|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-583 |
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: 1092.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 54 IPEYFNFAKDVLDQWTNMEKAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW 133
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMK 213
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 214 CASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 294 QGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIY 373
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLR 453
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSH 533
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 795246185 534 DQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
95-580 |
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: 621.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 175 DvlapavdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTHSsFGL 254
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLV 334
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 335 QNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG 414
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 415 NVLPPGQEGDIGIQVLPNrpfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:cd05972 268 RELPPGEEGDIAIKLPPP---GLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTK 574
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 795246185 575 RNELRK 580
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-583 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 590.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 51 KLEIPEYFNFAKDVLDQWtnmekAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRV 130
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHSKLIV---- 197
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 198 SENSREGWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSD 277
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 278 TGWAKSAWSSVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSA 352
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 353 GEPITPDVTGKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlp 431
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 432 nRPF-GLFAHYADDPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:COG0365 392 -GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 508 VVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-582 |
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: 589.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 43 YESMKQDFKLEIPEYFNFAKDVLDQWTNMEkagkkPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDR 122
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFF-KAMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 123 VILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCIITNDVLAPAVDAIAPKCENLHSKLIVSEN 200
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 201 SREGWGNIKEMMKCASDS----HTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 277 DTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPI 356
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 357 TPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFG 436
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 437 LFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 516
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 517 GEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:cd05970 474 GQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-582 |
8.67e-144 |
|
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: 422.75 E-value: 8.67e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitnd 175
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLAPAVDAiapkcenlhsklivsensregwgnikemmkcasdshtcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05974 74 VYAAVDEN----------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 256 lSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 336 NDMASYKFKsLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGN 415
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 416 vlpPGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVEN 495
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 496 ALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIqELPKTISGKTKR 575
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 795246185 576 NELRKKE 582
Cdd:cd05974 426 VELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
35-582 |
1.98e-137 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 411.60 E-value: 1.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 35 ATPQNFSNYESMKQDFKL-EIPEYF--------NFAKDVLDQWTNMEKAGKkpsnPAFWWInGKGEEVRWSFEELGSLSR 105
Cdd:PRK04319 10 KGEPNLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYL-DASRKEKYTYKELKELSN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaIA 185
Cdd:PRK04319 85 KFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 186 PKCENLHSKLIVSENSREGWG--NIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFW 263
Cdd:PRK04319 162 DDLPSLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 264 LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA--CVFAhhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ--NDMA 339
Cdd:PRK04319 241 LDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 340 S-YKFKSLKHCVSAGEPITPDVTgKWRNKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKIVDVNGN 415
Cdd:PRK04319 318 KkYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 416 VLPPGQEGDIGIQvlPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVEN 495
Cdd:PRK04319 396 ELPPNRMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVES 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 496 ALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:PRK04319 473 KLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
....*..
gi 795246185 576 NELRKKE 582
Cdd:PRK04319 551 RVLKAWE 557
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-582 |
9.08e-127 |
|
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: 379.54 E-value: 9.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 175 DVLAPavdaiapkcenlhsklivsensregwgnikemmkcasdshtcvKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlPRFEPTSVLQTLSKYPITVFCSAATVYRMLV 334
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 335 QND---MASYKFKSLKHCVSAGEPITPDVTgKW-RNKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVK 408
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 409 IVDVNGNVLPPGQEGDIGIQvlPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRI 488
Cdd:cd05969 273 VVDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 489 GPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKT 568
Cdd:cd05969 350 GPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP--SDELKEEIINFVRQKLGAHVAPREIEFVDNLPKT 427
|
490
....*....|....
gi 795246185 569 ISGKTKRNELRKKE 582
Cdd:cd05969 428 RSGKIMRRVLKAKE 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-584 |
2.88e-122 |
|
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: 368.37 E-value: 2.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDQWtnmekAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG0318 3 DLLRRA-----AARHPDRPALVF-----GGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITndvlapavdaiapkcenlhsklivsensregwgnikemmkcasdshtcv 222
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 223 ktkhneiMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTS----DTGWaksaWSSVFSPWIQGACV 298
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 299 faHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYG 377
Cdd:COG0318 171 --VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 378 QTET-VLICGNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:COG0318 249 LTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 456 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQ 535
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDA 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 536 EQLIKEIQEHVkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:COG0318 403 EELRAFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-579 |
4.51e-120 |
|
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: 362.13 E-value: 4.51e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 89 KGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 169 NCIITNDVLAPAVdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTAHT 248
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSsFGLGLSVNGRFWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 327 ATVYRML-VQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPA 404
Cdd:cd05971 189 PTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 405 FDVKIVDVNGNVLPPGQEGDIGIQvLPNrPFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVE-LPD-PV-AFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQE 564
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNE 423
|
490
....*....|....*
gi 795246185 565 LPKTISGKTKRNELR 579
Cdd:cd05971 424 LPRTATGKIRRRELR 438
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-580 |
6.66e-109 |
|
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: 333.72 E-value: 6.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNd 175
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 vlapavdaiapkCENLHsklivsensregwgnikemmKCASDshtcvktkhneIMAMFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05973 80 ------------AANRH--------------------KLDSD-----------PFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 336 NDMASYKFK--SLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIVD 411
Cdd:cd05973 195 AGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 412 VNGNVLPPGQEGDIGIQVlPNRPFGLFAHYADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPF 491
Cdd:cd05973 275 DDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISG 571
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
....*....
gi 795246185 572 KTKRNELRK 580
Cdd:cd05973 429 KIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-579 |
5.36e-104 |
|
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: 321.82 E-value: 5.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDqwtnmEKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:cd05936 3 DLLE-----EAARRFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLApavDAIAPKcenlHSKLIVSENSREgwgnikemmkcasdshtcv 222
Cdd:cd05936 72 AGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFT---DLLAAG----APLGERVALTPE------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 223 ktkhnEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWL--DLTPSDVMWNT-------SDTgwaksawSSVFSPWI 293
Cdd:cd05936 126 -----DVAVLQYTSGTTGVPKGAMLTHRNLVANALQI-KAWLedLLEGDDVVLAAlplfhvfGLT-------VALLLPLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 294 QGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDI 372
Cdd:cd05936 193 LGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKT 448
Cdd:cd05936 271 VEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELwvrGPQV--------MKGYWNRPEET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP 528
Cdd:cd05936 343 AEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 795246185 529 DykshdqEQLIK-EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05936 423 G------ASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
228-572 |
4.77e-102 |
|
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: 312.30 E-value: 4.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFahHLPRFE 307
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVV--LLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDM-ASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET--VLI 384
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGY 464
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-GPS----VMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQE 544
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330 340
....*....|....*....|....*...
gi 795246185 545 HVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-579 |
9.46e-102 |
|
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: 317.39 E-value: 9.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 56 EYFNFAKDVLDQwtnmeKAGKKPSNPAFwwINGKGEevrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWL 135
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSRE--GWGNIKEMMK 213
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 214 CASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSP-W 292
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 293 IQGACVFahhLP-RFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGL 370
Cdd:cd05959 230 VGATTVL---MPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 371 DIYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFglfahYADDPSKTA 449
Cdd:cd05959 307 DILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 450 STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd05959 381 DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 795246185 530 YKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05959 461 YE--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-579 |
2.40e-96 |
|
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: 301.32 E-value: 2.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaNCI 171
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLAPAVdaiapkcenlhsklivsensregwgnikemmkcasdshtcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05958 84 ITVALCAHAL------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 252 FGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYR 331
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 332 -MLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIV 410
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 411 DVNGNVLPPGQEGDIGIQvlpnRPFGlfAHYADDPSKtASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 490
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTG--CRYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 491 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTIS 570
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 795246185 571 GKTKRNELR 579
Cdd:cd05958 431 GKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
62-584 |
3.62e-91 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 290.16 E-value: 3.62e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 62 KDVLDQWtnmekAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACL 141
Cdd:PRK06187 9 GRILRHG-----ARKHPDKEAVYF-----DGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 142 RTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREG----WGNIKEMMKCASD 217
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 218 SHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWAksawssvFSP 291
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 292 WIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTGKWRNKTGL 370
Cdd:PRK06187 230 LMAGAKQVIPR--RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 371 DIYEGYGQTETV-LICGNF-----KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGqEGDIG-IQVL-PNrpfgLFAHYA 442
Cdd:PRK06187 308 DLVQGYGMTETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVRgPW----LMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 443 DDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 522
Cdd:PRK06187 383 NRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795246185 523 FIVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:PRK06187 463 VVVLKPG-ATLDAKELRAFLRGRL----AKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
71-581 |
7.90e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.92 E-value: 7.90e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 71 MEKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK07656 12 ARAARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV----SENSREGWGNIKEMMKCASDSHTCVKTKH 226
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 227 NEIMAMFFTSGTSGYPK--MTAHTHSsfglgLSvNGRFW---LDLTPSD---------------VMWNTsdtgwaksaws 286
Cdd:PRK07656 166 DDVADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 287 svfsPWIQGACVFAHhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTGKWR 365
Cdd:PRK07656 229 ----PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 366 NKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHY 441
Cdd:PRK07656 303 SELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 442 ADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVV 520
Cdd:PRK07656 378 YDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795246185 521 KAFIVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK07656 458 KAYVVLKPG-AELTEEELIAYCREHL----AKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
74-572 |
7.07e-80 |
|
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: 258.31 E-value: 7.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd17631 5 ARRHPDRTALVF-----GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 LTQKDILYRLQSSKAnciitndvlapavdaiapkcenlhsKLIVSENSRegwgnikemmkcasdshtcvktkhneimaMF 233
Cdd:cd17631 79 LTPPEVAYILADSGA-------------------------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGwaksawSSVFSPWIQGACVfaHHLPRFE 307
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVllvvapLFHIGGLG------VFTLPTLLRGGTV--VILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRnKTGLDIYEGYGQTETV-LIC 385
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 GNFKGMKI-KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGY 464
Cdd:cd17631 255 FLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG-PH----VMAGYWNRPEATAAAFRDGWFHTGDLGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqE 544
Cdd:cd17631 330 LDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG-AELDEDELI----A 404
|
490 500
....*....|....*....|....*...
gi 795246185 545 HVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd17631 405 HCRERLARYKIPKSVEFVDALPRNATGK 432
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
96-579 |
1.04e-79 |
|
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: 257.78 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 vlapavDAIApkcenlhsklivsensregwgnikemmkcasdshtcvktkhneimAMFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05919 91 ------DDIA---------------------------------------------YLLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFAHHLPrfEPTSVLQTLSKYPITVFCSAATVY-RML 333
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYaNLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 334 VQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN 413
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 414 GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 493
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 494 ENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKT 573
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
....*.
gi 795246185 574 KRNELR 579
Cdd:cd05919 431 QRFKLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
77-572 |
1.50e-78 |
|
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: 259.05 E-value: 1.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 77 KPSNPAFWWINGKGEEVR-WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLT 155
Cdd:cd17634 66 NGDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 156 QKDILYRLQSSKANCIITND----------VLAPAVDAIAPKCENLHSKLIVSensREG---------WGNIKEMMKCAS 216
Cdd:cd17634 145 PEAVAGRIIDSSSRLLITADggvragrsvpLKKNVDDALNPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKAS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 217 DSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA 296
Cdd:cd17634 222 PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 297 CVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSAGEPITPDvTGKWR----NK 367
Cdd:cd17634 302 TTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPE-AYEWYwkkiGK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 368 TGLDIYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQV-LPNRPFGLFAhyaDD 444
Cdd:cd17634 381 EKCPVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpWPGQTRTLFG---DH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 445 PSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 522
Cdd:cd17634 458 ERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 795246185 523 FIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd17634 538 YVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGK 585
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
56-580 |
3.32e-78 |
|
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: 255.92 E-value: 3.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 56 EYFNFAKDVLDqwTNMEKAgkKPSNPAFwwINGKGeevRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWL 135
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVEG--RGGKTAF--IDDIS---SLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSkLIVSENSREGWGNIKEMMKCA 215
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 216 SDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQG 295
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 296 ACVFAHHlPRFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYE 374
Cdd:TIGR02262 230 ATTVLMG-ERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRG 454
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShd 534
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 795246185 535 qeqLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-580 |
4.46e-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: 253.25 E-value: 4.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 59 NFAKDVLDQWtnmekAGKKPSNPAFWWI-NGKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:cd05966 53 NISYNCLDRH-----LKERGDKVAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 138 VACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND---------VLAPAVDAIAPKCENLHsKLIVSENS---- 201
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTggev 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 202 -----REGWGNikEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05966 203 pmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 277 DTGWAKSAWSSVFSPWIQGAcvfahhlprfepTSVL--------------QTLSKYPITVFCSAATVYRMLVQ---NDMA 339
Cdd:cd05966 281 DIGWITGHSYIVYGPLANGA------------TTVMfegtptypdpgrywDIVEKHKVTIFYTAPTAIRALMKfgdEWVK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 340 SYKFKSLKHCVSAGEPITP-------DVTGKWRnktgLDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDV 407
Cdd:cd05966 349 KHDLSSLRVLGSVGEPINPeawmwyyEVIGKER----CPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 408 KIVDVNGNVLPPGQEGDIGIQvlpnRPFglfahyaddPSkTASTLRGN--------------FYITGDRGYMDEDGYFWF 473
Cdd:cd05966 422 AILDEEGNEVEGEVEGYLVIK----RPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLIKEIQEHVKKTTAPY 553
Cdd:cd05966 488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPI 565
|
570 580
....*....|....*....|....*..
gi 795246185 554 KYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05966 566 ATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
68-583 |
6.97e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 251.03 E-value: 6.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 68 WTNMEKAGKK-PSNPAFWWIngkGEEVrwSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTV 146
Cdd:PRK08314 13 FHNLEVSARRyPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 147 LIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAV------------------DAIAPKCE-----NLHSKLIVSENSRE 203
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 204 GWGNIKEMMKC--ASDSHTcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSD---- 277
Cdd:PRK08314 168 GVVAWKEALAAglAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 278 TGWAKSAWSSVFSpwiqGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATvyrMLV----QNDMASYKFKSLKHCVSAG 353
Cdd:PRK08314 244 TGMVHSMNAPIYA----GATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 354 EPITPDVTGKWRNKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GIQ 428
Cdd:PRK08314 315 AAMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIvvhGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 429 VlpnrpfglFAHYADDPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVA 504
Cdd:PRK08314 394 V--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795246185 505 ESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-484 |
1.11e-75 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 246.46 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFwwinGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:pfam00501 3 RQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 152 TQLTQKDILYRLQSSKANCIITNDVL-APAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSH-TCVKTKHNEI 229
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 230 MAMFFTSGTSGYPKMTAHTH---SSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFAHHLPR 305
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET--- 381
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKrALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDI---GIQVLPnrpfGlfahYADDPSKTASTL-RGNF 456
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELcvrGPGVMK----G----YLNDPELTAEAFdEDGW 389
|
410 420
....*....|....*....|....*...
gi 795246185 457 YITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
96-578 |
6.93e-74 |
|
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: 242.38 E-value: 6.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 vlapavdaiapkcenlHSKLivsensregwgnikemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 336 N-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDV-N 413
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIeT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 414 GNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 489
Cdd:cd05935 270 GRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKVEFIQELPKTI 569
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 795246185 570 SGKTKRNEL 578
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
77-580 |
3.85e-72 |
|
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: 242.99 E-value: 3.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 77 KPSNPAFWWING-KGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTV--LIPG--- 150
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 151 TTQLTQkdilyRLQSSKANCIITNDV---------LAPAVD-AIA------PKCENLHSKLIVSENSREG-WGNIKEMMK 213
Cdd:cd05967 143 AKELAS-----RIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHHVLVLNRPQVPADLTKPGrDLDWSELLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 214 CASdSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05967 218 KAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 294 QGA-CVFAHHLPRF--EPTSVLQTLSKYPITVFCSAATVYRMLVQND-----MASYKFKSLKHCVSAGEPITPDvTGKW- 364
Cdd:cd05967 297 HGAtTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPP-TLEWa 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 365 RNKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGLFAH 440
Cdd:cd05967 376 ENTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 441 YADDP---SKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:cd05967 455 WKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKG 533
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795246185 518 EVVKAFIVLNPDYKShDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05967 534 QVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
91-572 |
1.45e-71 |
|
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: 237.88 E-value: 1.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITN----DVLAPAVDAIAPKcenlhSKLIVSENSREGWGNIKEMMK---CASDSH--TCVKTKHNEIMAMFFTSGTSGY 241
Cdd:cd05911 86 IFTDpdglEKVKEAAKELGPK-----DKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 242 PKMTAHTHSSFGLGL-SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWiQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:cd05911 161 PKGVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TVFCSAATVYRMLVQNDMA-SYKFKSLKHCVSAGEPITPDVTGKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSM 398
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLdKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWF 473
Cdd:cd05911 318 GRLLPNVEAKIVDDDGKdSLGPNEPGEIcvrGPQV--------MKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqliKEIQEHVKKTTAPY 553
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASY 464
|
490 500
....*....|....*....|
gi 795246185 554 KYPRK-VEFIQELPKTISGK 572
Cdd:cd05911 465 KQLRGgVVFVDEIPKSASGK 484
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-579 |
6.13e-71 |
|
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: 234.11 E-value: 6.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 ndvlAPAvdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhneimAMFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05934 82 ----DPA--------------------------------------------------SILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 254 LGLSVNGRfWLDLTPSDVMW--------NTSDTGWAkSAWSSvfspwiQGACVFahhLPRFEPTSVLQTLSKYPITVFCS 325
Cdd:cd05934 108 FAGYYSAR-RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 326 AATVYRMLVQ-----NDMAsykfkslkHCVSA--GEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSM 398
Cdd:cd05934 177 LGAMLSYLLAqppspDDRA--------HRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd05934 249 GRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK-SHDqeqlikEIQEHVKKTTAPYKYPR 557
Cdd:cd05934 327 DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE------ELFAFCEGQLAYFKVPR 400
|
490 500
....*....|....*....|..
gi 795246185 558 KVEFIQELPKTISGKTKRNELR 579
Cdd:cd05934 401 YIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
48-584 |
6.00e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 224.91 E-value: 6.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 48 QDFKLEIPEYFNFAKDVLDQWTNmEKAGKKPSNPAFWWIngkGEEVrwSFEELGSLSRKFANILsEACSLQRGDRVILIL 127
Cdd:PRK06710 9 KSYPEEIPSTISYDIQPLHKYVE-QMASRYPEKKALHFL---GKDI--TFSVFHDKVKRFANYL-QKLGVEKGDRVAIML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 128 PRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAV-------------------------D 182
Cdd:PRK06710 82 PNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVtnvqsatkiehvivtriadflpfpkN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 183 AIAPKCENLHSKLIVSENSREG---WGNIKEMMKCASDShTCvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVN 259
Cdd:PRK06710 162 LLYPFVQKKQSNLVVKVSESETihlWNSVEKEVNTGVEV-PC--DPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 260 GRFWLD--LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQND 337
Cdd:PRK06710 238 GVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 338 M-ASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFDVKIVDV-NG 414
Cdd:PRK06710 316 LlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLeTG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 415 NVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPF 491
Cdd:PRK06710 396 EALPPGEIGEIvvkGPQIMKG--------YWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISG 571
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE-----ELNQFARKYLAAYKVPKVYEFRDELPKTTVG 542
|
570
....*....|...
gi 795246185 572 KTKRNELRKKEWK 584
Cdd:PRK06710 543 KILRRVLIEEEKR 555
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-580 |
2.23e-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: 217.54 E-value: 2.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCiit 173
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 ndVLAPAVdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05941 88 --VLDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 254 LGLSVNGRFWlDLTPSDV------------MWNtsdtgwaksawsSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYPIT 321
Cdd:cd05941 116 ANVRALVDAW-RWTEDDVllhvlplhhvhgLVN------------ALLCPLFAGASV--EFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 322 VFCSAATVYRMLVQ---------NDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGN-FKGm 391
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDG- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 392 KIKPGSMGKPSPAFDVKIVDVNGNvlPPGQEGDIG-IQVlpnRPFGLFAHYADDPSKTASTLRG-NFYITGDRGYMDEDG 469
Cdd:cd05941 260 ERRPGTVGMPLPGVQARIVDEETG--EPLPRGEVGeIQV---RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 470 YFWFVAR-SDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLIkeiqEHVKK 548
Cdd:cd05941 335 YYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWAKQ 410
|
490 500 510
....*....|....*....|....*....|..
gi 795246185 549 TTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05941 411 RLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
95-580 |
2.43e-64 |
|
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: 218.72 E-value: 2.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 NDVLAPAVD-AIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEIMAMF-FTSGTSGYPKMTAHTHSS 251
Cdd:cd05926 94 KGELGPASRaASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALIlHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 252 fgLGLSV-NGRFWLDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiQGACVFAhhlPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05926 174 --LAASAtNITNTYKLTPDDrtlvVMPLFHVHGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYNATWYTAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 327 ATVYRMLVQNDMASY--KFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETV--LICGNFKGMKIKPGSMGKPS 402
Cdd:cd05926 246 PTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 403 PAfDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTA-STLRGNFYITGDRGYMDEDGYFWFVARSDDII 481
Cdd:cd05926 326 GV-EVRILDEDGEILPPGVVGEICLRG-PNVTRG----YLNNPEANAeAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 482 LSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKVEF 561
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-----TEEELRAFCRKHLAAFKVPKKVYF 474
|
490
....*....|....*....
gi 795246185 562 IQELPKTISGKTKRNELRK 580
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-579 |
1.25e-63 |
|
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: 220.05 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 59 NFAKDVLDQWTnmekaGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHSKLIVSENSRE-GWGNI 208
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 209 K-----EMMKCASDSHTcvKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:cd05968 215 RdlsydEEKETAGDGAE--RTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 284 AWSsVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLV---QNDMASYKFKSLKHCVSAGEPITP 358
Cdd:cd05968 293 PWL-IFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 359 DvTGKW----RNKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPgQEGDIGIQvlpnR 433
Cdd:cd05968 372 E-PWNWlfetVGKGRNPIINYSGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL----A 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 434 PF-GLFAHYADDPSKTASTLRG---NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd05968 446 PWpGMTRGFWRDEDRYLETYWSrfdNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795246185 510 SSPDPIRGEVVKAFIVLNPDYKSHD--QEQLIKEIQEHVKKttaPYKyPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05968 526 GVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGK---PLS-PERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
106-580 |
3.16e-62 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 216.55 E-value: 3.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND------- 175
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 --VLAPAVD-AIApKCENLHSKLIVS--------ENSREGWGNikEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKM 244
Cdd:PRK00174 186 piPLKANVDeALA-NCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 245 TAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhlprFE--PT--------SVLQt 314
Cdd:PRK00174 263 VLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLM-----FEgvPNypdpgrfwEVID- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 315 lsKYPITVFCSAATVYRMLVQ---NDMASYKFKSLKHCVSAGEPITPDVtgkWR---NKTGLD---IYEGYGQTET--VL 383
Cdd:PRK00174 337 --KHKVTIFYTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINPEA---WEwyyKVVGGErcpIVDTWWQTETggIM 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 384 IC---GnfkGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPF-----GLFAhyadDPS---KTA-ST 451
Cdd:PRK00174 412 ITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPWpgmmrTIYG----DHErfvKTYfST 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 452 LRGNfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK 531
Cdd:PRK00174 481 FKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE 559
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 532 SHDqeQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK00174 560 PSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-580 |
1.48e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 209.40 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSRE---GWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 248 THSSFgLGLSVNGRFWLDLTPSDVMWNtsdtgwA----KSAWSSVF-SPWIQ-GACVfaHHLPRFEPTSVLQTLSKYPIT 321
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 322 VFCSAATVYRMLVQN-DMASYKFKSLKHCVSaGEPITP-DVTGKWRNK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 393
Cdd:PRK08316 263 SFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 394 KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWF 473
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI-----VHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqEHVKKTTAPY 553
Cdd:PRK08316 414 VDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTEDELI----AHCRARLAGF 488
|
490 500
....*....|....*....|....*..
gi 795246185 554 KYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK08316 489 KVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
72-578 |
1.86e-59 |
|
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: 205.93 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFwwING-KGEEVrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd05904 13 LFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTC-VKTKHNEI 229
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPvVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 230 MAMFFTSGTSGYPK-----------MTAHTHSSFGLGLSVNGRFWLDLTPSDVMwntsdtGWAKSAWSSVFSpwiqGACV 298
Cdd:cd05904 161 AALLYSSGTTGRSKgvmlthrnliaMVAQFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 299 FAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMA-SYKFKSLKHCVSAGEPITPDVTGKWRNK-TGLDIYEGY 376
Cdd:cd05904 231 VV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTL 452
Cdd:cd05904 309 GMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 RGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyk 531
Cdd:cd05904 384 DKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 795246185 532 SHDQEQlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05904 462 SSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
88-584 |
1.76e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 200.52 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 88 GKGEEvrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 167
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 168 ANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEimaMFFTSGTSGYPK---- 243
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD---MLYSSGTTGRPKgikr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 244 --MTAHTHSSFGLGLSVNGrFWLDLTPSDV------MWNTSDTGWaksawssvfspwiqgaCVFAHHL-------PRFEP 308
Cdd:PRK08276 161 plPGLDPDEAPGMMLALLG-FGMYGGPDSVylspapLYHTAPLRF----------------GMSALALggtvvvmEKFDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 309 TSVLQTLSKYPITVFCSAATVY-RML-----VQndmASYKFKSLKHCVSAGEPITPDVtgKWR--NKTGLDIYEGYGQTE 380
Cdd:PRK08276 224 EEALALIERYRVTHSQLVPTMFvRMLklpeeVR---ARYDVSSLRVAIHAAAPCPVEV--KRAmiDWWGPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 381 ----TVLICGNFKGmkiKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFglfaHYADDPSKTASTLRGNF 456
Cdd:PRK08276 299 gggvTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 457 YIT-GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQ 535
Cdd:PRK08276 370 WVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 536 EQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:PRK08276 448 DALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
94-581 |
6.48e-57 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 199.33 E-value: 6.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 NDVLAPAVDAIAPKCENLHskliVSENSREGWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPK--MTAHTH-S 250
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFGLGLSVNGRFwldlTPSDVMwntsdtgwaksawssvfspwIQGACVFAHH------------------LPRFEPTSVL 312
Cdd:PRK07514 183 SNALTLVDYWRF----TPDDVL--------------------IHALPIFHTHglfvatnvallagasmifLPKFDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 313 QTLSKypITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGN-FKG 390
Cdd:PRK07514 239 ALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 391 MKIkPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGN-FYITGDRGYMDED 468
Cdd:PRK07514 317 ERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG-PN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDER 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 469 GYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIKEIQEHVkk 548
Cdd:PRK07514 391 GYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL-- 467
|
490 500 510
....*....|....*....|....*....|...
gi 795246185 549 ttAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK07514 468 --ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
95-580 |
9.27e-56 |
|
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: 193.72 E-value: 9.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEEL----GSLSRKFANIlseacSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05912 2 YTFAELfeevSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 iitndvlapavdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhNEIMAMFFTSGTSGYPK---MTAH 247
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKgvqQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 248 TH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPIT 321
Cdd:cd05912 101 NHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 322 VFCSAATVYRMLVQNDMASYKfKSLKHCVSAGEPITPDVTGKWRNKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 399
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 400 KPSPAFDVKIVDVNGnvlPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDD 479
Cdd:cd05912 246 KPLFPVELKIEDDGQ---PPYEVGEILLKG-PNVTKG----YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 480 IILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQLIKEIQEHVKKttapYKYPRKV 559
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKVPKKI 390
|
490 500
....*....|....*....|.
gi 795246185 560 EFIQELPKTISGKTKRNELRK 580
Cdd:cd05912 391 YFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-578 |
4.11e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 195.64 E-value: 4.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDQWtnmekAGKKPSNPAFWWIngkGEEVrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK06178 37 EYLRAW-----ARERPQRPAIIFY---GHVI--TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLH------SKLIVSENSR-------------E 203
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHvivtslADVLPAEPTLplpdslraprlaaA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 204 GWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:PRK06178 186 GAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 284 AWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVfcsaaTVyrMLVQN--------DMASYKFKSLKH--CVSAG 353
Cdd:PRK06178 266 ENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTR-----TV--MLVDNavelmdhpRFAEYDLSSLRQvrVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 354 EPITPDVTGKWRNKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEG 423
Cdd:PRK06178 337 KKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 424 DIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSV 503
Cdd:PRK06178 416 EIVV-----RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 504 AESAVVSSPDPIRGEVVKAFIVLNPDyksHDQEQliKEIQEHVKKTTAPYKYPrKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK06178 491 LGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
92-579 |
8.94e-55 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 194.21 E-value: 8.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLAPAVDAIAPKCENLHSKLIVSENSRE----GWGNIKemMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVsvpaGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 248 THSSFglglsvngrFW--------LDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYP 319
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 320 ITV-FCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPitPDVTGKWRNKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 398
Cdd:PRK06155 269 ATVtYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 478
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRK 558
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALV----RHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|.
gi 795246185 559 VEFIQELPKTISGKTKRNELR 579
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLR 519
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
94-580 |
1.70e-54 |
|
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: 191.05 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPrvpEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVlapavdaiapkcenlhsklivsensregWG--NIKEMmkcasdshtcvktkHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:cd05903 77 FVVPER----------------------------FRqfDPAAM--------------PDAVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSfglgLSVNGRFW---LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYPITVFCS 325
Cdd:cd05903 115 HNT----LSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 326 AAT-VYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICGNfkgmkIKPG-------S 397
Cdd:cd05903 189 ATPfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrlyT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 398 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 477
Cdd:cd05903 264 DGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 478 DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEHV-KKTTAPYKYP 556
Cdd:cd05903 339 KDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS-----GALLTFDELVAYLdRQGVAKQYWP 413
|
490 500
....*....|....*....|....
gi 795246185 557 RKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05903 414 ERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
304-582 |
3.61e-53 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 190.26 E-value: 3.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 304 PRFEPTSVlQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTE-T 381
Cdd:PRK08974 285 PRDIPGFV-KELKKYPFTAITGVNTLFNALLNNeEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGNFYI 458
Cdd:PRK08974 364 PLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELwvkGPQVMLG--------YWQRPEATDEVIKDGWLA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdyKSHDQEQL 538
Cdd:PRK08974 436 TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEEL 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 795246185 539 IKEIQEHVkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK08974 514 ITHCRRHL----TGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-582 |
7.19e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 187.86 E-value: 7.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPKcenlhsklivsensregwgNIKEMMKCASDSHTCVKTKH-NEIMAMFFTSGTSGYPK---MTA 246
Cdd:PRK03640 103 LITDDDFEAKLIPGISV-------------------KFAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKgviQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 247 HTH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK03640 164 GNHwwsavgSALNLGLTEDDC-WLAAVP---IFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TVFCSAAT-VYRMLVQNDMASYKfKSLKHCVSAGEPITPDVTGKWRNKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 397
Cdd:PRK03640 231 TIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 398 MGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 477
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKG-PNVTKG----YLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 478 DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyKSHDQEQLIKEIQEHVkkttAPYKYPR 557
Cdd:PRK03640 383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRHFCEEKL----AKYKVPK 455
|
490 500
....*....|....*....|....*
gi 795246185 558 KVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK03640 456 RFYFVEELPRNASGKLLRHELKQLV 480
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
76-575 |
1.59e-52 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 189.77 E-value: 1.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 76 KKPSNPAFWWINGK-GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPG- 150
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 151 -TTQLTQkdilyRLQSSKANCIITND-------VLA--PAVDAIAPKCENLHSK-LIVSENsregwgnIKEMMKCASDSH 219
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADagsrggkVVPykPLLDEAIALAQHKPRHvLLVDRG-------LAPMARVAGRDV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 220 --TCVKTKH------------NEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAW 285
Cdd:PRK10524 212 dyATLRAQHlgarvpvewlesNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 286 SSVFSPWIQG-ACVFAHHLP-RFEPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSAGEPITpDV 360
Cdd:PRK10524 292 YIVYAPLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEPLD-EP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 361 TGKWRNKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQV-LPnr 433
Cdd:PRK10524 371 TASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGpLP-- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 434 PFGLFAHYADDP---SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVS 510
Cdd:PRK10524 449 PGCMQTVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 511 SPDPIRGEVVKAFIVLNPDYKSHDQEQ---LIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:PRK10524 529 VKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-578 |
1.85e-52 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 186.99 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDShtcvktkhneiMAMFFTSGTSGYPKMTAHTH 249
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESAS-----------FIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSFGLGlSVNGRFWLDLTPSDV------MWNTSDTGWAksawssVFSPWIQGACVFAHHlpRFEPTSVLQTLSKYPITVF 323
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 324 CSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKtGLDIYEGYGQTET-----VLICGNFKGmkiKPGS 397
Cdd:PRK06839 243 MGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 398 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 477
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRG-PN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 478 DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqliKEIQEHVKKTTAPYKYPR 557
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPK 468
|
490 500
....*....|....*....|.
gi 795246185 558 KVEFIQELPKTISGKTKRNEL 578
Cdd:PRK06839 469 EIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-583 |
3.02e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 187.12 E-value: 3.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 78 PSNPAFWWINGkgeevRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIP-GTTQ 153
Cdd:PRK06188 26 PDRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 ltqkDILYRLQSSKANCIITNDvlAPAVD---AIAPKCENLhsKLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEIM 230
Cdd:PRK06188 100 ----DHAYVLEDAGISTLIVDP--APFVEralALLARVPSL--KHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 231 AMFFTSGTSGYPKMTAHTHSSFG---------LGLSVNGRFwLDLTPsdvmwnTSDTGWAKsawssvFSPWIQ-GACVfa 300
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIAtmaqiqlaeWEWPADPRF-LMCTP------LSHAGGAF------FLPTLLrGGTV-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 301 HHLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDvtgkwRNKTGLDIY-----E 374
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITaTFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERFgpifaQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTE-----TVLICGNFKGMKIKP-GSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKT 448
Cdd:PRK06188 312 YYGQTEapmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP 528
Cdd:PRK06188 387 AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 529 DyKSHDQEqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:PRK06188 467 G-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW 516
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
96-579 |
3.33e-52 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 187.54 E-value: 3.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLAPAVDAIAPKCENLH------------SKLIVSENSRegwgNIKEMMkcasdshtcvktkhneimamfftsgtsgyPK 243
Cdd:PRK07059 129 NFATTVQQVLAKTAVKHvvvasmgdllgfKGHIVNFVVR----RVKKMV-----------------------------PA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 244 MTAHTHSSFGLGLSVNGRFWL---DLTPSDV---MWNTSDTGWAKSA-------WSSVF--SPWIQGA------------ 296
Cdd:PRK07059 176 WSLPGHVRFNDALAEGARQTFkpvKLGPDDVaflQYTGGTTGVSKGAtllhrniVANVLqmEAWLQPAfekkprpdqlnf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 297 -C------VFA-------------HHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVS 351
Cdd:PRK07059 256 vCalplyhIFAltvcgllgmrtggRNIlipnPRDIP-GFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 352 AGEPITPDVTGKWRNKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---G 426
Cdd:PRK07059 335 GGMAVQRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEIcirG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 427 IQVLpnrpfglfAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAE 505
Cdd:PRK07059 414 PQVM--------AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 506 SAVVSSPDPIRGEVVKAFIVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK07059 486 VAAVGVPDEHSGEAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
68-581 |
4.11e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 186.91 E-value: 4.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 68 WTNM--EKAGKKPSNPAFWWingKGEEVRWSfeELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGT 145
Cdd:PRK07786 19 WVNQlaRHALMQPDAPALRF---LGNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 146 VLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP---AVDAIAPKcenLHSKLIVSENSREGWGNIKEMMKCASDSHTCV 222
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPvatAVRDIVPL---LSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 223 KTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGlGLSVNG-RFWLDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVFAH 301
Cdd:PRK07786 170 DIPNDSPALIMYTSGTTGRPKGAVLTHANLT-GQAMTClRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 302 HLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLvqnDMASYKFKSLK-HCVSAGEPITPDVTGKWRNKT--GLDIYEGYG 377
Cdd:PRK07786 248 PLGAFDPGQLLDVLEAEKVTgIFLVPAQWQAVC---AEQQARPRDLAlRVLSWGAAPASDTLLRQMAATfpEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 378 QTE----TVLICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFAHYADDPSKTASTLR 453
Cdd:PRK07786 325 QTEmspvTCMLLGEDAIRKL--GSVGKVIPTVAARVVDENMNDVPVGEVGEI-----VYRAPTLMSGYWNNPEATAEAFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyksh 533
Cdd:PRK07786 398 GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 795246185 534 DQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
303-575 |
5.39e-52 |
|
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: 181.31 E-value: 5.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 303 LPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHcVSAGEpiTPDVTGKWRNKTGLDIYEGYGQTET 381
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILsNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 ---VLICGNFKgmkiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI 458
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 459 TGDRGYMDEDGYFWFVARS--DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQE 536
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG-ATLTAD 298
|
250 260 270
....*....|....*....|....*....|....*....
gi 795246185 537 QLIkeiqEHVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:cd17637 299 ELI----EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-580 |
2.25e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 185.59 E-value: 2.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDQwtNMEKAGKKPsnpAFWWInGKGEevrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK05605 36 DLYDN--AVARFGDRP---ALDFF-GATT----TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP---------------AVDAIA--PKCENLHSKLIVS--ENSRE 203
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAamPLLQRLALRLPIPalRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 204 G----------WGNI-KEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVN---GRFWLDLTPS 269
Cdd:PRK05605 185 AltgpapgtvpWETLvDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR----NLFANaaqGKAWVPGLGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 270 D----------------VMWNTsdtgwaksawssvFSPWIQGACVFahhLPRFEPTSVLQTLSKYPITVFCSAATVYRML 333
Cdd:PRK05605 261 GpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 334 VqnDMASYK---FKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKI 409
Cdd:PRK05605 325 A--EAAEERgvdLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 410 VDVN--GNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:PRK05605 403 VDPEdpDETMPDGEEGELlvrGPQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLikeiQEHVKKTTAPYKYPRKVEFIQE 564
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGL----RAYCREHLTRYKVPRRFYHVDE 549
|
570
....*....|....*.
gi 795246185 565 LPKTISGKTKRNELRK 580
Cdd:PRK05605 550 LPRDQLGKVRRREVRE 565
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-579 |
9.83e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 182.52 E-value: 9.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK13390 22 GEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIitndVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDShtcvKTKHNEIMAMFFTSGTSGYPK-----M 244
Cdd:PRK13390 99 VL----VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPR----LTEQPCGAVMLYSSGTTGFPKgiqpdL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 245 TAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS-AWSSVFSPwIQGACVFAHhlpRFEPTSVLQTLSKYPITVF 323
Cdd:PRK13390 171 PGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 324 CSAATVY-RMLVQND--MASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTE----TVLICGNFKGmkiKPG 396
Cdd:PRK13390 247 QMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 397 SMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIQ--VLPNRpfglfahYADDPSKTASTLRGN--FYIT-GDRGYMDEDGYF 471
Cdd:PRK13390 324 SVGR-SVLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTA 551
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELARELIDYTRSRIA 473
|
490 500
....*....|....*....|....*...
gi 795246185 552 PYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK13390 474 HYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-579 |
1.63e-50 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 182.19 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANiLSEACSLQRGDRVILILPRVPEW---WLAnVACLrtGTVLI 148
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 149 PGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCEN-LHSKLIVSENSREGWGNIKEMMKCASDSHTCVKT--- 224
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPADDGVSSFTQLKAQQPATLCYAppl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 225 KHNEIMAMFFTSGTSGYPKMTAHTHSsfglglsvNGRFwldltpsdvmwntsdtgwaksawSSVFSPWiQGA-------- 296
Cdd:PRK08008 171 STDDTAEILFTSGTTSRPKGVVITHY--------NLRF-----------------------AGYYSAW-QCAlrdddvyl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 297 -CVFAHH--------LPRFEPTSVLQTLSKYPITVFCSAATVYR-------------MLVQNDMASYKfkslKHC---VS 351
Cdd:PRK08008 219 tVMPAFHidcqctaaMAAFSAGATFVLLEKYSARAFWGQVCKYRatitecipmmirtLMVQPPSANDR----QHClreVM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 352 AGEPITPDVTGKWRNKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVL 430
Cdd:PRK08008 295 FYLNLSDQEKDAFEERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 431 PNRPfgLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK08008 375 PGKT--IFKEYYLDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795246185 510 SSPDPIRGEVVKAFIVLNPDykshdqEQL-IKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK08008 453 GIKDSIRDEAIKAFVVLNEG------ETLsEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-579 |
3.52e-50 |
|
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: 176.70 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSFglgLSvNGRF---WLDLTPSDVM----------------WNTSDTGwaksawssvfspw 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI---VN-NGYFigeRLGLTEQDRLcipvplfhcfgsvlgvLACLTHG------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 293 iqGACVFAHhlPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGL- 370
Cdd:cd05917 70 --ATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 371 DIYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKIVDVNGNVLPP-GQEGDIGIqvlpnRPFGLFAHYADD 444
Cdd:cd05917 146 DVTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCI-----RGYSVMKGYWND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 445 PSKTASTLRG-NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:cd05917 219 PEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 524 IVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05917 299 IRLKEGAELTEE-----DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
89-578 |
9.21e-50 |
|
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: 178.49 E-value: 9.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 89 KGEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05930 7 VDGDQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 169 NCIITNdvlapavdaiapkcenlhsklivsensregwgnikemmkcasdshtcvktkHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:cd05930 86 KLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLP---RFEPTSVLQTLSKYPIT 321
Cdd:cd05930 115 HRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEALADLLAEEGIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 322 VFCSAATVYRMLVQnDMASYKFKSLKHCVSAGEPITPDVTGKWR-NKTGLDIYEGYGQTETVLICGNF--KGMKIKPGSM 398
Cdd:cd05930 187 VLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWReLLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglfAH-YADDPSKTASTLRGN-------FYITGDRGYM 465
Cdd:cd05930 266 piGRPIPNTRVYVLDENLRPVPPGVPGELyigGAGL---------ARgYLNRPELTAERFVPNpfgpgerMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 466 DEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEH 545
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEELRAH 411
|
490 500 510
....*....|....*....|....*....|...
gi 795246185 546 VKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-580 |
1.22e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 180.33 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 -----------------NDV--LAP--AVDAIAPKcenlHSKLIVSEnsregwgnIKEMMKCASDShtcVKTKHNEIMAM 232
Cdd:PRK06087 128 ptlfkqtrpvdlilplqNQLpqLQQivGVDKLAPA----TSSLSLSQ--------IIADYEPLTTA---ITTHGDELAAV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 233 FFTSGTSGYPKMTAHTHSSFGLG-LSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSV 311
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDAC 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 312 LQTLSKYPITvfCS-AAT--VYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGK-WRNktGLDIYEGYGQTETV--LIC 385
Cdd:PRK06087 269 LALLEQQRCT--CMlGATpfIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQR--GIKLLSVYGSTESSphAVV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDiGIQVLPNrpfgLFAHYADDPSKTASTL--RGNFYiTGDRG 463
Cdd:PRK06087 345 NLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGE-EASRGPN----VFMGYLDEPELTARALdeEGWYY-SGDLC 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLIKEIQ 543
Cdd:PRK06087 419 RMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFS 498
|
490 500 510
....*....|....*....|....*....|....*..
gi 795246185 544 EhvkKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK06087 499 R---KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-579 |
1.53e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 180.35 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPA-----VDAIAP----------KCENL-HSKLIVS--ENSREG---WGNIKEMMKCASDSHTCVKT---KH 226
Cdd:PRK12583 121 VICADAFKTSdyhamLQELLPglaegqpgalACERLpELRGVVSlaPAPPPGflaWHELQARGETVSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 227 NEIMAMFFTSGTSGYPKMTAHTHSSfglgLSVNGRF---WLDLTPSDVM------WNTSDTGWAKSAWSSVfspwiqGAC 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLcvpvplYHCFGMVLANLGCMTV------GAC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 298 VFahhLPR--FEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGL-DIY 373
Cdd:PRK12583 271 LV---YPNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 374 EGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDigiqvLPNRPFGLFAHYADDPSKTAS 450
Cdd:PRK12583 348 IAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGE-----LCTRGYSVMKGYWNNPEATAE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:PRK12583 423 SIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 795246185 530 YKSHDQeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK12583 503 HAASEE-----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
96-579 |
2.00e-49 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 180.07 E-value: 2.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLAPAV-DAIA------------------PKCENL-----HSKLIVSENSREGWGNIKEMMKCASdSHTC--VKTKHNEI 229
Cdd:PRK08751 132 NFGTTVqQVIAdtpvkqvittglgdmlgfPKAALVnfvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 230 MAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTpsdvmwNTSDTG-------------WAKSAWSSVFSPWiqGA 296
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAGT------GKLEEGcevvitalplyhiFALTANGLVFMKI--GG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 297 CvfaHHL---PRFEPTSVlQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDI 372
Cdd:PRK08751 282 C---NHLisnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKT 448
Cdd:PRK08751 358 VEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELcikGPQVMKG--------YWKRPEET 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVln 527
Cdd:PRK08751 430 AKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-- 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 795246185 528 pdykSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK08751 508 ----KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
91-582 |
1.05e-47 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 176.30 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELgsLSR--KFANILSeACSLQRGDRVILILPRVPE----WW---LANVAC--------------LR-TGT- 145
Cdd:PRK07529 55 RPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPEthfaLWggeAAGIANpinpllepeqiaelLRaAGAk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 146 VLI-----PGTtQLTQK--DILYRLQSSKAncIIT---NDVLAPAVDAIAPKCENLHSKLIVSENSregwgnikEMMKCA 215
Cdd:PRK07529 132 VLVtlgpfPGT-DIWQKvaEVLAALPELRT--VVEvdlARYLPGPKRLAVPLIRRKAHARILDFDA--------ELARQP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 216 SDSHTCVKTKH-NEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMW--------NTSDTGwa 281
Cdd:PRK07529 201 GDRLFSGRPIGpDDVAAYFHTGGTTGMPKLAQHTHG----NEVANA--WlgallLGLGPGDTVFcglplfhvNALLVT-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 282 ksawssVFSPWIQGACVFahhLPR---FEPTSVLQTLSK----YPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGE 354
Cdd:PRK07529 273 ------GLAPLARGAHVV---LATpqgYRGPGVIANFWKiverYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 355 PITPDVTGKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLP 431
Cdd:PRK07529 344 PLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLCIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 432 NrPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSS 511
Cdd:PRK07529 424 G-P-NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGR 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795246185 512 PDPIRGEVVKAFIVLNPDyKSHDQEQLIKEIQEHVKKTTApykYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK07529 502 PDAHAGELPVAYVQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
92-580 |
1.06e-47 |
|
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: 173.64 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 IT------NDVLA---PAVDAIAPKCEnlhsklivsensregWGNIkemmkcasdshtcvktkhneimAMFFTSGTSGYP 242
Cdd:cd12118 106 FVdrefeyEDLLAegdPDFEWIPPADE---------------WDPI----------------------ALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 243 KMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MWNTSD---TGWAksawssvfSPWIQGAcVFAHH--LPRFEPTSVLQTLS 316
Cdd:cd12118 149 KGVVYHHRGAYLNALANILEW-EMKQHPVyLWTLPMfhcNGWC--------FPWTVAA-VGGTNvcLRKVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 317 KYPITVFCSAATVYRMLVqNDMASYKfKSLKHCVS---AGEPITPDVTGKWRNKtGLDIYEGYGQTET---VLICgnfkg 390
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVC----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 391 mKIKPGSMGKPSP---------------AFDVKIVDVNGNVLPPGQEGDIGIQVLpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:cd12118 291 -AWKPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPRDGKTIGEIVF--RGNIVMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 456 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 535
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 795246185 536 eqlikEIQEHVKKTTAPYKYPRKVEFiQELPKTISGKTKRNELRK 580
Cdd:cd12118 448 -----EIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-581 |
2.06e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 173.69 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07470 17 ARRFPDRIALVW----GDR-SWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLhsKLIVSENSREGWGNIKEMMKC-ASDSHTCVKTKHNEIMAM 232
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVARhLGARVANAAVDHDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 233 FFTSGTSGYPKMTAHTHSSfgLGLSVNGRFwLDLTPsdvmwntsdtGWAKSAWSSVFSPWIQGACVfaHHL--------- 303
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGQ--MAFVITNHL-ADLMP----------GTTEQDASLVVAPLSHGAGI--HQLcqvargaat 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 304 -----PRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYG 377
Cdd:PRK07470 234 vllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 378 QTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPS 446
Cdd:PRK07470 314 LGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEIcviGPAV--------FAGYYNNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 447 KTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVL 526
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 527 NpDYKSHDQEqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK07470 466 R-DGAPVDEA----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
96-584 |
4.75e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 173.41 E-value: 4.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLAPAVDAIAPKCENLHskLIVSE-------------NSREGWgnIKEMM----------------KCASDSHTCVKTKH 226
Cdd:PRK05677 131 NMAHLAEKVLPKTGVKH--VIVTEvadmlpplkrlliNAVVKH--VKKMVpayhlpqavkfndalaKGAGQPVTEANPQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 227 NEIMAMFFTSGTSGYPKMTAHTHSSfglgLSVNgrfWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQgaCVF----- 299
Cdd:PRK05677 207 DDVAVLQYTGGTTGVAKGAMLTHRN----LVAN---MLQCRAlmGSNLNEGCEILIAPLPLYHIYAFTFH--CMAmmlig 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 AHHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYE 374
Cdd:PRK05677 278 NHNIlisnPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTAS 450
Cdd:PRK05677 357 GYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELcvkGPQVMKG--------YWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:PRK05677 428 ILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 530 ykshdqEQLIKE-IQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:PRK05677 508 ------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELK 557
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
74-578 |
8.90e-47 |
|
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: 170.12 E-value: 8.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttq 153
Cdd:cd05945 1 AAANPDRPAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 ltqkdilyrlqsskanciitndvlapaVDAIAPKcenlhsklivsensrEGWGNIKEMMKCASdshtcVKTKHNEIMAMF 233
Cdd:cd05945 71 ---------------------------LDASSPA---------------ERIREILDAAKPAL-----LIADGDDNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHS---SFGLGLsvNGRFwlDLTPSDVMWNTSDtgwaksaWS---SVFS---PWIQGACVFAhhLP 304
Cdd:cd05945 104 FTSGSTGRPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 305 RFE---PTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKT-GLDIYEGYGQT 379
Cdd:cd05945 171 RDAtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 380 ETVLICgnfKGMKIKPGSM--------GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKT 448
Cdd:cd05945 251 EATVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELvisGPSV--------SKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTLRGNF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFI 524
Cdd:cd05945 320 AAAFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFV 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 795246185 525 VLNPdyksHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05945 400 VPKP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
78-584 |
1.36e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 171.03 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 78 PSNPAFWwINGKGEEVrwSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEwwlANVACLRTGTVLIPGTTQL 154
Cdd:PRK13391 11 PDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 155 TQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV-SENSREGWGNIKEMMKCASDShtcVKTKHNEIMAMF 233
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPAT---PIADESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPK----------------MTAHTHSSFGLGlsvNGRFWLDLTPsdvMWNTsdtgwAKSAWSSVfspwIQ--G 295
Cdd:PRK13391 161 YSSGTTGRPKgikrplpeqppdtplpLTAFLQRLWGFR---SDMVYLSPAP---LYHS-----APQRAVML----VIrlG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 296 ACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVY-RML-----VQNdmaSYKFKSLKHCVSAGEPITPDVTGKWRNKTG 369
Cdd:PRK13391 226 GTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLklpeeVRD---KYDLSSLEVAIHAAAPCPPQVKEQMIDWWG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 370 LDIYEGYGQTETVLICG-NFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFglfaHYADDPSKT 448
Cdd:PRK13391 301 PIIHEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTL--RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVL 526
Cdd:PRK13391 374 AEARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 527 NP--DYKSHDQEQLIKEIQEHVkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:PRK13391 454 VDgvDPGPALAAELIAFCRQRL----SRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-580 |
1.53e-46 |
|
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: 167.27 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 226 HNEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVF 299
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHS----NEVYNA--WmlalnSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 AHHLPRFEPTSV---LQTLSKYPITVFCSAATVYRMLVQNDMASyKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGY 376
Cdd:cd05944 75 AGPAGYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLPNRpfGLFAHYADDPSKTASTLR 453
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDEVGEICVAGP--GVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSh 533
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 795246185 534 DQEQLIKEIQEHVKKTTApykYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05944 311 EEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
235-581 |
1.59e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 171.48 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 235 TSGTSGYPKMTAHTHSSFGLGLSVngrfWLDLTPsdvmWNTSDTGWAKSAwssVFSPWIQGACVFAHHLP-------RFE 307
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKA----ILDRTP----WRAEEPTVIVAP---MFHAWGFSQLVLAASLActivtrrRFD 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRM---LVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLI 384
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMI 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 385 C-GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYAddPSKTASTLRGnFYITGDRG 463
Cdd:PRK13382 353 AtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-FMASGDVG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQ 543
Cdd:PRK13382 425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLK 499
|
330 340 350
....*....|....*....|....*....|....*...
gi 795246185 544 EHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK13382 500 QHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-580 |
2.70e-46 |
|
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: 170.50 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 87 NGKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEWWLAnVAClrTGTVLIPGTTQLTQKDILYRL 163
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYA-VPG--MGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 164 QSSKANCIITNDVLAPAVDAIAPKC--------------------ENLHS--KLIVSENSREGWGNIKEmmkcasdshtc 221
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLptvehvvvmtddaampepagVGVLAyeELLAAESPEYDWPDFDE----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 222 vktkhNEIMAMFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQ 294
Cdd:cd12119 163 -----NTAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GAC-VFAHhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKtGLDI 372
Cdd:cd12119 231 GAKlVLPG--PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 373 YEGYGQTET--VLICGnfkgmKIKPG--------------SMGKPSPAFDVKIVDVNGNVLP--PGQEGDIgiQVlpnR- 433
Cdd:cd12119 308 IHAWGMTETspLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGEL--QV---Rg 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 434 PFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 513
Cdd:cd12119 378 PW-VTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPH 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795246185 514 PIRGEVVKAFIVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd12119 457 PKWGERPLAVVVLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
96-582 |
5.02e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 170.49 E-value: 5.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSlqRGDRVILILPRVPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKAN 169
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGV--RAGDGVAVLARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLAPAVDAIAPKCENLHSKLIVSEN---SREGWGNIKEMMKCASDSHTCVKTKHNEIMAMffTSGTSGYPKMTA 246
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSSTAPLPKPPKPGGIVIL--TSGTTGTPKGAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 247 HTHSSfglGLSVNGRFwLDLTP---SDVMWNTS----DTGWAKSAWSSVFspwiqGACVFAHHlpRFEPTSVLQTLSKYP 319
Cdd:PRK07788 227 RPEPS---PLAPLAGL-LSRVPfraGETTLLPApmfhATGWAHLTLAMAL-----GSTVVLRR--RFDPEATLEDIAKHK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 320 ITVFCSAAT-VYRML--VQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTE----TVlicGNFKGMK 392
Cdd:PRK07788 296 ATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDLA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 393 IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKtaSTLRGnFYITGDRGYMDEDGYfW 472
Cdd:PRK07788 373 EAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL-L 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 473 FVA-RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTA 551
Cdd:PRK07788 444 FVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLA 518
|
490 500 510
....*....|....*....|....*....|.
gi 795246185 552 PYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK07788 519 RYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-579 |
1.85e-45 |
|
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: 166.85 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 117 LQRGDRVILILPRVPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENlh 192
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 193 SKLIVSEnsrEGWgnikemmKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRfwLDLTPSDV 271
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 272 MWNTSDTGWAkSAWSSVFSPWIQGACVFAHHLPRFePTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVS 351
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 352 AGEPITPDVTGKWRNK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQE 422
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 423 GDIGiqvlPNRPFGLfAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHP 501
Cdd:cd05922 313 GEIV----HRGPNVM-KGYWNDPPYRRKEGRGGGVLhTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 502 SVAESAVVSSPDPIrGEVVKAFIVLNPDYKSHDqeqlikeIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05922 388 LIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-581 |
3.90e-45 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 167.46 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFwwINGKGEEVrWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 152 TQLTQKDILYRLQSSKANCIITndvLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEIMA 231
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSsfGLGLSV---------NgrfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhh 302
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 303 LPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDM-ASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIY-EGYGQTE 380
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVvEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 381 --TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTL-R 453
Cdd:PLN02246 336 agPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDPEtGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK-S 532
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEiT 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 533 HDqeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PLN02246 491 ED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
96-508 |
6.36e-45 |
|
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: 164.36 E-value: 6.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 169 NCIITNDVLAPAVDAIAPKCENLHSKLIVSENSregwgnikemmkCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDD------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF--AHHLPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 327 ATVYRMLVqnDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTG-LDIYEGYGQTETVLICgnfkGMKIKPGSM------- 398
Cdd:TIGR01733 220 PSLLALLA--AALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWS----TATLVDPDDaprespv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTA---------STLRGNFYITGDRGYMDE 467
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYLP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 795246185 468 DGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
231-579 |
1.04e-44 |
|
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: 165.24 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 231 AMFFTSGTSGYPKmtahthssfglGLSVNGRFWLDLTPSDVMWNTSDtGWakSAWSSVFSP----------WIQGACVFA 300
Cdd:cd05929 129 KMLYSGGTTGRPK-----------GIKRGLPGGPPDNDTLMAAALGF-GP--GADSVYLSPaplyhaapfrWSMTALFMG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 301 HHL---PRFEPTSVLQTLSKYPITVFCSAATVY-RM--LVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYE 374
Cdd:cd05929 195 GTLvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIgiQVLPNRPFglfaHYADDPSKTA-STL 452
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEV--YFANGPGF----EYTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAfiVLNPDYKS 532
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 795246185 533 HDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
90-583 |
7.32e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 163.72 E-value: 7.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK12406 8 GDRRR-SFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITN-DVLAPAVDAIAPKCENLH--------SKLIVSENSR---------EGWgnikemmkcASDSHTCVKTKHNEIMA 231
Cdd:PRK12406 86 VLIAHaDLLHGLASALPAGVTVLSvptppeiaAAYRISPALLtppagaidwEGW---------LAQQEPYDGPPVPQPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPK------MTAHTHSSFGL------GLSVNGRFWLdltpSDVMWNTSDTGWAksawssVFSPWIQGACVF 299
Cdd:PRK12406 157 MIYTSGTTGHPKgvrraaPTPEQAAAAEQmraliyGLKPGIRALL----TGPLYHSAPNAYG------LRAGRLGGVLVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 ahhLPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQND--MASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGY 376
Cdd:PRK12406 227 ---QPRFDPEELLQLIERHRITHMHMVPTMFiRLLKLPEevRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTET--VLICGNFKGMKiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfahYADDPSKTASTLRG 454
Cdd:PRK12406 304 GSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHD 534
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 535 QEqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:PRK12406 458 EA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-579 |
1.36e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 160.60 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWIN-GKGEEVRWSFEELGSLSRKFANILSEaCSLQRGDRVILilpRVPEWWLANV---ACLRTGTVLIP 149
Cdd:PRK13295 34 VASCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSC---QLPNWWEFTVlylACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 150 GTTQLTQKDILYRLQSSKANCIITNDVL-----APAVDAIAPKCENLHSKLIVSENSREGW-----GNIKEMMKCASDSH 219
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGGDGADSFealliTPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 220 TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSS-FGLGLSVNGRfwLDLTPSDVMWNTS----DTGWAKSAwssvFSPWIQ 294
Cdd:PRK13295 190 ARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GACVFAHHLprFEPTSVLQTLSKYPITvFCSAATVYRM-LVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDI 372
Cdd:PRK13295 264 GATAVLQDI--WDPARAAELIRTEGVT-FTMASTPFLTdLTRAvKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 373 YEGYGQTETVLICGnfkgmkIKPG--------SMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiQVlpnRPFGLFAHYADD 444
Cdd:PRK13295 341 VSAWGMTENGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRL--QV---RGCSNFGGYLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 445 PSKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFI 524
Cdd:PRK13295 410 PQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 525 VLNPDyKSHDQEQLIKEIQEHvkKTTAPYkYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK13295 489 VPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
59-580 |
6.70e-42 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 160.45 E-value: 6.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 59 NFAKDVLDQwtNMEkAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:PLN02654 88 NICYNCLDR--NVE-AGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAML 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT-NDV--------LAPAVDAIAPKCENLHSKL---IVSENS----R 202
Cdd:PLN02654 164 ACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITcNAVkrgpktinLKDIVDAALDESAKNGVSVgicLTYENQlamkR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 203 EG--WGNIKEMMkcASDSHTCVKTK-------HNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMW 273
Cdd:PLN02654 244 EDtkWQEGRDVW--WQDVVPNYPTKcevewvdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 274 NTSDTGWAKSAWSSVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKH 348
Cdd:PLN02654 322 CTADCGWITGHSYVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 349 CVSAGEPITPDVtgkWR---NKTG---LDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKIVDVNGNV 416
Cdd:PLN02654 402 LGSVGEPINPSA---WRwffNVVGdsrCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGKE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 417 LppgqEGDI-GIQVLPNRPFGLFAHYADDPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFE 492
Cdd:PLN02654 475 I----EGECsGYLCVKKSWPGAFRTLYGDHERYETTYFKPFagyYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 493 VENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:PLN02654 551 VESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGK 628
|
....*...
gi 795246185 573 TKRNELRK 580
Cdd:PLN02654 629 IMRRILRK 636
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
74-579 |
1.35e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 156.97 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWingKGEEVrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK06145 12 ARRTPDRAALVY---RDQEI--SYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKC-ENLHSKlivSENSREGWGN--IKEMMKCASDshtcvktkhnEIM 230
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIvIDAAAQ---ADSRRLAQGGleIPPQAAVAPT----------DLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 231 AMFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFW----------LDLTPSDVMWntsdtgwaksawssvfsp 291
Cdd:PRK06145 153 RLMYTSGTTDRPKGVMHSYGNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW------------------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 292 wiQGACVFAHHlpRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPiTP-----DVTGKWR 365
Cdd:PRK06145 215 --VGGTLRIHR--EFDPEAVLAAIERHRLTcAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEK-TPesrirDFTRVFT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 366 NKTGLDiyeGYGQTETvliCGNFKGMKI-----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfah 440
Cdd:PRK06145 290 RARYID---AYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG---- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 441 YADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVV 520
Cdd:PRK06145 359 YWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERI 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 795246185 521 KAFIVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK06145 439 TAVVVLNP-----GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
301-579 |
3.24e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 155.53 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 301 HHLPRFEPTSVLQTLSKyPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTE 380
Cdd:PRK07787 199 VHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 381 TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnRPFGLFAHYADDPSKTASTLRGN-FYIT 459
Cdd:PRK07787 278 TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPDATAAAFTADgWFRT 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 460 GDRGYMDEDGYFWFVAR-SDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQL 538
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV---AADEL 431
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 795246185 539 IkeiqEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK07787 432 I----DFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
295-571 |
4.48e-41 |
|
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: 151.69 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GACVFahhLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGE---PITPDVTgKWRNKTGl 370
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndMATVDTS-PWGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 371 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTA 449
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 450 STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 795246185 530 yKSHDQEQLIkeiqEHVKKTTAPYKYPRKVEFIQELPKTISG 571
Cdd:cd17636 292 -ASVTEAELI----EHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-581 |
6.23e-39 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 150.51 E-value: 6.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 175 DvlapavdAIAPKCENLHSKLIV-SENSREGWGNIKEMMKCA---SDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTH- 249
Cdd:PLN02330 135 D-------TNYGKVKGLGLPVIVlGEEKIEGAVNWKELLEAAdraGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHr 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 --------SSFGLGLSVNGRF-WLDLTPSDVMWNTsdTGWAKSAWSSvfspwiQGACVFahhLPRFEPTSVLQTLSKYPI 320
Cdd:PLN02330 208 nlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYGI--TGICCATLRN------KGKVVV---MSRFELRTFLNALITQEV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TVFCSAATVYRMLVQN------DMASYKFKSLkhcVSAGEPITPDVTGKWRNK-TGLDIYEGYGQTETVLICGNF----K 389
Cdd:PLN02330 277 SFAPIVPPIILNLVKNpiveefDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 390 GMKI-KPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRGYMD 466
Cdd:PLN02330 354 GHGIaKKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYID 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 467 EDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHV 546
Cdd:PLN02330 429 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE-----DILNFV 503
|
490 500 510
....*....|....*....|....*....|....*
gi 795246185 547 KKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
228-572 |
6.53e-39 |
|
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: 145.72 E-value: 6.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPK--MTAHTHSsfgLGLSVNgrfWldltpSDVMWNTSDTGWA-----------KSAWSSVFspwIQ 294
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GACVFAHHLprFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLD-I 372
Cdd:cd17638 67 GATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 373 YEGYGQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDvNGNVLPPGqegdigiqvlPNRPFGlfahYADDPSKTAS 450
Cdd:cd17638 145 LTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRG----------YNVMQG----YLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd17638 210 AIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795246185 530 yKSHDQEQLIKEIQEHVkkttAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd17638 290 -VTLTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGK 327
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-578 |
3.12e-38 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 147.42 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 152 TQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPkcenlhskliVSENSREGWGNikemmkcASDSHTCVKTKHNEIMA 231
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGD----------VALLGDEALAA-------PPATPPLVPPRPDNLAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSFglglsVNGRFWL----DLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRF 306
Cdd:cd17646 143 VIYTSGSTGRPKGVMVTHAGI-----VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 307 EPTSVLQTLSKYPITV--FcsaatVYRMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET- 381
Cdd:cd17646 217 DPAYLAALIREHGVTTchF-----VPSMLRVflAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAa 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 --VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV---LPNRPfGLFA-HYADDPSKTASTL 452
Cdd:cd17646 292 idVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELylgGVQLargYLGRP-ALTAeRFVPDPFGPGSRM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 rgnfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKS 532
Cdd:cd17646 371 ----YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 795246185 533 HDQEQLikeiQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17646 447 PDTAAL----RAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
93-579 |
3.75e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 148.43 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 93 VRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 173 TNDVLAPAVDAIAPKCENLH---SKLIVSENSREGW------GNIKEMMKC----------------ASDSHTCVKTKHN 227
Cdd:PRK12492 128 YLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqavpfkqalrqgRGLSLKPVPVGLD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPKMTAHTHSSfglgLSVN--------GRFWLDLTPsdVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGN----LVANmlqvraclSQLGPDGQP--LMKEGQEVMIAPLPLYHIYAFTANCMCMM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 A---HHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLD 371
Cdd:PRK12492 282 VsgnHNVlitnPRDIP-GFIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSK 447
Cdd:PRK12492 361 IVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELcikGPQVMKG--------YWQQPEA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 448 TASTLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVl 526
Cdd:PRK12492 433 TAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV- 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 795246185 527 npdykSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK12492 512 -----ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-579 |
4.47e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 149.80 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNdvlAPAVDAIAPKcENLHSKLI 196
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS---DALRDRFQPS-RVAEAAEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 197 VSENSREGWGNIKEMMKCASDSHTcvktkhneimamfFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:PRK06060 128 MSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 277 DT----GWAKSAW-------SSVFSPWIQGACVFAHHLPRFEPtSVLQTLSKYPITVF--CSAATvyrmlvqndmasykF 343
Cdd:PRK06060 195 RMyfayGLGNSVWfplatggSAVINSAPVTPEAAAILSARFGP-SVLYGVPNFFARVIdsCSPDS--------------F 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 344 KSLKHCVSAGEPITPDVTGKWRNK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKIVDVNGNVLPP 419
Cdd:PRK06060 260 RSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 420 GQEGDIGI------QVLPNRPFGLFAHyaddpsktastlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 493
Cdd:PRK06060 337 GVEGDLWVrgpaiaKGYWNRPDSPVAN-------------EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 494 ENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKT 573
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKL 481
|
....*.
gi 795246185 574 KRNELR 579
Cdd:PRK06060 482 VRGALR 487
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
94-579 |
7.01e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 146.49 E-value: 7.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILsEACSLQRGDRvILILPRVPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PRK09088 22 RWTYAELDALVGRLAAVL-RRRGCVDGER-LAVLARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 173 TNDVLApavdAIAPKCENLhsklivsensregwgnikEMMKCASDSHTCVKTKH---NEIMAMFFTSGTSGYPK--MTA- 246
Cdd:PRK09088 100 GDDAVA----AGRTDVEDL------------------AAFIASADALEPADTPSippERVSLILFTSGTSGQPKgvMLSe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 247 ----HTHSSFGLGLSVNGR--FWLDlTPsdvMWNTsdTGWAksawSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK09088 158 rnlqQTAHNFGVLGRVDAHssFLCD-AP---MFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TV---FCSAATVYRMLVQNDMASYKFKSLKHCVSAGEP-ITPDVTGkWRNKtGLDIYEGYGQTE--TVLicgnfkGMKI- 393
Cdd:PRK09088 226 GIthyFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILG-WLDD-GIPMVDGFGMSEagTVF------GMSVd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 394 ------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGN-FYITGDRGYMD 466
Cdd:PRK09088 298 cdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG-PN----LSPGYWRRPQATARAFTGDgWFRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 467 EDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEHV 546
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD-----GAPLDLERIRSHL 447
|
490 500 510
....*....|....*....|....*....|...
gi 795246185 547 KKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK09088 448 STRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
228-575 |
2.55e-37 |
|
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: 141.63 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFE 307
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAG--EPITPDVTGKWRNKTgLDIYEGYGQTET-VLI 384
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVRFIEATGL-TNTAQVYGLSETgTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnrPFGLFAHYaDDPSKTASTLRGNFYITGDRGY 464
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS----PANMLGYW-NNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdykSHDQEQLIKEIQE 544
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|.
gi 795246185 545 HVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:cd17635 310 TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-581 |
3.65e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 142.93 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWINGkGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:COG1022 21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 LTQKDILYRLQSSKANCIIT-NDVLAPAVDAIAPKCENLhsKLIVSENSREGWG-----NIKEMMKCASDSHT------- 220
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 221 CVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWaksawsSVFSpWIQ 294
Cdd:COG1022 177 RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GACV--------FAHHLPRFEPT--------------SVLQTLSKYPIT---VFCSAATV------YRMLVQNDMASYKF 343
Cdd:COG1022 249 GATVafaespdtLAEDLREVKPTfmlavprvwekvyaGIQAKAEEAGGLkrkLFRWALAVgrryarARLAGKSPSLLLRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 344 K------------------SLKHCVSAGEPITPDVtGKWRNKTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMGKPSPA 404
Cdd:COG1022 329 KhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLPG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 405 FDVKIvdvngnvlppGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTLR--GNFYiTGDRGYMDEDGYFWFVARSDD 479
Cdd:COG1022 407 VEVKI----------AEDGEIlvrGPNV--------MKGYYKNPEATAEAFDadGWLH-TGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 480 II-LSSGYRIGPFEVENALNEHPSVAESAVVsspdpirGE----VVkAFIVLNPD------------YKSHDQ----EQL 538
Cdd:COG1022 468 LIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEalgewaeenglpYTSYAElaqdPEV 539
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 539 IKEIQEHVKKTT---APYKYPRKVEFiqeLPK---------TISGKTKRNELRKK 581
Cdd:COG1022 540 RALIQEEVDRANaglSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILEK 591
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
221-580 |
3.75e-36 |
|
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: 141.31 E-value: 3.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 221 CVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 AHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQNdMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQT 379
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 380 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNV-LPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFY 457
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRG-PN----VMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 458 ITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PFE-VENALNEH-PSVAESAVVSSPDPIRGEVVKAFivlnpdYK 531
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------TT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 795246185 532 SHDQEQLikEIQEHVKKTTAPYKY-PRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05909 441 TTDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
93-581 |
4.65e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 142.26 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 93 VRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANC 170
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSgcKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 II----TNDVLApAVDAIAPKCE-----NLHSK--------LIVSENSREGWGNIKEMMKCASDSHtcvKTKHNEIMA-- 231
Cdd:PRK08315 121 AAdgfkDSDYVA-MLYELAPELAtcepgQLQSArlpelrrvIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 -------MFFTSGTSGYPKMTAHTHSSFGLglsvNGRF---WLDLTPSD--------------VMWN----TSdtgwaks 283
Cdd:PRK08315 197 dpddpinIQYTSGTTGFPKGATLTHRNILN----NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNlacvTH------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 284 awssvfspwiqGAC-VFAhhLPRFEPTSVLQTLSK------Y--PiTVFCSaatvyrMLVQNDMASYKFKSLKHCVSAGE 354
Cdd:PRK08315 266 -----------GATmVYP--GEGFDPLATLAAVEEerctalYgvP-TMFIA------ELDHPDFARFDLSSLRTGIMAGS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 355 PITPDVTGKWRNKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFDVKIVD-VNGNVL 417
Cdd:PRK08315 326 PCPIEVMKRVIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 418 PPGQEGDigiqvLPNRPFGLFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENA 496
Cdd:PRK08315 394 PRGEQGE-----LCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 497 LNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRN 576
Cdd:PRK08315 469 LYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKF 543
|
....*
gi 795246185 577 ELRKK 581
Cdd:PRK08315 544 KMREM 548
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
90-579 |
4.75e-36 |
|
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: 140.94 E-value: 4.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLAPAVDAIAPkcenlhsklIVSENSREGWGNikemmkCASDSHTCVKTKHNEIMAMFfTSGTSGYPKMTAHTH 249
Cdd:cd17651 95 LVLTHPALAGELAVELV---------AVTLLDQPGAAA------GADAEPDPALDADDLAYVIY-TSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfahHLP----RFEPTSVLQTLSKYPIT 321
Cdd:cd17651 159 RSL-----ANLVAWQArassLGPGARTLQFAGLGFDVSVQE-IFSTLCAGATL---VLPpeevRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 322 -VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEP--ITPDVTGKWRNKTGLDIYEGYGQTE----TVLICGNFKGMKIK 394
Cdd:cd17651 230 rVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 395 PGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPfGLFAH-YADDPSKTASTLrgnfYITGDRGYMDE 467
Cdd:cd17651 310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELyigGAGLARgylNRP-ELTAErFVPDPFVPGARM----YRTGDLARWLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 468 DGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEHVK 547
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDP-----EAPVDAAELRAALA 459
|
490 500 510
....*....|....*....|....*....|..
gi 795246185 548 KTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd17651 460 THLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
91-578 |
1.11e-35 |
|
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: 140.03 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPKCenlhskLIVSENSREGWGNIKEmmKCASDSHTCVktkhneimamFFTSGTSGYPKMTAHTHS 250
Cdd:cd12117 98 LLTDRSLAGRAGGLEVAV------VIDEALDAGPAGNPAV--PVSPDDLAYV----------MYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFgLGLsVNGRFWLDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAATV 329
Cdd:cd12117 160 GV-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTF-EIWGALLNGArLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 330 YRMLVQNDMASykFKSLKHCVSAGEPITPDVTGKWRNKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKPSPA 404
Cdd:cd12117 237 FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 405 FDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTASTLrgnfYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGELyvgGDGLALgylNRPALTAERFVADPFGPGERL----YRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 479 DIILSSGYRIGPFEVENALNEHPSVAESAV-VSSPDPIRGEVVkAFIVLNPDyKSHDqeqlikEIQEHVKKTTAPYKYPR 557
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAYMVPA 462
|
490 500
....*....|....*....|.
gi 795246185 558 KVEFIQELPKTISGKTKRNEL 578
Cdd:cd12117 463 AFVVLDELPLTANGKVDRRAL 483
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
90-578 |
1.66e-35 |
|
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: 138.88 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 ciitndvlapavdaiapkcenlhsKLIVSENSregwgnikemmkcasdSHTCVktkhneIMamfFTSGTSGYPKMTAHTH 249
Cdd:cd05907 79 ------------------------KALFVEDP----------------DDLAT------II---YTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSFglglsvngrfwldltpsdvMWN--TSDTGWAKSA--WSSVFSP--------WIQGACVFAHHLPRFEP--TSVLQTL 315
Cdd:cd05907 110 RNI-------------------LSNalALAERLPATEgdRHLSFLPlahvferrAGLYVPLLAGARIYFASsaETLLDDL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 316 SKYPITVFCSAATVYRML----VQNDMASYK--------FKSLKHCVSAGEPITPDVtGKWRNKTGLDIYEGYGQTETV- 382
Cdd:cd05907 171 SEVRPTVFLAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSa 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlppgqEgdigIQVlpnRPFGLFAHYADDPSKTA-STLRGNFYITGD 461
Cdd:cd05907 250 VVTLNPPG-DNRIGTVGKPLPGVEVRIADDG--------E----ILV---RGPNVMLGYYKNPEATAeALDADGWLHTGD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 462 RGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPirgeVVKAFIVLNPDY-----KSHD- 534
Cdd:cd05907 314 LGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaEEHGi 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 535 ----------QEQLIKEIQEHVK---KTTAPYKYPRKVEFIQElPKTI-------SGKTKRNEL 578
Cdd:cd05907 390 aytdvaelaaNPAVRAEIEAAVEaanARLSRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
92-580 |
2.56e-35 |
|
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: 139.58 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLAPAVDAIAPKceNLHSKLIVSENSREGWGNIKEMMK----------CASDSHTCVKTKHNEIMAMFFTSGTSGY 241
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTfitqnlppgfNEYDFKPPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 242 PKMTAHTHssfglgLSVNGRFWLDLTPSDVMWNTSDTgwaksAWSSVFsPWIQG---------ACVFAH--HLPRFEPTS 310
Cdd:cd17642 199 PKGVQLTH------KNIVARFSHARDPIFGNQIIPDT-----AILTVI-PFHHGfgmfttlgyLICGFRvvLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 311 VLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTGKWRNKTGLD-IYEGYGQTET---VLIC 385
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaILIT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 GNfkgMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRG 463
Cdd:cd17642 347 PE---GDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykSHDQEQLIKEIQ 543
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKEVM 493
|
490 500 510
....*....|....*....|....*....|....*...
gi 795246185 544 EHVKKTTAPYKYPR-KVEFIQELPKTISGKTKRNELRK 580
Cdd:cd17642 494 DYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
91-581 |
7.00e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 138.54 E-value: 7.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIK-----EMMKCASDSHTCVKTKHNE--IMAMFFTSGTSGYPK 243
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIgaldyEAFLASGDPDFAWTLPADEwdAIALNYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 244 MTAHTHSSFGLGLSVNGRFWlDLTPSDV-MW-------NtsdtGWAksawssvFsPW----IQGACVFahhLPRFEPTSV 311
Cdd:PRK08162 199 GVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWtvaaRAGTNVC---LRKVDPKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 312 LQTLSKYPITVFCSAATVYRMLVqNDMASYKfKSLKHCVS---AGEPITPDVTGKWRNkTGLDIYEGYGQTET---VLIC 385
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAAPPAAVIAKMEE-IGFDLTHVYGLTETygpATVC 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 --------------GNFKGMK------------IKPGSMgKPSPAFDVKI--VDVNGNVLPPGqegdigiqvlpnrpfgl 437
Cdd:PRK08162 340 awqpewdalplderAQLKARQgvryplqegvtvLDPDTM-QPVPADGETIgeIMFRGNIVMKG----------------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 438 fahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:PRK08162 402 ---YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 518 EVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKVEFiQELPKTISGKTKRNELRKK 581
Cdd:PRK08162 479 EVPCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
90-580 |
3.08e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 135.68 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRwSFEELGSLSRKFANILSEACSLQRgdRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK07638 23 NDRVL-TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLApavdaiapkcenlhSKLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:PRK07638 100 MIVTERYKL--------------NDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSfglglsvngrfWL---DLTPSDV-MWNTSDTGWAKSAWSSVF-----SPWIQGACVfaHHLPRFEPTSVLQTLSKYPI 320
Cdd:PRK07638 166 QS-----------WLhsfDCNVHDFhMKREDSVLIAGTLVHSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TVFCSAATVYRMLVQNDmaSYKFKSLKhCVSAGEPITPDVTGKWRNK-TGLDIYEGYGQTE----TVLICGNFKgmkIKP 395
Cdd:PRK07638 233 SVMYTVPTMLESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 396 GSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 475
Cdd:PRK07638 307 NSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV----KSPQ-FFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIvlnpdykshDQEQLIKEIQEHVKKTTAPYKY 555
Cdd:PRK07638 382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKI 452
|
490 500
....*....|....*....|....*
gi 795246185 556 PRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK07638 453 PKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
96-579 |
1.31e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 134.97 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLipgttqlTQKDILYRLQSSKANCIITND 175
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIV-------TTMNPSSSLGEIKKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLAPAVDAIAPKCENLHSKLI-VSEN-----SREGWGNIKEMMKcaSDSHTCVK--TKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIgVPENydfdsKRIEFPKFYELIK--EDFDFVPKpvIKQDDVAAIMYSSGTTGASKGVVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 248 THSSFGLGLSVNGRFwldltpsdvmwntSDTGWAKSAWSSVFSP-----WIQGACVFAHHL----------PRFEPTSVL 312
Cdd:PLN02574 219 THRNLIAMVELFVRF-------------EASQYEYPGSDNVYLAalpmfHIYGLSLFVVGLlslgstivvmRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 313 QTLSKYPITVFCSAATVYRMLVQN--DMASYKFKSLKHCVSAGEPITPDVTGKW-RNKTGLDIYEGYGQTETVLICG--- 386
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTESTAVGTrgf 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMKiKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQvlpnRPfGLFAHYADDPSKTASTLRGNFYI-TGDRGY 464
Cdd:PLN02574 366 NTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKATQSTIDKDGWLrTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqE 544
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG-STLSQEAVI----N 514
|
490 500 510
....*....|....*....|....*....|....*
gi 795246185 545 HVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PLN02574 515 YVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-572 |
3.24e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 133.47 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 58 FNFAkDVLDqwtnmEKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:PRK07798 3 WNIA-DLFE-----AVADAVPDRVALVC----GDR-RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 138 VACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV---SENSREGWGNIKEMMKC 214
Cdd:PRK07798 71 LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgSGNDLLPGAVDYEDALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 215 ASDSHTCVKTKHNEIMAMFFTSGTSGYPK--MTAHT---HSSFGLGLSVNGRF------------------WLDLTPsdV 271
Cdd:PRK07798 151 AGSPERDFGERSPDDLYLLYTGGTTGMPKgvMWRQEdifRVLLGGRDFATGEPiedeeelakraaagpgmrRFPAPP--L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 272 MWNTSDtgWAksAWSSVFSpwiqGACVFAHHLPRFEPTSVLQTLSKYPITV-FCSAATVYRMLVQ--NDMASYKFKSLKH 348
Cdd:PRK07798 229 MHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDADEVWRTIEREKVNViTIVGDAMARPLLDalEARGPYDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 349 CVSAGEPITPDVTGKWR----NKTGLDiyeGYGQTETvlicgNFKGMKI-KPGSMGKPSPAF----DVKIVDVNGNVLPP 419
Cdd:PRK07798 301 IASGGALFSPSVKEALLellpNVVLTD---SIGSSET-----GFGGSGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 420 GqEGDIG-IQVLPNRPFGlfahYADDPSKTASTLR---GNFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:PRK07798 373 G-SGEIGwIARRGHIPLG----YYKDPEKTAETFPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:PRK07798 448 EALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-579 |
4.98e-33 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 131.72 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 217 DS-HTCVKTKHNEIMA-MFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQ 294
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GACVFAHHLPRFEPTSVLQTL-SKYPITVFCSAATVYRMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTGKWRnKTGLD 371
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPfGLFAH 440
Cdd:cd17649 239 LFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-ELTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 441 -YADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 519
Cdd:cd17649 318 rFVPDPFGAPG---SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 520 VkAFIVLNPDYKshdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:cd17649 395 V-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
232-581 |
9.42e-33 |
|
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: 128.22 E-value: 9.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHT-----HSSFG----LGLSVNGRfWLDLTPS------DVMWNtsdtgWAKSAWSSVFSPWIQGA 296
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDS-WLLSLPLyhvgglAILVR-----SLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 297 cvfahhlprfeptsvLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKtGLDIYEGY 376
Cdd:cd17630 79 ---------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTETV-LICGNFKGMKiKPGSMGKPSPAFDVKIVDvngnvlppgqEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:cd17630 143 GMTETAsQVATKRPDGF-GRGGVGVLLPGRELRIVE----------DGEIWV-----GGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 456 FYiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykSHDQ 535
Cdd:cd17630 207 FT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADP 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 795246185 536 EQLIkeiqEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:cd17630 283 AELR----AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
90-578 |
3.34e-32 |
|
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: 129.75 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLAPaVDaiapkcenlHSKLivsenSREgwgnikemmkcasdshtcVKTKHNEImAMFFTS-GTSGYPKMTAHT 248
Cdd:cd05920 115 AYIVPDRHAG-FD---------HRAL-----ARE------------------LAESIPEV-ALFLLSgGTTGTPKLIPRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSFGLGLSvngrfwldlTPSDVMWNTSDT----------GWAKSAWSSVFSPWIQGACVFAhhlPRFEPTSVLQTLSKY 318
Cdd:cd05920 161 HNDYAYNVR---------ASAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLIERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 319 PITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLicgNFKGM----KI 393
Cdd:cd05920 229 GVTVTALVPALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddpdEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 394 KPGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiQVLPNRPFGLFAHY-ADDPSKTASTLRGnFYITGDRGYMDEDGYF 471
Cdd:cd05920 306 IIHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPYTIRGYYrAPEHNARAFTPDG-FYRTGDLVRRTPDGYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdykshDQEQLIKEIQEHVKKT-T 550
Cdd:cd05920 381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERgL 454
|
490 500
....*....|....*....|....*...
gi 795246185 551 APYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05920 455 AAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
306-578 |
5.88e-32 |
|
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: 129.17 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVli 384
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALAAAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 385 cgNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNV---LPPGQEGDIGIQVLPNRPFglfAHYADDPSKTASTLRGNFYITG 460
Cdd:cd05923 306 --NSLYMRdARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 461 DRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqlik 540
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ 454
|
250 260 270
....*....|....*....|....*....|....*....
gi 795246185 541 EIQEHVKKTT-APYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05923 455 ELDQFCRASElADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
232-575 |
1.06e-31 |
|
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: 125.21 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSfglglsvngrfWLDLTPSDVMwntsdtGWAKSAWSSVFSPwiqGACVFAHHL-------- 303
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------WIESFVCNED------LFNISGEDAILAP---GPLSHSLFLygaisaly 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 304 --------PRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLkhcVSAGEPITPDVTGKWRNKT-GLDIYE 374
Cdd:cd17633 65 lggtfigqRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqegdIG-IQVLPNRpfgLFAHYADDPSKTAstlr 453
Cdd:cd17633 142 FYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKSEM---VFSGYVRGGFSNP---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyKSH 533
Cdd:cd17633 207 DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795246185 534 DQEQLIKeiqehVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:cd17633 284 YKQLKRF-----LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
90-575 |
2.07e-31 |
|
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: 127.17 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 ciitndvlapavdaiapkcenlhSKLIVSENsregwgnikemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:cd05914 81 -----------------------KAIFVSDE--------------------------DDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSfgLGLSVNGRFWLD-LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfaHHLPRFePTSVLQTLSKYPITVFCSAAT 328
Cdd:cd05914 112 RN--IVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRM--------LVQNDMASYKFK------------------------SLKHCVSAGEPITPDVTGKWRnKTGLDIYEGY 376
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlPPGQEGDIgiQVlpnRPFGLFAHYADDPSKTAS--TLR 453
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEI--IV---RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYiTGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVVsspdpIRGEVVKAFIVLNPDY-- 530
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 795246185 531 -KSHDQEQLIKEIQEHVKK----TTAPYKYPRKVEFI-QELPKTISGKTKR 575
Cdd:cd05914 410 vKALKQRNIIDAIKWEVRDkvnqKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
93-581 |
3.49e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 128.04 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 93 VRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 173 TNDVLAP----AVDAIAPKCENLHSK--LIVSENSREGWGNIKEMM-KCASDSHTCVKTKHNEI-----------MAMFF 234
Cdd:PLN02479 123 VDQEFFTlaeeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALgKGAIEYEKFLETGDPEFawkppadewqsIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 235 TSGTSGYPKmtahthssfGLGLSVNGRFWLDLTpSDVMWNTSD-------------TGWAKSaWSsvfspwIQGACVFAH 301
Cdd:PLN02479 203 TSGTTASPK---------GVVLHHRGAYLMALS-NALIWGMNEgavylwtlpmfhcNGWCFT-WT------LAALCGTNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 302 HLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVqNDMASYKFKSLKHCV---SAGEPITPDVTGKWrNKTGLDIYEGYGQ 378
Cdd:PLN02479 266 CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAM-SEKGFRVTHTYGL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 379 TETVlicgnfkgmkiKPGSMGKPSPAFD-----------------------VKIVDVNGNVLPPGQEGDIGIQVLpnRPF 435
Cdd:PLN02479 344 SETY-----------GPSTVCAWKPEWDslppeeqarlnarqgvryiglegLDVVDTKTMKPVPADGKTMGEIVM--RGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 436 GLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PLN02479 411 MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 516 RGEVVKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFiQELPKTISGKTKRNELRKK 581
Cdd:PLN02479 491 WGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
63-580 |
7.45e-31 |
|
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: 126.41 E-value: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDQWtnmekAGKKPSNPAFwwINGkgeEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG1021 29 DLLRRR-----AERHPDRIAV--VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGtvLIPGTT--QLTQKDILYRLQSSKANCIITNDV-----LAPAVDAIAPKCENLhsKLIVSENSREGWGNIKEMmkCA 215
Cdd:COG1021 98 AG--AIPVFAlpAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSL--RHVLVVGDAGEFTSLDAL--LA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 216 SDSHTCVKTKHNEIMAMFFTS-GTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMW-------NtsdtgwakSAWSS 287
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVYLaalpaahN--------FPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 288 --VFSPWIQGAC-VFAhhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ-NDMASYKFKSLKHCVSAGEPITPDVTGK 363
Cdd:COG1021 243 pgVLGVLYAGGTvVLA---PDPSPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 364 WRNKTGLDIYEGYG-------QT------ETVLicgnfkgmkikpGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiqV 429
Cdd:COG1021 320 VRPALGCTLQQVFGmaeglvnYTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVG-----E 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 430 LPNRPFGLFAHYADDPSKTAS--TLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARafTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 508 VVSSPDPIRGEVVKAFIVLNpdykshDQEQLIKEIQEHVK-KTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVPR------GEPLTLAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
91-578 |
3.94e-30 |
|
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: 123.56 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPkcenlhSKLIVSENSREGWGNIKEMMKCASDSHtcvktkhneimaMFFTSGTSGYPKMTAHTHS 250
Cdd:cd12116 88 VLTDDALPDRLPAGLP------VLLLALAAAAAAPAAPRTPVSPDDLAY------------VIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SF-GLGLSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd12116 150 NLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQNDmasykFKSLKH----CvsAGEPITPDVTGKWRNKTGlDIYEGYGQTETVL------ICGNFKGMKIkpgsm 398
Cdd:cd12116 227 TWRMLLDAG-----WQGRAGltalC--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTAstlRGNFYITGDRGYMDEDGYFW 472
Cdd:cd12116 294 GRPLANTQVYVLDAALRPVPPGVPGELyigGDGVAQgylGRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADGRLE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 473 FVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFIVLnPDYKSHDqeqlIKEIQEHVKKTTAP 552
Cdd:cd12116 371 YLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPD----AAALRAHLRATLPA 444
|
490 500
....*....|....*....|....*.
gi 795246185 553 YKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd12116 445 YMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
72-578 |
5.32e-30 |
|
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: 123.59 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPA--FwwingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP 149
Cdd:cd17655 5 EQAEKTPDHTAvvF-------EDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDaiapkcenlHSKLIVSENSREGWGNIKEMMKCASDShtcvktkhNEI 229
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIA---------FIGLIDLLDEDTIYHEESENLEPVSKS--------DDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 230 MAMFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF-AHHLP 304
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGV-----VNLVEWANkviyQGEHLRVALFASISFDASVTE-IFASLLSGNTLYiVRKET 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 305 RFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASykFKSLKHCVSAGEPITPDVTGKW--RNKTGLDIYEGYGQTETV 382
Cdd:cd17655 214 VLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 LIC--GNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFAHYADDPSKTAstl 452
Cdd:cd17655 292 VDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRPELTAEKFVDDPFVPG--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 rGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKs 532
Cdd:cd17655 369 -ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP- 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 795246185 533 hdqeqlIKEIQEHVKKTTAPYKYPRKveFIQ--ELPKTISGKTKRNEL 578
Cdd:cd17655 447 ------VAQLREFLARELPDYMIPSY--FIKldEIPLTPNGKVDRKAL 486
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
232-580 |
6.52e-30 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 124.85 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKsawssvFSPWIQGACVFAHHLPRFE---- 307
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 -----PTSVLQTLSKYPITVFCSAATVYRMLVQND------MASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGY 376
Cdd:PTZ00237 333 knkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRP-FGLFAHYADDPSKTASTLRG 454
Cdd:PTZ00237 413 GQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPsFATTFYKNDEKFKQLFSKFP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSH- 533
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQs 571
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795246185 534 -DQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PTZ00237 572 iDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-579 |
2.19e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.82 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 105 RKFANILSeaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP----A 180
Cdd:PLN03102 51 RLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlareV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 181 VDAIAPKCENLHSKLIV------------SENSREGWGNIKEMMKCASDSHTCVKTKHNEImAMFFTSGTSGYPKMTAHT 248
Cdd:PLN03102 129 LHLLSSEDSNLNLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKGVVIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSFGL-GLSVNGRFWLDLTPSdVMWNTSD---TGWAKSaWSSVFSpwiQGACVFAHHLPRFEptsVLQTLSKYPITVFC 324
Cdd:PLN03102 208 HRGAYLsTLSAIIGWEMGTCPV-YLWTLPMfhcNGWTFT-WGTAAR---GGTSVCMRHVTAPE---IYKNIEMHNVTHMC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 325 SAATVYRMLVQNDMASYKFKSLK-HCVSAGEPiTPDVTGKWRNKTGLDIYEGYGQTET---VLIC-----------GNFK 389
Cdd:PLN03102 280 CVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlpeNQQM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 390 GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDED 468
Cdd:PLN03102 359 ELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVI-----KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 469 GYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVL--NPDYKSHDQEQLI---KEIQ 543
Cdd:PLN03102 434 GHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLI 513
|
490 500 510
....*....|....*....|....*....|....*.
gi 795246185 544 EHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PLN03102 514 EYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
234-578 |
3.67e-29 |
|
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: 120.49 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA--CVFAHHLPRfEPTSV 311
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrlVVVPYEVAR-SPEDF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 312 LQTLSKYPITVFCSAATVYRMLVQNDMASYKFK-SLKHCVSAGEPITPDVTGKWRNKTGL---DIYEGYGQTET-VLIcg 386
Cdd:cd17643 177 ARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV-- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMK---IKPGSM---GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPfGLFA-HYADDPsKTASTLR 453
Cdd:cd17643 255 TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELyvsGAGVARgylGRP-ELTAeRFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GnfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyksH 533
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 795246185 534 DQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
80-585 |
4.18e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 121.33 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 80 NPAFWWingkgEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP-GTTQL---T 155
Cdd:PRK07867 19 DRGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGlNPTRRgaaL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 156 QKDILyrlqssKANC--IITNDVLAPAVDAIAPKCEnlhsklIVSENSREgWGNikEMMKCASDSHTCVKTKHNEIMAMF 233
Cdd:PRK07867 94 ARDIA------HADCqlVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSF-GLGLSVNGRFwlDLTPSDVMWntsdtgwaksawssVFSPWIQGACVFAHHLP-------- 304
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasi 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 305 ----RFEPTSVLQTLSKYPITvfcsaatvYrmlvqndmASYKFKSLKHCVSAgePITPD--------VTG---------K 363
Cdd:PRK07867 223 alrrKFSASGFLPDVRRYGAT--------Y--------ANYVGKPLSYVLAT--PERPDdadnplriVYGnegapgdiaR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 364 WRNKTGLDIYEGYGQTETvlicgnfkGMKIK------PGSMGKPSPafDVKIVDVN-GNVLPPGQEGD---------IGI 427
Cdd:PRK07867 285 FARRFGCVVVDGFGSTEG--------GVAITrtpdtpPGALGPLPP--GVAIVDPDtGTECPPAEDADgrllnadeaIGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 428 QVLPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:PRK07867 355 LVNTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 508 VVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIKEIqeHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKT 585
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDC 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-580 |
6.74e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.14 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFwwingKGEEVRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 4559 ERARMTPDAVAV-----VFDEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaiaPKCENLHSKLIVSENSREGWgnikemmkcaSDSHTCVKTKHN 227
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL----PIPDGLASLALDRDEDWEGF----------PAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFE 307
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGK-WRNKTGLDIYEGYGQTETVLICG 386
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMK-IKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFAHYADDPSKTASTL------- 452
Cdd:PRK12316 4853 LWKARDgDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGElyLGGE-------GVARGYLERPALTAERFvpdpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 -RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK 531
Cdd:PRK12316 4926 pGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALA 5005
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 795246185 532 SHDQEQ--LIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK12316 5006 DADEAQaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
90-580 |
3.08e-28 |
|
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: 117.41 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDvlapAVDAIApkcenlhskLIVsensregwgnikemmkcasdshtcvktkhneimamfFTSGTSGYPKMTAHTH 249
Cdd:cd17653 97 LLLTTD----SPDDLA---------YII------------------------------------FTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRFepTSVLQTLSKYPITvfcsaAT 328
Cdd:cd17653 128 RGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGGTlVLADPSDPF--AHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQNDmasykFKSLKHCVSAGEPITPDVTGKWRNktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVK 408
Cdd:cd17653 199 ILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 409 IVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd17653 272 ILDADLQPVPEGVVGEIcisGVQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSpdpIRGEVVkAFIVlnPDykSHDQEQLIKEIQEHVkkttAPYKYPRK 558
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL----PSYAVPDR 411
|
490 500
....*....|....*....|..
gi 795246185 559 VEFIQELPKTISGKTKRNELRK 580
Cdd:cd17653 412 IIALDSFPLTANGKVDRKALRE 433
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
492-572 |
3.23e-28 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 107.63 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshdqEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISG 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 795246185 572 K 572
Cdd:pfam13193 76 K 76
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
74-575 |
6.42e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 117.68 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAFWWINgkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK05852 26 ATRLPEAPALVVTA---DRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 154 LTQKDILYRLQSSKANCIITnDVLAPAvDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTCVKT----KHNEI 229
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLI-DADGPH-DRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 230 MAMFfTSGTSGYPKMTAHTHSSfgLGLSVNGRFW-LDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiqGACVFAHHLP 304
Cdd:PRK05852 180 MIMF-TGGTTGLPKMVPWTHAN--IASSVRAIITgYRLSPRDatvaVMPLYHGHGLIAALLATLAS----GGAVLLPARG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 305 RFEPTSVLQTLSKYPITVFCSAATVYRMLVQ---NDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET 381
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 --------VLICGNFKGMKIKPGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLR 453
Cdd:PRK05852 333 thqvtttqIEGIGQTENPVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnPDYKSH 533
Cdd:PRK05852 407 DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795246185 534 DQEQlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKR 575
Cdd:PRK05852 485 PTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
234-580 |
1.79e-27 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 116.82 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSF---GLG-LSVNGrfwldLTPSDVMWNTS---DTGwaksAWSSVFSPWIQGAC-VFahhLPR 305
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALivqSLAkIAIVG-----YGEDDVYLHTAplcHIG----GLSSALAMLMVGAChVL---LPK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 306 FEPTSVLQTLSKYPITVFCSAATVYRMLV---QNDMASYKFKSLKHCVSAGEPIT----PDVTGKWRNKtglDIYEGYGQ 378
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSsrllPDAKKLFPNA---KLFSAYGM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 379 TET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFDVKIvdvngnvlppGQEGDIGIQVLPNRPF 435
Cdd:PLN02860 324 TEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKI----------GLDESSRVGRILTRGP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 436 GLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 514
Cdd:PLN02860 394 HVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795246185 515 IRGEVVKAFIVLNPDYK-SHDQEQLIK--------EIQEHV-KKTTAPYKYPRK-VEFIQELPKTISGKTKRNELRK 580
Cdd:PLN02860 474 RLTEMVVACVRLRDGWIwSDNEKENAKknltlsseTLRHHCrEKNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
90-579 |
4.43e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 115.23 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIitndVLAPA---------VDAIAPKCENLHSKLIVSENS--------REGWGNIKEMMKCASDSHTCVKTKHNEIMAM 232
Cdd:PRK06164 110 WL----VVWPGfkgidfaaiLAAVPPDALPPLRAIAVVDDAadatpapaPGARVQLFALPDPAPPAAAGERAADPDAGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 233 FFT-SGTSGYPKMTAHTHSSF---------GLGLSVNGRFWLDLTPSDVMwntsdtgwaksAWSSVFSPWIQGACVfaHH 302
Cdd:PRK06164 186 LFTtSGTTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 303 LPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDmASYKFKSLKHCVSAgepitpDVTGKWRN------KTGLDIYEG 375
Cdd:PRK06164 253 EPVFDAARTARALRRHRVThTFGNDEMLRRILDTAG-ERADFPSARLFGFA------SFAPALGElaalarARGVPLTGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 376 YGQTE--TVLICGNFK---GMKIKPGsmGKP-SPAFDVKIVDV-NGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKT 448
Cdd:PRK06164 326 YGSSEvqALVALQPATdpvSVRIEGG--GRPaSPEARVRARDPqDGALLPDGESGEIEIRA-PS----LMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 449 ASTLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpdPIRGEVVKAFIVLN 527
Cdd:PRK06164 399 ARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIP 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 528 PDYKSHDQEQLIKeiqeHVKKTTAPYKYPRKVEFIQELPKTISG---KTKRNELR 579
Cdd:PRK06164 477 TDGASPDEAGLMA----ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
87-581 |
4.98e-27 |
|
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: 114.87 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 87 NGKGEEVRWSfeELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 167 KANCIIT-----NDVLAPAVDAIAPKCE-NLHSKLivseNSREGWGNIkemMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:cd05932 78 ESKALFVgklddWKAMAPGVPEGLISISlPPPSAA----NCQYQWDDL---IAQHPPLEERPTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 241 YPKMTAHTHSSFGLGLSvNGRFWLDLTPSDVMWntSDTGWAKSAWSS-VFSPWIQGACV--FAHHLPRFeptsvLQTLSK 317
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQ-AGIEHIGTEENDRML--SYLPLAHVTERVfVEGGSLYGGVLvaFAESLDTF-----VEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 318 YPITVFCSAA---TVYRMLVQNDMASYKFKSL----------KHCVSAG-------------EPITPDVTgKWRNKTGLD 371
Cdd:cd05932 223 ARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPPALL-EWYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIvdvngnvlppGQEGDIGIqvlpnRPFGLFAHYADDPSKTAST 451
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALMMGYYKDPEATAEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 452 LRGN-FYITGDRGYMDEDGYFWFVARSDDIILSS-GYRIGPFEVENALNEHPSVAESAVVSS--PDPIRGEVVKAFIVLN 527
Cdd:cd05932 367 FTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLR 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795246185 528 PDYKSHDQ-EQLIKEIQEHVKKTTAPYKYPRKVEFIQElPKTISG-------KTKRNELRKK 581
Cdd:cd05932 447 ADAFARAElEASLRAHLARVNSTLDSHEQLAGIVVVKD-PWSIDNgiltptlKIKRNVLEKA 507
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-572 |
6.64e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 112.48 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSFGLGLS-----VNGRFWLDLTPSDVMWNTSDTGW--------AKSAWSSVFSPWIQGACV 298
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 299 FahHLPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTGKW-RNKTGLDIYE 374
Cdd:cd05924 88 L--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfahYADDPSKTASTLR 453
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARRGHIPLG----YYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 ---GNFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd05924 240 evdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795246185 530 YKSHDQeqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd05924 320 AGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
346-578 |
2.65e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.78 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 346 LKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGD 424
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 425 I--GIQVLPNRpfglfahYADDPSKtaSTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPS 502
Cdd:PRK13383 374 IfvGGELAGTR-------YTDGGGK--AVVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 503 VAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQlikeIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
91-529 |
9.31e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 113.03 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNikemmkcASDSHTCVktkhneIMamfFTSGTSGYPKMTAHTHS 250
Cdd:COG1020 577 VLTQSALAARLPELGVPVLALDALALAAEPATNPPVP-------VTPDDLAY------VI---YTSGSTGRPKGVMVEHR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFG-LGLSVNGRFwlDLTPSDVM-WNTS---DTgwakSAWSsVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYPITVFC 324
Cdd:COG1020 641 ALVnLLAWMQRRY--GLGPGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 325 SAATVYRMLVQNDMASykFKSLKHCVSAGEPITPDVTGKWRNKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM--G 399
Cdd:COG1020 714 LTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSVpiG 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 400 KPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglfAH-YADDPSKTA--------STLRGNFYITGDRGYMDE 467
Cdd:COG1020 792 RPIANTRVYVLDAHLQPVPVGVPGELyigGAGL---------ARgYLNRPELTAerfvadpfGFPGARLYRTGDLARWLP 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 468 DGYFWFVARSDD---IilsSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:COG1020 863 DGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
90-580 |
1.01e-25 |
|
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: 111.22 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPR----VPEWWlanvACLRTGTVLIPGTTQLTqkdilYRLQS 165
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----YDEPN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 166 SKAN------------CIITNDVLAPAVDAIAPKCENLHSKLIVSENSREgwgnikemmkCASDSHTCVKTKhNEIMAMF 233
Cdd:cd05906 105 ARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLD----------TAADHDLPQSRP-DDLALLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSF---GLGLSVNGRFwldlTPSDVMWNtsdtgwaksawssvfspWIQ----GACVFAHHLPRF 306
Cdd:cd05906 174 LTSGSTGFPKAVPLTHRNIlarSAGKIQHNGL----TPQDVFLN-----------------WVPldhvGGLVELHLRAVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 307 ---------------EPTSVLQTLSKYPITVFCSAATVYRMLVQ----NDMASYKFKSLKHCVSAGEPITPDVTGKWRN- 366
Cdd:cd05906 233 lgcqqvhvpteeilaDPLRWLDLIDRYRVTITWAPNFAFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 367 --KTGLD---IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPnrp 434
Cdd:cd05906 313 lePYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 435 fgLFAHYADDPSKTASTLR-GNFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAES--AVVSS 511
Cdd:cd05906 390 --VTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 512 PDPIRGEVVKAfIVLNPDYKSHDQ-EQLIKEIQEHV-KKTTAPYKY----PRkvefiQELPKTISGKTKRNELRK 580
Cdd:cd05906 467 RDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVsREVGVSPAYliplPK-----EEIPKTSLGKIQRSKLKA 535
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
71-578 |
1.66e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 110.48 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 71 MEKAGKKPSNPAFWWINGKGEevrWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 151 TTQLTQKDIlyrlqssKANCIITNdvlaPAVDAIAPKC--------ENLHSKLIVSENSREGWGNikemMKCASDSH--- 219
Cdd:PRK05857 97 DGNLPIAAI-------ERFCQITD----PAAALVAPGSkmassavpEALHSIPVIAVDIAAVTRE----SEHSLDAAsla 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 220 TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLG---LSVNGRFWLDltpsdvmWNTSDTGWAKSAWSSVFSPW---- 292
Cdd:PRK05857 162 GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVT-------WVVGETTYSPLPATHIGGLWwilt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 293 --IQGA-CVFAHHlprfEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAG-EPITPDVtgKWRNK 367
Cdd:PRK05857 235 clMHGGlCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADV--RFIEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 368 TGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG---NVLPPGQEGDIGIQVLPNrPFGLFA 439
Cdd:PRK05857 309 TGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSASFGTLWIKS-PANMLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 440 hYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 519
Cdd:PRK05857 388 -YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 795246185 520 VKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK05857 467 VGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
289-573 |
3.26e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 111.17 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 289 FSPWIQGACVFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTGKWRNK 367
Cdd:PRK08633 843 WLPLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHpLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 368 TGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GIQVLpnr 433
Cdd:PRK08633 922 FGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLIligGPQVM--- 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 434 pfglfAHYADDPSKTASTLR----GNFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PF-EVENALNE--HPS 502
Cdd:PRK08633 999 -----KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalGGE 1068
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 503 VAESAVVSSPDPIRGEVVkafIVLnpdyksHDQEQL-IKEIQEHVKKTTAP--YKyPRKVEFIQELPKTISGKT 573
Cdd:PRK08633 1069 EVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKL 1132
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
91-582 |
1.07e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.78 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITNdvlaPAVDAIAPKCENLHSkLIVSENSREGWGnikemmkcASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:PRK12467 613 LLTQ----SHLLAQLPVPAGLRS-LCLDEPADLLCG--------YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLPR---FEPTSVLQTLSKYPITVFCSAA 327
Cdd:PRK12467 680 ALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 328 TVYRMLVQnDMASYKFKSLKHCVSAGEPITPDVTGKWRNKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMGKPS 402
Cdd:PRK12467 756 SHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 403 PAFDVKIVDVNGNVLPPGQEGD--IGIQVLPN----RPfGLFAHY-ADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVA 475
Cdd:PRK12467 835 ANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRP-ALTAERfVPDPFGADG---GRLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFIVlnPDYKSHDQEQLIK--EIQEHVKKTTAPY 553
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHQATrdELKAQLRQVLPDY 987
|
490 500
....*....|....*....|....*....
gi 795246185 554 KYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLDRKALPKPD 1016
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
92-578 |
2.53e-23 |
|
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: 103.50 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12114 10 DGTLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLAPAVDAIAPKcenlhskLIVSENSREGWgniKEMMKCASDSHTcvktkhneiMA-MFFTSGTSGYPKMTAHTHS 250
Cdd:cd12114 89 LTDGPDAQLDVAVFDV-------LILDLDALAAP---APPPPVDVAPDD---------LAyVIFTSGSTGTPKGVMISHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 S-FGLGLSVNGRFwlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd12114 150 AaLNTILDINRRF--AVGPDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQNDMASYKFK-SLKHCVSAGEPITPDVTGKWRNKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 399
Cdd:cd12114 227 LLEMLLDVLEAAQALLpSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 400 KPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTAS-----TLRGNFYITGDRGYMDEDGYF 471
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGELwigGR--------GVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAFIVLNPDYKSHDQEqlikEIQEHVKKTTA 551
Cdd:cd12114 376 EFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPD----ALRAFLAQTLP 450
|
490 500
....*....|....*....|....*..
gi 795246185 552 PYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd12114 451 AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
234-580 |
3.03e-23 |
|
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: 103.01 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPS-----------DVMWNtsdtgwaksawsSVFSPWIQGACVFA-- 300
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRA-LGLTSEsrvlqfasytfDVSIL------------EIFTTLAAGGCLCIps 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 301 -----HHLPRFeptsvlqtLSKYPITVFCSAATVYRMLVQNDmasykFKSLKHCVSAGEPITPDVTGKWRNKTGLdiYEG 375
Cdd:cd05918 180 eedrlNDLAGF--------INRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTWADRVRL--INA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 376 YGQTE-TVLICGNFKGMKIKPGSMGKPSPAFdVKIVDVNGN--VLPPGQEGDI---GIQVLPnrpfGlfahYADDPSKTA 449
Cdd:cd05918 245 YGPAEcTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHdrLVPIGAVGELlieGPILAR----G----YLNDPEKTA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 450 --------------STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:cd05918 316 aafiedpawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 516 RGEVVK---AFIVLNPDYKSHDQEQ------------LIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05918 396 DGSSSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-580 |
4.51e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 103.32 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 NDVLAPAVDAIAPKCENLHSKLIVSENS-REGWGNIKEMMKCAS-----DSHTCV----KTKHNEIMAMFFTSGTSGYPK 243
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 244 MTAHTHSSFGL---------GLSV-NGRFWLDLTPsdvMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQ 313
Cdd:PRK05620 198 GVVYSHRSLYLqslslrttdSLAVtHGESFLCCVP---IYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 314 TLSKYPiTVFCSaatvyrMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLIcgnfkGMKI 393
Cdd:PRK05620 275 VAHGVP-TLWIQ------LMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----GTVA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 394 KPG-------------SMGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVLPNRpfgLFAHYADDPSKT----ASTLRGN- 455
Cdd:PRK05620 343 RPPsgvsgearwayrvSQGRFPASLEYRIVN-DGQVMESTDRNEGEIQVRGNW---VTASYYHSPTEEgggaASTFRGEd 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 456 ------------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:PRK05620 419 vedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 795246185 524 IVLNPDYKSHDQ--EQLIKEIQEHVKKTTAPYKYprkvEFIQELPKTISGKTKRNELRK 580
Cdd:PRK05620 499 TVLAPGIEPTREtaERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
399-580 |
7.32e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 102.38 E-value: 7.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVLPNR-PFgLFAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFVA 475
Cdd:PRK10946 356 GRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKS-----HDQEQLIkeiqehvkktt 550
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAvqlrrFLREQGI----------- 498
|
170 180 190
....*....|....*....|....*....|
gi 795246185 551 APYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK10946 499 AEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
96-545 |
8.49e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 102.28 E-value: 8.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKANCII 172
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 173 TNDvLAPAVDAIAP-KCENLHSKLIVSenSREGWGN--IKEMMKCASD-SHTCVKTKHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:PRK09274 119 GIP-KAHLARRLFGwGKPSVRRLVTVG--GRLLWGGttLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGVVYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 249 HSSF---------GLGLSVNGRfwlDLTPSDVMwntsdtgwaksawsSVFSPWIQGACVfahhLPRFEPT--------SV 311
Cdd:PRK09274 196 HGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGPALGMTSV----IPDMDPTrpatvdpaKL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 312 LQTLSKYPIT-VFCSAA---TVYRMLVQNDMasyKFKSLKHCVSAGEPITPDVTGKWRN--KTGLDIYEGYGQTETVLIC 385
Cdd:PRK09274 255 FAAIERYGVTnLFGSPAlleRLGRYGEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 gnfkgmKIkpGS------------------MGKPSPAFDVKIVDVNGN---------VLPPGQEGDI---GIQVLP---N 432
Cdd:PRK09274 332 ------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAISDApipewddalRLATGEIGEIvvaGPMVTRsyyN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 433 RPfglfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSP 512
Cdd:PRK09274 404 RP------EATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
490 500 510
....*....|....*....|....*....|....
gi 795246185 513 DPirGEVVKAFIV-LNPDyKSHDQEQLIKEIQEH 545
Cdd:PRK09274 478 VP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
96-578 |
1.07e-22 |
|
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: 101.18 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd17652 14 TYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 vlapavdaiapKCENLhsklivsensregwgnikemmkcasdshtcvktkhneiMAMFFTSGTSGYPKMTAHTHSSFGlG 255
Cdd:cd17652 91 -----------TPDNL--------------------------------------AYVIYTSGSTGRPKGVVVTHRGLA-N 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfahHLPrfePTSVLQ-------TLSKYPITVFCSAAT 328
Cdd:cd17652 121 LAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL---VLA---PAEELLpgepladLLREHRITHVTLPPA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQNDMASykfksLKHCVSAGEPITPDVTGKWrnKTGLDIYEGYGQTETVL---ICGNFKGMKIKPgsMGKPSPAF 405
Cdd:cd17652 194 ALAALPPDDLPD-----LRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVcatMAGPLPGGGVPP--IGRPVPGT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 406 DVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTA--------STLRGNFYITGDRGYMDEDGYFWFV 474
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELyiaGA--------GLARGYLNRPGLTAerfvadpfGAPGSRMYRTGDLARWRADGQLEFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 475 ARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLikeiQEHVKKTTAPYK 554
Cdd:cd17652 337 GRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG-AAPTAAEL----RAHLAERLPGYM 411
|
490 500
....*....|....*....|....
gi 795246185 555 YPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17652 412 VPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
234-578 |
1.37e-22 |
|
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: 100.85 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSfglglSVNGRFWLDLT-PSD----VMWNTSdTGWAKSAWSsVFSPWIQGACVF----AHHL- 303
Cdd:cd12115 112 YTSGSTGRPKGVAIEHRN-----AAAFLQWAAAAfSAEelagVLASTS-ICFDLSVFE-LFGPLATGGKVVladnVLALp 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 304 --PRFEPTSVLQTLskyPitvfcSAAtvyRMLVQNDMASykfKSLKHCVSAGEPITPDVTGK-WRNKTGLDIYEGYGQTE 380
Cdd:cd12115 185 dlPAAAEVTLINTV---P-----SAA---AELLRHDALP---ASVRVVNLAGEPLPRDLVQRlYARLQVERVVNLYGPSE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 381 -----TVLICGnfKGMKIKPgSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTASTL 452
Cdd:cd12115 251 dttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELyigGA--------GVARGYLGRPGLTAERF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 RGN-------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIV 525
Cdd:cd12115 320 LPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 795246185 526 LNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd12115 400 AEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
229-585 |
3.41e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 100.49 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 229 IMAMFFTSGTSGYPKMTAHTHSSFG-LGLSVNGRFwlDLTPSDVMW--------NTSDTGWAKSAwssvfspwIQGACVF 299
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV--------ASGAAVA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 AHhlPRFEPTSVLQTLSKYPITVFcsaATVYRMLvqndmaSYKFKSLKHCVSAGEPIT--------PDVTGKWRNKTGLD 371
Cdd:PRK13388 222 LP--AKFSASGFLDDVRRYGATYF---NYVGKPL------AYILATPERPDDADNPLRvafgneasPRDIAEFSRRFGCQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTETVLICGNFKGMKikPGSMGKPSPafDVKIVDV-------------NGNVLPPgqegDIGIQVLPNRP-FGL 437
Cdd:PRK13388 291 VEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIYNPetltecavarfdaHGALLNA----DEAIGELVNTAgAGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 438 FAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:PRK13388 363 FEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795246185 518 EVVKAFIVLNPDYKS---------HDQEQLikeiqehvkkttAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKT 585
Cdd:PRK13388 443 DQVMAALVLRDGATFdpdafaaflAAQPDL------------GTKAWPRYVRIAADLPSTATNKVLKRELIAQGWAT 507
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
224-578 |
5.12e-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: 99.43 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 224 TKHNEIMAMFFTSGTSGYPKMTAHTHSS---FGLGLSVNgrfwLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VF 299
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSlvnLSHGLIKE----YGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 300 AHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVqNDMASYKF---KSLKHCVSAGEPITPDVTGKWRNKTGLDI--YE 374
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLV-LELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 375 GYGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA 449
Cdd:cd17644 257 VYGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 450 STLRGN---------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVV 520
Cdd:cd17644 332 EKFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 521 KAFIVlnPDYkshDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17644 412 VAYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-580 |
5.25e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 99.95 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 63 DVLDQWtnmekAGKKPSNPAFwwingKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK08279 41 DVFEEA-----AARHPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 143 TGTV--LIpgTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHT 220
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 221 CVKTKHNEIMA-----MFFTSGTSGYPKMTAHTH-----SSFGLGLSvngrfwLDLTPSDVMWNT----SDTGwAKSAWS 286
Cdd:PRK08279 188 TNPASRSGVTAkdtafYIYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 287 SVFSPwiqGACV-----FAhhLPRFEPTSVlqtlsKYPITVFCSAATVYRMLV-QNDMASYKFKSLKHCVSAGepITPDV 360
Cdd:PRK08279 261 SVLAA---GATLalrrkFS--ASRFWDDVR-----RYRATAFQYIGELCRYLLnQPPKPTDRDHRLRLMIGNG--LRPDI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 361 TGKWRNKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFDVK---IV-----------DVNGNVLP--PGQ 421
Cdd:PRK08279 329 WDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLAHpyaIVkydvdtgepvrDADGRCIKvkPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 422 EGD-IGiQVLPNRPF-GlfahYAdDPSKT-ASTLRGNF------YITGDRGYMDEDGYFWFVARSDDIilssgYR----- 487
Cdd:PRK08279 403 VGLlIG-RITDRGPFdG----YT-DPEASeKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgen 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 488 IGPFEVENALNEHPSVAESAV--VSSPDpIRGEVVKAFIVLnpdyksHDQEQL-IKEIQEHVKKTTAPYKYPRKVEFIQE 564
Cdd:PRK08279 472 VATTEVENALSGFPGVEEAVVygVEVPG-TDGRAGMAAIVL------ADGAEFdLAALAAHLYERLPAYAVPLFVRLVPE 544
|
570
....*....|....*.
gi 795246185 565 LPKTISGKTKRNELRK 580
Cdd:PRK08279 545 LETTGTFKYRKVDLRK 560
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
92-509 |
7.86e-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: 98.59 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKanci 171
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 itndvlapavdaiapkcenlhSKLIVSENSregwgnikemmkcasdshtcvktkHNEIMAMFFTSGTSGYPKMTAHTHSS 251
Cdd:cd17640 78 ---------------------SVALVVEND------------------------SDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 252 FGLGLSvngRFW--LDLTPSDVMWntsdtgwaksawsSVFSPW-----------IQGACVFAHHLPRFeptsVLQTLSKY 318
Cdd:cd17640 113 LLHQIR---SLSdiVPPQPGDRFL-------------SILPIWhsyersaeyfiFACGCSQAYTSIRT----LKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 319 PITVFCSAATVYRMLVQN------DMASYKFKSLKHCVSAGE---PIT-----PDVTGKWRNKTGLDIYEGYGQTET--V 382
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGiqkqvsKSSPIKQFLFLFFLSGGIfkfGISgggalPPHVDTFFEAIGIEVLNGYGLTETspV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 LICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGN-FY 457
Cdd:cd17640 253 VSARRLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVwvrGPQVMKG--------YYKNPEATSKVLDSDgWF 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 795246185 458 ITGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd17640 323 NTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
92-580 |
4.51e-21 |
|
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: 96.73 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLApavdAIAPKCENLHSKLIVSENSREGWGNIKEMMKCASDSHTCVK-TKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:cd05915 101 LFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFGLGLSVNGRF-WLDLTPSDVMWNTSDTgWAKSAWSSVFS-PWIQGACVFAHHLPRFEptSVLQTLSKYPITVFCSAAT 328
Cdd:cd05915 177 ALVLHSLAASLVdGTALSEKDVVLPVVPM-FHVNAWCLPYAaTLVGAKQVLPGPRLDPA--SLVELFDGEGVTFTAGVPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQ-NDMASYKFKSLKHCVSAGEPiTPDVTGKWRNKTGLDIYEGYGQTETVLI------------CGNFKGMKIK- 394
Cdd:cd05915 254 VWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVvvqnfvkshlesLSEEEKLTLKa 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 395 ---------------PGSMGKPSPAFDVKIVDVNGNVLPPGqegdigiqvlpnrpfglfaHYADDPSKTASTLRGNFYIT 459
Cdd:cd05915 333 ktglpiplvrlrvadEEGRPVPKDGKALGEVQLKGPWITGG-------------------YYGNEEATRSALTPDGFFRT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 460 GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdykshDQEQLI 539
Cdd:cd05915 394 GDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------GEKPTP 467
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795246185 540 KEIQEHVKKTTAPYKY-PRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05915 468 EELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
94-578 |
1.42e-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: 94.54 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 NdvlapavdaiapkcenlhsklivSENsregwgnikemmkcasdshtcvktkhneIMAMFFTSGTSGYPKMTAHTHSSFg 253
Cdd:cd17645 102 N-----------------------PDD----------------------------LAYVIYTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 254 lglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLPRfEPTSVLQTLSKY------PITVF 323
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPS-ERRLDLDALNDYfnqegiTISFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 324 CSAATVYRMLVQNdmasykfKSLKHCVSAGepitpDVTGKWRNKtGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPS 402
Cdd:cd17645 202 PTGAAEQFMQLDN-------QSLRVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 403 PAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVA 475
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLIKEIQEHVKKTTAPYKY 555
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMI 416
|
490 500
....*....|....*....|...
gi 795246185 556 PRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
234-584 |
1.86e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.38 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFEPTSVLQ 313
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQ 3321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 314 TLSKYPITVFCSAATVYRMLVQN-DMASYKfkSLKHCVSAGEPITPDVTGKWRNKTG-LDIYEGYGQTETVLI-----CG 386
Cdd:PRK12467 3322 AIHAHRISIACFPPAYLQQFAEDaGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCG 3399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA--------STLRGNFYI 458
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYR 3474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFIVLNPdykshDQEQL 538
Cdd:PRK12467 3475 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDW 3548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 795246185 539 IKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWK 584
Cdd:PRK12467 3549 RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK 3594
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-580 |
2.49e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 172 ITNDVLA-PAVDAIAPKCENLHSKLIVSENSRegwgnikemmkcasdshtcVKTKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLDLDRGDENYAEANPA-------------------IRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFGLGLSVNGRFwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACV-FAHHLPRFEPTSVLQTLSKYPITVFCSAATV 329
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVvLAGPEDWRDPALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 330 YRMLVQNDMASyKFKSLKHCVSAGEPITPDVTGKWrnKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFDV 407
Cdd:PRK12316 3298 LQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRAC 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 408 KIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDI 480
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDpfvpgerLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 481 ILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFIVLnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKVE 560
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP-----EDEAGDLREALKAHLKASLPEYMVPAHLL 3520
|
490 500
....*....|....*....|
gi 795246185 561 FIQELPKTISGKTKRNELRK 580
Cdd:PRK12316 3521 FLERMPLTPNGKLDRKALPR 3540
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
178-579 |
4.26e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 94.00 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 178 APAVDAIAPKCENLHSKLIVSENSREGWGNI-----KEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSS- 251
Cdd:PRK07008 122 LPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSt 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 252 ----FGLGLSVNgrfwLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQGA-CVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK07008 202 vlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSAPLTGAkLVLPG--PDLDGKSLYELIEAERV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 321 TVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLIcGNFKGMKIKPGSM- 398
Cdd:PRK07008 269 TFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCKLKWKHSQLp 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 -----------GKPSPAFDVKIVDVNGNVLP-PGQE-GDIgiqvLPNRPFGLFAHYADDpsktASTLRGNFYITGDRGYM 465
Cdd:PRK07008 348 ldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDL----QVRGPWVIDRYFRGD----ASPLVDGWFPTGDVATI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 466 DEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShDQEQLIKeiqeH 545
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEV-TREELLA----F 494
|
410 420 430
....*....|....*....|....*....|....
gi 795246185 546 VKKTTAPYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PRK07008 495 YEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
74-580 |
5.09e-20 |
|
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: 93.84 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 74 AGKKPSNPAF-WWINGKGEEVRWSFEELGSLSRKFANILSEACslQRGDRVILILPRVPEWWLANVACLRTGTV---LIP 149
Cdd:cd05931 3 AAARPDRPAYtFLDDEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDA-IAPKCENLHSKLIVSENSREGwgnikemmkcASDSHTCVKTKHNE 228
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAfAASRPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 229 IMAMFFTSGTSGYPK--MTAHT--HSSFGLGLSVngrfwLDLTPSDVMWNtsdtgwaksaW----------SSVFSPWIQ 294
Cdd:cd05931 151 IAYLQYTSGSTGTPKgvVVTHRnlLANVRQIRRA-----YGLDPGDVVVS----------WlplyhdmgliGGLLTPLYS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 295 GA-CVFAHhlPR-F--EPTSVLQTLSKYPITvfCSAAT--VYRMLVQ----NDMASYKFKSLKHCVSAGEPITPDVTGKW 364
Cdd:cd05931 216 GGpSVLMS--PAaFlrRPLRWLRLISRYRAT--ISAAPnfAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 365 RNK---TGLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFDVKIVDV 412
Cdd:cd05931 292 AEAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 413 NGN-VLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLR-------GNFYITGDRGYMDeDGYFWFVARSDDIILSS 484
Cdd:cd05931 372 ETGrELPDGEVGEIWVRG-PS----VASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 485 GYRIGPFEVENAL-NEHPSVAES--AVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLIKEIQ-----EH-VKkttapyky 555
Cdd:cd05931 446 GRNHYPQDIEATAeEAHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRaavarEHgVA-------- 516
|
570 580
....*....|....*....|....*..
gi 795246185 556 PRKVEFI--QELPKTISGKTKRNELRK 580
Cdd:cd05931 517 PADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-578 |
5.15e-20 |
|
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: 93.31 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSeaCSLQRGDRVILI-LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLR--EKGVKKDSIVAImMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 170 CIITNDVLApavdaIAPKCENLHSKLIVSENSREGWGNIKemmkcasdshtcVKTKHNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:cd17656 88 VVLTQRHLK-----SKLSFNKSTILLEDPSISQEDTSNID------------YINNSDDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 250 SSFGLGLSVNGRFWLDLTPSDVMWNTSDTgwAKSAWSSVFSPWIQGACVF-AHHLPRFEPTSVLQTLSKYPI-TVFCSAA 327
Cdd:cd17656 151 KNMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIeVVFLPVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 328 TVYRMLVQNDMASYKFKSLKHCVSAGEP-ITPDVTGKWRNKTGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------MG 399
Cdd:cd17656 229 FLKFIFSEREFINRFPTCVKHIITAGEQlVITNEFKEMLHEHNVHLHNHYGPSETHVV----TTYTINPEAeipelppIG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 400 KPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV---LPNRPFGLFAHYADDPSKTASTLrgnfYITGDRGYMDEDGYFWF 473
Cdd:cd17656 305 KPISNTWIYILDQEQQLQPQGIVGELyisGASVargYLNRQELTAEKFFPDPFDPNERM----YRTGDLARYLPDGNIEF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLIKEIQEHVKKTTAPY 553
Cdd:cd17656 381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNISQLREYLAKQLPEY 453
|
490 500
....*....|....*....|....*
gi 795246185 554 KYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17656 454 MIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-580 |
7.97e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 2011 EQAARAPEAIAVVF----GDQ-HLSYAELDSRANRLAHRL-----RARGvgpeVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLApavdAIAPKCENLHSKLIVSENSREGWgnikemmkcaSDSHTCVKTKHN 227
Cdd:PRK12316 2081 VPLDPNYPAERLAYMLEDSGAALLLTQRHLL----ERLPLPAGVARLPLDRDAEWADY----------PDTAPAVQLAGE 2146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFE 307
Cdd:PRK12316 2147 NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPD-VTGKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:PRK12316 2225 PEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAAsLRLAWEALRPVYLFNGYGPTEAVVTPL 2304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMKIKPGS-----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFAHYADDPSKTA--------ST 451
Cdd:PRK12316 2305 LWKCRPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGElyLGGE-------GLARGYLNRPGLTAerfvpdpfSA 2377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 452 LRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFIVlnPDyk 531
Cdd:PRK12316 2378 SGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD-- 2452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 795246185 532 sHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK12316 2453 -DAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
122-578 |
2.09e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.30 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 122 RVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaiaPKCENLHSKLIVSENs 201
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQED- 1700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 202 regwgnikEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWA 281
Cdd:PRK12467 1701 --------DWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFD 1771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 282 KSAWSsVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDV 360
Cdd:PRK12467 1772 VSVWE-LFWPLINGArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEA 1850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 361 TGKWRNKTG-LDIYEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqv 429
Cdd:PRK12467 1851 LRPWLERLPdTGLFNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELylgGV-- 1926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 430 lpnrpfGLFAHYADDPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHP 501
Cdd:PRK12467 1927 ------GLARGYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQG 2000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 502 SVAESAVVSSpDPIRGEVVKAFIV-LNPDYKSHDQEQ--LIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK12467 2001 GVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAQvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-528 |
2.89e-19 |
|
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: 91.33 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 175 DvlAPAVDAIAPKCENLHS--KLIVSE-----NSREGW----GNIKEMMKCASDSHTCV------KTKHNEIMAMFFTSG 237
Cdd:cd17641 91 D--EEQVDKLLEIADRIPSvrYVIYCDprgmrKYDDPRlisfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 238 TSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfahHLPRfEPTSVLQTLSK 317
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPE-EPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 318 YPITVFCSAATV------------------------------YRMLVQN---------DMASYK---------------F 343
Cdd:cd17641 244 IGPTFVLLPPRVwegiaadvrarmmdatpfkrfmfelgmklgLRALDRGkrgrpvslwLRLASWladallfrplrdrlgF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 344 KSLKHCVSAGEPITPDVTGKWRnKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVnGNVLPPGQeg 423
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-GEILVRSP-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 424 digiqvlpnrpfGLFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDI-ILSSGYRIGPFEVENALNEHP 501
Cdd:cd17641 400 ------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSP 467
|
490 500
....*....|....*....|....*..
gi 795246185 502 SVAESAVVSSPDPIrgevVKAFIVLNP 528
Cdd:cd17641 468 YIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
96-582 |
6.23e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 91.26 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 176 VLA---PAVDAIAPKCENlhSKLIVSENSREGWGnikemmkcaSDSHTCVktkhneimaMFFTSGTSGYPKMTAHTHSSF 252
Cdd:PRK10252 564 DQLprfADVPDLTSLCYN--APLAPQGAAPLQLS---------QPHHTAY---------IIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 253 glglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF-----AHHlprfEPTSVLQTLSKYPITV- 322
Cdd:PRK10252 624 -----VNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTt 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 323 ---------FCSAATVyrmlvqnDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET-VLICGNFKGMK 392
Cdd:PRK10252 694 hfvpsmlaaFVASLTP-------EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 393 IKPGSMGKPSP-AFDV-----KIVDVNGNVLPPGQEGDI---GIQvlpnrpfgLFAHYADDPSKTASTLRGN-------F 456
Cdd:PRK10252 767 ELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfapgerM 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 457 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA----VVSSPDPIRGEVVK--AFIVLNPDY 530
Cdd:PRK10252 839 YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDARQlvGYLVSQSGL 918
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 795246185 531 kSHDQEQLikeiQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK10252 919 -PLDTSAL----QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPE 965
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
376-580 |
6.70e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 89.67 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 376 YGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFDVKIVdvngnvlpPGQEGDIGIQVlPNRPFGLFAHYADDPsk 447
Cdd:PRK07445 261 YGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITIP--------ANQTGNITIQA-QSLALGYYPQILDSQ-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 448 tastlrgNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVln 527
Cdd:PRK07445 324 -------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV-- 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 795246185 528 PDYKSHDQEqlikEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK07445 395 PKDPSISLE----ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-582 |
1.04e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.79 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK12316 519 EQVERTPEAPALAF----GEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 152 TQLTQKDILYRLQSSKANCIITNDVLAPAVDaIAPKCENLHSKLIVSENSREGWGNIKemmkcasdshTCVktkHNEIMA 231
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYSEENPG----------TEL---NPENLA 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 -MFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAHHLPR 305
Cdd:PRK12316 659 yVIYTSGSTGKPKGAGNRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDH 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQnDMASYKFKSLKHCVSAGEPITPD----VTGKwRNKTGLdiYEGYGQTET 381
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLRRIVCSGEALPADaqeqVFAK-LPQAGL--YNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 382 VLICGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqVLPNRpfGLFAHYADDPSKTASTLRGN---- 455
Cdd:PRK12316 809 AIDVTHWTCVEEGGDSvpIGRPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfva 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 456 ---FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFIVLNPDYKS 532
Cdd:PRK12316 884 gerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD 959
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 795246185 533 hdqeqLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK12316 960 -----WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPE 1004
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
459-582 |
3.48e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 87.01 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnpdykSHDQEQL 538
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 795246185 539 IkEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKE 582
Cdd:PRK08308 369 V-QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
90-581 |
8.63e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 86.73 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILI---LPRVPEWWLAnvaCLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQAL-DRDGIKLGDRVATIawnTWRHLEAWYG---IMGIGAICHTVNPRLFPEQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 167 KANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNIK------EMMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:PRK06018 111 EDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKnavayeEWIAEADGDFAWKTFDENTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 241 YPKMTAHTHSSFGL-GLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFahhLP--RFEPTSVLQTLSK 317
Cdd:PRK06018 191 DPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 318 YPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPItPDVTGKWRNKTGLDIYEGYGQTETVLI--CGNFKG---- 390
Cdd:PRK06018 267 EKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgtLAALKPpfsk 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 391 ------MKIKPgSMGKPSPAFDVKIVDVNGNVLPpgQEGDIGIQVLPNRP------FGLFAHYADDpsktastlRGnFYI 458
Cdd:PRK06018 346 lpgdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDGKTFGRLKVRGPavaaayYRVDGEILDD--------DG-FFD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQL 538
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG-ETATREEI 492
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 795246185 539 IKEIQEHVKKttapYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK06018 493 LKYMDGKIAK----WWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
372-581 |
1.46e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.72 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqVLPNRPFGlfahYA 442
Cdd:PRK04813 289 IYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGPSVSKG----YL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 443 DDPSKTAS---TLRGN-FYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVsspdPI-RG 517
Cdd:PRK04813 360 NNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYnKD 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 518 EVVK---AFIVLNPdyksHDQE---QLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKK 581
Cdd:PRK04813 435 HKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEE 500
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
234-572 |
6.63e-17 |
|
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: 83.60 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPK--MTAHtHSSFGLGLSVNGRFWLDLTPSDVMWNTSdtgwaksawSSVFSPWIQGAC--VFAHH----LP- 304
Cdd:cd17648 101 YTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS---------NYVFDFFVEQMTlaLLNGQklvvPPd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 305 --RFEPTSVLQTLSKYPITVFCSAATVyrmLVQNDMASykFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETV 382
Cdd:cd17648 171 emRFDPDRFYAYINREKVTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 L--ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTAS-TLR 453
Cdd:cd17648 246 VtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELylgGDGVARgylNRPELTAERFLPNPFQTEQeRAR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 454 GNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP-IRGEVVKAFIVlnpD 529
Cdd:cd17648 326 GRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---G 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 795246185 530 YKSHDQEQLIK-EIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:cd17648 403 YYLPEPGHVPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTINGK 446
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
94-580 |
1.29e-16 |
|
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: 82.86 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKANC 170
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 171 IITN--DVLAPAVDAIAPKCE--NLHSKLIvsensregwgnikemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTA 246
Cdd:cd05939 79 LIFNllDPLLTQSSTEPPSQDdvNFRDKLF-----------------------------------YIYTSGTTGLPKAAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 247 HTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05939 124 IVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRK--KFSASNFWDDCVKYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 327 ATVYRMLVQndmASYKFKSLKHCVSAG------EPITPDVTGKWRNKtglDIYEGYGQTETVLICGNFKG---------- 390
Cdd:cd05939 201 GEICRYLLA---QPPSEEEQKHNVRLAvgnglrPQIWEQFVRRFGIP---QIGEFYGATEGNSSLVNIDNhvgacgfnsr 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 391 --MKIKPGSMGKPSPAFDVKIVDVNGNVLP--PGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLRGNF------YITG 460
Cdd:cd05939 275 ilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFLSG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 461 DRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpIRGEVVKAFIVlNPDYKShDQEQL 538
Cdd:cd05939 355 DVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DPERKV-DLDRF 431
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795246185 539 IKEIQehvkKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05939 432 SAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-557 |
4.20e-16 |
|
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: 81.18 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 91 EEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 167
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 168 ANCIITNDVLAPAVDAIAP--KCENLHSKLIVSENSREGWGNIKEMMKCASD--------SHTCVKTKhneimAMF-FTS 236
Cdd:cd05938 79 AKVLVVAPELQEAVEEVLPalRADGVSVWYLSHTSNTEGVISLLDKVDAASDepvpaslrAHVTIKSP-----ALYiYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 237 GTSGYPKMTAHTHSSFglgLSVNGRFWL-DLTPSDVMWNTSDTgWAKSAWSSVFSPWIQ-GA-CVFAhhlPRFEPTSVLQ 313
Cdd:cd05938 154 GTTGLPKAARISHLRV---LQCSGFLSLcGVTADDVIYITLPL-YHSSGFLLGIGGCIElGAtCVLK---PKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 314 TLSKYPITVFCSAATVYRMLVQ-----NDMAsykfkslkHCV--SAGEPITPDVtgkWRN---KTG-LDIYEGYGQTETV 382
Cdd:cd05938 227 DCRKHNVTVIQYIGELLRYLCNqpqspNDRD--------HKVrlAIGNGLRADV---WREflrRFGpIRIREFYGSTEGN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 LICGNFKGmkiKPGSMGKPS-------P----AFDVK----IVDVNGNVLP--PGQEGDIGIQVLPNRPF-GlfahYADD 444
Cdd:cd05938 296 IGFFNYTG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSPFlG----YAGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 445 PSKTASTL------RGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpI 515
Cdd:cd05938 369 KEQTEKKLlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-H 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 795246185 516 RGEVVKAFIVLNPDYkSHDQEQLIkeiqEHVKKTTAPYKYPR 557
Cdd:cd05938 448 EGRIGMAAVKLKPGH-EFDGKKLY----QHVREYLPAYARPR 484
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-509 |
9.78e-16 |
|
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: 79.81 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 224 TKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWLDLTPSDVMWntsdtgwAKSAWSSVFSPWIQGACVFA--- 300
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEVDL-------ATFPLFALFGPALGLTSVIPdmd 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 301 HHLP-RFEPTSVLQTLSKYPIT-VFCSAA---TVYRMLVQNDMasyKFKSLKHCVSAGEPITPDVTGKWRN--KTGLDIY 373
Cdd:cd05910 154 PTRPaRADPQKLVGAIRQYGVSiVFGSPAlleRVARYCAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 374 EGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKIVDVN---------GNVLPPGQEGDI---GIQVLP 431
Cdd:cd05910 231 TPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEIDdepiaewddTLELPRGEIGEItvtGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 432 ---NRPFGLFAHYADDPSKtastlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:cd05910 311 tyvNRPVATALAKIDDNSE------GFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
.
gi 795246185 509 V 509
Cdd:cd05910 385 V 385
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
131-586 |
2.67e-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: 75.71 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapaVDaiapKCENLHSklivsensregWGNIKE 210
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF--------CD----AGVKVYS-----------LEEFEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 211 MMKcaSDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLtpsdVMWNTSDTGWAKSAWSSVFS 290
Cdd:cd05927 100 LGK--KNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYISYLPLAHIFE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 291 PWIQ------GACV-FAHHLPRfEPTSVLQTLSkyPiTVFCSAATVY-RML--VQNDMA--------------SYKFKSL 346
Cdd:cd05927 174 RVVEalflyhGAKIgFYSGDIR-LLLDDIKALK--P-TVFPGVPRVLnRIYdkIFNKVQakgplkrklfnfalNYKLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 347 KH---------------------------CVSAGEPITPDVTGKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIkPGSM 398
Cdd:cd05927 250 RSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTS-VGHV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDV---NGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFV 474
Cdd:cd05927 329 GGPLPCAEVKLVDVpemNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKII 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 475 ARSDDII-LSSGYRIGPFEVENALNEHPSVAESAVvsspdpiRGEVVKAF----IVLNPDY------------KSHDQ-- 535
Cdd:cd05927 404 DRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDVlkewaaskgggtGSFEElc 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 536 --EQLIKEIQEHVKKTTAPYKYpRKVEFIQEL---PK---------TISGKTKRNELRKKEWKTI 586
Cdd:cd05927 477 knPEVKKAILEDLVRLGKENGL-KGFEQVKAIhlePEpfsvengllTPTFKLKRPQLKKYYKKQI 540
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
96-578 |
3.46e-14 |
|
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: 74.82 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 96 SFEELGSLSRKFANILSEacSLQRGDRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17654 18 SYADLAEKISNLSNFLRK--KFQTEERAIgLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 175 dvlapavdaiapkCENLHSKLIVSENSRegwgnikemmkcasdsHTCVKTKHNeIMAMFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd17654 96 -------------KELDNAPLSFTPEHR----------------HFNIRTDEC-LAYVIHTSGTTGTPKIVAVPHKCI-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYP-ITVFCSAATVYRM 332
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATlLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 333 LVQNDMASY---KFKSLKHCVSAGEPITPDVTGK-WRNK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:cd17654 224 FGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSsWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 408 KI--VDVNGNVlPPGQEGDIGIqvlpNRpfglfAHYADDPSKTAstlRGNFYITGDRGYMdEDGYFWFVARSDDIILSSG 485
Cdd:cd17654 303 VIevRDQNGSE-GTGQVFLGGL----NR-----VCILDDEVTVP---KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 486 YRIGPFEVENALNEHPSVAESAVVSSPDpirgEVVKAFIVLNPdykSHDQEQliKEIQEHVKKTTApykYPRKVEFIQEL 565
Cdd:cd17654 369 KRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLSSHA---IPDTFVQIDKL 436
|
490
....*....|...
gi 795246185 566 PKTISGKTKRNEL 578
Cdd:cd17654 437 PLTSHGKVDKSEL 449
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
127-579 |
5.71e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 74.47 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 127 LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLA------PAVDAIAPKCENLHSKLIVSEN 200
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 201 S-----REGWGNIKEMMKCASDSH-------TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTP 268
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 269 SDVM-WNTSdTGWAKSAWsSVFSPWIQGACVFAHHlprFEPTS--VLQTLSKYPITVFCSAATV---YRMLVQNDMASYK 342
Cdd:PLN03051 160 GDVVcWPTN-LGWMMGPW-LLYSAFLNGATLALYG---GAPLGrgFGKFVQDAGVTVLGLVPSIvkaWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 343 FKSLKHCVSAGEPITPD-------VTGKWRNKT----GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKIVD 411
Cdd:PLN03051 235 WSKLRVFASTGEASAVDdvlwlssVRGYYKPVIeycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 412 VNGNVLPPGQE--GDIGIqvlpnRPFGLFA------------HYADDP--SKTASTLRGNfyitGDRGYMDEDGYFWFVA 475
Cdd:PLN03051 307 DNGVPYPDDQPcvGEVAL-----APPMLGAsdrllnadhdkvYYKGMPmyGSKGMPLRRH----GDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNE-HPSVAESAVVSSPDPIRGE----VVKAFIVLNPDYKSHDQEQLIKEIQEHVKKTT 550
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNL 457
|
490 500
....*....|....*....|....*....
gi 795246185 551 APYKYPRKVEFIQELPKTISGKTKRNELR 579
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
94-580 |
5.80e-14 |
|
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: 74.31 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIt 173
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 174 ndvlapaVDAiapkcenlhsklivsensregwgnikemmkcasdshtcvktkhneimAMF-FTSGTSGYPKMTAHTHSSF 252
Cdd:cd05940 81 -------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 253 GLGLSVNGrFWLDLTPSDVMWNT----SDTGwAKSAWSSVFspwIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd05940 107 WRGGAFFA-GSGGALPSDVLYTClplyHSTA-LIVGWSACL---ASGATLVIRK--KFSASNFWDDIRKYQATIFQYIGE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 329 VYRMLVQndmASYKFKSLKHCVSA--GEPITPDVTGKWRNKTGL-DIYEGYGQTETVLICGNFKGmkiKPGSMGKPSP-- 403
Cdd:cd05940 180 LCRYLLN---QPPKPTERKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFG---KPGAIGRNPSll 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 404 --AFDVKIV-----------DVNGNV--LPPGQEGDIGIQVLPNRPF-GlfahYADDPSKTASTLRGNF------YITGD 461
Cdd:cd05940 254 rkVAPLALVkydlesgepirDAEGRCikVPRGEPGLLISRINPLEPFdG----YTDPAATEKKILRDVFkkgdawFNTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 462 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpIRGEVVKAFIVLNPDYkSHDQEQLi 539
Cdd:cd05940 330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNE-EFDLSAL- 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 795246185 540 keiQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:cd05940 407 ---AAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
51-572 |
5.85e-14 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 75.00 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 51 KLEIPEYF-----NFAKDVLdqwtnmekAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVIL 125
Cdd:cd05943 58 IMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 126 ILPRVPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHS 193
Cdd:cd05943 129 YLPNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 194 KLIVSENSREGWGNIKEMMKCASDSHTCVKTKHNEI----------MAMFFTSGTSGYPKmtAHTHSSFGLGLSVNGRFW 263
Cdd:cd05943 206 VVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPK--CIVHGAGGTLLQHLKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 264 L--DLTPSDVM-WNTSdTGWAksAWSSVFSPWIQGA-CVFAHHLPRFEPTSVLQTL-SKYPITVFCSAATVYRMLVQNDM 338
Cdd:cd05943 284 LhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGAtIVLYDGSPFYPDTNALWDLaDEEGITVFGTSAKYLDALEKAGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 339 ---ASYKFKSLKHCVSAGEPITPD----VTGKWrnKTGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFDV 407
Cdd:cd05943 361 kpaETHDLSSLRTILSTGSPLKPEsfdyVYDHI--KPDVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 408 KIVDVNGNVLPpGQEGDIGI-QVLPNRPFGL-------------FAHYaddpsktastlrGNFYITGDRGYMDEDGYFWF 473
Cdd:cd05943 436 EAFDEEGKPVW-GEKGELVCtKPFPSMPVGFwndpdgsryraayFAKY------------PGVWAHGDWIEITPRGGVVI 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQLIKEIQEHVKKTTAPY 553
Cdd:cd05943 503 LGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRSA 576
|
570 580
....*....|....*....|...
gi 795246185 554 KYPRKV--EFIQ--ELPKTISGK 572
Cdd:cd05943 577 LSPRHVpaKIIAvpDIPRTLSGK 599
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
234-578 |
1.39e-13 |
|
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: 72.89 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKMTAHTHSSFG-LGLSVNGRFWLDLTPSDVMWNTS---DTGWAKSAWSSVFSpwiqGACVFAHHLPRFEPT 309
Cdd:cd17650 100 YTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQMASfsfDVFAGDFARSLLNG----GTLVICPDEVKLDPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 310 SVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCV--SAGEPITPDVTGKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:cd17650 176 ALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIvgSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDST 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFK-GMKIKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLR-------G 454
Cdd:cd17650 256 YYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----GAGVARGYLNRPELTAERFVenpfapgE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEV-VKAFIVlnPDYKSH 533
Cdd:cd17650 331 RMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEArLCAYVV--AAATLN 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 795246185 534 dqeqlIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17650 408 -----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
227-581 |
2.04e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 72.91 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 227 NEIMAMFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDVMWN--TSDTGWAksawSSVFSPWIQGACVFAHHL 303
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNmFAILNSTEWKTKDRILSWMplTHDMGLI----AFHLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 304 PRF--EPTSVLQTLSKYPITVFCSAATVYRMLVQ----NDMASYKFKSLKHCVSAGEPITP---DVTGKWRNKTGLD--- 371
Cdd:cd05908 182 RLFirRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpEKANDWDLSSIRMILNGAEPIDYelcHEFLDHMSKYGLKrna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 IYEGYGQTE-TVLICGNFKGMKIKPGSM-------GKPSPAFD--------------------VKIVDVNGNVLPPGQEG 423
Cdd:cd05908 262 ILPVYGLAEaSVGASLPKAQSPFKTITLgrrhvthGEPEPEVDkkdsecltfvevgkpidetdIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 424 DIGIqvlpnRPFGLFAHYADDPSKTASTLRGN-FYITGDRGYMdEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPS 502
Cdd:cd05908 342 HIQI-----RGKNVTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 503 VAESAVVS---SPDPIRGEVVKAFIVLNpdyKSHDQ-EQLIKEIQEHVKKTTApyKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd05908 416 VELGRVVAcgvNNSNTRNEEIFCFIEHR---KSEDDfYPLGKKIKKHLNKRGG--WQINEVLPIRRIPKTTSGKVKRYEL 490
|
...
gi 795246185 579 RKK 581
Cdd:cd05908 491 AQR 493
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
340-580 |
3.17e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.08 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 340 SYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKIVDVngnvl 417
Cdd:PRK06814 903 PYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLEPV----- 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 418 pPGQEGDIGIQVL-PNRPFGlfahY--ADDPSkTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:PRK06814 976 -PGIDEGGRLFVRgPNVMLG----YlrAENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 495 NALNEHPSVAESAVVSSPDPIRGEVvkafIVLNPDYKSHDQEqlikEIQEHVKKTTAPYKY-PRKVEFIQELPKTISGKT 573
Cdd:PRK06814 1050 ELAAELWPDALHAAVSIPDARKGER----IILLTTASDATRA----AFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
....*..
gi 795246185 574 KRNELRK 580
Cdd:PRK06814 1122 DYVAVTK 1128
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-585 |
1.43e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 72 EKAGKKPSNPAFWWINGKgeevrWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05691 1139 EQARQTPERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 152 TQLTQKDILYRLQSSKANCIITNDVL---APAVDAIAPKC-ENLHSklivsensrEGWgnikemmkcasDSHTCVKTKHN 227
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---------DSW-----------PSQAPGLHLHG 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 228 EIMA-MFFTSGTSGYPKMTAHTHSSFGLGLSvngrfWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAH 301
Cdd:PRK05691 1273 DNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGCrLVLAG 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 302 HLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASyKFKSLKHCVSAGEPITPDVtgkwRNKT-----GLDIYEGY 376
Cdd:PRK05691 1347 PGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAEL----RNRVlqrlpQVQLHNRY 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTETVL-----ICGNFKGMKikpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA-- 449
Cdd:PRK05691 1422 GPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAer 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 450 ------STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVsspdpIRGEVVKAF 523
Cdd:PRK05691 1494 fvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQ 1568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795246185 524 IVlnpDYKSHDQEQliKEIQEHVKKTTA----PYKYPRKVEFIQELPKTISGKTKRNELRKKEWKT 585
Cdd:PRK05691 1569 LV---GYYTGEAGQ--EAEAERLKAALAaelpEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-581 |
1.57e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 70.49 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 57 YFNFAKDVLdqwtnMEKAGKKPSNPAFWWINGKGEEV---RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEW 133
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVL----------APAVDAIAPKCENLHSK-LIVSENSR 202
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplySRVVEAKAPKAIVLPADgKSVRVKLR 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 203 EGWGNIKEMMKCAS-----DSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTPSDVM-WNTs 276
Cdd:PLN03052 327 EGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIVcWPT- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 277 DTGWAKSAWSsVFSPWIQGACVFAHH-------LPRFEPTSVLQTLSKYPITVFCSAATvyrmlvqNDMASYKFKSLKHC 349
Cdd:PLN03052 405 NLGWMMGPWL-VYASLLNGATLALYNgsplgrgFAKFVQDAKVTMLGTVPSIVKTWKNT-------NCMAGLDWSSIRCF 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 350 VSAGEPITPD----VTGKWRNKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFDVKIVDVNGNVLPPGQ 421
Cdd:PLN03052 477 GSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPYPDDA 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 422 EGdIGIQVLPNRPFG-----LFA-----HYADDPSKTASTLRGNfyitGDRGYMDEDGYFWFVARSDDIILSSGYRIGPF 491
Cdd:PLN03052 551 PC-TGELALFPLMFGasstlLNAdhykvYFKGMPVFNGKILRRH----GDIFERTSGGYYRAHGRADDTMNLGGIKVSSV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 492 EVENALNE-HPSVAESAVVSSPDPIRG--EVVKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKT 568
Cdd:PLN03052 626 EIERVCNAaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRT 705
|
570
....*....|...
gi 795246185 569 ISGKTKRNELRKK 581
Cdd:PLN03052 706 ASNKVMRRVLRQQ 718
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
222-580 |
3.07e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 69.35 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 222 VKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAH 301
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 302 HLP---RFEPTSVLQTlskyPITVFCSAATV---YRMLVQndmaSYKFKSLKHCVSAGEPITPDVTGKWRNKTGLDIYEG 375
Cdd:PRK08043 439 PSPlhyRIVPELVYDR----NCTVLFGTSTFlgnYARFAN----PYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEG 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 376 YGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PN---------RPFGLFAHYADDP 445
Cdd:PRK08043 511 YGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV------PGIEQGGRLQLKgPNimngylrveKPGVLEVPTAENA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 446 sktASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEvvkAFIV 525
Cdd:PRK08043 585 ---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVL 658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 526 LNPDyKSHDQEQLIKEIQEHVKKTTApykYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK08043 659 FTTD-SELTREKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
457-580 |
3.76e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.15 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 457 YITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnpdyKSHDQE 536
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPA 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 795246185 537 QLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRK 580
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-578 |
1.95e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 234 FTSGTSGYPKmtahthssfglGLSVNGRF----------WLDLTPSDVMWNTSDTGWAKSAWSSVFSPwIQGACV----- 298
Cdd:PRK05691 3876 YTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAP-LFGARVeivpn 3943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 299 -FAHHlprfePTSVLQTLSKYPITVFCSAAT-VYRMLVQNDMAsykFKSLKHCVSAGEPITPDVTGKWRNK-TGLDIYEG 375
Cdd:PRK05691 3944 aIAHD-----PQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNA 4015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 376 YGQTETVLICGNFK-GMKIKPGS---MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTAST 451
Cdd:PRK05691 4016 YGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTALA 4090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 452 LRGN--------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAF 523
Cdd:PRK05691 4091 FVPHpfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGY 4169
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 524 IVlnPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK05691 4170 LV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
71-579 |
2.66e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 71 MEKAGKKPSNPAFWWINGKGEE-VRWSFEELGSLSRKFANILSEACSLqrGDRVILILPRVPEWWLANVACLRTGTVLIP 149
Cdd:PRK05691 16 QRRAAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 150 G-----TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPkcenlhskliVSENSREGWGNIKEMMKCASDSHTCVKT 224
Cdd:PRK05691 94 AyppesARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEE----------LAAANAPELLCVDTLDPALAEAWQEPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 225 KHNEIMAMFFTSGTSGYPKMTAHTHSSfglgLSVNGR-----FWLDLTPSDVM--WNT--SDTGWAKSAWSSVFS--Pwi 293
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGN----LVANEQlirhgFGIDLNPDDVIvsWLPlyHDMGLIGGLLQPIFSgvP-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 294 qgaCVF---AHHLPRfePTSVLQTLSKYPITV---------FCSAATVYRMLVQNDMASYKFkslkhCVSAGEPITPDVT 361
Cdd:PRK05691 238 ---CVLmspAYFLER--PLRWLEAISEYGGTIsggpdfayrLCSERVSESALERLDLSRWRV-----AYSGSEPIRQDSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 362 GKWRNK---TGLD---IYEGYGQTE-TVLICGNFKGMKI---------------KPG------SMGKPSPAFDVKIVD-V 412
Cdd:PRK05691 308 ERFAEKfaaCGFDpdsFFASYGLAEaTLFVSGGRRGQGIpaleldaealarnraEPGtgsvlmSCGRSQPGHAVLIVDpQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 413 NGNVLPPGQEGDI---GIQVlpnrpfglfAH-YADDPSKTAST---LRGNFYI-TGDRGYMdEDGYFWFVARSDDIILSS 484
Cdd:PRK05691 388 SLEVLGDNRVGEIwasGPSI---------AHgYWRNPEASAKTfveHDGRTWLrTGDLGFL-RDGELFVTGRLKDMLIVR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 485 GYRIGPFEVENALNEhpsvaESAVVsspdpiRGEVVKAFIVlnpdykSHDQEQLI---KEIQEHVKKTTAP---YKYPRK 558
Cdd:PRK05691 458 GHNLYPQDIEKTVER-----EVEVV------RKGRVAAFAV------NHQGEEGIgiaAEISRSVQKILPPqalIKSIRQ 520
|
570 580 590
....*....|....*....|....*....|....*
gi 795246185 559 V--EFIQE------------LPKTISGKTKRNELR 579
Cdd:PRK05691 521 AvaEACQEapsvvlllnpgaLPKTSSGKLQRSACR 555
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
308-575 |
8.03e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.55 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 308 PTSVLQTLSKYPITVFCSAATVY-----RMLVQNDMASYKFKSLKHCVSAGEPITPDV------TGKwrnKTGLD---IY 373
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAPNFAYallarRLRRQAKPGAFDLSSLRFALNGAEPIDPADvedlldAGA---RFGLRpeaIL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 374 EGYGQTETVLI-----CGNfkGMKI------------------KPG-----SMGKPSPAFDVKIVDVNGNVLPPGQEGDI 425
Cdd:PRK07768 312 PAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 426 GIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAE 505
Cdd:PRK07768 390 EL-----RGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRP 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795246185 506 SAVVSSPDPiRGEVVKAFIVLNPDYKSHDQE---QLIKEIQEHVKKTTApyKYPRKVEFIQ--ELPKTISGKTKR 575
Cdd:PRK07768 465 GNAVAVRLD-AGHSREGFAVAVESNAFEDPAevrRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-578 |
1.18e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 232 MFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQGACVFAHHLPRFEPTS 310
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 311 VLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGLD-IYEGYGQTETV---LICG 386
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACL 2494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 387 NFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA--------STLRGNF 456
Cdd:PRK05691 2495 APEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRL 2569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 457 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAEsAVVSSPDPIRGEVVKAFIVLNPDYKSHDQE 536
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795246185 537 QLIKE-IQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:PRK05691 2649 AALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
399-580 |
3.23e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMdEDGYFWFVARSD 478
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 479 DIILSSGYRIGPFEVENALNEHPSV--AESAVVSSPDPiRGEVVKAFI---VLNPDykshDQEQLIKEIQEHVKKTTApy 553
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 795246185 554 kYPRKVEFI--QELPKTISGKTKRNELRK 580
Cdd:PRK09192 535 -VEAAVELVppHSLPRTSSGKLSRAKAKK 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
131-499 |
2.38e-08 |
|
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: 56.98 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN-CIITNDVLAPAVDAIAPKCENLHSKLIVSENSRE------ 203
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANiLVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEkepnly 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 204 GWGNIKEMMKCASDS--HTCVKT-KHNEIMAMFFTSGTSGYPK--MTAHTHSSFGLGLSVNGrfwLDLTPSDVMwntsdt 278
Cdd:cd05933 124 SWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWTAKAASQH---MDLRPATVG------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 279 gwAKSAWS------------SVFSPWIQGACV-FAH----------HLPRFEPTS------VLQTLSKYPITVFCSAATV 329
Cdd:cd05933 195 --QESVVSylplshiaaqilDIWLPIKVGGQVyFAQpdalkgtlvkTLREVRPTAfmgvprVWEKIQEKMKAVGAKSGTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 330 YRMLV-----------QNDMAS-----YKFKSLKH-----------------CVSAGEPITPDvTGKWRNKTGLDIYEGY 376
Cdd:cd05933 273 KRKIAswakgvgletnLKLMGGespspLFYRLAKKlvfkkvrkalgldrcqkFFTGAAPISRE-TLEFFLSLNIPIMELY 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 377 GQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIVDVNGNvlppGQeGDIGIqvlpnRPFGLFAHYADDPSKTAST 451
Cdd:cd05933 352 GMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDAD----GI-GEICF-----WGRHVFMGYLNMEDKTEEA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 795246185 452 LRGNFYI-TGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNE 499
Cdd:cd05933 417 IDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKK 466
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
231-583 |
3.53e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 55.90 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 231 AMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFepts 310
Cdd:cd05937 91 ILIYTSGTTGLPKAAAISWRRTLVTSNLLSH-DLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSR--KF---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 311 vlqTLSKYPITVFCSAAT--VY-----RMLVqNDMASYKFKSLKHCVSAGEPITPDVTGKWRNKTGL-DIYEGYGQTETV 382
Cdd:cd05937 164 ---SASQFWKDVRDSGATiiQYvgelcRYLL-STPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVpEIGEFYAATEGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 383 LICGNFKGMKIKPGSMGKPSP------AFDVKIVDVNGN--------------VLPPGQEGDIgIQVLPNRPFGLFAHYA 442
Cdd:cd05937 240 FALTNHNVGDFGAGAIGHHGLirrwkfENQVVLVKMDPEtddpirdpktgfcvRAPVGEPGEM-LGRVPFKNREAFQGYL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 443 DDPSKTASTL------RGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP- 514
Cdd:cd05937 319 HNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPg 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 515 IRGEVVKAFIVLNPdyKSHDQEQLIK-EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEW 583
Cdd:cd05937 399 HDGRAGCAAITLEE--SSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
59-572 |
1.32e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 54.42 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 59 NFAKDVLDQwtnmekagKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEwwlANV 138
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 139 ACLRT--------------GT-------------VLIP-------GTTQ-LTQK--DILYRLQSSKANCIITNdvLAPAV 181
Cdd:PRK03584 155 AMLATaslgaiwsscspdfGVqgvldrfgqiepkVLIAvdgyrygGKAFdRRAKvaELRAALPSLEHVVVVPY--LGPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 182 DAIAPkcENLHSklivsensregWGNIKEMMKCASDSHTCVKTKHN-EIMamfFTSGTSGYPKMTAHTHssfG------- 253
Cdd:PRK03584 233 AAAAL--PGALL-----------WEDFLAPAEAAELEFEPVPFDHPlWIL---YSSGTTGLPKCIVHGH---Ggillehl 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 254 --LGLSvngrfwLDLTPSD-VMWNTSdTGWAksAWSSVFSPWIQGACVF------AHhlPrfEPTSVLQTLSKYPITVFC 324
Cdd:PRK03584 294 keLGLH------CDLGPGDrFFWYTT-CGWM--MWNWLVSGLLVGATLVlydgspFY--P--DPNVLWDLAAEEGVTVFG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 325 SAATVYRMLVQNDM---ASYKFKSLKHCVSAGEPITPDVTgKWrnktgldIYEGYGQ----------TEtvlICGNFKG- 390
Cdd:PRK03584 361 TSAKYLDACEKAGLvpgETHDLSALRTIGSTGSPLPPEGF-DW-------VYEHVKAdvwlasisggTD---ICSCFVGg 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 391 ---MKIKPGSMGKPSPAFDVKIVDVNGN-VLppGQEGDIGI-QVLPNRPFGLFahyaDDPSKtaSTLRGNFYIT------ 459
Cdd:PRK03584 430 nplLPVYRGEIQCRGLGMAVEAWDEDGRpVV--GEVGELVCtKPFPSMPLGFW----NDPDG--SRYRDAYFDTfpgvwr 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 460 -GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqL 538
Cdd:PRK03584 502 hGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA--L 579
|
570 580 590
....*....|....*....|....*....|....
gi 795246185 539 IKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:PRK03584 580 RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGK 613
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
86-511 |
2.44e-07 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 53.51 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 86 INGKGEE-VRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQ 164
Cdd:cd05905 5 LDSKGKEaTTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 165 SSKANCIITNDVLAP----AVDAIAPKCENLHSKLIvsENSREGWGNIKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:cd05905 85 TCKVRVALTVEACLKglpkKLLKSKTAAEIAKKKGW--PKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 241 YPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWN----TSDTGWAKSAWSSVFSpwiqGACV--FAHHLPRFEPTSVLQT 314
Cdd:cd05905 163 SLSGVAVSHSSL-LAHCRALKEACELYESRPLVTvldfKSGLGLWHGCLLSVYS----GHHTilIPPELMKTNPLLWLQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 315 LSKYPI-TVFCSAATVYRMLVQ--NDMASYK-----FKSLKHC-VSAGEPITPDVTGKWRN---KTGL------------ 370
Cdd:cd05905 238 LSQYKVrDAYVKLRTLHWCLKDlsSTLASLKnrdvnLSSLRMCmVPCENRPRISSCDSFLKlfqTLGLspravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 371 ----------------DIY---------------EGYGQTETVLICGnfkgmKIKPGsmgkpspafdVKIVDVNGNVLPP 419
Cdd:cd05905 318 vnpficwqgtsgpepsRVYldmralrhgvvrldeRDKPNSLPLQDSG-----KVLPG----------AQVAIVNPETKGL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 420 GQEGDIG-IQVL-PNRPFGLFA-------HYADDPSKTASTLRGN-FYI-TGDRGY----------MDEDGYFWFVARSD 478
Cdd:cd05905 383 CKDGEIGeIWVNsPANASGYFLldgetndTFKVFPSTRLSTGITNnSYArTGLLGFlrptkctdlnVEEHDLLFVVGSID 462
|
490 500 510
....*....|....*....|....*....|....
gi 795246185 479 DIILSSGYRIGPFEVEN-ALNEHPSVAESAVVSS 511
Cdd:cd05905 463 ETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVFSI 496
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
180-529 |
3.61e-07 |
|
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: 53.20 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 180 AVDAIAPkcenLHSKLIVSENSREGWGNIKemmkCASDSHTCVKTKHNE---------IMAMFFTSGTSGYPKMTAHTHS 250
Cdd:cd05921 117 ALAAIFP----LGTPLVVSRNAVAGRGAIS----FAELAATPPTAAVDAafaavgpdtVAKFLFTSGSTGLPKAVINTQR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 251 SFGLGLSVNGRFWLDLTPSD-VM-----WNTSDTGwaksawSSVFSPWIQGACVFahHLPRFEPT-----SVLQTLSKYP 319
Cdd:cd05921 189 MLCANQAMLEQTYPFFGEEPpVLvdwlpWNHTFGG------NHNFNLVLYNGGTL--YIDDGKPMpggfeETLRNLREIS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 320 ITVFCSAATVYRMLVQ---NDMASYK--FKSLKHCVSAGEPITPDVtgkWRNKTGLDI---------YEGYGQTETVLIC 385
Cdd:cd05921 261 PTVYFNVPAGWEMLVAaleKDEALRRrfFKRLKLMFYAGAGLSQDV---WDRLQALAVatvgeripmMAGLGATETAPTA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 386 GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqEGDI-GIQVLPNrpfglfahYADDPSKTASTL-RGNFYITGDRG 463
Cdd:cd05921 338 TFTHWPTERSGLIGLPAPGTELKLVPSGGKY-----EVRVkGPNVTPG--------YWRQPELTAQAFdEEGFYCLGDAA 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795246185 464 YM----DEDGYFWFVAR-SDDIILSSG--YRIGPFEVEnALNEHPSVAESAVVSSPDpirGEVVKAFIVLNPD 529
Cdd:cd05921 405 KLadpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAEVGALVFPDLL 473
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
350-522 |
8.31e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 52.02 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 350 VSAGEPITPDVTGKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVngnvlP---------P 419
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDV-----PemnytsedqP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 420 GQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVENAL 497
Cdd:PLN02736 456 YPRGEICV-----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVY 530
|
170 180 190
....*....|....*....|....*....|....*.
gi 795246185 498 NEHPSVAESAV-----------VSSPDPirgEVVKA 522
Cdd:PLN02736 531 AKCKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
346-582 |
2.89e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.91 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 346 LKHCVSAGEPITPDvTGKWRNKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFDVKIVDV----NGNV 416
Cdd:cd17639 252 LRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCEIKLVDWeeggYSTD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 417 LPPGQeGDIGIQvlpnRPFgLFAHYADDPSKTASTLRGN--FYiTGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEV 493
Cdd:cd17639 326 KPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 494 ENALNEHPSVAESAVVSspDPIRGEVVkAFIVLNpdykshdQEQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKT 573
Cdd:cd17639 399 ESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETA 468
|
....*....
gi 795246185 574 KRNELRKKE 582
Cdd:cd17639 469 RAAGLEKFE 477
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
453-578 |
3.74e-06 |
|
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: 49.82 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAES------------AVVS--SPDPIRGE 518
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795246185 519 VVKAFIVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNEL 578
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
222-500 |
1.06e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 48.27 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 222 VKTKHNEIMA-MFFTSGTSGYPKMTAHTHSSfglgLSVNGRFWLDL---TPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 297
Cdd:PRK06334 177 VSDKDPEDVAvILFTSGTEKLPKGVPLTHAN----LLANQRACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 298 VFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYrmlvqndmaSYKFKSLKHCVSAGEPITPDVTG------KWRNKTGLD 371
Cdd:PRK06334 253 VVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFF---------DYILKTAKKQESCLPSLRFVVIGgdafkdSLYQEALKT 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 372 -----IYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlpPGQEGDIGIQVLpnRPFGLFAHY-ADD 444
Cdd:PRK06334 323 fphiqLRQGYGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKV--PVSSGETGLVLT--RGTSLFSGYlGED 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795246185 445 PSKTASTLRG-NFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIGPFEV-----ENALNEH 500
Cdd:PRK06334 399 FGQGFVELGGeTWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
398-580 |
9.69e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 398 MGKPSPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFAHY-ADDPSKtastlRGNFYITGDRGYMDEDGYFwFVA 475
Cdd:PRK05851 347 LGNPIPGMEVRISPGDGAAGVAGREiGEIEI-----RGASMMSGYlGQAPID-----PDDWFPTGDLGYLVDGGLV-VCG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGevVKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTApyKY 555
Cdd:PRK05851 416 RAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VV 491
|
170 180
....*....|....*....|....*..
gi 795246185 556 PRKVEFIQ--ELPKTISGKTKRNELRK 580
Cdd:PRK05851 492 PSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
453-572 |
9.46e-04 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 42.36 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 453 RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAE----------------SAVVSSPDPir 516
Cdd:TIGR03443 676 RDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS-- 753
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795246185 517 gEVVKAFIVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYPRKVEFIQELPKTISGK 572
Cdd:TIGR03443 754 -DELEEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGK 816
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
306-483 |
1.83e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 41.24 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPitpdvTGKWRNKTGL----DIYEGYGQTE 380
Cdd:PRK07868 681 LDPDRFVQEVRQYGVTVVSYTWAMLREVVDDpAFVLHGNHPVRLFIGSGMP-----TGLWERVVEAfapaHVVEFFATTD 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795246185 381 TVLICGNFKGMKIkpGSMGKPSP--------AFDVK----IVDVNGNVlppgQEGDIG-IQVLPNRPFGLFahyadDPsk 447
Cdd:PRK07868 756 GQAVLANVSGAKI--GSKGRPLPgagrvelaAYDPEhdliLEDDRGFV----RRAEVNeVGVLLARARGPI-----DP-- 822
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 795246185 448 TASTLRGNFyITGDR----GYM---DEDGYFWFVARSDDIILS 483
Cdd:PRK07868 823 TASVKRGVF-APADTwistEYLfrrDDDGDYWLVDRRGSVIRT 864
|
|
| |
