 -DNRIGTVGKPLPGVEVRI----------ADDGEILV-----RGPNVMLGYYKNPEATAEALdaDGWLH-TGDLGEIDED 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 463 GYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPirgeVVKAFIVLNPDY-----KSHD-------- 528
Cdd:cd05907 321 GFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaEEHGiaytdvae 396
|
490
....*....|....*..
gi 568949898 529 ---QEQLKKEIQEHVKK 542
Cdd:cd05907 397 laaNPAVRAEIEAAVEA 413
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
98-553 |
5.26e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 142.04 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 98 SRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDA 177
Cdd:PLN02330 65 TRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 178 VAAKCenlhskLIVSQHSREG---WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH---------SS 245
Cdd:PLN02330 144 LGLPV------IVLGEEKIEGavnWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHrnlvanlcsSL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 246 FGLGLSVNGRF-WLDLIASDVMWNTSDTGWAKSAwssvfspwTQGACVFahyLPRFESTSILQTLSKFPITVFCSAPTAY 324
Cdd:PLN02330 218 FSVGPEMIGQVvTLGLIPFFHIYGITGICCATLR--------NKGKVVV---MSRFELRTFLNALITQEVSFAPIVPPII 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 325 RMLVQN------DMSSYKfnsLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICGNF----KGMKI-KPGSM 392
Cdd:PLN02330 287 LNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeKGHGIaKKNSV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 GKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVAR 470
Cdd:PLN02330 364 GFILPNLEVKFIDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYP 550
Cdd:PLN02330 439 IKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE-----DILNFVAANVAHYKKV 513
|
...
gi 568949898 551 RKV 553
Cdd:PLN02330 514 RVV 516
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
85-559 |
3.82e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 139.31 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYAS-----DSHTCVDTKHDEMMAIY--FTSGTTGPPK 237
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAflasgDPDFAWTLPADEWDAIAlnYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 238 MIGHTHSSFGLGLSVNGRFWlDLIASDV-MW-------NtsdtGWAksawssvFsPWT----QGACVFahyLPRFESTSI 305
Cdd:PRK08162 199 GVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTvaarAGTNVC---LRKVDPKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 306 LQTLSKFPITVFCSAPTAYRMLVqnDMSSYKFNSLKHCVS---AGEPINPEVMEQwRKKTGLDIYEGYGQTET---VLIC 379
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALI--NAPAEWRAGIDHPVHamvAGAAPPAAVIAK-MEEIGFDLTHVYGLTETygpATVC 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 380 GNFKGMKIKP--------GSMGKPSPAFD-VKILD-ENGATLPPGQE--GDIALqvlpeRPFGLFTHYVDNPSKTASTLR 447
Cdd:PRK08162 340 AWQPEWDALPlderaqlkARQGVRYPLQEgVTVLDpDTMQPVPADGEtiGEIMF-----RGNIVMKGYLKNPKATEEAFA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 448 GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyksh 527
Cdd:PRK08162 415 GGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD----- 489
|
490 500 510
....*....|....*....|....*....|....*
gi 568949898 528 DQEQLKKEIQEHVKKTTAPYKYPRKV---GVPGTS 559
Cdd:PRK08162 490 GASATEEEIIAHCREHLAGFKVPKAVvfgELPKTS 524
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-534 |
5.17e-34 |
|
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: 135.15 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 215 CVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 AHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQNdMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQT 373
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGAT-LPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFY 451
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLV-----RGPNVMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 452 ITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PFE-VESALIEH-PSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 525
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDP 446
|
....*....
gi 568949898 526 SHDQEQLKK 534
Cdd:cd05909 447 SSLNDILKN 455
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-564 |
6.85e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.10 E-value: 6.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 66 EKAGKRLSN-PAFwwiDGNGEELrwSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK12492 31 ERSCKKFADrPAF---SNLGVTL--SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 TTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLH---SKLIVSQHSREGW------GNLKEMMKY------- 208
Cdd:PRK12492 106 NPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 209 ---------ASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsfglglsvngrfwlDLIAS--DVMWNTSDTGwaks 277
Cdd:PRK12492 186 pfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG--------------NLVANmlQVRACLSQLG---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 278 awSSVFSPWTQGACVFAHYLPRFE---------------STSILQT-----------LSKFPITVFCSAPTAYRMLVQN- 330
Cdd:PRK12492 248 --PDGQPLMKEGQEVMIAPLPLYHiyaftancmcmmvsgNHNVLITnprdipgfikeLGKWRFSALLGLNTLFVALMDHp 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 331 DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGA 409
Cdd:PRK12492 326 GFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 410 TLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 488
Cdd:PRK12492 406 ELPLGERGELCIKG-PQVMKG----YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 489 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLKKeiqeHVKKTTAPYKYPRKVGVPGTSDVSPV 564
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPV 550
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-553 |
5.92e-33 |
|
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: 128.96 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 289 GACVFahyLPRFESTSILQTLSKFPIT-VFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGE--PINPEVMEQWRKKTGld 365
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 366 iyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTAS 444
Cdd:cd17636 142 ---GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 445 TLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDy 524
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG- 291
|
250 260
....*....|....*....|....*....
gi 568949898 525 kSHDQEQlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:cd17636 292 -ASVTEA---ELIEHCRARIASYKKPKSV 316
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
87-553 |
1.24e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 131.47 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 87 LRWSFEEL-GLLSRKFANILTEACSlqRGDRVMViLPKIPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK09088 21 RRWTYAELdALVGRLAAVLRRRGCV--DGERLAV-LARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLApavdavAAKCENLHSKLIVSQhsregwgnlkemmkyaSDSHTCVDTKH---DEMMAIYFTSGTTGPPK--MI 239
Cdd:PRK09088 98 LLGDDAVA------AGRTDVEDLAAFIAS----------------ADALEPADTPSippERVSLILFTSGTSGQPKgvML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 G-----HTHSSFGLGLSVNGR--FWLDLiasdVMWNTsdTGWAksawSSVFSPWTQGACVFAHylPRFESTSILQTLSKF 312
Cdd:PRK09088 156 SernlqQTAHNFGVLGRVDAHssFLCDA----PMFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 313 PITV---FCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPiNPEVMEQWRKKTGLDIYEGYGQTE--TVLicgnfkGMKI 387
Cdd:PRK09088 224 ALGIthyFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSEagTVF------GMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 388 -------KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGS-FYITGDRGYM 459
Cdd:PRK09088 297 dcdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLL-----RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 460 DEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlkkEIQEH 539
Cdd:PRK09088 372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSH 446
|
490
....*....|....
gi 568949898 540 VKKTTAPYKYPRKV 553
Cdd:PRK09088 447 LSTRLAKYKVPKHL 460
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
111-555 |
1.65e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 132.85 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD----DTLAPAVDAVAAKcenlh 186
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 187 sklIVSQHSREGWGNLKEMMKYASDSHTcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVM 266
Cdd:PRK06060 127 ---LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 267 WNTSDTGWAKSAWSSVFSPWTQGACVFAHYLP-RFESTSILQTlsKFPITVFCSAPTAYRMLVqNDMSSYKFNSLKHCVS 345
Cdd:PRK06060 191 LCSARMYFAYGLGNSVWFPLATGGSAVINSAPvTPEAAAILSA--RFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 346 AGEPINPEVMEQWRKK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL 421
Cdd:PRK06060 268 AGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 422 qvlpeRPFGLFTHYVDNPSKTASTlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:PRK06060 345 -----RGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568949898 502 VVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLKKEIQEHVKKTTAPYKYPRKVGV 555
Cdd:PRK06060 418 VVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAV 469
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-553 |
2.22e-32 |
|
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: 127.76 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 225 AIYFTSGTTGPPKMIGHTHSSFGLGLSVngrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYL-----PR 299
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 300 FESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAG--EPINPEV-MEQWRKKTglDIYEGYGQTET- 375
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVrFIEATGLT--NTAQVYGLSETg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGSFYITGD 455
Cdd:cd17635 156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 456 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykSHDQEQLKKE 535
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRA 306
|
330
....*....|....*...
gi 568949898 536 IQEHVKKTTAPYKYPRKV 553
Cdd:cd17635 307 LKHTIRRELEPYARPSTI 324
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
90-550 |
2.70e-31 |
|
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: 127.39 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCENLHSKLIVSQHSREGwgnlkemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPK--MIGHThssfg 247
Cdd:cd17646 104 DLAARLPAGGDVALLGDEALAAPPATPPL-----------------VPPRPDNLAYVIYTSGSTGRPKgvMVTHA----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 lGLsVNGRFWL----DLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFA--------HYLPRFestsilqtLSKFPI 314
Cdd:cd17646 162 -GI-VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVArpgghrdpAYLAAL--------IREHGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 315 TVFCSAPTAYRMLVQnDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 391
Cdd:cd17646 231 TTCHFVPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 392 MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL------RGS-FYITGDRGYMDEDGY 464
Cdd:cd17646 310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALTAERFvpdpfgPGSrMYRTGDLARWRPDGA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 465 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLkkeiQEHVKKTT 544
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERL 460
|
....*.
gi 568949898 545 APYKYP 550
Cdd:cd17646 461 PEYMVP 466
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
216-553 |
4.87e-31 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 128.32 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 216 VDTKHDemMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKsawssvFSPWTQGACVFAH 295
Cdd:PTZ00237 251 VESSHP--LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 296 YLPRFES---------TSILQTLSKFPITVFCSAPTAYRMLVQND------MSSYKFNSLKHCVSAGEPINPEVMEQWRK 360
Cdd:PTZ00237 323 TFVMFEGgiiknkhieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 361 KTGLDIYEGYGQTE---TVLICgnFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvLPERPFGLFTHYV- 436
Cdd:PTZ00237 403 KLKIKSSRGYGQTEigiTYLYC--YGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKn 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 437 DNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 516
Cdd:PTZ00237 480 DEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559
|
330 340 350
....*....|....*....|....*....|....*....
gi 568949898 517 FIVLNPDYKSH--DQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PTZ00237 560 LLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKI 598
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-540 |
8.34e-31 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 125.92 E-value: 8.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLAPAVDAVAAkcenlhsklIVSQHSREGWGNLkemmkyASDSHTcVDTKHDEMMAIYFTSGTTGPPKmighth 243
Cdd:cd17651 95 LVLTHPALAGELAVELV---------AVTLLDQPGAAAG------ADAEPD-PALDADDLAYVIYTSGSTGRPK------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 ssfglGLSVNGRFWLDLIAsdvmWNT----SDTGWAKSAWSS---------VFSPWTQGACVfaHYLP---RFESTSILQ 307
Cdd:cd17651 153 -----GVVMPHRSLANLVA----WQArassLGPGARTLQFAGlgfdvsvqeIFSTLCAGATL--VLPPeevRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 308 TLSKFPITVfCSAPTAYRMLVQNDM--SSYKFNSLKHCVSAGEP--INPEVMEQWRKKTGLDIYEGYGQTE----TVLIC 379
Cdd:cd17651 222 WLDEQRISR-VFLPTVALRALAEHGrpLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 380 GNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL-------RGSFYI 452
Cdd:cd17651 301 PGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAERFvpdpfvpGARMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 453 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQL 532
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAAEL 454
|
....*...
gi 568949898 533 KKEIQEHV 540
Cdd:cd17651 455 RAALATHL 462
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-553 |
1.38e-30 |
|
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: 124.86 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANiLTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05914 82 AIFV--------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSfgLGLSVNGRFWLDLI-ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFeSTSILQTLSKFPITVFCSAPT 322
Cdd:cd05914 112 RN--IVSNVDGVKEVVLLgKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 323 AYRM--------LVQNDMSSYKF------------------------NSLKHCVSAGEPINPEVmEQWRKKTGLDIYEGY 370
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFklakkinnrkirklafkkvheafgGNIKEFVIGGAKINPDV-EEFLRTIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKILDENgatlPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTAS--TLR 447
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV-----RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 448 GSFYiTGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAFIVLNPDY-- 524
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510
....*....|....*....|....*....|....
gi 568949898 525 -----KSHDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd05914 410 vkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKV 443
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-553 |
5.33e-30 |
|
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: 120.68 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPK--MIGHTHSsfgLGLSVNgrfWldliaSDVMWNTSDTGWA-----------KSAWSSVFspwTQGACV 292
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 293 FAHYLprFESTSILQTLSKFPITVFCSAPTAYR-MLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGY 370
Cdd:cd17638 71 VPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKILDEngatlppgqeGDIALqvlpeRPFGLFTHYVDNPSKTASTLRG 448
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLV-----RGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 449 SFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSH 527
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTL 292
|
330 340
....*....|....*....|....*.
gi 568949898 528 DQEQLKKEIQEHVkkttAPYKYPRKV 553
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFV 314
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-553 |
1.27e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 123.38 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 87 LRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCII 166
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 167 TDD------------TLAP------AVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHtcvDTKHDEMMA--- 225
Cdd:PRK08315 121 AADgfkdsdyvamlyELAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 ------IYFTSGTTGPPKmiGHTHSSFGLGLsvNGRF---WLDLIASD--------------VMWNTSDTgwaksawssv 282
Cdd:PRK08315 198 pddpinIQYTSGTTGFPK--GATLTHRNILN--NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNLACV---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 283 fspwTQGAC-VFAhyLPRFESTSILQTLSKFPITVFCSAPTAY-RMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRK 360
Cdd:PRK08315 264 ----THGATmVYP--GEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVID 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 361 KTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFDVKILD-ENGATLPPGQEGDIAlqv 423
Cdd:PRK08315 338 KMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGELC--- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 lpERPFGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 502
Cdd:PRK08315 403 --TRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568949898 503 VSSPDPIRGEVVKAFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYI 526
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-553 |
2.21e-29 |
|
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: 121.67 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGeelRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 160 SKAKCIITDDTLAPaVDAVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkHDEMMAIYFTSGTTGPPKMI 239
Cdd:cd05920 111 AEAVAYIVPDRHAG-FDHRALARELAES--------------------------------IPEVALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTHSSFGLGLSVngrfwldliASDVMWNTSDT----------GWAKSAWSSVFSPWTQGACVFAhylPRFESTSILQTL 309
Cdd:cd05920 158 PRTHNDYAYNVRA---------SAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 310 SKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLicgNFKGM--- 385
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 386 -KIKPGSMGKP-SPAFDVKILDENGATLPPGQEGdialQVLPERPFgLFTHYVDNPSKTAS--TLRGsFYITGDRGYMDE 461
Cdd:cd05920 303 dEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPY-TIRGYYRAPEHNARafTPDG-FYRTGDLVRRTP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 462 DGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyKSHDQEQLKKEIQEhvk 541
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD--PPPSAAQLRRFLRE--- 451
|
490
....*....|..
gi 568949898 542 KTTAPYKYPRKV 553
Cdd:cd05920 452 RGLAAYKLPDRI 463
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
90-553 |
2.79e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 122.26 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLipgttqlTQKDILYRLQSSKAKCIITDD 169
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIV-------TTMNPSSSLGEIKKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCENLHSKLIVSQHS------REGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIGVPENydfdskRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSFGLGLSVNGRFWldliASDVMWNTSDTGWAksAWSSVFSPWtqGACVFAHYL----------PRFESTSILQTLSKFP 313
Cdd:PLN02574 221 RNLIAMVELFVRFE----ASQYEYPGSDNVYL--AALPMFHIY--GLSLFVVGLlslgstivvmRRFDASDMVKVIDRFK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 314 ITVFCSAPTAYRMLVQN--DMSSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICG---NFKGMKi 387
Cdd:PLN02574 293 VTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlPHVDFIQGYGMTESTAVGTrgfNTEKLS- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 388 KPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALQvlpeRPfGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYF 465
Cdd:PLN02574 372 KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 466 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQlkkeIQEHVKKTTA 545
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG-STLSQEA----VINYVAKQVA 521
|
....*...
gi 568949898 546 PYKYPRKV 553
Cdd:PLN02574 522 PYKKVRKV 529
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
111-529 |
3.35e-29 |
|
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: 121.08 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKAKCIITDDTLAPAVDAVAAKcenlhskli 190
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMA--------IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIA 262
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKGAVIPQRA---------------AE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 263 SDVMWNTSDTGWAKSAWSSVFS--PWTQGACVFA-----------HYLPR-FESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05923 177 SRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAvlvaalaldgtYVVVEeFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 329 QN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPSPAFDVKILDE 406
Cdd:cd05923 257 AAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRPGFFSEVRIVRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 407 NGAT---LPPGQEGDIALQVLPERPFglfTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 483
Cdd:cd05923 333 GGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIH 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568949898 484 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 529
Cdd:cd05923 410 PSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
84-550 |
3.44e-29 |
|
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: 121.79 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGtvLIPGTT--QLTQKDILYRLQSSK 161
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFAlpAHRRAEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 162 AKCIITDDT-----LAPAVDAVAAKCENLHSKLIVsqHSREGWGNLKEMmkYASDSHTCVDTKHDEMMAIYFTS-GTTGP 235
Cdd:COG1021 123 AVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDAL--LAAPADLSEPRPDPDDVAFFQLSgGTTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 236 PKMIGHTH---------SSFGLGLSVNGRFwldLIASDVMWNtsdtgwakSAWSS--VFSPWTQGAC-VFAhylPRFEST 303
Cdd:COG1021 199 PKLIPRTHddylysvraSAEICGLDADTVY---LAALPAAHN--------FPLSSpgVLGVLYAGGTvVLA---PDPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 304 SILQTLSKFPITVFCSAPTAYRMLVQ-NDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG-------QT-- 373
Cdd:COG1021 265 TAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvnYTrl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ----ETVLicgnfkgmkikpGSMGKP-SPAFDVKILDENGATLPPGQEGdiALQVlpeRPFGLFTHYVDNPSKTAS--TL 446
Cdd:COG1021 345 ddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVG--ELLT---RGPYTIRGYYRAPEHNARafTP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGsFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdyks 526
Cdd:COG1021 408 DG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP------ 480
|
490 500
....*....|....*....|....*.
gi 568949898 527 hDQEQLK-KEIQEHVK-KTTAPYKYP 550
Cdd:COG1021 481 -RGEPLTlAELRRFLReRGLAAFKLP 505
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
99-553 |
5.02e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.49 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 99 RKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---TLAP-A 174
Cdd:PLN02479 56 RRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQeffTLAEeA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 175 VDAVAAKCENLHSK--LIVSQHSREGWGNLK--------EMMKYASDSHTCVDTK--HDEM--MAIYFTSGTTGPPK-MI 239
Cdd:PLN02479 135 LKILAEKKKSSFKPplLIVIGDPTCDPKSLQyalgkgaiEYEKFLETGDPEFAWKppADEWqsIALGYTSGTTASPKgVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTHSSFGLGLSvNGRFWLDLIASDVMWNTSD---TGWAksawssvfSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PLN02479 215 LHHRGAYLMALS-NALIWGMNEGAVYLWTLPMfhcNGWC--------FTWTLAAlCGTNICLRQVTAKAIYSAIANYGVT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVqNDMSSYKFNSLKHCV---SAGEPINPEVMEQWRKKtGLDIYEGYGQTETV---LICG--------- 380
Cdd:PLN02479 286 HFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETYgpsTVCAwkpewdslp 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 381 -------------NFKGMK----IKPGSMgKPSPAfdvkildeNGATLppgqeGDIALqvlpeRPFGLFTHYVDNPSKTA 443
Cdd:PLN02479 364 peeqarlnarqgvRYIGLEgldvVDTKTM-KPVPA--------DGKTM-----GEIVM-----RGNMVMKGYLKNPKANE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 444 STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 523
Cdd:PLN02479 425 EAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPG 504
|
490 500 510
....*....|....*....|....*....|
gi 568949898 524 YKSHDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PLN02479 505 VDKSDEAALAEDIMKFCRERLPAYWVPKSV 534
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
88-550 |
7.47e-29 |
|
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: 120.00 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd12117 22 SLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DDTLAPAVDAVAAKcenlhskLIVSQHSREGwgnlkemmkYASDSHTCVDTkhDEMMAIYFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd12117 101 DRSLAGRAGGLEVA-------VVIDEALDAG---------PAGNPAVPVSP--DDLAYVMYTSGSTGRPKGVAVTHRGV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLsVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FESTSILQTLSKFPITV-FCSAPTa 323
Cdd:cd12117 162 VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARL--VLAPKgtlLDPDALGALIAEEGVTVlWLTAAL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 324 YRMLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKPSPA 398
Cdd:cd12117 237 FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 399 FDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTA------STLRGS-FYITGDRGYMDEDGYFWFVARS 471
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGE--LYVGGD---GLALGYLNRPALTAerfvadPFGPGErLYRTGDLARWLPDGRLEFLGRI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 472 DDIILSSGYRIGPFEVESALIEHPSIAESAV-VSSPDPIRGEVVkAFIVLNPDyKSHDqeqlkkEIQEHVKKTTAPYKYP 550
Cdd:cd12117 390 DDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAYMVP 461
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
74-523 |
2.28e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.02 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 74 NPAFWWidgngEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIpGTTQLTQKDI 153
Cdd:PRK07867 19 DRGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV-GLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 154 LYR-LQSSKAKCIITDDTLAPAVDAVAAKCEnlhsklIVSQHSREgWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGT 232
Cdd:PRK07867 93 LARdIAHADCQLVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 233 TGPPKMIGHTHSSF-GLGLSVNGRFwlDLIASDVMWntsdtgwaksawssVFSPWTQGACVFAHYLP------------R 299
Cdd:PRK07867 164 SGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasialrrK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 300 FESTSILQTLSKFPITVF--CSAPTAYrMLVQNDMSSYKFNSLKhcVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETvl 377
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSY-VLATPERPDDADNPLR--IVYGNEGAPGDIARFARRFGCVVVDGFGSTEG-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 378 icgnfkGMKIK------PGSMGKPSPafDVKILD-ENGATLPPGQEGDIALQ---------VLPERPfGLFTHYVDNPSK 441
Cdd:PRK07867 303 ------GVAITrtpdtpPGALGPLPP--GVAIVDpDTGTECPPAEDADGRLLnadeaigelVNTAGP-GGFEGYYNDPEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 442 TASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
..
gi 568949898 522 PD 523
Cdd:PRK07867 454 PG 455
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
211-550 |
2.45e-28 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 118.24 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 211 DS-HTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFwLDLIASDVMWNTSDTGWaKSAWSSVFSPWTQ 288
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 289 GACVFAHYLPRFESTSILQTL-SKFPITVFcSAPTAY-RMLVQ--NDMSSYKFNSLKHCVSAGEPINPEVMEQWRKkTGL 364
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVL-DLPPAYlQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWLK-APV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 365 DIYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKILDENGATLPPGQEGD--IALQVLP----ERPfGLfT 433
Cdd:cd17649 238 RLFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-EL-T 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 434 H--YVDNPSKTAStlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRG 511
Cdd:cd17649 316 AerFVPDPFGAPG---SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGK 392
|
330 340 350
....*....|....*....|....*....|....*....
gi 568949898 512 EVVkAFIVLNPDYKshdQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:cd17649 393 QLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVP 427
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
90-539 |
2.58e-28 |
|
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: 118.58 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd17655 24 TYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVdAVAAKCENLHSKLIVSQHSRegwgNLKemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPK--MIGHtHSSFG 247
Cdd:cd17655 103 HLQPPI-AFIGLIDLLDEDTIYHEESE----NLE------------PVSKSDDLAYVIYTSGSTGKPKgvMIEH-RGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfahYLPRFES----TSILQTLSKFPITVFCSAPTA 323
Cdd:cd17655 165 LVEWANKVIYQG--EHLRVALFASISFDASVTE-IFASLLSGNTL---YIVRKETvldgQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 324 YRMLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKKTGL--DIYEGYGQTETVLIC--GNFKGMKIKPGS--MGKPSP 397
Cdd:cd17655 239 LKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 398 AFDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTASTL-------RGSFYITGDRGYMDEDGYFWFVAR 470
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGE--LYIGGE---GVARGYLNRPELTAEKFvddpfvpGERMYRTGDLARWLPDGNIEFLGR 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshdQEQLKKEIQEH 539
Cdd:cd17655 392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP---VAQLREFLARE 457
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
88-553 |
3.75e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 118.45 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYfTSGTTGPPK--MIGH 241
Cdd:PRK07798 107 EREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 242 T---HSSFGLGLSVNGRFWLD----------------LIASDVMWNTSDtgWAksAWSSVFSpwtqGACVFAHYLPRFES 302
Cdd:PRK07798 186 EdifRVLLGGRDFATGEPIEDeeelakraaagpgmrrFPAPPLMHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 303 TSILQTLSKFPITVFCSAPTAY-RMLVQ--NDMSSYKFNSLKHCVSAGEPINPEVMEQWRK-KTGLDIYEGYGQTETvli 378
Cdd:PRK07798 258 DEVWRTIEREKVNVITIVGDAMaRPLLDalEARGPYDLSSLFAIASGGALFSPSVKEALLElLPNVVLTDSIGSSET--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 379 cgNFKGMKI-KPGSMGKPSPAF----DVKILDENGATLPPGQE--GDIALQvlPERPFGlfthYVDNPSKTASTLR---G 448
Cdd:PRK07798 335 --GFGGSGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGSGeiGWIARR--GHIPLG----YYKDPEKTAETFPtidG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 449 SFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSH 527
Cdd:PRK07798 407 VRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARP 485
|
490 500
....*....|....*....|....*.
gi 568949898 528 DQEqlkkEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07798 486 DLA----ELRAHCRSSLAGYKVPRAI 507
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-553 |
4.60e-28 |
|
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: 114.81 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfWldlIASDVMwntSDTGWAKSAWSSVFSPWTQG------ACVFAHYLPR 299
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------W---IESFVC---NEDLFNISGEDAILAPGPLShslflyGAISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 300 -------FESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSykfNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYG 371
Cdd:cd17633 68 tfigqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 372 QTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGatlppGQEGDIALQvlpeRPFgLFTHYVDNPSKTAstlrGSFY 451
Cdd:cd17633 145 TSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK----SEM-VFSGYVRGGFSNP----DGWM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 452 ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykshdqEQ 531
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------KL 282
|
330 340
....*....|....*....|..
gi 568949898 532 LKKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd17633 283 TYKQLKRFLKQKLSRYEIPKKI 304
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
85-523 |
4.69e-28 |
|
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: 119.96 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAVAAKCENLhSKLIVSQHSregwgnlkemmkyASDSHTCVDTKHdemMA-IYFTSGTTGPPK--MIgh 241
Cdd:COG1020 577 VLTQSALAARLPELGVPVLAL-DALALAAEP-------------ATNPPVPVTPDD---LAyVIYTSGSTGRPKgvMV-- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 242 THSSFG-LGLSVNGRFWLDliASDVM-WNTS---DTgwakSAWSsVFSPWTQGAC-VFAHYLPRFESTSILQTLSKFPIT 315
Cdd:COG1020 638 EHRALVnLLAWMQRRYGLG--PGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVT 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM 392
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSV 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 --GKPSPAFDVKILDENGATLPPGQEGDI-------ALqvlperpfGlfthYVDNPSKTAS-------TLRGS-FYITGD 455
Cdd:COG1020 789 piGRPIANTRVYVLDAHLQPVPVGVPGELyiggaglAR--------G----YLNRPELTAErfvadpfGFPGArLYRTGD 856
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949898 456 RGYMDEDGYFWFVARSDD---IilsSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 523
Cdd:COG1020 857 LARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-551 |
7.88e-28 |
|
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: 114.35 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 228 FTSGTTGPPKMIGHT-----HSSFG----LGLSVNGRFWLDLIASDV-----MWNtsdtgWAKSAWSSVFSPWTQGAcvf 293
Cdd:cd17630 7 LTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDSWLLSLPLYHVgglaiLVR-----SLLAGAELVLLERNQAL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 ahylprfestsiLQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQT 373
Cdd:cd17630 79 ------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ETV-LICGNFKGMKiKPGSMGKPSPAFDVKILDEngatlppgqeGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYi 452
Cdd:cd17630 146 ETAsQVATKRPDGF-GRGGVGVLLPGRELRIVED----------GEIWV-----GGASLAMGYLRGQLVPEFNEDGWFT- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 453 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykSHDQEql 532
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADPA-- 283
|
330
....*....|....*....
gi 568949898 533 kkEIQEHVKKTTAPYKYPR 551
Cdd:cd17630 284 --ELRAWLKDKLARFKLPK 300
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
90-550 |
1.90e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 116.52 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVAAKCENLhsKLIVSQHSREGWGNLKEMMKYASDSHTCVDT----KHDEMMaIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 246 fgLGLSVNGrfwldLIAS----------DVMWNTSDTGWAKSAWSSVFSpwtqGACVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK05852 201 --IASSVRA-----IITGyrlsprdatvAVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQ---NDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--------VLICGNFKG 384
Cdd:PRK05852 270 WYTAVPTIHQILLEraaTEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 385 MKIKPGSMGKpSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGY 464
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 465 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQlkkEIQEHVKKTT 544
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERL 498
|
....*.
gi 568949898 545 APYKYP 550
Cdd:PRK05852 499 AAFEIP 504
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-546 |
9.03e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.79 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 217 DTKHDEMMAIYFTSGTTGPPK--MIGHT----------------------------HSsfgLGLSVNgrFWLDLIasdvm 266
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWLPLL----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 267 wntsdtgwaksawssvfspwtQGACVFAHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQN-----DMssykFNSLK 341
Cdd:PRK08633 848 ---------------------EGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNkklhpLM----FASLR 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 342 HCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKILD-ENGAT 410
Cdd:PRK08633 902 LVVAGAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEE 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 411 LPPGQEGDIAL---QVLperpfglfTHYVDNPSKTASTLR----GSFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIG 483
Cdd:PRK08633 982 LPPGEDGLILIggpQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIG 1048
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949898 484 ----PF-EVESALIE--HPSIAESAVVSSPDPIRGEVVkafIVLnpdyksHDQEQLKKE-IQEHVKKTTAP 546
Cdd:PRK08633 1049 gemvPLgAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEDVEeLKRAIKESGLP 1110
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
100-552 |
1.31e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.34 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 100 KFANILTEACSLQRgdRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVA 179
Cdd:PRK07638 38 KVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 180 AKcenlhsklIVSqhsregWGNLKEMM-KYASDSHTCVDTKHDEM-MAiyFTSGTTGPPKMIGHTHSSFGLGLSVNGR-F 256
Cdd:PRK07638 116 GR--------VIE------IDEWKRMIeKYLPTYAPIENVQNAPFyMG--FTSGSTGKPKAFLRAQQSWLHSFDCNVHdF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 257 WLD-----LIASDVMwntsdtgwaksawSSVF-----SPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSAPTAYRM 326
Cdd:PRK07638 180 HMKredsvLIAGTLV-------------HSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 327 LVQNDmsSYKFNSLKhCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPGSMGKPSPAFDV 401
Cdd:PRK07638 245 LYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPNSVGRPFHNVQV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 402 KILDENGATLPPGQEGDIALQvlpeRPFgLFTHYVdNPSKTASTLRGSFYIT-GDRGYMDEDGYFWFVARSDDIILSSGY 480
Cdd:PRK07638 319 RICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949898 481 RIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdykshDQEQLKKEIQEHVKKTTAPYKYPRK 552
Cdd:PRK07638 393 NIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-540 |
2.05e-26 |
|
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: 112.02 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdilyrlqs 159
Cdd:cd17653 16 VESLGGSL--TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 160 skakciitDDTLAPAvDAVAAKCENLHSKLIVsqhsregwgnlkemmkyasdshtCVDTKHDEMMAIyFTSGTTGPPKMI 239
Cdd:cd17653 77 --------LDAKLPS-ARIQAILRTSGATLLL-----------------------TTDSPDDLAYII-FTSGSTGIPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 240 GHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWsSVFSPWTQGAC-VFAHYLPRFesTSILQTLSKFPITvfc 318
Cdd:cd17653 124 MVPHRGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIG-EIFSTLCNGGTlVLADPSDPF--AHVARTVDALMST--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 319 saPTAYRMLVQNDmssykFNSLKHCVSAGEPINPEVMEQWRKktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPA 398
Cdd:cd17653 197 --PSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 399 FDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTASTLR------GS-FYITGDRGYMDEDGYFWFVARS 471
Cdd:cd17653 268 STCYILDADLQPVPEGVVGEICISGV-----QVARGYLGNPALTASKFVpdpfwpGSrMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 472 DDIILSSGYRIGPFEVESALIEHPSIAESAVVSSpdpIRGEVVkAFIVlnPDykSHDQEQLKKEIQEHV 540
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL 403
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-541 |
2.65e-26 |
|
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: 112.56 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 81 DGNGEELRWSfeELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 160
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 161 KAKCIIT---DD--TLAPAV-DAVAAKCENLHSKLivsqHSREGWGNLKEMMKYASDSHTcvdTKHDEMMAIYFTSGTTG 234
Cdd:cd05932 78 ESKALFVgklDDwkAMAPGVpEGLISISLPPPSAA----NCQYQWDDLIAQHPPLEERPT---RFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 235 PPKMIGHTHSSFG---------LGLSVNGRF--WLDL--IASDVMwntsdtgwaksawssVFSPWTQGACV--FAHYLPR 299
Cdd:cd05932 151 QPKGVMLTFGSFAwaaqagiehIGTEENDRMlsYLPLahVTERVF---------------VEGGSLYGGVLvaFAESLDT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 300 FestsiLQTLSKFPITVFCSAP---TAYRMLVQNDMSSYKFNSL----------KHCVSAG-------------EPINPE 353
Cdd:cd05932 216 F-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPPA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 354 VMEqWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIldengatlppGQEGDIALqvlpeRPFGLFT 433
Cdd:cd05932 291 LLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALMM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 434 HYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSS-GYRIGPFEVESALIEHPSIAESAVVSS--PDPI 509
Cdd:cd05932 355 GYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPL 434
|
490 500 510
....*....|....*....|....*....|..
gi 568949898 510 RGEVVKAFIVLNPDykSHDQEQLKKEIQEHVK 541
Cdd:cd05932 435 ALVVLSEEARLRAD--AFARAELEASLRAHLA 464
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-539 |
5.67e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 112.30 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKAKCII 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 167 TddtlAPAvdAVAAKC------ENLHSKLIVSQhsREGWGN--LKEMM-KYASDSHTCVDTKHDEMMAIYFTSGTTGPPK 237
Cdd:PRK09274 119 G----IPK--AHLARRlfgwgkPSVRRLVTVGG--RLLWGGttLATLLrDGAAAPFPMADLAPDDMAAILFTSGSTGTPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 238 MIGHTHSSF---------GLGLSVNGRfwlDLIASDVMwntsdtgwaksawsSVFSPwtqgACVFAHYLPRFEST----- 303
Cdd:PRK09274 191 GVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGP----ALGMTSVIPDMDPTrpatv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 304 ---SILQTLSKFPITVFCSAPtAY-----RMLVQNDMssyKFNSLKHCVSAGEPINPEVMEQWRK--KTGLDIYEGYGQT 373
Cdd:PRK09274 250 dpaKLFAAIERYGVTNLFGSP-ALlerlgRYGEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGAT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ETVLICgnfkgmKIkpGS------------------MGKPSPAFDVKIL---DENGAT------LPPGQEGDIALQ---V 423
Cdd:PRK09274 326 EALPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIaisDAPIPEwddalrLATGEIGEIVVAgpmV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 LPErpfglfthYVDNPSKTA-----STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIA 498
Cdd:PRK09274 398 TRS--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVK 469
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 568949898 499 ESAVVSSPDPirGEVVKAFIV-LNPDyKSHDQEQLKKEIQEH 539
Cdd:PRK09274 470 RSALVGVGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
213-523 |
7.27e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 111.66 E-value: 7.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 213 HTCVDTKHDEMMaiYFTSGTTGPPKMIGHTHSSFG-LGLSVNGRFwlDLIASDVMW--------NTSDTGWAKSAwssvf 283
Cdd:PRK13388 144 HREVDAMDPFML--IFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 284 spwTQGACVFAHylPRFESTSILQTLSKFPITVF--CSAPTAYrMLVQNDMSSYKFNSLKhcVSAGEPINPEVMEQWRKK 361
Cdd:PRK13388 215 ---ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAY-ILATPERPDDADNPLR--VAFGNEASPRDIAEFSRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 362 TGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafDVKI-------------LDENGATLPPgqegDIAL-QVLPER 427
Cdd:PRK13388 287 FGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIynpetltecavarFDAHGALLNA----DEAIgELVNTA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 428 PFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPD 507
Cdd:PRK13388 359 GAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPD 438
|
330
....*....|....*.
gi 568949898 508 PIRGEVVKAFIVLNPD 523
Cdd:PRK13388 439 ERVGDQVMAALVLRDG 454
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
226-557 |
9.16e-26 |
|
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: 110.48 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYfTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTS 304
Cdd:cd17643 99 IY-TSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrLVVVPYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 305 ILQTLSKFPITVFCSAPTAYRMLVQNDMSSYK-FNSLKHCVSAGEPINPEVMEQWRKKTGL---DIYEGYGQTET-VLIc 379
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRdPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 380 gNFKGMK---IKPGSM---GKPSPAFDVKILDENGATLPPGQEGDIAL---QVLP---ERPFGLFTHYVDNPsKTASTLR 447
Cdd:cd17643 255 -TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 448 GsfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyksH 527
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350
....*....|....*....|....*....|.
gi 568949898 528 DQEQLKKEIQEHVKKTTAPYKYP-RKVGVPG 557
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPaRYVPLDA 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
85-539 |
2.49e-25 |
|
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: 109.30 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLA-------PAVDAVAAKCENLHSKLIVSQHSregwGNLKEMMkyasdshtcvdtkhdemmaiyFTSGTTGPPK 237
Cdd:cd12116 88 VLTDDALPdrlpaglPVLLLALAAAAAAPAAPRTPVSP----DDLAYVI---------------------YTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 238 MIGHTHSSF-GLGLSVNGRfwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:cd12116 143 GVVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQNDMSsyKFNSLkHCVSAGEPINPEVMEQWRKKTGlDIYEGYGQTETVL------ICGNFKGMKIkp 389
Cdd:cd12116 220 VMQATPATWRMLLDAGWQ--GRAGL-TALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 390 gsmGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLP---ERPFGLFTHYVDNPSKTAstlRGSFYITGDRGYMDEDG 463
Cdd:cd12116 294 ---GRPLANTQVYVLDAALRPVPPGVPGELYIggdGVAQgylGRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADG 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 464 YFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLnPDYKSHDQEQLKKEIQEH 539
Cdd:cd12116 368 RLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
226-551 |
2.57e-25 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 110.27 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGrfwLDLIA------SDVMWNTS---DTGWAKSAWSSVFSpwtqGAC-VFah 295
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSA----LIVQS---LAKIAivgygeDDVYLHTAplcHIGGLSSALAMLMV----GAChVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 296 yLPRFESTSILQTLSKFPITVFCSAPTAYRMLV---QNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYG 371
Cdd:PLN02860 244 -LPKFDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 372 QTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFDVKI-LDEngatlpPGQEGDIAlqvlpER 427
Cdd:PLN02860 323 MTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRIL-----TR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 428 PFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 506
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568949898 507 DPIRGEVVKAFIVLNPDYK-SHDQEQLKK--------EIQEHV-KKTTAPYKYPR 551
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGWIwSDNEKENAKknltlsseTLRHHCrEKNLSRFKIPK 526
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
110-553 |
2.78e-25 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 110.11 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 110 SLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAV----AAKCENL 185
Cdd:PLN03102 60 NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVlhllSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 186 HSKLIV------------SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMmAIYFTSGTTGPPK--MIGHTHSSFGLGLS 251
Cdd:PLN03102 140 NLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKgvVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 252 VNGrfWLDLIASDVMWNTSD---TGWAKSaWSSVFSPWTQgACVFAHYLPRfestsILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:PLN03102 219 IIG--WEMGTCPVYLWTLPMfhcNGWTFT-WGTAARGGTS-VCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 329 QNDMSSYKFNSLK-HCVSAGEPiNPEVMEQWRKKTGLDIYEGYGQTET---VLICG---------NFKGMKIKPGSMGKP 395
Cdd:PLN03102 290 KGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKARQGVSI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 396 SPAFDVKIldENGATLPPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDII 475
Cdd:PLN03102 369 LGLADVDV--KNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 476 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLK-----KEIQEHVKKTTAPYKYP 550
Cdd:PLN03102 447 ISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtreRDLIEYCRENLPHFMCP 526
|
...
gi 568949898 551 RKV 553
Cdd:PLN03102 527 RKV 529
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
113-553 |
1.56e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 104.44 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 113 RGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCII----------------TDDTLAPAVD 176
Cdd:PRK06164 59 RGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaaVPPDALPPLR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 177 AVAAKCENLHSkliVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFT-SGTTGPPKMIGHTHSSF--------- 246
Cdd:PRK06164 139 AIAVVDDAADA---TPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLlrharaiar 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 247 GLGLSVNGRFWLDLIASDVMwntsdtgwaksAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSAPTAYRM 326
Cdd:PRK06164 216 AYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVFDAARTARALRRHRVTHTFGNDEMLRR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 327 LVQNDMSSYKFNSLKHC-VSAGEPINPEVMeQWRKKTGLDIYEGYGQTE--TVLICGNFK---GMKIKPGsmGKP-SPAF 399
Cdd:PRK06164 283 ILDTAGERADFPSARLFgFASFAPALGELA-ALARARGVPLTGLYGSSEvqALVALQPATdpvSVRIEGG--GRPaSPEA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 400 DVKILD-ENGATLPPGQEGDIALQVlperPfGLFTHYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILS 477
Cdd:PRK06164 360 RVRARDpQDGALLPDGESGEIEIRA----P-SLMRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRL 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 478 SGYRIGPFEVESALIEHPSIAESAVVSSpdPIRGEVVKAFIVLNPDYKSHDQEQLKKeiqeHVKKTTAPYKYPRKV 553
Cdd:PRK06164 435 GGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPTDGASPDEAGLMA----ACREALAGFKVPARV 504
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-550 |
1.80e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.19 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEacslqRG----DRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 160
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIA-----RGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDS 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 161 KAKCIITDDTLAPAVDAVAAkcenLHSKLIVSQHSREGWgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIG 240
Cdd:PRK12316 4648 GAALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGF----------PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVA 4713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 241 HTHSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSA 320
Cdd:PRK12316 4714 VSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFP 4791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 321 PTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQ-WRKKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MGK 394
Cdd:PRK12316 4792 PVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGT 4871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 395 PSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL--------RGSFYITGDRGYMDEDGYFW 466
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLPVGVAGELYLG-----GEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVID 4946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 467 FVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQ--LKKEIQEHVKKTT 544
Cdd:PRK12316 4947 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERL 5026
|
....*.
gi 568949898 545 APYKYP 550
Cdd:PRK12316 5027 PEYMVP 5032
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-553 |
3.95e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 103.16 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 65 MEKAGKRLSNPAFWWIDGNGEelrWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 145 TTQLTQKDIlyrlqssKAKCIITDdtlaPAVDAVAAKC--------ENLHSKLIVSQHSREGWGNLKEMMKYASDShTCV 216
Cdd:PRK05857 97 DGNLPIAAI-------ERFCQITD----PAAALVAPGSkmassavpEALHSIPVIAVDIAAVTRESEHSLDAASLA-GNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLG---LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:PRK05857 165 DQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 AHYlprfESTSILQTLSKFPITVFCSAPTAYRMLVqndmSSYKFN-----SLKHCVSAG-EPINPEVmeQWRKKTGLDIY 367
Cdd:PRK05857 245 GGE----NTTSLLEILTTNAVATTCLVPTLLSKLV----SELKSAnatvpSLRLVGYGGsRAIAADV--RFIEATGVRTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 368 EGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGA--TLPPGQEGDIALQVLPERPFGLFThYVDNPS 440
Cdd:PRK05857 315 QVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgpTAPGAGPSASFGTLWIKSPANMLG-YWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 441 KTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 520
Cdd:PRK05857 394 RTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVA 473
|
490 500 510
....*....|....*....|....*....|...
gi 568949898 521 NPDYKSHDQEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK05857 474 SAELDESAARALKHTIAARFRRESEPMARPSTI 506
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-563 |
4.31e-23 |
|
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: 101.30 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 DEMMAIYfTSGTTGPPKMIGHTHSSFGLGLS-----VNGRFWLDLIASDVMWNTSDTGW--------AKSAWSSVFSPWT 287
Cdd:cd05924 4 DDLYILY-TGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 288 QGACVFAHylPRFESTSILQTLSKFPITVFCSAPTAY-RMLVQ--NDMSSYKFNSLKHCVSAGEPINPEVMEQW-RKKTG 363
Cdd:cd05924 83 GQTVVLPD--DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 364 LDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKILDENGATLPPGQEGdiaLQVLPER---PFGlfthYVDNP 439
Cdd:cd05924 161 ITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGG---VGWIARRghiPLG----YYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKTASTLR---GSFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 515
Cdd:cd05924 232 AKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568949898 516 AFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKVGVPGTSDVSP 563
Cdd:cd05924 312 AVVQLREGAGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSP 354
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
88-590 |
2.87e-22 |
|
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: 100.13 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIt 167
Cdd:cd17640 5 RITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 ddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFG 247
Cdd:cd17640 83 ------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLSvngRFW--LDLIASDVMWntsdtgwaksawsSVFSPW--TQGAC---VFA-----HYlprfesTSI---LQTLSKF 312
Cdd:cd17640 115 HQIR---SLSdiVPPQPGDRFL-------------SILPIWhsYERSAeyfIFAcgcsqAY------TSIrtlKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 313 PITVFCSAPTAYRMLVQN------DMSSYK---------FNSLKHCVSAGEPINPEVmEQWRKKTGLDIYEGYGQTET-- 375
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGiqkqvsKSSPIKqflflfflsGGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETsp 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VLICGNFKGMKIkpGSMGKPSPAFDVKILDENG-ATLPPGQEGdIALQVLPERPFGlfthYVDNPSKTASTLRGS-FYIT 453
Cdd:cd17640 252 VVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGnVVLPPGEKG-IVWVRGPQVMKG----YYKNPEATSKVLDSDgWFNT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 454 GDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIaESAVVSSPDPIRgevVKAFIVlnPDYkshdqEQL 532
Cdd:cd17640 325 GDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIV--PNF-----EEL 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 533 KKEIQEhvkkttapykyprkVGVPGTSDVSPVLwtvfSSDILCERFQTELMTIVNQKL 590
Cdd:cd17640 394 EKWAKE--------------SGVKLANDRSQLL----ASKKVLKLYKNEIKDEISNRP 433
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
340-555 |
3.51e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.07 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 340 LKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGD 418
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 419 IALQvlperpfGLF--THYVDNPSKTASTLRGSfyiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 496
Cdd:PRK13383 374 IFVG-------GELagTRYTDGGGKAVVDGMTS---TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 497 IAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVKKttapYKYPRKVGV 555
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQLRDYLKDRVSR----FEQPRDINI 497
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
218-519 |
3.56e-22 |
|
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: 99.82 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 218 TKHDEMMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFwlDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGAC-VFA 294
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 295 HYLPRFESTSILQTLSKFPITVFcSAPTAYRMLVQNDMSSYKF---NSLKHCVSAGEPINPEVMEQWRKKTGLDI--YEG 369
Cdd:cd17644 179 PEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 370 YGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA- 443
Cdd:cd17644 258 YGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTAe 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 444 --------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 515
Cdd:cd17644 333 kfishpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
....
gi 568949898 516 AFIV 519
Cdd:cd17644 413 AYIV 416
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-550 |
5.18e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.31 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLA---PAVDAVAAKCENLHSKLIvsQHSregwgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12467 613 LLTQSHLLaqlPVPAGLRSLCLDEPADLL--CGY--------------SGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 242 THSSFGLGLSVNGRfWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FESTSILQTLSKFPITVFC 318
Cdd:PRK12467 677 SHGALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLK 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 319 SAPTAYRMLVQnDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMG 393
Cdd:PRK12467 753 IVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIG 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 394 KPSPAFDVKILDENGATLPPGQEGD--IALQVLPE----RPFGLFTHYVDNPSKTAStlrGSFYITGDRGYMDEDGYFWF 467
Cdd:PRK12467 832 QPLANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEY 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 468 VARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAPY 547
Cdd:PRK12467 909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDY 987
|
...
gi 568949898 548 KYP 550
Cdd:PRK12467 988 MVP 990
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
68-540 |
8.13e-21 |
|
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: 96.15 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 68 AGKRLSNPAF-WWIDGNGEELRWSFEELGLLSRKFANILTEACslQRGDRVMVILPKIPEWWLANVACLRTGTV---LIP 143
Cdd:cd05931 3 AAARPDRPAYtFLDDEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 144 GTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAK-CENLHSKLIVSQHSREGwgnlkemmkyASDSHTCVDTKHDE 222
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASrPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 223 MMAIYFTSGTTGPPK--MIGHthssfgLGLSVNgrfwLDLIASDVMWNTSDTGwakSAW----------SSVFSPWTQGA 290
Cdd:cd05931 151 IAYLQYTSGSTGTPKgvVVTH------RNLLAN----VRQIRRAYGLDPGDVV---VSWlplyhdmgliGGLLTPLYSGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 291 -CVF---AHYL--P-RFestsiLQTLSKFPITvFCSAPT-AYRMLVQ----NDMSSYKFNSLKHCVSAGEPINPEVMEQW 358
Cdd:cd05931 218 pSVLmspAAFLrrPlRW-----LRLISRYRAT-ISAAPNfAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 359 RKK---TGLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFDVKILDE 406
Cdd:cd05931 292 AEAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 407 NGAT-LPPGQEGDIALQ---VLPerpfGlfthYVDNPSKTASTLR-------GSFYITGDRGYMDeDGYFWFVARSDDII 475
Cdd:cd05931 372 ETGReLPDGEVGEIWVRgpsVAS----G----YWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLI 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 476 LSSGYRIGPFEVESALIE-HPSIAES--AVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLKKEIQEHV 540
Cdd:cd05931 443 IVRGRNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAV 509
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
214-550 |
1.03e-20 |
|
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: 95.01 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 214 TCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGlGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVf 293
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 aHYLPRFESTS---ILQTLSKFPITVFCSAPTAYRMLVQNDMSSykfnsLKHCVSAGEPINPEVMEQWrkKTGLDIYEGY 370
Cdd:cd17652 163 -VLAPAEELLPgepLADLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVDRW--APGRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTETVL---ICGNFKGMKIKPgsMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTA---- 443
Cdd:cd17652 235 GPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAerfv 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 444 ----STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 519
Cdd:cd17652 308 adpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
330 340 350
....*....|....*....|....*....|.
gi 568949898 520 LNPDyKSHDQEQLKkeiqEHVKKTTAPYKYP 550
Cdd:cd17652 388 PAPG-AAPTAAELR----AHLAERLPGYMVP 413
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
84-546 |
1.22e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 84 GEElRWSFEELGLLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK12316 533 GEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 164 CIITDDTLAPAVDaVAAKCENL---HSKLIVSQHSREgwgNLKemmkyasdshTCVDTKHdeMMAIYFTSGTTGPPKMIG 240
Cdd:PRK12316 611 LLLSQSHLGRKLP-LAAGVQVLdldRPAAWLEGYSEE---NPG----------TELNPEN--LAYVIYTSGSTGKPKGAG 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 241 HTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK12316 675 NRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQnDMSSYKFNSLKHCVSAGEPINPEVMEQ-WRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--M 392
Cdd:PRK12316 749 TLHFVPSMLQAFLQ-DEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvpI 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 GKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMDEDGYF 465
Cdd:PRK12316 828 GRPIANLACYILDANLEPVPVGVLGELYLA-----GRGLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGVI 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 466 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNpDYKSHDQEQLKKEIQEHVKKTTA 545
Cdd:PRK12316 903 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-SEGGDWREALKAHLAASLPEYMV 977
|
.
gi 568949898 546 P 546
Cdd:PRK12316 978 P 978
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-550 |
3.07e-20 |
|
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: 93.77 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DDtlapavdavaakcenlhsklivsqhsregwGNLKEMMkyasdshtcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 lglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFESTSILQTLSKFPITV-FCS 319
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPserRLDLDALNDYFNQEGITIsFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 320 APTAYR-MLVQNdmssykfNSLKHCVSAGEPINPEvmeqwrKKTGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPSP 397
Cdd:cd17645 203 TGAAEQfMQLDN-------QSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPID 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 398 AFDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMDEDGYFWFVAR 470
Cdd:cd17645 270 NTRVYILDEALQLQPIGVAGE--LCIAGE---GLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:cd17645 345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMIP 417
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-553 |
4.13e-20 |
|
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: 84.52 E-value: 4.13e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 486 EVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYkshdqEQLKKEIQEHVKKTTAPYKYPRKV 553
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEV 63
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-550 |
7.24e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLA-PAVDAVAAKCenlhsklivsqhsregwgnLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLD-------------------LDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SFGLGLSVNGRFwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFES-TSILQTLSKFPITVFCSAPTA 323
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 324 YRMLVQnDMSSYKFNSLKHCVSAGEPINPEVMEQWrkKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFDV 401
Cdd:PRK12316 3298 LQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRAC 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 402 KILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDDI 474
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVpdpfvpgERLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 475 ILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLnpdykSHDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP-----EDEAGDLREALKAHLKASLPEYMVP 3516
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-550 |
8.36e-20 |
|
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: 92.72 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLAPAVDAVAAkcenLHSKLIVSQHsregwgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd12114 89 LTDGPDAQLDVAVFD----VLILDLDALA--------------APAPPPPVDVAPDDLAYVIFTSGSTGTPKgvMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 244 SSFGLgLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFESTSILQTLSKFPITVFCSAPT 322
Cdd:cd12114 151 ALNTI-LDINRRFAVG--PDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 323 AYRMLVQNDMSSYKFN-SLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 393
Cdd:cd12114 227 LLEMLLDVLEAAQALLpSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 394 KPSPAFDVKILDENGATLPPGQEGDIalqvlperpF----GLFTHYVDNPSKTAS-----TLRGSFYITGDRGYMDEDGY 464
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGEL---------WiggrGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 465 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTT 544
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYM 453
|
....*.
gi 568949898 545 APYKYP 550
Cdd:cd12114 454 IPSRVI 459
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-540 |
1.17e-19 |
|
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: 92.73 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPK----IPEWWlanvACLRTGTVLIPGTTQLTqkdilY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 156 RLQSSKAK------------CIITDDTLAPAVDAVAAKCENLHSKLIVSQhsregwgnlkEMMKYASDSHTcVDTKHDEM 223
Cdd:cd05906 101 DEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHDL-PQSRPDDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 224 MAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRF--------W--LDLIASDVMWNTSDtgwaksawssVFSPWTQGA 290
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNIlarSAGKIQHNGLtpqdvflnWvpLDHVGGLVELHLRA----------VYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 291 CVFAHYLPrfESTSILQTLSKFPITV-FcsAPT-AYRMLVQ----NDMSSYKFNSLKHCVSAGEPINPEVMEQWR---KK 361
Cdd:cd05906 240 VPTEEILA--DPLRWLDLIDRYRVTItW--APNfAFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLrllEP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 362 TGLD---IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFDVKILDENGATLPPGQEGDiaLQVlpeRPFGL 431
Cdd:cd05906 316 YGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGR--LQV---RGPVV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 432 FTHYVDNPSKTASTLR-GSFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES--AVVSSPDP 508
Cdd:cd05906 391 TKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDP 469
|
490 500 510
....*....|....*....|....*....|...
gi 568949898 509 IRGEVVKAfIVLNPDYKSHDQ-EQLKKEIQEHV 540
Cdd:cd05906 470 GAETEELA-IFFVPEYDLQDAlSETLRAIRSVV 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
117-550 |
1.75e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.30 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL-----APAVDAVaakcenlhskLIV 191
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLleqlpAPAGDTA----------LTL 3217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 192 SQHSREGWgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWlDLIASDVMWNTSD 271
Cdd:PRK12467 3218 DRLDLNGY----------SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMS 3286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 272 TGWAKSAWSsVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQnDMSSYKFNSLKHCVSAGEPIN 351
Cdd:PRK12467 3287 FSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVP 3364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 352 PEVMEQWRKKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLp 425
Cdd:PRK12467 3365 PAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV- 3443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 426 erpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSI 497
Cdd:PRK12467 3444 ----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568949898 498 AESAVVSSpDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK12467 3520 REAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASLPDYMVP 3566
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
79-546 |
2.47e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.77 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 79 WIDGNGEELrwSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWW--LANVACLrtGTVLIPGTTQLTQKDILYR 156
Cdd:PRK05620 31 WGGAEQEQT--TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 157 LQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHS-REGWGNLKEMMKYAS-----DSHTCV----DTKHDEMMAI 226
Cdd:PRK05620 107 INHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 227 YFTSGTTGPPKMIGHTHSSFGLGLsvngrfwLDLIASDVMWNTSDTGWAKS-------AWSSVFSPWTQGA-CVF----- 293
Cdd:PRK05620 187 CYSTGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESFLCCvpiyhvlSWGVPLAAFMSGTpLVFpgpdl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 -AHYLPRFESTSILQTLSKFPiTVFCSaptayrMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQ 372
Cdd:PRK05620 260 sAPTLAKIIATAMPRVAHGVP-TLWIQ------LMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 373 TETVLIcgnfkGMKIKPG-------------SMGKPSPAFDVKILDEnGATLPPGQEGDIALQVlpeRPFGLFTHYVDNP 439
Cdd:PRK05620 333 TETSPV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTDRNEGEIQV---RGNWVTASYYHSP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKT----ASTLRGS-------------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 502
Cdd:PRK05620 404 TEEgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568949898 503 VSSPDPIRGEVVKAFIVLNPDYKSHDQ--EQLKKEIQEHVKKTTAP 546
Cdd:PRK05620 484 IGYPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
226-523 |
5.23e-19 |
|
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: 90.07 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSfglglSVNGRFWldliasdvmwntSDTGWAKSAWSSV---------------FSPWTQGA 290
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRN-----AAAFLQW------------AAAAFSAEELAGVlastsicfdlsvfelFGPLATGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 291 CVF----AHYL---PRFESTSILQTLskfpitvfcsaPTAYRMLVQNDmssyKFNSLKHCVS-AGEPINPEVMEQWRKKT 362
Cdd:cd12115 173 KVVladnVLALpdlPAAAEVTLINTV-----------PSAAAELLRHD----ALPASVRVVNlAGEPLPRDLVQRLYARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 363 GLD-IYEGYGQTE-----TVLICGnfKGMKIKPgSMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYV 436
Cdd:cd12115 238 QVErVVNLYGPSEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG-----GAGVARGYL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 437 DNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 509
Cdd:cd12115 310 GRPGLTAERFLpdpfgpgARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAA 389
|
330
....*....|....
gi 568949898 510 RGEVVKAFIVLNPD 523
Cdd:cd12115 390 GERRLVAYIVAEPG 403
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-508 |
6.23e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 90.15 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTeACSLQRGDRVMVIlpkipEW-----WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 162
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALA-ALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 163 KCIITDDTLAPAVDAVAAKCENLhsklivsqhsrEGWGNLKEMMKYASDS--HTCVDT------------KHDEMMAIY- 227
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNV-----------KGWVAMTDAAHLPAGStpLLCYETlvgaqdgdydwpRFDENQASSl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 228 -FTSGTTGPPKMIGHTHSS-----FGLGLSVNgrfwLDLIASDV------MWNTSdtgwaksAWSSVFS-PWTQGACVFA 294
Cdd:PRK07008 182 cYTSGTTGNPKGALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSaPLTGAKLVLP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 295 HylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQT 373
Cdd:PRK07008 251 G--PDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 374 ETVLIcGNFKGMKIKPGSM------------GKPSPAFDVKILDENGATLP-PGQE-GDiaLQVlpeRPFGLFTHYVDNp 439
Cdd:PRK07008 329 EMSPL-GTLCKLKWKHSQLpldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGD--LQV---RGPWVIDRYFRG- 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 440 skTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP 508
Cdd:PRK07008 402 --DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
80-553 |
1.03e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 89.66 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 80 IDGngeELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV------------LIPGTTQ 147
Cdd:PRK10946 43 ICG---ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrseLNAYASQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 148 LTQKdilyRLQSSKAKCIITDDTLapaVDAVAAKCENLhskLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIY 227
Cdd:PRK10946 119 IEPA----LLIADRQHALFSDDDF---LNTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 228 FTSGTTGPPKMIGHTHSSFGL---------GLSVNGRFWLDLIASDvmwntsdtgwaKSAWSS-----VFspWTQGACVF 293
Cdd:PRK10946 189 LSGGSTGTPKLIPRTHNDYYYsvrrsveicGFTPQTRYLCALPAAH-----------NYPMSSpgalgVF--LAGGTVVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 AhylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDM---SSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGY 370
Cdd:PRK10946 256 A---PDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAeggSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 371 GQTETVLicgNFKGMKIKP----GSMGKP-SPAFDVKILDENGATLPPGQEGdialqVLPER-PFgLFTHYVDNPSKTAS 444
Cdd:PRK10946 333 GMAEGLV---NYTRLDDSDerifTTQGRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 445 TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 523
Cdd:PRK10946 404 AFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP 483
|
490 500 510
....*....|....*....|....*....|
gi 568949898 524 YKShdqEQLKKEIQEHvkkTTAPYKYPRKV 553
Cdd:PRK10946 484 LKA---VQLRRFLREQ---GIAEFKLPDRV 507
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-522 |
1.59e-18 |
|
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: 89.02 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 89 WSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 169 DTlaPAVDAVAAKCENLHS--KLIVS--------QHSREGW-GNLKEMMKYASDSHTCV------DTKHDEMMAIYFTSG 231
Cdd:cd17641 91 DE--EQVDKLLEIADRIPSvrYVIYCdprgmrkyDDPRLISfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 232 TTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACV-FAHylprfESTSILQTLS 310
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnFPE-----EPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 311 KFPITVFCSAP------------------------------TAYRMLVQN---------DMSSYK--------------- 336
Cdd:cd17641 243 EIGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGkrgrpvslwLRLASWladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 337 FNSLKHCVSAGEPINPEVMEQWRKkTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIlDENGatlppgqe 416
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVG-------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 417 gdialQVLPERPfGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDI-ILSSGYRIGPFEVESALIEH 494
Cdd:cd17641 393 -----EILVRSP-GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
490 500
....*....|....*....|....*...
gi 568949898 495 PSIAESAVVSSPDPIrgevVKAFIVLNP 522
Cdd:cd17641 467 PYIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
116-550 |
2.22e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 116 RVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLA---PAVDAVAAkcenlhskLIVS 192
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQarlPLPDGLRS--------LVLD 1697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 193 QhsregwgnLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:PRK12467 1698 Q--------EDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSF 1768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 273 GWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPIN 351
Cdd:PRK12467 1769 AFDVSVWE-LFWPLINGArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALE 1847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 352 PEVMEQWRKKTG-LDIYEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFDVKILDENGATLPPGQEGDIALQV 423
Cdd:PRK12467 1848 VEALRPWLERLPdTGLFNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLGG 1925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 LperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHP 495
Cdd:PRK12467 1926 V-----GLARGYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQG 2000
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 496 SIAESAVVSSpDPIRGEVVKAFIV-LNPDYKSHDQEQ--LKKEIQEHVKKTTAPYKYP 550
Cdd:PRK12467 2001 GVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAQvaLRAILKNHLKASLPEYMVP 2057
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
88-523 |
3.39e-18 |
|
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: 87.60 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP-GTTQLTQkdilyRLQSskakciI 166
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPlDPSHPLQ-----RLQE------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 167 TDDTLAPAVdavaakcenlhsklIVSQHSRegwgnlkemmkyasdshtcvdtkhdemmAIY--FTSGTTGPPKMIGHTHS 244
Cdd:cd05918 92 LQDTGAKVV--------------LTSSPSD----------------------------AAYviFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SF---------GLGLSVNGRfWLDL--IASDVMWNtsdtgwaksawsSVFSPWTQGACV-----------FAHYLPRFES 302
Cdd:cd05918 130 ALstsalahgrALGLTSESR-VLQFasYTFDVSIL------------EIFTTLAAGGCLcipseedrlndLAGFINRLRV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 303 TSILQTlskfpitvfcsaPTAYRMLVQNDmssykFNSLKHCVSAGEPINPEVMEQWRKKTGLdiYEGYGQTE-TVLICGN 381
Cdd:cd05918 197 TWAFLT------------PSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATVS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 382 FKGMKIKPGSMGKPSPAFdVKILDENGAT--LPPGQEGDIAL---QVLPErpfglfthYVDNPSKTA------------- 443
Cdd:cd05918 258 PVVPSTDPRNIGRPLGAT-CWVVDPDNHDrlVPIGAVGELLIegpILARG--------YLNDPEKTAaafiedpawlkqe 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 444 -STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK---AFIV 519
Cdd:cd05918 329 gSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVV 408
|
....
gi 568949898 520 LNPD 523
Cdd:cd05918 409 LDGS 412
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-573 |
9.73e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 86.33 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLApavdAVAAKCENLHSKLI 190
Cdd:cd05915 46 VGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL----PLVEAIRGELKTVQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHD-EMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNT 269
Cdd:cd05915 122 HFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 270 SDTGWAKSAWSSVFSPWTQGACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEP 349
Cdd:cd05915 202 VVPMFHVNAWCLPYAATLVGAKQVL-PGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 350 INPEVMEQWRKKTGLDIYEGYGQTETVLI---CGNFKGMKIKPGSMGKPSPAFD--------VKILDENGATLPpgQEGD 418
Cdd:cd05915 281 AAPRSLIARFERMGVEVRQGYGLTETSPVvvqNFVKSHLESLSEEEKLTLKAKTglpiplvrLRVADEEGRPVP--KDGK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 419 iALQVLPERPFGLFTHYV-DNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSI 497
Cdd:cd05915 359 -ALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKV 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568949898 498 AESAVVSSPDPIRGEVVKAFIVLNpdykshDQEQLKKEIQEHVKKTTAPYKYprkvgVPGTsdvspvlwTVFSSDI 573
Cdd:cd05915 438 KEAAVVAIPHPKWQERPLAVVVPR------GEKPTPEELNEHLLKAGFAKWQ-----LPDA--------YVFAEEI 494
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
163-533 |
1.46e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 85.96 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 163 KCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKY----ASDSHTCVDTKHDEMMA--IYFTSGTTGPP 236
Cdd:PRK06018 113 RVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiAEADGDFAWKTFDENTAagMCYTSGTTGDP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 237 KMIGHTHSSFGL-GLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFahyLP--RFESTSILQTLSKFP 313
Cdd:PRK06018 193 KGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDTEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 314 ITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPInPEVMEQWRKKTGLDIYEGYGQTETVLI--CGNFKG------ 384
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgtLAALKPpfsklp 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 385 ----MKIKPgSMGKPSPAFDVKILDENGATLPpgQEGdialqvlpeRPFGLFThyVDNPSKTASTLRGS--------FYI 452
Cdd:PRK06018 348 gdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDG---------KTFGRLK--VRGPAVAAAYYRVDgeildddgFFD 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 453 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQL 532
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEIL 493
|
.
gi 568949898 533 K 533
Cdd:PRK06018 494 K 494
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
85-560 |
1.56e-17 |
|
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: 85.60 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLApavdaVAAKCENLHSKLIVSQHSREgwgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd17656 89 VLTQRHLK-----SKLSFNKSTILLEDPSISQE------------DTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTgwAKSAWSSVFSPWTQGACVfahYLPRFESTSILQTLSKF----PITVFcSA 320
Cdd:cd17656 152 NMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTL---YIIREETKRDVEQLFDLvkrhNIEVV-FL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 321 PTAYRMLVQNDMSSYK--FNSLKHCVSAGEP--INPEVMEQWRKKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS----- 391
Cdd:cd17656 226 PVAFLKFIFSEREFINrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeipel 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 392 --MGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMDED 462
Cdd:cd17656 301 ppIGKPISNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 463 GYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDqEQLKKEIQEHVKK 542
Cdd:cd17656 376 GNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLREYLAKQLPE 452
|
490
....*....|....*...
gi 568949898 543 TTAPYKYPRKVGVPGTSD 560
Cdd:cd17656 453 YMIPSFFVPLDQLPLTPN 470
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-503 |
2.44e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 86.25 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 170 TLAPAVDAVaakcenlhSKLIVSQHSREGWgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPK--MIGHThssfg 247
Cdd:PRK10252 564 DQLPRFADV--------PDLTSLCYNAPLA---------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 lgLSVNGRFWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF-----AHYLPrfesTSILQTLSKFPITV-- 316
Cdd:PRK10252 622 --AIVNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHRDP----LAMQQFFAEYGVTTth 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 317 --------FCSAPTayrmlvqNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKI 387
Cdd:PRK10252 695 fvpsmlaaFVASLT-------PEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGEE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 388 KPGSMGKPSP-AFDV-----KILDENGATLPPGQEGDIAL---QvlperpfgLFTHYVDNPSKTAST-LRGSF------Y 451
Cdd:PRK10252 768 LAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLYLtgiQ--------LAQGYLGRPDLTASRfIADPFapgermY 839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568949898 452 ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVV 503
Cdd:PRK10252 840 RTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
57-507 |
4.99e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.54 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 57 DVLDQWtnmekAGKRLSNPAFwwIDGNGeelRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK08279 41 DVFEEA-----AARHPDRPAL--LFEDQ---SISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 137 TGTV--LIpgTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQ---HSREGWGNLKEMMKYASD 211
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 212 ---SHTCVDTKHDEmmAIY-FTSGTTGPPKMIGHTH-----SSFGLGLSvngrfwLDLIASDVMWNT----SDTGwAKSA 278
Cdd:PRK08279 188 tnpASRSGVTAKDT--AFYiYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 279 WSSVFSPwtqGACVFAHylPRFESTSILQTLSKFPITVFCsaptaY-----RMLVQNDMSSY-KFNSLKHCVSAGepINP 352
Cdd:PRK08279 259 WSSVLAA---GATLALR--RKFSASRFWDDVRRYRATAFQ-----YigelcRYLLNQPPKPTdRDHRLRLMIGNG--LRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 353 EVMEQWRKKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFD------VKILDENGATL----------PP 413
Cdd:PRK08279 327 DIWDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLahpyaiVKYDVDTGEPVrdadgrcikvKP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 414 GQEGDIALQVLPERPfglFTHYVDnPSKT-ASTLRGSF------YITGDRGYMDEDGYFWFVARSDDIilssgYR----- 481
Cdd:PRK08279 401 GEVGLLIGRITDRGP---FDGYTD-PEASeKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgen 471
|
490 500
....*....|....*....|....*...
gi 568949898 482 IGPFEVESALIEHPSIAESAV--VSSPD 507
Cdd:PRK08279 472 VATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-550 |
5.80e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.39 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 166 ITDDTLAPAVdAVAAKCENLhsklivsQHSREGWgnlkemMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12316 2105 LTQRHLLERL-PLPAGVARL-------PLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 246 FGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFA----HYLPRfestSILQTLSKFPITVFCSAP 321
Cdd:PRK12316 2171 LVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIrddeLWDPE----QLYDEMERHGVTILDFPP 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 322 TAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTETVLICGNFKGMKIKPGS-----MGKP 395
Cdd:PRK12316 2245 VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRA 2324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 396 SPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWF 467
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEY 2399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 468 VARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVlnPDyksHDQEQLKKEIQEHVKKTTAPY 547
Cdd:PRK12316 2400 LGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPAY 2473
|
...
gi 568949898 548 KYP 550
Cdd:PRK12316 2474 MVP 2476
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
219-552 |
1.92e-16 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 82.25 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 219 KHDEMMAIYFTSGTTGPPKMIGHTHSS-----------FGLGlsvNGRFWL-------DLiasDVMwntsdtgwaksaws 280
Cdd:PRK04813 141 KGDDNYYIIFTSGTTGKPKGVQISHDNlvsftnwmledFALP---EGPQFLnqapysfDL---SVM-------------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 281 SVFSPWTQGACVFAhyLPRfESTS----ILQTLSKFPITVFCSAPTAYRM-LVQNDMSSYKFNSLKHCVSAGEPINPEVM 355
Cdd:PRK04813 201 DLYPTLASGGTLVA--LPK-DMTAnfkqLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 356 EQWRKK-TGLDIYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqVLP 425
Cdd:PRK04813 278 KKLLERfPSATIYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 426 ERPFGlfthYVDNPSKTAS---TLRGS-FYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:PRK04813 353 SVSKG----YLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAV 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568949898 502 VVsspdPI-RGEVVK---AFIVLNPdyksHDQE---QLKKEIQEHVKKTTAPYKYPRK 552
Cdd:PRK04813 428 VV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
284-552 |
2.63e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 81.58 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 284 SPWTQGACVFAHYlPRFESTsilQTLSKFPITVFCS-APTAYRMLVQNDMSSY-KFNSLkhcVSAGEPINPEVMEQWRKK 361
Cdd:PRK07445 181 SFLTGGKLVILPY-KRLKSG---QELPPNPSDFFLSlVPTQLQRLLQLRPQWLaQFRTI---LLGGAPAWPSLLEQARQL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 362 tGLDIYEGYGQTETV-LICgnfkgmKIKPG-------SMGKPSPafDVKIldengaTLPPGQEGDIALQVlPERPFGLFT 433
Cdd:PRK07445 254 -QLRLAPTYGMTETAsQIA------TLKPDdflagnnSSGQVLP--HAQI------TIPANQTGNITIQA-QSLALGYYP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 434 HYVDNPSktastlrgsFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEV 513
Cdd:PRK07445 318 QILDSQG---------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEV 388
|
250 260 270
....*....|....*....|....*....|....*....
gi 568949898 514 VKAFIVlnPDYKSHDQEqlkkEIQEHVKKTTAPYKYPRK 552
Cdd:PRK07445 389 VTAIYV--PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-557 |
1.14e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 79.86 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 121 LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPA----------VDAVAAKCENL-HSKL 189
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplyskvVEAAPAKAIVLpAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 190 IVSQHSREGWGNLKEMMKYASDSHtCVDTKH--------DEMMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLI 261
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQG-SVGGNEyspvyapvESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 262 ASDVM-WNTSdTGWAKSAWsSVFSPWTQGACVfAHYLPRFESTSILQTLSKFPITVFCSAPT---AYRMLVQNDMSSYKF 337
Cdd:PLN03051 159 PGDVVcWPTN-LGWMMGPW-LLYSAFLNGATL-ALYGGAPLGRGFGKFVQDAGVTVLGLVPSivkAWRHTGAFAMEGLDW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 338 NSLKHCVSAGEPINPE------VMEQWRKKT-----GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKILDE 406
Cdd:PLN03051 236 SKLRVFASTGEASAVDdvlwlsSVRGYYKPVieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLLND 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 407 NGATLPPGQE--GDIALQVlperPFGLFTHYVDNPSKTASTLRG-SFYIT--------GDRGYMDEDGYFWFVARSDDII 475
Cdd:PLN03051 308 NGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmPMYGSkgmplrrhGDIMKRTPGGYFCVQGRADDTM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 476 LSSGYRIGPFEVESALIE-HPSIAESAVVSSPDPIRGE----VVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAP-YKY 549
Cdd:PLN03051 384 NLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPlFKV 463
|
....*...
gi 568949898 550 PRKVGVPG 557
Cdd:PLN03051 464 SRVKIVPE 471
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-503 |
1.26e-15 |
|
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: 79.43 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 218 TKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLsvngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSPwtqgACVFAHYL 297
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--------DALRQLYGIRPGEVDLATFPLFALFGP----ALGLTSVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 298 PRFESTS--------ILQTLSKFPITVFCSAPTAYRML----VQNDMssyKFNSLKHCVSAGEPINPEVMEQWRK--KTG 363
Cdd:cd05910 150 PDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 364 LDIYEGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKILD---------ENGATLPPGQEGDIAL--- 421
Cdd:cd05910 227 AEILTPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVtgp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 422 QVLPErpfglfthYVDNPSKTA----STLRGSF-YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 496
Cdd:cd05910 307 TVTPT--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPG 378
|
....*..
gi 568949898 497 IAESAVV 503
Cdd:cd05910 379 VRRSALV 385
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
226-550 |
8.91e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 76.61 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFWLD-----LIASDVmwnTSDTGWAksawSSVFSPWTQGA--CVFAHYL 297
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeAYNEALNCEqdetpIVACPV---THSYGLI----CGVLAALTRGSkpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 298 PRFestsILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLkhcVSAGEPINPEVMEQWRKKTgLDIYEGYGQTET-- 375
Cdd:PRK08308 179 PKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAgc 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VLICGNFKgmkiKPGSMGKPSPAFDVKIldenGATlpPGQEGDIALQVLPERPFglfthyvdnpsktastlrgsfyiTGD 455
Cdd:PRK08308 251 VSICPDMK----SHLDLGNPLPHVSVSA----GSD--ENAPEEIVVKMGDKEIF-----------------------TKD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 456 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdykSH---DQEQL 532
Cdd:PRK08308 298 LGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHeeiDPVQL 371
|
330
....*....|....*...
gi 568949898 533 KKEIQEHVkkttAPYKYP 550
Cdd:PRK08308 372 REWCIQHL----APYQVP 385
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
85-551 |
3.48e-14 |
|
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: 75.41 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 85 EELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 161
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 162 AKCIITDDTLAPAVDAV--AAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTK-HDEMM--AIY-FTSGTTGP 235
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRaHVTIKspALYiYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 236 PK--MIGHTHSSFGLG-LSVNGrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAhylPRFESTSILQTLSK 311
Cdd:cd05938 159 PKaaRISHLRVLQCSGfLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGAtCVLK---PKFSASQFWDDCRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 312 FPITVFCSAPTAYRMLVQndmSSYKFNSLKHCV--SAGEPINPEVMEQWRKKTG-LDIYEGYGQTETVLICGNFKGmkiK 388
Cdd:cd05938 231 HNVTVIQYIGELLRYLCN---QPQSPNDRDHKVrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYTG---K 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 389 PGSMGKPS-------P----AFDVK----ILDENG--ATLPPGQEGDIALQVLPERPfglFTHYVDNPSKTASTL----- 446
Cdd:cd05938 305 IGAVGRVSylykllfPfeliKFDVEkeepVRDAQGfcIPVAKGEPGLLVAKITQQSP---FLGYAGDKEQTEKKLlrdvf 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 -RGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVLNP 522
Cdd:cd05938 382 kKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKLKP 460
|
490 500
....*....|....*....|....*....
gi 568949898 523 DYkSHDQEQLkkeiQEHVKKTTAPYKYPR 551
Cdd:cd05938 461 GH-EFDGKKL----YQHVREYLPAYARPR 484
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-544 |
3.64e-14 |
|
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: 75.33 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLApavdavaakcenlhsklIVSqhsregwgnLKE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVK-----------------VYS---------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 205 MMK-YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLiasdVMWNTSDTGWAksawssvF 283
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYIS-------Y 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 284 SPwtqgacvFAHYLPRF-ESTSI-------------------LQTLSkfPiTVFCSAPTAY-RML--VQNDMS------- 333
Cdd:cd05927 166 LP-------LAHIFERVvEALFLyhgakigfysgdirlllddIKALK--P-TVFPGVPRVLnRIYdkIFNKVQakgplkr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 334 -------SYKFNSLKH---------------------------CVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVliC 379
Cdd:cd05927 236 klfnfalNYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECT--A 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 380 GNFKGM--KIKPGSMGKPSPAFDVKILD--ENG--ATLPPGqEGDIALqvlpeRPFGLFTHYVDNPSKTASTLR--GsFY 451
Cdd:cd05927 314 GATLTLpgDTSVGHVGGPLPCAEVKLVDvpEMNydAKDPNP-RGEVCI-----RGPNVFSGYYKDPEKTAEALDedG-WL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 452 ITGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVESALIEHPSIAESAVvsspdpiRGEVVKAF----IVLNPDY-- 524
Cdd:cd05927 387 HTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDVlk 459
|
490 500 510
....*....|....*....|....*....|....
gi 568949898 525 ----------KSHDQ----EQLKKEIQEHVKKTT 544
Cdd:cd05927 460 ewaaskgggtGSFEElcknPEVKKAILEDLVRLG 493
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
116-503 |
5.97e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 116 RVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL---APAVDAVAAKC-ENLHSkliv 191
Cdd:PRK05691 1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---- 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 192 sqhsrEGWgnlkemmkyasDSHTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFGLGLSvngrfWLD----LIASDVM 266
Cdd:PRK05691 1259 -----DSW-----------PSQAPGLHLHGDNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVL 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 267 WNTSDTGWAKSAWSsVFSPWTQGA-CVFA----HYLPRfestSILQTLSKFPITVFCSAPTAYRMLVQNDMSSyKFNSLK 341
Cdd:PRK05691 1318 MQKAPISFDVSVWE-CFWPLITGCrLVLAgpgeHRDPQ----RIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLR 1391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 342 HCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVL-----ICGNFKGMKikpGSMGKPSPAFDVKILDENGATLPPGQ 415
Cdd:PRK05691 1392 RLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGV 1468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 416 EGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 487
Cdd:PRK05691 1469 AGELCIGGA-----GLARGYLGRPALTAerfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEI 1543
|
410
....*....|....*.
gi 568949898 488 ESALIEHPSIAESAVV 503
Cdd:PRK05691 1544 QARLLAQPGVAQAAVL 1559
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
226-553 |
1.36e-13 |
|
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: 73.20 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFWLDLIASDVMwntsdtgwaksawsSVFSPWtqgacVFAHYLPRFeST 303
Cdd:cd17648 99 AIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAV--------------LFFSNY-----VFDFFVEQM-TL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 304 SIL--QTLSKFPITVFCSAPTAYR---------------MLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKKTGLDI 366
Cdd:cd17648 158 ALLngQKLVVPPDEMRFDPDRFYAyinrekvtylsgtpsVLQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 367 YEGYGQTETVL--ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQ---VLP---ERPFGLFTHYVDN 438
Cdd:cd17648 236 INAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGgdgVARgylNRPELTAERFLPN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 439 PSKTAS-TLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP-IRGEV 513
Cdd:cd17648 316 PFQTEQeRARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSR 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568949898 514 VKAFIVlnpDYKSHDQEQL-KKEIQEHVKKTTAPYKYPRKV 553
Cdd:cd17648 396 IQKYLV---GYYLPEPGHVpESDLLSFLRAKLPRYMVPARL 433
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
51-556 |
2.18e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 73.19 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 51 YFNFAKDVLdqwtnMEKAGKRLSNPAFWWIDGNGEEL---RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEW 127
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL-----------------APAVDAVAAKCENLHSKLi 190
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 191 vsqhsREGWGNLKEMMKYAS-----DSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLIASDV 265
Cdd:PLN03052 326 -----REGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 266 M-WNTsDTGWAKSAWsSVFSPWTQGACvfahyLPRFESTSILQTLSKF----PITVFCSAPTAYRML-VQNDMSSYKFNS 339
Cdd:PLN03052 400 VcWPT-NLGWMMGPW-LVYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWkNTNCMAGLDWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 340 LKHCVSAGEPINPE----VMEQWRKKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFDVKILDENGATL 411
Cdd:PLN03052 473 IRCFGSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 412 PPGQE--GDIALQVLperPFGLFT----------HYVDNPSKTASTLRGSfyitGDRGYMDEDGYFWFVARSDDIIlssg 479
Cdd:PLN03052 547 PDDAPctGELALFPL---MFGASStllnadhykvYFKGMPVFNGKILRRH----GDIFERTSGGYYRAHGRADDTM---- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 480 yRIGPFEVESALIE------HPSIAESAVVSSPDPIRG--EVVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAP-YKYP 550
Cdd:PLN03052 616 -NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlFKVS 694
|
....*.
gi 568949898 551 RKVGVP 556
Cdd:PLN03052 695 AVVIVP 700
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-491 |
6.68e-13 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 70.92 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDdtlapavdavaakcenlHSKLIVSQHSREgwgnlkemmkyasdSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05939 79 LIFN-----------------LLDPLLTQSSTE--------------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 SFgLGLSVNGRFWLDLIASDVMWNTsdtgwaKSAWSSVFSPWTQGACVFahylprFESTSILQtlSKFPITVFCSAPTAY 324
Cdd:cd05939 128 RY-YRIAAGAYYAFGMRPEDVVYDC------LPLYHSAGGIMGVGQALL------HGSTVVIR--KKFSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 325 RMLVQN---DMSSYKFNS------LKHCV--SAGEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKG-------- 384
Cdd:cd05939 193 NCTIVQyigEICRYLLAQppseeeQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 385 ----MKIKPGSMGKPSPAFDVKILDENGATLP--PGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRG------SFYI 452
Cdd:cd05939 273 srilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDvfkkgdSAFL 352
|
410 420 430
....*....|....*....|....*....|....*....
gi 568949898 453 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESAL 491
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL 391
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
218-507 |
2.64e-12 |
|
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: 69.03 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 218 TKHDEMMAIYFTSGTTGPPK--MIGH---THSSFGL-------GLSVN----GRFWLDLIASDvmwntsdtgWAKSAWS- 280
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHrnvAHAAHAWrreyeldSFPVRllqmASFSFDVFAGD---------FARSLLNg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 281 SVFSPWTQGAcvfahylpRFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCV--SAGEPINPEVMEQ 357
Cdd:cd17650 161 GTLVICPDEV--------KLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIvgSDGCKAQDFKTLA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 358 WRKKTGLDIYEGYGQTETVLICGNFK-GMKIKPGS----MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLF 432
Cdd:cd17650 233 ARFGQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----GAGVA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 433 THYVDNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSS 505
Cdd:cd17650 308 RGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR 387
|
..
gi 568949898 506 PD 507
Cdd:cd17650 388 ED 389
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-550 |
4.37e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 226 IYfTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWaKSAWSSVFSPWTQGACVFAHYLPRFESTS 304
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 305 ILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTETV---LICG 380
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACL 2494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 381 NFKGMKIKPGS--MGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGSF 450
Cdd:PRK05691 2495 APEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRL 2569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 451 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQE 530
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQA 2649
|
330 340
....*....|....*....|
gi 568949898 531 QLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK05691 2650 ALREALKAHLKQQLPDYMVP 2669
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
209-490 |
5.60e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.02 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 209 ASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHssfglglsvnGRFWLDL----------IASDVMwntsdtgwakSA 278
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITH----------GNLYANAeamfvaaefdVETDVM----------VS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 279 WSSVF----------SPWTQGACVfAHYLP-RFESTSIL--QTLSKFPITV-----FCSAPTAYRMLVQNDMSSYKFNSL 340
Cdd:PRK07768 200 WLPLFhdmgmvgfltVPMYFGAEL-VKVTPmDFLRDPLLwaELISKYRGTMtaapnFAYALLARRLRRQAKPGAFDLSSL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 341 KHCVSAGEPINPEVMEQWR---KKTGLD---IYEGYGQTETVLI-----CGNfkGMKI------------------KPG- 390
Cdd:PRK07768 279 RFALNGAEPIDPADVEDLLdagARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNt 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 391 ----SMGKPSPAFDVKILDENGATLPPGQEGDIALQ---VLPerpfglftHYVDNPSKTASTLRGSFYITGDRGYMDEDG 463
Cdd:PRK07768 357 rrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRgesVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEEG 428
|
330 340
....*....|....*....|....*..
gi 568949898 464 YFWFVARSDDIILSSGYRIGPFEVESA 490
Cdd:PRK07768 429 EVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
207-545 |
7.53e-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: 64.42 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 207 KYASDSHTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAwSSVFSP 285
Cdd:cd17654 103 LSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 286 WTQGACVFAHYLPRFESTSILQTL--SKFPITVFCSAPTAYRMLVQNDMSSY---KFNSLKHCVSAGEPInPE--VMEQW 358
Cdd:cd17654 181 LSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPF-PSlvILSSW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 359 RKK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDVKI--LDENGATlppgQEGDIALQVLPERpfGLFTHY 435
Cdd:cd17654 260 RGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGTVIevRDQNGSE----GTGQVFLGGLNRV--CILDDE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 436 VDNPsktastlRGSFYITGDRGYMdEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDpirgEVVK 515
Cdd:cd17654 333 VTVP-------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLI 400
|
330 340 350
....*....|....*....|....*....|
gi 568949898 516 AFIVLNPDYKShdqeqLKKEIQEHVKKTTA 545
Cdd:cd17654 401 AFIVGESSSSR-----IHKELQLTLLSSHA 425
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-551 |
1.40e-10 |
|
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: 63.53 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 168 DdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshTCvdtkhdemMAIYfTSGTTGPPKMIGHTHSSFG 247
Cdd:cd05940 82 D---------------------------------------------AA--------LYIY-TSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 248 LGLSVNGrFWLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRFESTSILQTLS-------------KFPI 314
Cdd:cd05940 108 RGGAFFA-GSGGALPSDVLYTC---------------------------LPLYHSTALIVGWSaclasgatlvirkKFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 315 TVFCSAPTAYR-MLVQ--NDMSSYKFNS------LKHCVSA--GEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNF 382
Cdd:cd05940 160 SNFWDDIRKYQaTIFQyiGELCRYLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 383 KGmkiKPGSMG-------KPSPAFDVKILDENGATL----------PPGQEGDIALQVLPERPFglfTHYVDNPSKTAST 445
Cdd:cd05940 240 FG---KPGAIGrnpsllrKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPF---DGYTDPAATEKKI 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 446 LRGSF------YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAF 517
Cdd:cd05940 314 LRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAA 392
|
490 500 510
....*....|....*....|....*....|....
gi 568949898 518 IVLNPDYkshdQEQLKKeIQEHVKKTTAPYKYPR 551
Cdd:cd05940 393 IVLQPNE----EFDLSA-LAAHLEKNLPGYARPL 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-550 |
3.41e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 221 DEMMAIYFTSGTTGPPKmighthssfglGLSVNGRF----------WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTqGA 290
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLF-GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 291 CV------FAHylprfESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSSykFNSLKHCVSAGEPINPEVMEQWRKK-TG 363
Cdd:PRK05691 3937 RVeivpnaIAH-----DPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA--LDGLRWMLPTGEAMPPELARQWLQRyPQ 4009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 364 LDIYEGYGQTETVLICGNFK-GMKIKPGS---MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNP 439
Cdd:PRK05691 4010 IGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDP 4084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 440 SKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRG 511
Cdd:PRK05691 4085 LRTAlafvphpfGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NG 4163
|
330 340 350
....*....|....*....|....*....|....*....
gi 568949898 512 EVVKAFIVlnPDYKSHDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK05691 4164 KHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-546 |
3.46e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 63.06 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 225 AIYFTSGTTGPPKMIGHTHSSFglgLS----VNGRfwLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRF 300
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 301 ES---TS--ILQTLSKFPITVFCSaPTAYR------------MLVQNDM---------SSYKFNSLKHCVSAGEPINPEV 354
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeliydtnatILFGTDTflngyaryaHPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 355 MEQWRKKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKI-----LDENGATLPPGQegDIALQVL-PE 426
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLepvpgIDEGGRLFVRGP--NVMLGYLrAE 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 427 RPfglfthYVDNPsktastLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 506
Cdd:PRK06814 1000 NP------GVLEP------PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIP 1067
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568949898 507 DPIRGEVvkafIVLNPDYKSHDQEqlkkEIQEHVKKTTAP 546
Cdd:PRK06814 1068 DARKGER----IILLTTASDATRA----AFLAHAKAAGAS 1099
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-503 |
1.40e-09 |
|
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: 60.83 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDtlAPAVDAVAAKCENL-HSKLIVsQHSRE------ 197
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKILQIQDKLpHLKAII-QYKEPlkekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 198 ---GWGNLKEMMKYASDS--HTCVDT-KHDEMMAIYFTSGTTGPPK--MIGHTHSSF-GLGLSVNGRF------------ 256
Cdd:cd05933 121 nlySWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLrpatvgqesvvs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 257 WLDL--IASDVMwntsdtgwaksawsSVFSPWTQGACV-FAHylPRFESTSILQTLSKFPITVFCSAP------------ 321
Cdd:cd05933 201 YLPLshIAAQIL--------------DIWLPIKVGGQVyFAQ--PDALKGTLVKTLREVRPTAFMGVPrvwekiqekmka 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 322 -----TAYRMLV------------QNDM-----SSYKFNSLKH-----------------CVSAGEPINPEVMEQWrkkT 362
Cdd:cd05933 265 vgaksGTLKRKIaswakgvgletnLKLMggespSPLFYRLAKKlvfkkvrkalgldrcqkFFTGAAPISRETLEFF---L 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 363 GLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIL--DENGatlppgqEGDIALqvlpeRPFGLFT 433
Cdd:cd05933 342 SLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHnpDADG-------IGEICF-----WGRHVFM 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949898 434 HYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVV 503
Cdd:cd05933 405 GYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKKELPIISNAML 476
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
217-494 |
1.38e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.52 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHAN----LLANQRACLKFFSpkeDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 294 AHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQN-DMSSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYG 371
Cdd:PRK06334 255 FAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 372 QTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENgaTLPPGQEGDIALQVLpeRPFGLFTHYVDN-PSKTASTLRG- 448
Cdd:PRK06334 334 TTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEE--TKVPVSSGETGLVLT--RGTSLFSGYLGEdFGQGFVELGGe 409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568949898 449 SFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIGPFEV-----ESALIEH 494
Cdd:PRK06334 410 TWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
111-516 |
2.03e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 57.03 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdiLY-RLQSSKAKCIITDDTLApAVDAVAAKCENLHS-- 187
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVA-AIFCVPQTLNTLLScl 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 188 ------KLIV----------SQHSREGwgnlKEMMKYA-------SDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHs 244
Cdd:PLN02736 169 seipsvRLIVvvggadeplpSLPSGTG----VEIVTYSkllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 245 sfglglsvngrfwLDLIAS------DVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPI---T 315
Cdd:PLN02736 244 -------------GNLIANvagsslSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAAlrpT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 316 VFCSAPTAYRMLVQNDMSSYK-------------FNSLKHC------------------------------VSAGEPINP 352
Cdd:PLN02736 311 IFCSVPRLYNRIYDGITNAVKesgglkerlfnaaYNAKKQAlengknpspmwdrlvfnkikaklggrvrfmSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 353 EVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKILD--ENGATL--PPGQEGDIALqvlpeR 427
Cdd:PLN02736 391 DVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDvpEMNYTSedQPYPRGEICV-----R 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 428 PFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVESALIEHPSIAESAV--- 502
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVygd 544
|
490 500
....*....|....*....|..
gi 568949898 503 --------VSSPDPirgEVVKA 516
Cdd:PLN02736 545 slnsslvaVVVVDP---EVLKA 563
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
347-553 |
5.77e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 347 GEPINPEVMEQwRKKTGLDIYEGYGQTETvliCGnfkgmkikpGSM--GKPSPAFDVKILDEN----GATLPPGQEGdia 420
Cdd:PRK07824 160 GGPAPAPVLDA-AAAAGINVVRTYGMSET---SG---------GCVydGVPLDGVRVRVEDGRialgGPTLAKGYRN--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 421 lqvLPERPFglFThyvdNPSktastlrgsFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES 500
Cdd:PRK07824 224 ---PVDPDP--FA----EPG---------WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568949898 501 AVVSSPDPIRGEVVKAFIVLNPdyksHDQEQLkKEIQEHVKKTTAPYKYPRKV 553
Cdd:PRK07824 285 AVFGLPDDRLGQRVVAAVVGDG----GPAPTL-EALRAHVARTLDRTAAPREL 332
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
216-539 |
1.42e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.72 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 216 VDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA- 294
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLy 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 295 ----HY--LPR----------FESTSILQTLSKFpitvfcSAPtayrmlvqndmssYKFNSLKHCVSAGEPINPEVMEQW 358
Cdd:PRK08043 439 psplHYriVPElvydrnctvlFGTSTFLGNYARF------ANP-------------YDFARLRYVVAGAEKLQESTKQLW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 359 RKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILD----ENGATL----PPGQEGdiALQVlpERPFG 430
Cdd:PRK08043 500 QDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNG--YLRV--EKPGV 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 431 LFTHYVDNPsktASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVES-ALIEHPSiAESAVVSSPDPI 509
Cdd:PRK08043 576 LEVPTAENA---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDAS 651
|
330 340 350
....*....|....*....|....*....|
gi 568949898 510 RGEvvkAFIVLNPDyKSHDQEQLKKEIQEH 539
Cdd:PRK08043 652 KGE---ALVLFTTD-SELTREKLQQYAREH 677
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-543 |
2.20e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 53.76 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSF-----GLGLSVNGRFW--------------LDLIASDV--MWNT------ 269
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLvagiaGLGDRVPELLGpddrylaylplahiFELAAENVclYRGGtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 270 ----SDTGWAKSAWS-SVFSPwTQGACVfahylPR-FEST-----SILQTLSKFPITVFCSAPTAYRMLVQNDMSSYKFN 338
Cdd:cd17639 164 prtlTDKSKRGCKGDlTEFKP-TLMVGV-----PAiWDTIrkgvlAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 339 S-------------LKHCVSAGEPINPEVMEqWRKKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFD 400
Cdd:cd17639 238 ElvfkkvraalggrLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 401 VKILD--ENG--ATLPPGQeGDIALQvlpeRPFgLFTHYVDNPSKT--ASTLRGSFYiTGDRGYMDEDGYFWFVARSDDI 474
Cdd:cd17639 312 IKLVDweEGGysTDKPPPR-GEILIR----GPN-VFKGYYKNPEKTkeAFDGDGWFH-TGDIGEFHPDGTLKIIDRKKDL 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 475 I-LSSGYRIGPFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNpdykshdQEQLKKEIQEHVKKT 543
Cdd:cd17639 385 VkLQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVIN 444
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
344-523 |
2.71e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.20 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 344 VSAGEPINPEVMEQWRKKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPSpafDVKILDENGAtlpPGQEGDIALQV 423
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFPD---EMCMLGTVGA---PAVYNELRLEE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 424 LPE---RPFG-------------LFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFE 486
Cdd:PLN02430 452 VPEmgyDPLGepprgeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEY 531
|
170 180 190
....*....|....*....|....*....|....*..
gi 568949898 487 VESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNPD 523
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEE 565
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-558 |
3.87e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 49.79 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 53 NFAKDVLDQwtnmekagKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEwwlANV 132
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 133 ACLRT---GTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIVSQHSREG-- 198
Cdd:PRK03584 155 AMLATaslGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPYLGPAAaa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 199 --------WGNLkeMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHssfG---------LGLSvngrfwLDLI 261
Cdd:PRK03584 235 aalpgallWEDF--LAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---GgillehlkeLGLH------CDLG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 262 ASD-VMWNTSdTGWAksAWSSVFSPWTQGACVfahYL----PRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQNDMS-- 333
Cdd:PRK03584 304 PGDrFFWYTT-CGWM--MWNWLVSGLLVGATL---VLydgsPFYPDPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVpg 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 334 -SYKFNSLKHCVSAGEPINPEVMEqWrkktgldIYEGYGQ----------TEtvlICGNFKG----MKIKPGSMGKPSPA 398
Cdd:PRK03584 378 eTHDLSALRTIGSTGSPLPPEGFD-W-------VYEHVKAdvwlasisggTD---ICSCFVGgnplLPVYRGEIQCRGLG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 399 FDVKILDENGATLpPGQEGD-IALQVLPERPFGlFTHYVDNpsktaSTLRGSFYIT-------GDRGYMDEDGYFWFVAR 470
Cdd:PRK03584 447 MAVEAWDEDGRPV-VGEVGElVCTKPFPSMPLG-FWNDPDG-----SRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGR 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK03584 520 SDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD--ALRARIRTTIRTNLSPRHVP 597
|
570
....*....|..
gi 568949898 551 RKV----GVPGT 558
Cdd:PRK03584 598 DKIiavpDIPRT 609
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
341-503 |
1.19e-05 |
|
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: 48.20 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 341 KHCVSA--GEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP---------AFDVKILDENG 408
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfenqVVLVKMDPETD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 409 ATL-----------PPGQEGDIaLQVLPERPFGLFTHYVDNPSKTASTL------RGS-FYITGDRGYMDEDGYFWFVAR 470
Cdd:cd05937 281 DPIrdpktgfcvraPVGEPGEM-LGRVPFKNREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190
....*....|....*....|....*....|...
gi 568949898 471 SDDIILSSGYRIGPFEVESALIEHPSIAESAVV 503
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
393-541 |
1.40e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.08 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 393 GKPSPAFDVKILDENGatlppgqegdialQVLPERPFG--------LFTHYVDNPSKTASTLRGSFYITGDRGYMdEDGY 464
Cdd:PRK09192 388 GKALPGHEIEIRNEAG-------------MPLPERVVGhicvrgpsLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGY 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 465 FWFVARSDDIILSSGYRIGPFEVESALIEHPSI--AESAVVSSPDPiRGEVVKAFI---VLNPDykshDQEQLKKEIQEH 539
Cdd:PRK09192 454 LYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAAL 528
|
..
gi 568949898 540 VK 541
Cdd:PRK09192 529 VR 530
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
172-523 |
1.37e-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: 44.73 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 172 APAVDAVAAkCENLHSKLIVSQHSREGWGNLKemmkYASDSHTCVDTKHDEMMA---------IYFTSGTTGPPKMIGHT 242
Cdd:cd05921 112 APFARALAA-IFPLGTPLVVSRNAVAGRGAIS----FAELAATPPTAAVDAAFAavgpdtvakFLFTSGSTGLPKAVINT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 243 HSSFGLGLSVNGRFWLDLIASD-VMWNtsdtgWAksAWSSVFSpwtqGACVF--------AHYL----P---RFESTsiL 306
Cdd:cd05921 187 QRMLCANQAMLEQTYPFFGEEPpVLVD-----WL--PWNHTFG----GNHNFnlvlynggTLYIddgkPmpgGFEET--L 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 307 QTLSKFPITVFCSAPTAYRMLVQ---ND--MSSYKFNSLKHCVSAGEPINPEVMEQWR----KKTGLDI--YEGYGQTET 375
Cdd:cd05921 254 RNLREISPTVYFNVPAGWEMLVAaleKDeaLRRRFFKRLKLMFYAGAGLSQDVWDRLQalavATVGERIpmMAGLGATET 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 376 VLICGNFKGMKIKPGSMGKPSPAFDVKIldengatLPPGQEGDIAL---QVLPerpfglftHYVDNPSKTASTL-RGSFY 451
Cdd:cd05921 334 APTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVkgpNVTP--------GYWRQPELTAQAFdEEGFY 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949898 452 ITGDRGYM----DEDGYFWFVAR-SDDIILSSG--YRIGPFEVEsALIEHPSIAESAVVSSPDpirGEVVKAFIVLNPD 523
Cdd:cd05921 399 CLGDAAKLadpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAEVGALVFPDLL 473
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-261 |
1.56e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 41.50 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 165 IITDDTLAPAVDAvaakcenlHSKLIVSqhsregWGNLKEMMKYASDSHTC-VDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PTZ00216 221 IIYLDSLPASVDT--------EGCRLVA------WTDVVAKGHSAGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
90
....*....|....*....
gi 568949898 244 SSFGLG-LSVNGRFwLDLI 261
Cdd:PTZ00216 287 GSLTAGiLALEDRL-NDLI 304
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
447-550 |
5.77e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 39.42 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949898 447 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES------------AVVS--SPDPIRGE 512
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568949898 513 VVKAFIVLNPDYKSHDQ--------EQLKKEIQEHVKKTTAPYKYP 550
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
|
| |
