|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-559 |
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: 1047.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 54 IPEYFNFAKDVLDQWTNMEKAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW 133
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNLKEMMK 213
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 214 CASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 294 QGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY 373
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLR 453
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSH 533
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500
....*....|....*....|....*.
gi 967501916 534 DQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKV 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
95-559 |
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: 586.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 175 DvlapavdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTHSsFGL 254
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLV 334
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 335 QNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG 414
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 415 NVLPPGQEGDIGIQVLPNrpfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:cd05972 268 RELPPGEEGDIAIKLPPP---GLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREI 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-559 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 558.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 51 KLEIPEYFNFAKDVLDQWtnmekAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRV 130
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHSKLIV---- 197
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 198 SENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSD 277
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 278 TGWAKSAWSSVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSA 352
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 353 GEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlp 431
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 432 nRPF-GLFAHYADDPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:COG0365 392 -GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 967501916 508 VVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREI 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-559 |
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: 555.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 43 YESMKQDFKLEIPEYFNFAKDVLDQWTNMEkagkkPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDR 122
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFF-KAMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 123 VILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCIITNDVLAPAVDAIAPKCENLHSKLIVSEN 200
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 201 SREGWGNLKEMMKCASDS----HTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 277 DTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPI 356
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 357 TPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFG 436
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 437 LFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 516
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 967501916 517 GEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05970 474 GQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIV 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-561 |
3.94e-133 |
|
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: 395.78 E-value: 3.94e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitnd 175
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLAPAVDAiapkcenlhsklivsensregwgnlkemmkcasdshtcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05974 74 VYAAVDEN----------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 256 lSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 336 NDMASYKFKsLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGN 415
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 416 vlpPGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVEN 495
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 496 ALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVGI 561
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEF 412
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
35-557 |
3.98e-129 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 390.41 E-value: 3.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 35 ATPQNFSNYESMKQDFKL-EIPEYF--------NFAKDVLDQWTNMEKAGKkpsnPAFWWInGKGEEVRWSFEELGSLSR 105
Cdd:PRK04319 10 KGEPNLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYL-DASRKEKYTYKELKELSN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaIA 185
Cdd:PRK04319 85 KFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 186 PKCENLHSKLIVSENSREGWG--NLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFW 263
Cdd:PRK04319 162 DDLPSLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 264 LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA--CVFAhhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ--NDMA 339
Cdd:PRK04319 241 LDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 340 S-YKFKSLKHCVSAGEPITPDVTeKWRNKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKIVDVNGN 415
Cdd:PRK04319 318 KkYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 416 VLPPGQEGDIGIQvlPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVEN 495
Cdd:PRK04319 396 ELPPNRMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVES 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967501916 496 ALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPR 557
Cdd:PRK04319 473 KLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPR 532
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-559 |
6.15e-115 |
|
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: 349.49 E-value: 6.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 175 DVLAPavdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlPRFEPTSVLQTLSKYPITVFCSAATVYRMLV 334
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 335 QND---MASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKI 409
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 410 VDVNGNVLPPGQEGDIGIQvlPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 489
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP--SDELKEEIINFVRQKLGAHVAPREI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-559 |
2.17e-111 |
|
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: 340.63 E-value: 2.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDQWtnmekAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG0318 3 DLLRRA-----AARHPDRPALVF-----GGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITndvlapavdaiapkcenlhsklivsensregwgnlkemmkcasdshtcv 222
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 223 ktkhneiMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTS----DTGWaksaWSSVFSPWIQGACV 298
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 299 faHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 377
Cdd:COG0318 171 --VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 378 QTET-VLICGNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:COG0318 249 LTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 456 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQ 535
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDA 402
|
490 500
....*....|....*....|....
gi 967501916 536 EQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:COG0318 403 EELRAFLRERL----ARYKVPRRV 422
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-559 |
2.73e-107 |
|
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: 329.78 E-value: 2.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 89 KGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 169 NCIITNDVLAPAVdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTAHT 248
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSsFGLGLSVNGRFWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 327 ATVYRML-VQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPA 404
Cdd:cd05971 189 PTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 405 FDVKIVDVNGNVLPPGQEGDIGIQvLPNrPFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVE-LPD-PV-AFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREI 418
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-559 |
8.48e-97 |
|
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: 302.52 E-value: 8.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNd 175
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 vlapavdaiapkCENLHsklivsensregwgnlkemmKCASDshtcvktkhneIMAMFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05973 80 ------------AANRH--------------------KLDSD-----------PFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 336 NDMASYKFK--SLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIVD 411
Cdd:cd05973 195 AGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 412 VNGNVLPPGQEGDIGIQVlPNRPFGLFAHYADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPF 491
Cdd:cd05973 275 DDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTI 416
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
228-559 |
8.13e-96 |
|
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: 296.50 E-value: 8.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFahHLPRFE 307
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVV--LLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDM-ASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLI 384
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGY 464
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-GPS----VMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQE 544
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330
....*....|....*
gi 967501916 545 HVKKTTAPYKYPRKV 559
Cdd:cd04433 307 HVRERLAPYKVPRRV 321
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-559 |
2.37e-94 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 297.17 E-value: 2.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDqwtnmEKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:cd05936 3 DLLE-----EAARRFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLApavDAIAPKcenlHSKLIVSENSREgwgnlkemmkcasdshtcv 222
Cdd:cd05936 72 AGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFT---DLLAAG----APLGERVALTPE------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 223 ktkhnEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWL--DLTPSDVMWNT-------SDTgwaksawSSVFSPWI 293
Cdd:cd05936 126 -----DVAVLQYTSGTTGVPKGAMLTHRNLVANALQI-KAWLedLLEGDDVVLAAlplfhvfGLT-------VALLLPLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 294 QGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:cd05936 193 LGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKT 448
Cdd:cd05936 271 VEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELwvrGPQV--------MKGYWNRPEET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 449 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP 528
Cdd:cd05936 343 AEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE 422
|
490 500 510
....*....|....*....|....*....|..
gi 967501916 529 DykshdqEQLIK-EIQEHVKKTTAPYKYPRKV 559
Cdd:cd05936 423 G------ASLTEeEIIAFCREQLAGYKVPRQV 448
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-559 |
2.94e-92 |
|
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: 293.12 E-value: 2.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 56 EYFNFAKDVLDQwtnmeKAGKKPSNPAFwwINGKGEevrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWL 135
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSRE--GWGNLKEMMK 213
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 214 CASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSP-W 292
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 293 IQGACVFahhLP-RFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGL 370
Cdd:cd05959 230 VGATTVL---MPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 371 DIYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFglfahYADDPSKTA 449
Cdd:cd05959 307 DILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 450 STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd05959 381 DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
490 500 510
....*....|....*....|....*....|
gi 967501916 530 YKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05959 461 YE--DSEALEEELKEFVKDRLAPYKYPRWI 488
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-559 |
5.57e-87 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 277.05 E-value: 5.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaNCI 171
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLAPAVdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05958 84 ITVALCAHAL------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 252 FGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYR 331
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 332 -MLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIV 410
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 411 DVNGNVLPPGQEGDIGIQvlpnRPFGlfAHYADDPSKtASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 490
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTG--CRYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 491 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAI 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
62-559 |
3.31e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.05 E-value: 3.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 62 KDVLDQWtnmekAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACL 141
Cdd:PRK06187 9 GRILRHG-----ARKHPDKEAVYF-----DGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 142 RTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREG----WGNLKEMMKCASD 217
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 218 SHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWAksawssvFSP 291
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 292 WIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGL 370
Cdd:PRK06187 230 LMAGAKQVIPR--RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 371 DIYEGYGQTETV-LICGNF-----KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGqEGDIG-IQVL-PNrpfgLFAHYA 442
Cdd:PRK06187 308 DLVQGYGMTETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVRgPW----LMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 443 DDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 522
Cdd:PRK06187 383 NRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVA 462
|
490 500 510
....*....|....*....|....*....|....*..
gi 967501916 523 FIVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK06187 463 VVVLKPG-ATLDAKELRAFLRGRL----AKFKLPKRI 494
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-484 |
6.52e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 249.92 E-value: 6.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFwwinGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:pfam00501 3 RQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 152 TQLTQKDILYRLQSSKANCIITNDVL-APAVDAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSH-TCVKTKHNEI 229
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 230 MAMFFTSGTSGYPKMTAHTH---SSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFAHHLPR 305
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--- 381
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKrALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 382 VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDI---GIQVLPnrpfGlfahYADDPSKTASTL-RGNF 456
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELcvrGPGVMK----G----YLNDPELTAEAFdEDGW 389
|
410 420
....*....|....*....|....*...
gi 967501916 457 YITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
74-559 |
3.55e-73 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 240.98 E-value: 3.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd17631 5 ARRHPDRTALVF-----GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 LTQKDILYRLQSSKAnciitndvlapavdaiapkcenlhsKLIVSENSRegwgnlkemmkcasdshtcvktkhneimaMF 233
Cdd:cd17631 79 LTPPEVAYILADSGA-------------------------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGwaksawSSVFSPWIQGACVfaHHLPRFE 307
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVllvvapLFHIGGLG------VFTLPTLLRGGTV--VILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LIC 385
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 GNFKGMKI-KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGY 464
Cdd:cd17631 255 FLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG-PH----VMAGYWNRPEATAAAFRDGWFHTGDLGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqE 544
Cdd:cd17631 330 LDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG-AELDEDELI----A 404
|
490
....*....|....*
gi 967501916 545 HVKKTTAPYKYPRKV 559
Cdd:cd17631 405 HCRERLARYKIPKSV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
71-562 |
1.25e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 241.73 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 71 MEKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK07656 12 ARAARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV----SENSREGWGNLKEMMKCASDSHTCVKTKH 226
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 227 NEIMAMFFTSGTSGYPK--MTAHTHSsfglgLSvNGRFW---LDLTPSD---------------VMWNTsdtgwaksaws 286
Cdd:PRK07656 166 DDVADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 287 svfsPWIQGACVFAHhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEKWR 365
Cdd:PRK07656 229 ----PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 366 NKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHY 441
Cdd:PRK07656 303 SELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 442 ADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVV 520
Cdd:PRK07656 378 YDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 967501916 521 KAFIVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 562
Cdd:PRK07656 458 KAYVVLKPG-AELTEEELIAYCREHL----AKYKVPRSIEFL 494
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
77-559 |
3.01e-72 |
|
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: 242.87 E-value: 3.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 77 KPSNPAFWWINGKGEEVR-WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLT 155
Cdd:cd17634 66 NGDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 156 QKDILYRLQSSKANCIITND----------VLAPAVDAIAPKCENLHSKLIVSensREG---------WGNLKEMMKCAS 216
Cdd:cd17634 145 PEAVAGRIIDSSSRLLITADggvragrsvpLKKNVDDALNPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKAS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 217 DSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA 296
Cdd:cd17634 222 PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 297 CVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSAGEPITPDVTE-KWR--NKT 368
Cdd:cd17634 302 TTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 369 GLDIYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQV-LPNRPFGLFAhyaDDP 445
Cdd:cd17634 382 KCPVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpWPGQTRTLFG---DHE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 446 SKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:cd17634 459 RFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAY 538
|
490 500 510
....*....|....*....|....*....|....*.
gi 967501916 524 IVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd17634 539 VVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVV 572
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
96-562 |
1.82e-71 |
|
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: 236.59 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 vlapavDAIApkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimAMFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05919 91 ------DDIA---------------------------------------------YLLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFAHHLPrfEPTSVLQTLSKYPITVFCSAATVY-RML 333
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYaNLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 334 VQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN 413
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 414 GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 493
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 494 ENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFV 419
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
56-557 |
2.02e-69 |
|
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: 233.19 E-value: 2.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 56 EYFNFAKDVLDqwTNMEKAgkKPSNPAFwwINGKGeevRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWL 135
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVEG--RGGKTAF--IDDIS---SLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSkLIVSENSREGWGNLKEMMKCA 215
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 216 SDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQG 295
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 296 ACVFAHHlPRFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYE 374
Cdd:TIGR02262 230 ATTVLMG-ERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRG 454
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShd 534
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500
....*....|....*....|...
gi 967501916 535 qeqLIKEIQEHVKKTTAPYKYPR 557
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPR 481
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
68-559 |
3.64e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 233.31 E-value: 3.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 68 WTNMEKAGKK-PSNPAFWWIngkGEEVrwSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTV 146
Cdd:PRK08314 13 FHNLEVSARRyPDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 147 LIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAV------------------DAIAPKCE-----NLHSKLIVSENSRE 203
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 204 GWGNLKEMMKC--ASDSHTcvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSD---- 277
Cdd:PRK08314 168 GVVAWKEALAAglAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 278 TGWAKSAWSSVFSpwiqGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATvyrMLV----QNDMASYKFKSLKHCVSAG 353
Cdd:PRK08314 244 TGMVHSMNAPIYA----GATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 354 EPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GIQ 428
Cdd:PRK08314 315 AAMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIvvhGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 429 VlpnrpfglFAHYADDPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVA 504
Cdd:PRK08314 394 V--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 505 ESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIV 517
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-559 |
4.08e-68 |
|
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: 232.07 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 59 NFAKDVLDQWtnmekAGKKPSNPAFWWI-NGKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:cd05966 53 NISYNCLDRH-----LKERGDKVAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 138 VACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND---------VLAPAVDAIAPKCENLHsKLIVSENS---- 201
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTggev 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 202 -----REGWGNlkEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05966 203 pmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 277 DTGWAKSAWSSVFSPWIQGAcvfahhlprfepTSVL--------------QTLSKYPITVFCSAATVYRMLVQ---NDMA 339
Cdd:cd05966 281 DIGWITGHSYIVYGPLANGA------------TTVMfegtptypdpgrywDIVEKHKVTIFYTAPTAIRALMKfgdEWVK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 340 SYKFKSLKHCVSAGEPITPdvtEKWR---NKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDVK 408
Cdd:cd05966 349 KHDLSSLRVLGSVGEPINP---EAWMwyyEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 409 IVDVNGNVLPPGQEGDIGIQvlpnRPFglfahyaddPSkTASTLRGN--------------FYITGDRGYMDEDGYFWFV 474
Cdd:cd05966 423 ILDEEGNEVEGEVEGYLVIK----RPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWIT 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 475 ARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLIKEIQEHVKKTTAPYK 554
Cdd:cd05966 489 GRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIA 566
|
....*
gi 967501916 555 YPRKV 559
Cdd:cd05966 567 TPDKI 571
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
96-559 |
7.17e-67 |
|
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: 224.28 E-value: 7.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 vlapavdaiapkcenlHSKLivsensregwgnlkemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ 335
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 336 N-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDV-N 413
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIeT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 414 GNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 489
Cdd:cd05935 270 GRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREV 411
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
91-567 |
1.34e-65 |
|
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: 222.09 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITN----DVLAPAVDAIAPKcenlhSKLIVSENSREGWGNLKEMMK---CASDSH--TCVKTKHNEIMAMFFTSGTSGY 241
Cdd:cd05911 86 IFTDpdglEKVKEAAKELGPK-----DKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 242 PKMTAHTHSSFGLGL-SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWiQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:cd05911 161 PKGVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TVFCSAATVYRMLVQNDMA-SYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSM 398
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLdKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWF 473
Cdd:cd05911 318 GRLLPNVEAKIVDDDGKdSLGPNEPGEIcvrGPQV--------MKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqliKEIQEHVKKTTAPY 553
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASY 464
|
490
....*....|....
gi 967501916 554 KYPRKvGILIITNI 567
Cdd:cd05911 465 KQLRG-GVVFVDEI 477
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-562 |
6.58e-63 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 213.31 E-value: 6.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 ndvlAPAvdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimAMFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05934 82 ----DPA--------------------------------------------------SILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 254 LGLSVNGRfWLDLTPSDVMW--------NTSDTGWAkSAWSSvfspwiQGACVFahhLPRFEPTSVLQTLSKYPITVFCS 325
Cdd:cd05934 108 FAGYYSAR-RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 326 AATVYRMLVQ-----NDMAsykfkslkHCVSA--GEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSM 398
Cdd:cd05934 177 LGAMLSYLLAqppspDDRA--------HRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd05934 249 GRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK-SHDqeqlikEIQEHVKKTTAPYKYPR 557
Cdd:cd05934 327 DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE------ELFAFCEGQLAYFKVPR 400
|
....*
gi 967501916 558 KVGIL 562
Cdd:cd05934 401 YIRFV 405
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
77-559 |
1.31e-62 |
|
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: 217.57 E-value: 1.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 77 KPSNPAFWWING-KGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTV--LIPG--- 150
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 151 TTQLTQkdilyRLQSSKANCIITNDV---------LAPAVD-AIA------PKCENLHSKLIVSENSREG-WGNLKEMMK 213
Cdd:cd05967 143 AKELAS-----RIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHHVLVLNRPQVPADLTKPGrDLDWSELLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 214 CASdSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05967 218 KAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 294 QGA-CVFAHHLPRF--EPTSVLQTLSKYPITVFCSAATVYRMLVQND-----MASYKFKSLKHCVSAGEPITPDVTEKWR 365
Cdd:cd05967 297 HGAtTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 366 NKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGLFAHY 441
Cdd:cd05967 377 NTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTLW 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 442 ADDP---SKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 518
Cdd:cd05967 456 KNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQ 534
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 967501916 519 VVKAFIVLNPDYKShDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05967 535 VPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLV 574
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
48-557 |
2.08e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.58 E-value: 2.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 48 QDFKLEIPEYFNFAKDVLDQWTNmEKAGKKPSNPAFWWIngkGEEVrwSFEELGSLSRKFANILsEACSLQRGDRVILIL 127
Cdd:PRK06710 9 KSYPEEIPSTISYDIQPLHKYVE-QMASRYPEKKALHFL---GKDI--TFSVFHDKVKRFANYL-QKLGVEKGDRVAIML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 128 PRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAV-------------------------D 182
Cdd:PRK06710 82 PNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVtnvqsatkiehvivtriadflpfpkN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 183 AIAPKCENLHSKLIVSENSREG---WGNLKEMMKCASDShTCvkTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVN 259
Cdd:PRK06710 162 LLYPFVQKKQSNLVVKVSESETihlWNSVEKEVNTGVEV-PC--DPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 260 GRFWLD--LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQND 337
Cdd:PRK06710 238 GVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 338 M-ASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFDVKIVDV-NG 414
Cdd:PRK06710 316 LlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLeTG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 415 NVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPF 491
Cdd:PRK06710 396 EALPPGEIGEIvvkGPQIMKG--------YWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPR 557
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE-----ELNQFARKYLAAYKVPK 528
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-559 |
2.70e-59 |
|
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: 204.06 E-value: 2.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCiit 173
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 ndVLAPAVdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05941 88 --VLDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 254 LGLSVNGRFWlDLTPSDV------------MWNtsdtgwaksawsSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYPIT 321
Cdd:cd05941 116 ANVRALVDAW-RWTEDDVllhvlplhhvhgLVN------------ALLCPLFAGASV--EFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 322 VFCSAATVYRMLVQ---------NDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKGm 391
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDG- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 392 KIKPGSMGKPSPAFDVKIVDVNGNvlPPGQEGDIG-IQVlpnRPFGLFAHYADDPSKTASTLRG-NFYITGDRGYMDEDG 469
Cdd:cd05941 260 ERRPGTVGMPLPGVQARIVDEETG--EPLPRGEVGeIQV---RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 470 YFWFVAR-SDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLIkeiqEHVKK 548
Cdd:cd05941 335 YYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWAKQ 410
|
490
....*....|.
gi 967501916 549 TTAPYKYPRKV 559
Cdd:cd05941 411 RLAPYKRPRRL 421
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-552 |
5.01e-58 |
|
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: 205.03 E-value: 5.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 59 NFAKDVLDQWTnmekaGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHSKLIVSENSRE-GWGNL 208
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 209 K-----EMMKCASDSHTcvKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:cd05968 215 RdlsydEEKETAGDGAE--RTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 284 AWSsVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLV---QNDMASYKFKSLKHCVSAGEPITP 358
Cdd:cd05968 293 PWL-IFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 359 dvtEKW------RNKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPgQEGDIGIQvlp 431
Cdd:cd05968 372 ---EPWnwlfetVGKGRNPIINYSGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL--- 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 432 nRPF-GLFAHYADDPSKTASTLRG---NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:cd05968 445 -APWpGMTRGFWRDEDRYLETYWSrfdNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 967501916 508 VVSSPDPIRGEVVKAFIVLNPDYKSHD--QEQLIKEIQEHVKKTTAP 552
Cdd:cd05968 524 AIGVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGKPLSP 570
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
95-559 |
3.99e-56 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 197.15 E-value: 3.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 NDVLAPAVD-AIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMF-FTSGTSGYPKMTAHTHSS 251
Cdd:cd05926 94 KGELGPASRaASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALIlHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 252 fgLGLSV-NGRFWLDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiQGACVFAhhlPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05926 174 --LAASAtNITNTYKLTPDDrtlvVMPLFHVHGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYNATWYTAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 327 ATVYRMLVQNDMASY--KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV--LICGNFKGMKIKPGSMGKPS 402
Cdd:cd05926 246 PTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 403 PAfDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTA-STLRGNFYITGDRGYMDEDGYFWFVARSDDII 481
Cdd:cd05926 326 GV-EVRILDEDGEILPPGVVGEICLRG-PNVTRG----YLNNPEANAeAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 482 LSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-----TEEELRAFCRKHLAAFKVPKKV 472
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
106-559 |
1.54e-54 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 195.74 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND------- 175
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 --VLAPAVD-AIApKCENLHSKLIVS--------ENSREGWGNlkEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKM 244
Cdd:PRK00174 186 piPLKANVDeALA-NCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 245 TAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhlprFE--PT--------SVLQt 314
Cdd:PRK00174 263 VLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLM-----FEgvPNypdpgrfwEVID- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 315 lsKYPITVFCSAATVYRMLVQ---NDMASYKFKSLKHCVSAGEPITPdvtEKWR---NKTGLD---IYEGYGQTET--VL 383
Cdd:PRK00174 337 --KHKVTIFYTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINP---EAWEwyyKVVGGErcpIVDTWWQTETggIM 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 384 IC---GnfkGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPF-----GLFAhyadDPS---KTA-ST 451
Cdd:PRK00174 412 ITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPWpgmmrTIYG----DHErfvKTYfST 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 452 LRGNfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK 531
Cdd:PRK00174 481 FKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE 559
|
490 500
....*....|....*....|....*...
gi 967501916 532 SHDqeQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK00174 560 PSD--ELRKELRNWVRKEIGPIAKPDVI 585
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-559 |
2.40e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 190.14 E-value: 2.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSRE---GWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 248 THSSFgLGLSVNGRFWLDLTPSDVMWNtsdtgwA----KSAWSSVF-SPWIQ-GACVfaHHLPRFEPTSVLQTLSKYPIT 321
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 322 VFCSAATVYRMLVQN-DMASYKFKSLKHCVSaGEPITP-DVTEKWRNK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 393
Cdd:PRK08316 263 SFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 394 KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWF 473
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI-----VHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqEHVKKTTAPY 553
Cdd:PRK08316 414 VDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTEDELI----AHCRARLAGF 488
|
....*.
gi 967501916 554 KYPRKV 559
Cdd:PRK08316 489 KVPKRV 494
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
72-559 |
2.62e-53 |
|
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: 189.75 E-value: 2.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFwwING-KGEEVrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd05904 13 LFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAIAPKCENLHSKLIVSENSR-EGWGNLKEMMKCASDSHTCVKTKHNEI 229
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDSAEfDSLSFSDLLFEADEAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 230 MAMFFTSGTSGYPK-----------MTAHTHSSFGLGLSVNGRFWLDLTPSDVMwntsdtGWAKSAWSSVFSpwiqGACV 298
Cdd:cd05904 161 AALLYSSGTTGRSKgvmlthrnliaMVAQFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 299 FAhhLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMA-SYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGY 376
Cdd:cd05904 231 VV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTL 452
Cdd:cd05904 309 GMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 RGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyk 531
Cdd:cd05904 384 DKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG-- 461
|
490 500
....*....|....*....|....*...
gi 967501916 532 SHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05904 462 SSLTED---EIMDFVAKQVAPYKKVRKV 486
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
94-559 |
6.05e-51 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 183.15 E-value: 6.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 NDVLAPAVDAIAPKCENLHskliVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPK--MTAHTH-S 250
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFGLGLSVNGRFwldlTPSDVMwntsdtgwaksawssvfspwIQGACVFAHH------------------LPRFEPTSVL 312
Cdd:PRK07514 183 SNALTLVDYWRF----TPDDVL--------------------IHALPIFHTHglfvatnvallagasmifLPKFDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 313 QTLSKypITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKG 390
Cdd:PRK07514 239 ALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 391 MKIkPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGN-FYITGDRGYMDED 468
Cdd:PRK07514 317 ERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG-PN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDER 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 469 GYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIKEIQEHVkk 548
Cdd:PRK07514 391 GYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL-- 467
|
490
....*....|.
gi 967501916 549 ttAPYKYPRKV 559
Cdd:PRK07514 468 --ARFKQPKRV 476
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
88-559 |
2.28e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 178.94 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 88 GKGEEvrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 167
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 168 ANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEimaMFFTSGTSGYPK---- 243
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD---MLYSSGTTGRPKgikr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 244 --MTAHTHSSFGLGLSVNGrFWLDLTPSDV------MWNTSDTGWaksawssvfspwiqgaCVFAHHL-------PRFEP 308
Cdd:PRK08276 161 plPGLDPDEAPGMMLALLG-FGMYGGPDSVylspapLYHTAPLRF----------------GMSALALggtvvvmEKFDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 309 TSVLQTLSKYPITVFCSAATVY-RML-----VQndmASYKFKSLKHCVSAGEPITPDVTEK----WrnktGLDIYEGYGQ 378
Cdd:PRK08276 224 EEALALIERYRVTHSQLVPTMFvRMLklpeeVR---ARYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 379 TE----TVLICGNFKGmkiKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFglfaHYADDPSKTASTLRG 454
Cdd:PRK08276 297 SEgggvTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 455 NFYIT-GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKsh 533
Cdd:PRK08276 368 HGWVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD-- 445
|
490 500
....*....|....*....|....*.
gi 967501916 534 DQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08276 446 AGDALAAELIAWLRGRLAHYKCPRSI 471
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-556 |
9.63e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 178.31 E-value: 9.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDQWtnmekAGKKPSNPAFWWIngkGEEVrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK06178 37 EYLRAW-----ARERPQRPAIIFY---GHVI--TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLH------SKLIVSENSR-------------E 203
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHvivtslADVLPAEPTLplpdslraprlaaA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 204 GWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:PRK06178 186 GAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 284 AWSSVFSPWIQGACVFAhhLPRFEPTSVLQTLSKYPITVfcsaaTVyrMLVQN--------DMASYKFKSLKH--CVSAG 353
Cdd:PRK06178 266 ENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTR-----TV--MLVDNavelmdhpRFAEYDLSSLRQvrVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 354 EPITPDVTEKWRNKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEG 423
Cdd:PRK06178 337 KKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 424 DIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSV 503
Cdd:PRK06178 416 EIVV-----RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 967501916 504 AESAVVSSPDPIRGEVVKAFIVLNPDyksHDQEQliKEIQEHVKKTTAPYKYP 556
Cdd:PRK06178 491 LGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP 538
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-562 |
4.63e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 175.05 E-value: 4.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLAPAVDAIAPKCENLHSKLIVSensregwgnLKEMMKCASDShtCVKTKHNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSFGLGlSVNGRFWLDLTPSDV------MWNTSDTGWAksawssVFSPWIQGACVFAHHlpRFEPTSVLQTLSKYPITVF 323
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 324 CSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTET-----VLICGNFKGmkiKPGS 397
Cdd:PRK06839 243 MGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 398 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 477
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRG-PN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 478 DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqliKEIQEHVKKTTAPYKYPR 557
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPK 468
|
....*
gi 967501916 558 KVGIL 562
Cdd:PRK06839 469 EIVFL 473
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
92-562 |
2.33e-47 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 174.18 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLAPAVDAIAPKCENLHSKLIVSENSRE----GWGNLKemMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVsvpaGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 248 THSSFglglsvngrFW--------LDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYP 319
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 320 ITV-FCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPitPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 398
Cdd:PRK06155 269 ATVtYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpNRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 478
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPRK 558
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALV----RHCEPRLAYFAVPRY 498
|
....
gi 967501916 559 VGIL 562
Cdd:PRK06155 499 VEFV 502
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
94-562 |
3.76e-47 |
|
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: 171.41 E-value: 3.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPrvpEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVL-----APAVDAIApkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimAMFFTSGTSGYPKMT 245
Cdd:cd05903 77 FVVPERFrqfdpAAMPDAVA---------------------------------------------LLLFTSGTTGEPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 246 AHTHSSfglgLSVNGRFW---LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfaHHLPRFEPTSVLQTLSKYPITV 322
Cdd:cd05903 112 MHSHNT----LSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 323 FCSAAT-VYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNfkgmkIKPG----- 396
Cdd:cd05903 186 MMGATPfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 397 --SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFV 474
Cdd:cd05903 261 lyTDGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 475 ARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEHV-KKTTAPY 553
Cdd:cd05903 336 GRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS-----GALLTFDELVAYLdRQGVAKQ 410
|
....*....
gi 967501916 554 KYPRKVGIL 562
Cdd:cd05903 411 YWPERLVHV 419
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-559 |
1.19e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 172.88 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDQwtNMEKAGKKPsnpAFWWInGKGEevrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK05605 36 DLYDN--AVARFGDRP---ALDFF-GATT----TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP---------------AVDAIA--PKCENLHSKLIVS--ENSRE 203
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAamPLLQRLALRLPIPalRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 204 G----------WGNL-KEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVN---GRFWLDLTPS 269
Cdd:PRK05605 185 AltgpapgtvpWETLvDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR----NLFANaaqGKAWVPGLGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 270 D----------------VMWNTsdtgwaksawssvFSPWIQGACVFahhLPRFEPTSVLQTLSKYPITVFCSAATVYRML 333
Cdd:PRK05605 261 GpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 334 VqnDMASYK---FKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKI 409
Cdd:PRK05605 325 A--EAAEERgvdLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 410 VDVN--GNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSS 484
Cdd:PRK05605 403 VDPEdpDETMPDGEEGELlvrGPQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLikeiQEHVKKTTAPYKYPRKV 559
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGL----RAYCREHLTRYKVPRRF 544
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
95-559 |
2.77e-46 |
|
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: 168.29 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEEL----GSLSRKFANIlseacSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05912 2 YTFAELfeevSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 iitndvlapavdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhNEIMAMFFTSGTSGYPK---MTAH 247
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKgvqQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 248 TH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPIT 321
Cdd:cd05912 101 NHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 322 VFCSAATVYRMLVQNDMASYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 399
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 400 KPSPAFDVKIVDVNGnvlPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDD 479
Cdd:cd05912 246 KPLFPVELKIEDDGQ---PPYEVGEILLKG-PNVTKG----YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 480 IILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQLIKEIQEHVKKttapYKYPRKV 559
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKVPKKI 390
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
303-559 |
6.80e-46 |
|
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: 165.14 E-value: 6.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 303 LPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHcVSAGEpiTPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILsNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 382 ---VLICGNFKgmkiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI 458
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 459 TGDRGYMDEDGYFWFVARS--DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQE 536
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG-ATLTAD 298
|
250 260
....*....|....*....|...
gi 967501916 537 QLIkeiqEHVKKTTAPYKYPRKV 559
Cdd:cd17637 299 ELI----EFVGSRIARYKKPRYV 317
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
76-559 |
1.24e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 170.90 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 76 KKPSNPAFWWINGK-GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPG- 150
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 151 -TTQLTQkdilyRLQSSKANCIITND-------VLA--PAVDAIAPKCENLHSK-LIVS-----ENSREG----WGNLKE 210
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADagsrggkVVPykPLLDEAIALAQHKPRHvLLVDrglapMARVAGrdvdYATLRA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 211 mmKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFS 290
Cdd:PRK10524 219 --QHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 291 PWIQG-ACVFAHHLP-RFEPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKFKSLKHCVSAGEPITpDVTEKWR 365
Cdd:PRK10524 297 PLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEPLD-EPTASWI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 366 NKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQV-LPnrPFGLF 438
Cdd:PRK10524 376 SEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGpLP--PGCMQ 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 439 AHYADDP---SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PRK10524 454 TVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDAL 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 967501916 516 RGEVVKAFIVLNPDYKSHDQEQ---LIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK10524 534 KGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARV 580
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
68-562 |
1.77e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 168.80 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 68 WTNM--EKAGKKPSNPAFWWingKGEEVRWSfeELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGT 145
Cdd:PRK07786 19 WVNQlaRHALMQPDAPALRF---LGNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 146 VLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP---AVDAIAPKcenLHSKLIVSENSREGWGNLKEMMKCASDSHTCV 222
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPvatAVRDIVPL---LSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 223 KTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGlGLSVNG-RFWLDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVFAH 301
Cdd:PRK07786 170 DIPNDSPALIMYTSGTTGRPKGAVLTHANLT-GQAMTClRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 302 HLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLvqnDMASYKFKSLK-HCVSAGEPITPDVTEKWRNKT--GLDIYEGYG 377
Cdd:PRK07786 248 PLGAFDPGQLLDVLEAEKVTgIFLVPAQWQAVC---AEQQARPRDLAlRVLSWGAAPASDTLLRQMAATfpEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 378 QTE----TVLICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFAHYADDPSKTASTLR 453
Cdd:PRK07786 325 QTEmspvTCMLLGEDAIRKL--GSVGKVIPTVAARVVDENMNDVPVGEVGEI-----VYRAPTLMSGYWNNPEATAEAFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyksh 533
Cdd:PRK07786 398 GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---- 473
|
490 500
....*....|....*....|....*....
gi 967501916 534 DQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIV 502
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-559 |
2.08e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 168.24 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 78 PSNPAFWWINGkgeevRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIP-GTTQ 153
Cdd:PRK06188 26 PDRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 ltqkDILYRLQSSKANCIITNDvlAPAVD---AIAPKCENLhsKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIM 230
Cdd:PRK06188 100 ----DHAYVLEDAGISTLIVDP--APFVEralALLARVPSL--KHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 231 AMFFTSGTSGYPKMTAHTHSSFG---------LGLSVNGRFwLDLTPsdvmwnTSDTGWAKsawssvFSPWIQ-GACVfa 300
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIAtmaqiqlaeWEWPADPRF-LMCTP------LSHAGGAF------FLPTLLrGGTV-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 301 HHLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDvtekwRNKTGLDIY-----E 374
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITaTFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERFgpifaQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTE-----TVLICGNFKGMKIKP-GSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKT 448
Cdd:PRK06188 312 YYGQTEapmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 449 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP 528
Cdd:PRK06188 387 AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP 466
|
490 500 510
....*....|....*....|....*....|.
gi 967501916 529 DyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK06188 467 G-AAVDAA----ELQAHVKERKGSVHAPKQV 492
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-561 |
2.38e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 167.94 E-value: 2.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANiLSEACSLQRGDRVILILPRVPEW---WLAnVACLrtGTVLI 148
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 149 PGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCEN-LHSKLIVSENSREGWG-----NLKEMMKCASDSHTCV 222
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPADDGvssftQLKAQQPATLCYAPPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 223 KTkhNEIMAMFFTSGTSGYPKMTAHTHSsfglglsvNGRFwldltpsdvmwntsdtgwaksawSSVFSPWiQGA------ 296
Cdd:PRK08008 171 ST--DDTAEILFTSGTTSRPKGVVITHY--------NLRF-----------------------AGYYSAW-QCAlrdddv 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 297 ---CVFAHH--------LPRFEPTSVLQTLSKYPITVFCSAATVYR-------------MLVQNDMASYKfkslKHC--- 349
Cdd:PRK08008 217 yltVMPAFHidcqctaaMAAFSAGATFVLLEKYSARAFWGQVCKYRatitecipmmirtLMVQPPSANDR----QHClre 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 350 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQ 428
Cdd:PRK08008 293 VMFYLNLSDQEKDAFEERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 429 VLPNRPfgLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:PRK08008 373 GVPGKT--IFKEYYLDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 508 VVSSPDPIRGEVVKAFIVLNPDykshdqEQL-IKEIQEHVKKTTAPYKYPRKVGI 561
Cdd:PRK08008 451 VVGIKDSIRDEAIKAFVVLNEG------ETLsEEEFFAFCEQNMAKFKVPSYLEI 499
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
96-508 |
3.08e-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: 165.13 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 169 NCIITNDVLAPAVDAIAPKCENLHSKLIVSENSregwgnlkemmkCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDD------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF--AHHLPRFEPTSVLQTLSKYPITVFCSA 326
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 327 ATVYRMLVqnDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLICgnfkGMKIKPGSM------- 398
Cdd:TIGR01733 220 PSLLALLA--AALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWS----TATLVDPDDaprespv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTA---------STLRGNFYITGDRGYMDE 467
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYLP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 967501916 468 DGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
304-559 |
1.46e-44 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 166.77 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 304 PRFEPTSVlQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-T 381
Cdd:PRK08974 285 PRDIPGFV-KELKKYPFTAITGVNTLFNALLNNeEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 382 VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGNFYI 458
Cdd:PRK08974 364 PLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELwvkGPQVMLG--------YWQRPEATDEVIKDGWLA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdyKSHDQEQL 538
Cdd:PRK08974 436 TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEEL 513
|
250 260
....*....|....*....|.
gi 967501916 539 IKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK08974 514 ITHCRRHL----TGYKVPKLV 530
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
89-557 |
3.03e-44 |
|
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: 163.47 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 89 KGEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05930 7 VDGDQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 169 NCIITNdvlapavdaiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:cd05930 86 KLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLP---RFEPTSVLQTLSKYPIT 321
Cdd:cd05930 115 HRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEALADLLAEEGIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 322 VFCSAATVYRMLVQnDMASYKFKSLKHCVSAGEPITPDVTEKWR-NKTGLDIYEGYGQTETVLICGNF--KGMKIKPGSM 398
Cdd:cd05930 187 VLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWReLLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglfAH-YADDPSKTASTLRGN-------FYITGDRGYM 465
Cdd:cd05930 266 piGRPIPNTRVYVLDENLRPVPPGVPGELyigGAGL---------ARgYLNRPELTAERFVPNpfgpgerMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 466 DEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEH 545
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEELRAH 411
|
490
....*....|..
gi 967501916 546 VKKTTAPYKYPR 557
Cdd:cd05930 412 LAERLPDYMVPS 423
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-559 |
5.34e-44 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 163.59 E-value: 5.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPkcenlhskLIVSEnsregwgnlkeMMKCASDSHTCVKTKH-NEIMAMFFTSGTSGYPK---MTA 246
Cdd:PRK03640 103 LITDDDFEAKLIPGIS--------VKFAE-----------LMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKgviQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 247 HTH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK03640 164 GNHwwsavgSALNLGLTEDDC-WLAAVP---IFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TVFCSAAT-VYRMLVQNDMASYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 397
Cdd:PRK03640 231 TIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 398 MGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVlPNRPFGlfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 477
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKG-PNVTKG----YLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 478 DDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyKSHDQEQLIKEIQEHVkkttAPYKYPR 557
Cdd:PRK03640 383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRHFCEEKL----AKYKVPK 455
|
..
gi 967501916 558 KV 559
Cdd:PRK03640 456 RF 457
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
96-559 |
9.03e-44 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 164.42 E-value: 9.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLAPAVDAIAPKCENLH------------SKLIVSENSRegwgNLKEMMkcasdshtcvktkhneimamfftsgtsgyPK 243
Cdd:PRK07059 129 NFATTVQQVLAKTAVKHvvvasmgdllgfKGHIVNFVVR----RVKKMV-----------------------------PA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 244 MTAHTHSSFGLGLSVNGRFWL---DLTPSDV---MWNTSDTGWAKSA-------WSSVF--SPWIQGA------------ 296
Cdd:PRK07059 176 WSLPGHVRFNDALAEGARQTFkpvKLGPDDVaflQYTGGTTGVSKGAtllhrniVANVLqmEAWLQPAfekkprpdqlnf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 297 -C------VFA-------------HHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVS 351
Cdd:PRK07059 256 vCalplyhIFAltvcgllgmrtggRNIlipnPRDIP-GFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 352 AGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---G 426
Cdd:PRK07059 335 GGMAVQRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEIcirG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 427 IQVLpnrpfglfAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAE 505
Cdd:PRK07059 414 PQVM--------AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 967501916 506 SAVVSSPDPIRGEVVKAFIVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07059 486 VAAVGVPDEHSGEAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-559 |
2.75e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 162.52 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07470 17 ARRFPDRIALVW----GDR-SWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKlIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMF 233
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV-VAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSfgLGLSVNGRFwLDLTPsdvmwntsdtGWAKSAWSSVFSPWIQGACVfaHHL---------- 303
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQ--MAFVITNHL-ADLMP----------GTTEQDASLVVAPLSHGAGI--HQLcqvargaatv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 304 ----PRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQ 378
Cdd:PRK07470 235 llpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 379 TE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSK 447
Cdd:PRK07470 315 GEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEIcviGPAV--------FAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 448 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLN 527
Cdd:PRK07470 387 NAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510
....*....|....*....|....*....|..
gi 967501916 528 pDYKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07470 467 -DGAPVDEA----ELLAWLDGKVARYKLPKRF 493
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-559 |
3.31e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 161.71 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK13390 22 GEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIitndVLAPAVDAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDShtcvKTKHNEIMAMFFTSGTSGYPK-----M 244
Cdd:PRK13390 99 VL----VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPR----LTEQPCGAVMLYSSGTTGFPKgiqpdL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 245 TAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS-AWSSVFSPwIQGACVFAHhlpRFEPTSVLQTLSKYPITVF 323
Cdd:PRK13390 171 PGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 324 CSAATVY-RMLVQND--MASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVLICGNFKGmkiKPG 396
Cdd:PRK13390 247 QMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 397 SMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIQ--VLPNRpfglfahYADDPSKTASTLRGN--FYIT-GDRGYMDEDGYF 471
Cdd:PRK13390 324 SVGR-SVLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLIKEIQEHVKKTTA 551
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELARELIDYTRSRIA 473
|
....*...
gi 967501916 552 PYKYPRKV 559
Cdd:PRK13390 474 HYKAPRSV 481
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-557 |
1.12e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 161.48 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPA-----VDAIAP----------KCENL-HSKLIVS--ENSREG---WGNLKEMMKCASDSHTCVKT---KH 226
Cdd:PRK12583 121 VICADAFKTSdyhamLQELLPglaegqpgalACERLpELRGVVSlaPAPPPGflaWHELQARGETVSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 227 NEIMAMFFTSGTSGYPKMTAHTHSSfglgLSVNGRF---WLDLTPSDVM------WNTSDTGWAKSAWSSVfspwiqGAC 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLcvpvplYHCFGMVLANLGCMTV------GAC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 298 VFahhLPR--FEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIY 373
Cdd:PRK12583 271 LV---YPNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 374 EGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDigiqvLPNRPFGLFAHYADDPSKTAS 450
Cdd:PRK12583 348 IAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGE-----LCTRGYSVMKGYWNNPEATAE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:PRK12583 423 SIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG 502
|
490 500
....*....|....*....|....*...
gi 967501916 530 YKSHDQeqlikEIQEHVKKTTAPYKYPR 557
Cdd:PRK12583 503 HAASEE-----ELREFCKARIAHFKVPR 525
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
96-559 |
1.24e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 158.50 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLAPAV-DAIA------------------PKCENL-----HSKLIVSENSREGWGNLKEMMKCASdSHTC--VKTKHNEI 229
Cdd:PRK08751 132 NFGTTVqQVIAdtpvkqvittglgdmlgfPKAALVnfvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 230 MAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTpsdvmwNTSDTG-------------WAKSAWSSVFSPWiqGA 296
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAGT------GKLEEGcevvitalplyhiFALTANGLVFMKI--GG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 297 CvfaHHL---PRFEPTSVlQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK08751 282 C---NHLisnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKT 448
Cdd:PRK08751 358 VEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELcikGPQVMKG--------YWKRPEET 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 449 ASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVln 527
Cdd:PRK08751 430 AKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-- 507
|
490 500 510
....*....|....*....|....*....|..
gi 967501916 528 pdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08751 508 ----KKDPALTAEDVKAHARANLTGYKQPRII 535
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
74-558 |
1.53e-41 |
|
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: 155.87 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttq 153
Cdd:cd05945 1 AAANPDRPAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 ltqkdilyrlqsskanciitndvlapaVDAIAPKcenlhsklivsensrEGWGNLKEMMKCASdshtcVKTKHNEIMAMF 233
Cdd:cd05945 71 ---------------------------LDASSPA---------------ERIREILDAAKPAL-----LIADGDDNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHS---SFGLGLsvNGRFwlDLTPSDVMWNTSDtgwaksaWS---SVFS---PWIQGACVFAhhLP 304
Cdd:cd05945 104 FTSGSTGRPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 305 RFE---PTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQT 379
Cdd:cd05945 171 RDAtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 380 ETVLICgnfKGMKIKPGSM--------GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFAHYADDPSKT 448
Cdd:cd05945 251 EATVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELvisGPSV--------SKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 449 ASTLRGNF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFI 524
Cdd:cd05945 320 AAAFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFV 399
|
490 500 510
....*....|....*....|....*....|....
gi 967501916 525 VLNPdyksHDQEQLIKEIQEHVKKTTAPYKYPRK 558
Cdd:cd05945 400 VPKP----GAEAGLTKAIKAELAERLPPYMIPRR 429
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
91-546 |
2.96e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.19 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELgsLSR--KFANILSeACSLQRGDRVILILPRVPE----WW---LANVAC--------------LR-TGT- 145
Cdd:PRK07529 55 RPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPEthfaLWggeAAGIANpinpllepeqiaelLRaAGAk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 146 VLI-----PGTtQLTQK--DILYRLQSSKAncIIT---NDVLAPAVDAIAPKCENLHSKLIVSENSregwgnlkEMMKCA 215
Cdd:PRK07529 132 VLVtlgpfPGT-DIWQKvaEVLAALPELRT--VVEvdlARYLPGPKRLAVPLIRRKAHARILDFDA--------ELARQP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 216 SDSHTCVKTKH-NEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMW--------NTSDTGwa 281
Cdd:PRK07529 201 GDRLFSGRPIGpDDVAAYFHTGGTTGMPKLAQHTHG----NEVANA--WlgallLGLGPGDTVFcglplfhvNALLVT-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 282 ksawssVFSPWIQGACVFahhLPR---FEPTSVLQTLSK----YPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGE 354
Cdd:PRK07529 273 ------GLAPLARGAHVV---LATpqgYRGPGVIANFWKiverYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 355 PITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLP 431
Cdd:PRK07529 344 PLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLCIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 432 NrPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSS 511
Cdd:PRK07529 424 G-P-NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGR 501
|
490 500 510
....*....|....*....|....*....|....*
gi 967501916 512 PDPIRGEVVKAFIVLNPDyKSHDQEQLIKEIQEHV 546
Cdd:PRK07529 502 PDAHAGELPVAYVQLKPG-ASATEAELLAFARDHI 535
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
235-562 |
1.46e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 154.92 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 235 TSGTSGYPKMTAHTHSSFGLGLSVngrfWLDLTPsdvmWNTSDTGWAKSAwssVFSPWIQGACVFAHHLP-------RFE 307
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKA----ILDRTP----WRAEEPTVIVAP---MFHAWGFSQLVLAASLActivtrrRFD 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRM---LVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI 384
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMI 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 385 C-GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYAddPSKTASTLRGnFYITGDRG 463
Cdd:PRK13382 353 AtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-FMASGDVG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQ 543
Cdd:PRK13382 425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLK 499
|
330
....*....|....*....
gi 967501916 544 EHVKKTTAPYKYPRKVGIL 562
Cdd:PRK13382 500 QHVRDNLANYKVPRDIVVL 518
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-562 |
3.29e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 154.14 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 -----------------NDV--LAP--AVDAIAPKCENLHSKLIVSENSregwgNLKEMMKCASDshtcvktkhnEIMAM 232
Cdd:PRK06087 128 ptlfkqtrpvdlilplqNQLpqLQQivGVDKLAPATSSLSLSQIIADYE-----PLTTAITTHGD----------ELAAV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 233 FFTSGTSGYPKMTAHTHSSFGLG-LSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhhLPRFEPTSV 311
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDAC 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 312 LQTLSKYPITvfCS-AAT--VYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEK-WRNktGLDIYEGYGQTETV--LIC 385
Cdd:PRK06087 269 LALLEQQRCT--CMlGATpfIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQR--GIKLLSVYGSTESSphAVV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDiGIQVLPNrpfgLFAHYADDPSKTASTL--RGNFYiTGDRG 463
Cdd:PRK06087 345 NLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGE-EASRGPN----VFMGYLDEPELTARALdeEGWYY-SGDLC 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLIKEIQ 543
Cdd:PRK06087 419 RMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFS 498
|
490
....*....|....*....
gi 967501916 544 EhvkKTTAPYKYPRKVGIL 562
Cdd:PRK06087 499 R---KRVAKYKYPEHIVVI 514
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
96-559 |
7.59e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 153.16 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSlqRGDRVILILPRVPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKAN 169
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGV--RAGDGVAVLARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLAPAVDAIAPKCENLHSKLIVSEN---SREGWGNLKEMMKCASDSHTCVKTKHNEIMAMffTSGTSGYPKMTA 246
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSSTAPLPKPPKPGGIVIL--TSGTTGTPKGAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 247 HTHSSfglGLSVNGRFwLDLTP---SDVMWNTS----DTGWAKSAWSSVFspwiqGACVFAHHlpRFEPTSVLQTLSKYP 319
Cdd:PRK07788 227 RPEPS---PLAPLAGL-LSRVPfraGETTLLPApmfhATGWAHLTLAMAL-----GSTVVLRR--RFDPEATLEDIAKHK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 320 ITVFCSAAT-VYRML--VQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVlicGNFKGMK 392
Cdd:PRK07788 296 ATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDLA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 393 IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKtaSTLRGnFYITGDRGYMDEDGYfW 472
Cdd:PRK07788 373 EAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL-L 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 473 FVA-RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTA 551
Cdd:PRK07788 444 FVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLA 518
|
....*...
gi 967501916 552 PYKYPRKV 559
Cdd:PRK07788 519 RYKVPRDV 526
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
78-559 |
7.66e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 152.54 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 78 PSNPAFWwINGKGEEVrwSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEwwlANVACLRTGTVLIPGTTQL 154
Cdd:PRK13391 11 PDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 155 TQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV-SENSREGWGNLKEMMKCASDShtcVKTKHNEIMAMF 233
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPAT---PIADESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPK----------------MTAHTHSSFGLGlsvNGRFWLDLTPsdvMWNTsdtgwAKSAWSSVfspwIQ--G 295
Cdd:PRK13391 161 YSSGTTGRPKgikrplpeqppdtplpLTAFLQRLWGFR---SDMVYLSPAP---LYHS-----APQRAVML----VIrlG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 296 ACVFAhhLPRFEPTSVLQTLSKYPITVFCSAATVY-RML-----VQNdmaSYKFKSLKHCVSAGEPITPDVTEKWRNKTG 369
Cdd:PRK13391 226 GTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLklpeeVRD---KYDLSSLEVAIHAAAPCPPQVKEQMIDWWG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 370 LDIYEGYGQTETVLICG-NFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFglfaHYADDPSKT 448
Cdd:PRK13391 301 PIIHEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 449 ASTL--RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVL 526
Cdd:PRK13391 374 AEARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP 453
|
490 500 510
....*....|....*....|....*....|....*
gi 967501916 527 NP--DYKSHDQEQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK13391 454 VDgvDPGPALAAELIAFCRQRL----SRQKCPRSI 484
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-559 |
8.62e-40 |
|
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: 148.58 E-value: 8.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSFglgLSvNGRFW---LDLTPSDVM----------------WNTSDTGwaksawssvfspw 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI---VN-NGYFIgerLGLTEQDRLcipvplfhcfgsvlgvLACLTHG------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 293 iqGACVFAHhlPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGL- 370
Cdd:cd05917 70 --ATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 371 DIYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKIVDVNGNVLPP-GQEGDIGIqvlpnRPFGLFAHYADD 444
Cdd:cd05917 146 DVTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCI-----RGYSVMKGYWND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 445 PSKTASTLRG-NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:cd05917 219 PEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 967501916 524 IVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05917 299 IRLKEGAELTEE-----DIKAYCKGKIAHYKVPRYV 329
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-562 |
1.28e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 148.40 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 226 HNEIMAMFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVF 299
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHS----NEVYNA--WmlalnSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 AHHLPRFEPTSV---LQTLSKYPITVFCSAATVYRMLVQNDMASyKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:cd05944 75 AGPAGYRNPGLFdnfWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLPNRpfGLFAHYADDPSKTASTLR 453
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDEVGEICVAGP--GVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSh 533
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV- 310
|
330 340
....*....|....*....|....*....
gi 967501916 534 DQEQLIKEIQEHVKKTTApykYPRKVGIL 562
Cdd:cd05944 311 EEEELLAWARDHVPERAA---VPKHIEVL 336
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
92-559 |
1.87e-39 |
|
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: 150.91 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 IT------NDVLA---PAVDAIAPKCENlhsklivsensregwgnlkemmkcasdshtcvktkhnEIMAMFFTSGTSGYP 242
Cdd:cd12118 106 FVdrefeyEDLLAegdPDFEWIPPADEW-------------------------------------DPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 243 KMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MWNTSD---TGWAksawssvfSPWIQGAcVFAHH--LPRFEPTSVLQTLS 316
Cdd:cd12118 149 KGVVYHHRGAYLNALANILEW-EMKQHPVyLWTLPMfhcNGWC--------FPWTVAA-VGGTNvcLRKVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 317 KYPITVFCSAATVYRMLVqNDMASYKfKSLKHCVS---AGEPITPDVTEKWRNKtGLDIYEGYGQTET---VLICgnfkg 390
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVC----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 391 mKIKPGSMGKPSP---------------AFDVKIVDVNGNVLPPGQEGDIGIQVLpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:cd12118 291 -AWKPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPRDGKTIGEIVF--RGNIVMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 456 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 535
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500
....*....|....*....|....
gi 967501916 536 eqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd12118 448 -----EIIAFCREHLAGFMVPKTV 466
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-548 |
2.05e-39 |
|
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: 151.24 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 87 NGKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEWWLAnVAClrTGTVLIPGTTQLTQKDILYRL 163
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYA-VPG--MGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 164 QSSKANCIITNDVLAPAVDAIAPKC--------------------ENLHS--KLIVSENSREGWGNLKEmmkcasdshtc 221
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLptvehvvvmtddaampepagVGVLAyeELLAAESPEYDWPDFDE----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 222 vktkhNEIMAMFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQ 294
Cdd:cd12119 163 -----NTAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GAC-VFAHhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDI 372
Cdd:cd12119 231 GAKlVLPG--PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTET--VLICGnfkgmKIKPG--------------SMGKPSPAFDVKIVDVNGNVLP--PGQEGDIgiQVlpnR- 433
Cdd:cd12119 308 IHAWGMTETspLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGEL--QV---Rg 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 434 PFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 513
Cdd:cd12119 378 PW-VTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPH 456
|
490 500 510
....*....|....*....|....*....|....*
gi 967501916 514 PIRGEVVKAFIVLNPDyKSHDQEQLIKEIQEHVKK 548
Cdd:cd12119 457 PKWGERPLAVVVLKEG-ATVTAEELLEFLADKVAK 490
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
96-571 |
7.13e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 150.68 E-value: 7.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLAPAVDAIAPKCENLHskLIVSE-------------NSREGWgnLKEMM----------------KCASDSHTCVKTKH 226
Cdd:PRK05677 131 NMAHLAEKVLPKTGVKH--VIVTEvadmlpplkrlliNAVVKH--VKKMVpayhlpqavkfndalaKGAGQPVTEANPQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 227 NEIMAMFFTSGTSGYPKMTAHTHSSfglgLSVNgrfWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQgaCVF----- 299
Cdd:PRK05677 207 DDVAVLQYTGGTTGVAKGAMLTHRN----LVAN---MLQCRAlmGSNLNEGCEILIAPLPLYHIYAFTFH--CMAmmlig 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 AHHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYE 374
Cdd:PRK05677 278 NHNIlisnPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTAS 450
Cdd:PRK05677 357 GYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELcvkGPQVMKG--------YWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:PRK05677 428 ILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 967501916 530 ykshdqEQLIKE-IQEHVKKTTAPYKYPRKV---GILIITNICSVL 571
Cdd:PRK05677 508 ------ETLTKEqVMEHMRANLTGYKVPKAVefrDELPTTNVGKIL 547
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-562 |
1.69e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 147.59 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 117 LQRGDRVILILPRVPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENlh 192
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 193 SKLIVSEnsrEGWgnlkemmKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRfwLDLTPSDV 271
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 272 MWNTSDTGWAkSAWSSVFSPWIQGACVFAHHLPRFePTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVS 351
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 352 AGEPITPDVTEKWRNK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQE 422
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 423 GDIGiqvlPNRPFGLfAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHP 501
Cdd:cd05922 313 GEIV----HRGPNVM-KGYWNDPPYRRKEGRGGGVLhTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967501916 502 SVAESAVVSSPDPIrGEVVKAFIVLNPDYKSHDqeqlikeIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05922 388 LIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVV 440
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
231-559 |
2.91e-38 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 147.14 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 231 AMFFTSGTSGYPKmtahthssfglGLSVNGRFWLDLTPSDVMWNTSDtGWakSAWSSVFSP----------WIQGACVFA 300
Cdd:cd05929 129 KMLYSGGTTGRPK-----------GIKRGLPGGPPDNDTLMAAALGF-GP--GADSVYLSPaplyhaapfrWSMTALFMG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 301 HHL---PRFEPTSVLQTLSKYPITVFCSAATVY-RM--LVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYE 374
Cdd:cd05929 195 GTLvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIgiQVLPNRPFglfaHYADDPSKTA-STL 452
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEV--YFANGPGF----EYTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAfiVLNPDYKS 532
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340
....*....|....*....|....*..
gi 967501916 533 HDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSI 452
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-562 |
6.87e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 147.51 E-value: 6.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWIN-GKGEEVRWSFEELGSLSRKFANILSEaCSLQRGDRVILilpRVPEWWLANV---ACLRTGTVLIP 149
Cdd:PRK13295 34 VASCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSC---QLPNWWEFTVlylACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 150 GTTQLTQKDILYRLQSSKANCIITNDVL-----APAVDAIAPKCENLHSKLIVSENSREGWGNL-----KEMMKCASDSH 219
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALlitpaWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 220 TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSS-FGLGLSVNGRfwLDLTPSDVMWNTS----DTGWAKSAwssvFSPWIQ 294
Cdd:PRK13295 190 ARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACVFAHHLprFEPTSVLQTLSKYPITvFCSAATVYRM-LVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK13295 264 GATAVLQDI--WDPARAAELIRTEGVT-FTMASTPFLTdLTRAvKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTETVLICGnfkgmkIKPG--------SMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiQVlpnRPFGLFAHYADD 444
Cdd:PRK13295 341 VSAWGMTENGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRL--QV---RGCSNFGGYLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 445 PSKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFI 524
Cdd:PRK13295 410 PQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510
....*....|....*....|....*....|....*...
gi 967501916 525 VLNPDyKSHDQEQLIKEIQEHvkKTTAPYkYPRKVGIL 562
Cdd:PRK13295 489 VPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPERLVVR 522
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
74-559 |
7.75e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 146.57 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWingKGEEVrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK06145 12 ARRTPDRAALVY---RDQEI--SYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAIapkcenlHSKLIVSENSREGWGNLKEMMKCASDSHTCVKTkhnEIMAMF 233
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLLVDEEFDAIVALE-------TPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPT---DLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFW----------LDLTPSDVMWntsdtgwaksawssvfspwiQ 294
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------V 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACVFAHHlpRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPiTP-----DVTEKWRNKT 368
Cdd:PRK06145 216 GGTLRIHR--EFDPEAVLAAIERHRLTcAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEK-TPesrirDFTRVFTRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 369 GLDiyeGYGQTETvliCGNFKGMKI-----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfahYAD 443
Cdd:PRK06145 293 YID---AYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG----YWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 444 DPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:PRK06145 362 DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 967501916 524 IVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK06145 442 VVLNP-----GATLTLEALDRHCRQRLASFKVPRQL 472
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
301-559 |
8.99e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 145.90 E-value: 8.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 301 HHLPRFEPTSVLQTLSKyPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 380
Cdd:PRK07787 199 VHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 381 TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnRPFGLFAHYADDPSKTASTLRGN-FYIT 459
Cdd:PRK07787 278 TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPDATAAAFTADgWFRT 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 460 GDRGYMDEDGYFWFVAR-SDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQL 538
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV---AADEL 431
|
250 260
....*....|....*....|.
gi 967501916 539 IkeiqEHVKKTTAPYKYPRKV 559
Cdd:PRK07787 432 I----DFVAQQLSVHKRPREV 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-559 |
1.36e-37 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 146.28 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFwwINGKGEEVrWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 152 TQLTQKDILYRLQSSKANCIITndvLAPAVDAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMA 231
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSsfGLGLSV---------NgrfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAhh 302
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 303 LPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDM-ASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY-EGYGQTE 380
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVvEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 381 --TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTL-R 453
Cdd:PLN02246 336 agPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDPEtGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK-S 532
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEiT 490
|
490 500
....*....|....*....|....*..
gi 967501916 533 HDqeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PLN02246 491 ED------EIKQFVAKQVVFYKRIHKV 511
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
90-561 |
2.12e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 145.61 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK12406 8 GDRRR-SFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITN-DVLAPAVDAIAPKCENLH--------SKLIVSENSR---------EGWgnlkemmkcASDSHTCVKTKHNEIMA 231
Cdd:PRK12406 86 VLIAHaDLLHGLASALPAGVTVLSvptppeiaAAYRISPALLtppagaidwEGW---------LAQQEPYDGPPVPQPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPK------MTAHTHSSFGL------GLSVNGRFWLdltpSDVMWNTSDTGWAksawssVFSPWIQGACVF 299
Cdd:PRK12406 157 MIYTSGTTGHPKgvrraaPTPEQAAAAEQmraliyGLKPGIRALL----TGPLYHSAPNAYG------LRAGRLGGVLVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 ahhLPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQND--MASYKFKSLKHCVSAGEPITPDVT----EKWrnktGLDI 372
Cdd:PRK12406 227 ---QPRFDPEELLQLIERHRITHMHMVPTMFiRLLKLPEevRAKYDVSSLRHVIHAAAPCPADVKramiEWW----GPVI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTET--VLICGNFKGMKiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfahYADDPSKTAS 450
Cdd:PRK12406 300 YEYYGSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 451 TLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDy 530
Cdd:PRK12406 375 IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG- 453
|
490 500 510
....*....|....*....|....*....|.
gi 967501916 531 KSHDQEqlikEIQEHVKKTTAPYKYPRKVGI 561
Cdd:PRK12406 454 ATLDEA----DIRAQLKARLAGYKVPKHIEI 480
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
59-554 |
1.25e-36 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 145.04 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 59 NFAKDVLDQwtNMEkAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:PLN02654 88 NICYNCLDR--NVE-AGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAML 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIapkcenlHSKLIV----SENSREG--------WG 206
Cdd:PLN02654 164 ACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTI-------NLKDIVdaalDESAKNGvsvgicltYE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 207 NLKEMMKCAS-----------DSHTCVKTK-------HNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTP 268
Cdd:PLN02654 237 NQLAMKREDTkwqegrdvwwqDVVPNYPTKcevewvdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 269 SDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHH-LPRF-EPTSVLQTLSKYPITVFCSAATVYRMLVQND---MASYKF 343
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSR 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 344 KSLKHCVSAGEPITPDVTEKWRNKTG---LDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKIVDVNG 414
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 415 NVLppgqEGDI-GIQVLPNRPFGLFAHYADDPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 490
Cdd:PLN02654 473 KEI----EGECsGYLCVKKSWPGAFRTLYGDHERYETTYFKPFagyYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGT 548
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 491 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP--DYKSHDQEQLIKEIQEHVKKTTAPYK 554
Cdd:PLN02654 549 AEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDK 614
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
295-559 |
1.81e-36 |
|
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: 138.97 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACVFahhLPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGE---PITPDVTEkWRNKTGl 370
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndMATVDTSP-WGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 371 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTA 449
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 450 STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270
....*....|....*....|....*....|
gi 967501916 530 yKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 559
Cdd:cd17636 292 -ASVTEAELI----EHCRARIASYKKPKSV 316
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-548 |
3.12e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 143.32 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWINGkGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:COG1022 21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 LTQKDILYRLQSSKANCIIT-NDVLAPAVDAIAPKCENLhsKLIVSENSREGWG-----NLKEMMKCASDSHT------- 220
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 221 CVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWaksawsSVFSpWIQ 294
Cdd:COG1022 177 RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACV--------FAHHLPRFEPT--------------SVLQTLSKYPIT---VFCSAATV------YRMLVQNDMASYKF 343
Cdd:COG1022 249 GATVafaespdtLAEDLREVKPTfmlavprvwekvyaGIQAKAEEAGGLkrkLFRWALAVgrryarARLAGKSPSLLLRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 344 K------------------SLKHCVSAGEPITPDVTEKWRNkTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMGKPSPA 404
Cdd:COG1022 329 KhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLPG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 405 FDVKIvdvngnvlppGQEGDI---GIQVlpnrpfglFAHYADDPSKTASTLR--GNFYiTGDRGYMDEDGYFWFVARSDD 479
Cdd:COG1022 407 VEVKI----------AEDGEIlvrGPNV--------MKGYYKNPEATAEAFDadGWLH-TGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 480 II-LSSGYRIGPFEVENALNEHPSVAESAVVsspdpirGE----VVkAFIVLNPD------------YKSHDQ----EQL 538
Cdd:COG1022 468 LIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEalgewaeenglpYTSYAElaqdPEV 539
|
570
....*....|
gi 967501916 539 IKEIQEHVKK 548
Cdd:COG1022 540 RALIQEEVDR 549
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-556 |
8.23e-35 |
|
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: 137.79 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFWWingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 152 TQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPkcenlhskliVSENSREGWGNlkemmkcASDSHTCVKTKHNEIMA 231
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGD----------VALLGDEALAA-------PPATPPLVPPRPDNLAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSFglglsVNGRFWL----DLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRF 306
Cdd:cd17646 143 VIYTSGSTGRPKGVMVTHAGI-----VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 307 EPTSVLQTLSKYPITV--FcsaatVYRMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET- 381
Cdd:cd17646 217 DPAYLAALIREHGVTTchF-----VPSMLRVflAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAa 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 382 --VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV---LPNRPfGLFA-HYADDPSKTASTL 452
Cdd:cd17646 292 idVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELylgGVQLargYLGRP-ALTAeRFVPDPFGPGSRM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 rgnfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKS 532
Cdd:cd17646 371 ----YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG 446
|
490 500
....*....|....*....|....
gi 967501916 533 HDQEQLikeiQEHVKKTTAPYKYP 556
Cdd:cd17646 447 PDTAAL----RAHLAERLPEYMVP 466
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
90-548 |
3.52e-34 |
|
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: 135.03 E-value: 3.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 ciitndvlapavdaiapkcenlhsKLIVSENSregwgnlkemmkcasdSHTCVktkhneIMamfFTSGTSGYPKMTAHTH 249
Cdd:cd05907 79 ------------------------KALFVEDP----------------DDLAT------II---YTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSFglglsvngrfwldltpsdvMWN--TSDTGWAKSA--WSSVFSP--------WIQGACVFAHHLPRFEP--TSVLQTL 315
Cdd:cd05907 110 RNI-------------------LSNalALAERLPATEgdRHLSFLPlahvferrAGLYVPLLAGARIYFASsaETLLDDL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 316 SKYPITVFCSAATVYRML----VQNDMASYK--------FKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV- 382
Cdd:cd05907 171 SEVRPTVFLAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSa 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 383 LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlppgqEgdigIQVlpnRPFGLFAHYADDPSKTA-STLRGNFYITGD 461
Cdd:cd05907 250 VVTLNPPG-DNRIGTVGKPLPGVEVRIADDG--------E----ILV---RGPNVMLGYYKNPEATAeALDADGWLHTGD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 462 RGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPirgeVVKAFIVLNPDY-----KSHD- 534
Cdd:cd05907 314 LGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaEEHGi 389
|
490 500
....*....|....*....|....
gi 967501916 535 ----------QEQLIKEIQEHVKK 548
Cdd:cd05907 390 aytdvaelaaNPAVRAEIEAAVEA 413
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
93-559 |
3.72e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.88 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 93 VRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 173 TNDVLAPAVDAIAPKCENLH---SKLIVSENSREGW------GNLKEMMKC----------------ASDSHTCVKTKHN 227
Cdd:PRK12492 128 YLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqavpfkqalrqgRGLSLKPVPVGLD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPKMTAHTHSSfglgLSVN--------GRFWLDLTPsdVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGN----LVANmlqvraclSQLGPDGQP--LMKEGQEVMIAPLPLYHIYAFTANCMCMM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 A---HHL----PRFEPtSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD 371
Cdd:PRK12492 282 VsgnHNVlitnPRDIP-GFIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 372 IYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSK 447
Cdd:PRK12492 361 IVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELcikGPQVMKG--------YWQQPEA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 448 TASTLRGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVl 526
Cdd:PRK12492 433 TAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV- 511
|
490 500 510
....*....|....*....|....*....|...
gi 967501916 527 npdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK12492 512 -----ARDPGLSVEELKAYCKENFTGYKVPKHI 539
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
228-562 |
4.90e-34 |
|
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: 132.24 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPK--MTAHTHSsfgLGLSVNgrfWldltpSDVMWNTSDTGWA-----------KSAWSSVFspwIQ 294
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACVFAHHLprFEPTSVLQTLSKYPITVFCSAATVYR-MLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-I 372
Cdd:cd17638 67 GATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 373 YEGYGQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDvNGNVLPPGqegdigiqvlPNRPFGlfahYADDPSKTAS 450
Cdd:cd17638 145 LTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRG----------YNVMQG----YLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 451 TLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd17638 210 AIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350
....*....|....*....|....*....|...
gi 967501916 530 yKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 562
Cdd:cd17638 290 -VTLTEEDVIAWCRERL----ANYKVPRFVRFL 317
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
221-570 |
2.37e-33 |
|
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: 133.61 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 221 CVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 AHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQNdMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 379
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 380 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNV-LPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGNFY 457
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRG-PN----VMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 458 ITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PFE-VENALNEH-PSVAESAVVSSPDPIRGEVVKAFivlnpdYK 531
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------TT 440
|
330 340 350
....*....|....*....|....*....|....*....
gi 967501916 532 SHDQEQLikEIQEHVKKTTAPykyprkvGILIITNICSV 570
Cdd:cd05909 441 TTDTDPS--SLNDILKNAGIS-------NLAKPSYIHQV 470
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-562 |
3.07e-33 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 135.16 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNdvlAPAVDAIAPKcENLHSKLI 196
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS---DALRDRFQPS-RVAEAAEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 197 VSENSREGWGNLKEMMKCASDSHTcvktkhneimamfFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:PRK06060 128 MSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 277 DT----GWAKSAW-------SSVFSPWIQGACVFAHHLPRFEPtSVLQTLSKYPITVF--CSAATvyrmlvqndmasykF 343
Cdd:PRK06060 195 RMyfayGLGNSVWfplatggSAVINSAPVTPEAAAILSARFGP-SVLYGVPNFFARVIdsCSPDS--------------F 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 344 KSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKIVDVNGNVLPP 419
Cdd:PRK06060 260 RSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 420 GQEGDIGI------QVLPNRPFGLFAHyaddpsktastlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 493
Cdd:PRK06060 337 GVEGDLWVrgpaiaKGYWNRPDSPVAN-------------EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREV 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 494 ENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK06060 404 ERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVV 470
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
90-529 |
2.47e-32 |
|
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: 130.54 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLAPAVDAIAPkcenlhsklIVSENSREGWGNlkemmkCASDSHTCVKTKHNEIMAMFfTSGTSGYPKMTAHTH 249
Cdd:cd17651 95 LVLTHPALAGELAVELV---------AVTLLDQPGAAA------GADAEPDPALDADDLAYVIY-TSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfahHLP----RFEPTSVLQTLSKYPIT 321
Cdd:cd17651 159 RSL-----ANLVAWQArassLGPGARTLQFAGLGFDVSVQE-IFSTLCAGATL---VLPpeevRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 322 -VFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEP--ITPDVTEKWRNKTGLDIYEGYGQTE----TVLICGNFKGMKIK 394
Cdd:cd17651 230 rVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 395 PGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPfGLFAH-YADDPSKTASTLrgnfYITGDRGYMDE 467
Cdd:cd17651 310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELyigGAGLARgylNRP-ELTAErFVPDPFVPGARM----YRTGDLARWLP 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967501916 468 DGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE 446
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
94-559 |
8.93e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 128.77 E-value: 8.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILsEACSLQRGDRvILILPRVPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PRK09088 22 RWTYAELDALVGRLAAVL-RRRGCVDGER-LAVLARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 173 TNDVLApavdAIAPKCENLhsklivsensregwgnlkEMMKCASDSHTCVKTKH---NEIMAMFFTSGTSGYPK--MTA- 246
Cdd:PRK09088 100 GDDAVA----AGRTDVEDL------------------AAFIASADALEPADTPSippERVSLILFTSGTSGQPKgvMLSe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 247 ----HTHSSFGLGLSVNGR--FWLDlTPsdvMWNTsdTGWAksawSSVFSPWIQGACVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK09088 158 rnlqQTAHNFGVLGRVDAHssFLCD-AP---MFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TV---FCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTE--TVLicgnfkGMKI-- 393
Cdd:PRK09088 226 GIthyFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEagTVF------GMSVdc 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 394 -----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLRGN-FYITGDRGYMDE 467
Cdd:PRK09088 299 dviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG-PN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 468 DGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLIKEIQEHVK 547
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD-----GAPLDLERIRSHLS 448
|
490
....*....|..
gi 967501916 548 KTTAPYKYPRKV 559
Cdd:PRK09088 449 TRLAKYKVPKHL 460
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-559 |
1.56e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 128.94 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 175 DvlapavdAIAPKCENLHSKLIV-SENSREGWGNLKEMMKCA---SDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTH- 249
Cdd:PLN02330 135 D-------TNYGKVKGLGLPVIVlGEEKIEGAVNWKELLEAAdraGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHr 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 --------SSFGLGLSVNGRF-WLDLTPSDVMWNTsdTGWAKSAWSSvfspwiQGACVFahhLPRFEPTSVLQTLSKYPI 320
Cdd:PLN02330 208 nlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYGI--TGICCATLRN------KGKVVV---MSRFELRTFLNALITQEV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TVFCSAATVYRMLVQN------DMASYKFKSLkhcVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTETVLICGNF----K 389
Cdd:PLN02330 277 SFAPIVPPIILNLVKNpiveefDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 390 GMKI-KPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRGYMD 466
Cdd:PLN02330 354 GHGIaKKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYID 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 467 EDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHV 546
Cdd:PLN02330 429 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE-----DILNFV 503
|
490
....*....|...
gi 967501916 547 KKTTAPYKYPRKV 559
Cdd:PLN02330 504 AANVAHYKKVRVV 516
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
91-556 |
2.05e-31 |
|
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: 127.70 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPKCenlhskLIVSENSREGWGNLKEmmKCASDSHTCVktkhneimamFFTSGTSGYPKMTAHTHS 250
Cdd:cd12117 98 LLTDRSLAGRAGGLEVAV------VIDEALDAGPAGNPAV--PVSPDDLAYV----------MYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFgLGLsVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAATV 329
Cdd:cd12117 160 GV-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGArLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 330 YRMLVQNDMASykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKPSPA 404
Cdd:cd12117 237 FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPIAN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 405 FDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTASTLrgnfYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd12117 315 TRVYVLDEDGRPVPPGVPGELyvgGDGLALgylNRPALTAERFVADPFGPGERL----YRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 479 DIILSSGYRIGPFEVENALNEHPSVAESAV-VSSPDPIRGEVVkAFIVLNPDyKSHDqeqlikEIQEHVKKTTAPYKYP 556
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAYMVP 461
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
92-557 |
6.39e-31 |
|
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: 126.87 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLAPAVDAIAPKceNLHSKLIVSENSREGWGNLKEMMK----------CASDSHTCVKTKHNEIMAMFFTSGTSGY 241
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTfitqnlppgfNEYDFKPPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 242 PKMTAHTHssfglgLSVNGRFWLDLTPSDVMWNTSDTgwaksAWSSVFsPWIQG---------ACVFAH--HLPRFEPTS 310
Cdd:cd17642 199 PKGVQLTH------KNIVARFSHARDPIFGNQIIPDT-----AILTVI-PFHHGfgmfttlgyLICGFRvvLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 311 VLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-IYEGYGQTET---VLIC 385
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaILIT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 GNfkgMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRG 463
Cdd:cd17642 347 PE---GDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykSHDQEQLIKEIQ 543
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKEVM 493
|
490
....*....|....
gi 967501916 544 EHVKKTTAPYKYPR 557
Cdd:cd17642 494 DYVASQVSTAKRLR 507
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-559 |
1.05e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 126.15 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 58 FNFAkDVLDqwtnmEKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:PRK07798 3 WNIA-DLFE-----AVADAVPDRVALVC----GDR-RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 138 VACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPKCENLHSKLIV---SENSREGWGNLKEMMKC 214
Cdd:PRK07798 71 LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgSGNDLLPGAVDYEDALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 215 ASDSHTCVKTKHNEIMAMFFTSGTSGYPK--MTAHT---HSSFGLGLSVNGRF------------------WLDLTPsdV 271
Cdd:PRK07798 151 AGSPERDFGERSPDDLYLLYTGGTTGMPKgvMWRQEdifRVLLGGRDFATGEPiedeeelakraaagpgmrRFPAPP--L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 272 MWNTSDtgWAksAWSSVFSpwiqGACVFAHHLPRFEPTSVLQTLSKYPITV-FCSAATVYRMLVQ--NDMASYKFKSLKH 348
Cdd:PRK07798 229 MHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDADEVWRTIEREKVNViTIVGDAMARPLLDalEARGPYDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 349 CVSAGEPITPDVTEKWR----NKTGLDiyeGYGQTETvlicgNFKGMKI-KPGSMGKPSPAF----DVKIVDVNGNVLPP 419
Cdd:PRK07798 301 IASGGALFSPSVKEALLellpNVVLTD---SIGSSET-----GFGGSGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 420 GqEGDIG-IQVLPNRPFGlfahYADDPSKTASTLR---GNFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:PRK07798 373 G-SGEIGwIARRGHIPLG----YYKDPEKTAETFPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07798 448 EALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAI 507
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
228-567 |
1.08e-30 |
|
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: 122.75 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFE 307
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAG--EPITPDVTEKWRNKTgLDIYEGYGQTET-VLI 384
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVRFIEATGL-TNTAQVYGLSETgTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnrPFGLFAHYaDDPSKTASTLRGNFYITGDRGY 464
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS----PANMLGYW-NNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdykSHDQEQLIKEIQE 544
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRALKH 309
|
330 340
....*....|....*....|...
gi 967501916 545 HVKKTTAPYKYPRKvgILIITNI 567
Cdd:cd17635 310 TIRRELEPYARPST--IVIVTDI 330
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
93-559 |
2.81e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 122.23 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 93 VRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANC 170
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSgcKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 II----TNDVLApAVDAIAPKCE-----NLHSK--------LIVSENSREGWGNLKEMMKCASDSHtcvKTKHNEIMA-- 231
Cdd:PRK08315 121 AAdgfkDSDYVA-MLYELAPELAtcepgQLQSArlpelrrvIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 -------MFFTSGTSGYPKMTAHTHSSFGLglsvNGRF---WLDLTPSD--------------VMWN----TSdtgwaks 283
Cdd:PRK08315 197 dpddpinIQYTSGTTGFPKGATLTHRNILN----NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNlacvTH------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 284 awssvfspwiqGAC-VFAhhLPRFEPTSVLQTLSK------Y--PiTVFCSaatvyrMLVQNDMASYKFKSLKHCVSAGE 354
Cdd:PRK08315 266 -----------GATmVYP--GEGFDPLATLAAVEEerctalYgvP-TMFIA------ELDHPDFARFDLSSLRTGIMAGS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 355 PITPDVTEKWRNKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFDVKIVD-VNGNVL 417
Cdd:PRK08315 326 PCPIEVMKRVIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 418 PPGQEGDigiqvLPNRPFGLFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENA 496
Cdd:PRK08315 394 PRGEQGE-----LCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEF 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967501916 497 LNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08315 469 LYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYI 526
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
91-559 |
3.52e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 121.98 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNLK-----EMMKCASDSHTCVKTKHNE--IMAMFFTSGTSGYPK 243
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIgaldyEAFLASGDPDFAWTLPADEwdAIALNYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 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 967501916 312 LQTLSKYPITVFCSAATVYRMLVqNDMASYKfKSLKHCVS---AGEPITPDVTEKWRNkTGLDIYEGYGQTET---VLIC 385
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAAPPAAVIAKMEE-IGFDLTHVYGLTETygpATVC 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 --------------GNFKGMK------------IKPGSMgKPSPAFDVKI--VDVNGNVLPPGqegdigiqvlpnrpfgl 437
Cdd:PRK08162 340 awqpewdalplderAQLKARQgvryplqegvtvLDPDTM-QPVPADGETIgeIMFRGNIVMKG----------------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 438 fahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:PRK08162 402 ---YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 967501916 518 EVVKAFIVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08162 479 EVPCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAV 515
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
90-565 |
1.01e-28 |
|
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: 119.47 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 ciitndvlapavdaiapkcenlhSKLIVSENsregwgnlkemmkcasdshtcvktkhNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:cd05914 81 -----------------------KAIFVSDE--------------------------DDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSfgLGLSVNGRFWLD-LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfaHHLPRFePTSVLQTLSKYPITVFCSAAT 328
Cdd:cd05914 112 RN--IVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRM--------LVQNDMASYKFK------------------------SLKHCVSAGEPITPDVTEKWRnKTGLDIYEGY 376
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlPPGQEGDIgiQVlpnRPFGLFAHYADDPSKTAS--TLR 453
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEI--IV---RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYiTGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVVsspdpIRGEVVKAFIVLNPDY-- 530
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510
....*....|....*....|....*....|....*....
gi 967501916 531 -KSHDQEQLIKEIQEHVKK---TTAPyKYPRKVGILIIT 565
Cdd:cd05914 410 vKALKQRNIIDAIKWEVRDkvnQKVP-NYKKISKVKIVK 447
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
306-535 |
1.94e-28 |
|
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: 119.15 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVli 384
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALAAAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 385 cgNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNV---LPPGQEGDIGIQVLPNRPFglfAHYADDPSKTASTLRGNFYITG 460
Cdd:cd05923 306 --NSLYMRdARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTG 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 461 DRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 535
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
96-559 |
5.45e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.41 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLipgttqlTQKDILYRLQSSKANCIITND 175
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIV-------TTMNPSSSLGEIKKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLAPAVDAIAPKCENLHSKLI-VSEN-----SREGWGNLKEMMKcaSDSHTCVK--TKHNEIMAMFFTSGTSGYPKMTAH 247
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIgVPENydfdsKRIEFPKFYELIK--EDFDFVPKpvIKQDDVAAIMYSSGTTGASKGVVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 248 THSSFGLGLSVNGRFwldltpsdvmwntSDTGWAKSAWSSVFSP-----WIQGACVFAHHL----------PRFEPTSVL 312
Cdd:PLN02574 219 THRNLIAMVELFVRF-------------EASQYEYPGSDNVYLAalpmfHIYGLSLFVVGLlslgstivvmRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 313 QTLSKYPITVFCSAATVYRMLVQN--DMASYKFKSLKHCVSAGEPITPDVTEKW-RNKTGLDIYEGYGQTETVLICG--- 386
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTESTAVGTrgf 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMKiKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQvlpnRPfGLFAHYADDPSKTASTLRGNFYI-TGDRGY 464
Cdd:PLN02574 366 NTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKATQSTIDKDGWLrTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 465 MDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLIkeiqE 544
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG-STLSQEAVI----N 514
|
490
....*....|....*
gi 967501916 545 HVKKTTAPYKYPRKV 559
Cdd:PLN02574 515 YVAKQVAPYKKVRKV 529
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
87-570 |
5.79e-28 |
|
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: 117.95 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 87 NGKGEEVRWSfeELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 167 KANCIIT-----NDVLAPAVDAIAPKCE-NLHSKLivseNSREGWGNLkemMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:cd05932 78 ESKALFVgklddWKAMAPGVPEGLISISlPPPSAA----NCQYQWDDL---IAQHPPLEERPTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 241 YPKMTAHTHSSFGLGLSvNGRFWLDLTPSDVMWntSDTGWAKSAWSS-VFSPWIQGACV--FAHHLPRFeptsvLQTLSK 317
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQ-AGIEHIGTEENDRML--SYLPLAHVTERVfVEGGSLYGGVLvaFAESLDTF-----VEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 318 YPITVFCSAA---TVYRMLVQNDMASYKFKSL----------KHCVSAG-------------EPITPDVTEkWRNKTGLD 371
Cdd:cd05932 223 ARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPPALLE-WYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 372 IYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIvdvngnvlppGQEGDIGIqvlpnRPFGLFAHYADDPSKTAST 451
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALMMGYYKDPEATAEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 452 LRGN-FYITGDRGYMDEDGYFWFVARSDDIILSS-GYRIGPFEVENALNEHPSVAESAVVSS--PDPIRGEVVKAFIVLN 527
Cdd:cd05932 367 FTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLR 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 967501916 528 PDykSHDQEQLIKEIQEHVKKTTAPY-KYPRKVGILIITNICSV 570
Cdd:cd05932 447 AD--AFARAELEASLRAHLARVNSTLdSHEQLAGIVVVKDPWSI 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
232-557 |
1.64e-27 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 113.19 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHT-----HSSFG----LGLSVNGRfWLDLTPS------DVMWNtsdtgWAKSAWSSVFSPWIQGA 296
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDS-WLLSLPLyhvgglAILVR-----SLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 297 cvfahhlprfeptsvLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGY 376
Cdd:cd17630 79 ---------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTETV-LICGNFKGMKiKPGSMGKPSPAFDVKIVDvngnvlppgqEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN 455
Cdd:cd17630 143 GMTETAsQVATKRPDGF-GRGGVGVLLPGRELRIVE----------DGEIWV-----GGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 456 FYiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPdykSHDQ 535
Cdd:cd17630 207 FT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADP 282
|
330 340
....*....|....*....|..
gi 967501916 536 EQLIkeiqEHVKKTTAPYKYPR 557
Cdd:cd17630 283 AELR----AWLKDKLARFKLPK 300
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
90-528 |
2.92e-27 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 115.50 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLAPaVDaiapkcenlHSKLivsenSREgwgnlkemmkcasdshtcVKTKHNEImAMFFTS-GTSGYPKMTAHT 248
Cdd:cd05920 115 AYIVPDRHAG-FD---------HRAL-----ARE------------------LAESIPEV-ALFLLSgGTTGTPKLIPRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSSFGLGLSvngrfwldlTPSDVMWNTSDT----------GWAKSAWSSVFSPWIQGACVFAhhlPRFEPTSVLQTLSKY 318
Cdd:cd05920 161 HNDYAYNVR---------ASAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLIERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 319 PITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLicgNFKGM----KI 393
Cdd:cd05920 229 GVTVTALVPALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddpdEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 394 KPGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiQVLPNRPFGLFAHY-ADDPSKTASTLRGnFYITGDRGYMDEDGYF 471
Cdd:cd05920 306 IIHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPYTIRGYYrAPEHNARAFTPDG-FYRTGDLVRRTPDGYL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 967501916 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNP 528
Cdd:cd05920 381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD 437
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-556 |
3.92e-27 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 114.39 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 217 DS-HTCVKTKHNEIMA-MFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQ 294
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GACVFAHHLPRFEPTSVLQTL-SKYPITVFCSAATVYRMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTEKWRnKTGLD 371
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 372 IYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPfGLFAH 440
Cdd:cd17649 239 LFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-ELTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 441 -YADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 519
Cdd:cd17649 318 rFVPDPFGAPG---SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
330 340 350
....*....|....*....|....*....|....*..
gi 967501916 520 VkAFIVLNPDYKshdQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17649 395 V-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVP 427
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
90-558 |
6.08e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.49 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRwSFEELGSLSRKFANILSEACSLQRgdRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK07638 23 NDRVL-TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLApavdaiapkcenlhSKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:PRK07638 100 MIVTERYKL--------------NDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSfglglsvngrfWL---DLTPSDV-MWNTSDTGWAKSAWSSVF-----SPWIQGACVfaHHLPRFEPTSVLQTLSKYPI 320
Cdd:PRK07638 166 QS-----------WLhsfDCNVHDFhMKREDSVLIAGTLVHSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TVFCSAATVYRMLVQNDmaSYKFKSLKhCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE----TVLICGNFKgmkIKP 395
Cdd:PRK07638 233 SVMYTVPTMLESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 396 GSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPFgLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 475
Cdd:PRK07638 307 NSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV----KSPQ-FFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIvlnpdykshDQEQLIKEIQEHVKKTTAPYKY 555
Cdd:PRK07638 382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKI 452
|
...
gi 967501916 556 PRK 558
Cdd:PRK07638 453 PKE 455
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
232-559 |
1.84e-26 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 110.19 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSfglglsvngrfWLDLTPSDVMwntsdtGWAKSAWSSVFSPwiqGACVFAHHL-------- 303
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------WIESFVCNED------LFNISGEDAILAP---GPLSHSLFLygaisaly 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 304 --------PRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLkhcVSAGEPITPDVTEKWRNKT-GLDIYE 374
Cdd:cd17633 65 lggtfigqRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqegdIG-IQVLPNRpfgLFAHYADDPSKTAstlr 453
Cdd:cd17633 142 FYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKSEM---VFSGYVRGGFSNP---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyKSH 533
Cdd:cd17633 207 DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLT 283
|
330 340
....*....|....*....|....*.
gi 967501916 534 DQEQLIKeiqehVKKTTAPYKYPRKV 559
Cdd:cd17633 284 YKQLKRF-----LKQKLSRYEIPKKI 304
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
91-529 |
2.34e-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: 114.95 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPKCENLHSKLIVSENSregwGNLKEMmkcASDSHTCVktkhneIMamfFTSGTSGYPKMTAHTHS 250
Cdd:COG1020 577 VLTQSALAARLPELGVPVLALDALALAAEPA----TNPPVP---VTPDDLAY------VI---YTSGSTGRPKGVMVEHR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFG-LGLSVNGRFwlDLTPSDVM-WNTS---DTgwakSAWSsVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYPITVFC 324
Cdd:COG1020 641 ALVnLLAWMQRRY--GLGPGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 325 SAATVYRMLVQNDMASykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM--G 399
Cdd:COG1020 714 LTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSVpiG 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 400 KPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglfAH-YADDPSKTA--------STLRGNFYITGDRGYMDE 467
Cdd:COG1020 792 RPIANTRVYVLDAHLQPVPVGVPGELyigGAGL---------ARgYLNRPELTAerfvadpfGFPGARLYRTGDLARWLP 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 468 DGYFWFVARSDD---IilsSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:COG1020 863 DGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
80-529 |
5.94e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.08 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 80 NPAFWWingkgEEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP-GTTQL---T 155
Cdd:PRK07867 19 DRGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGlNPTRRgaaL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 156 QKDILyrlqssKANC--IITNDVLAPAVDAIAPKCEnlhsklIVSENSREgWGNlkEMMKCASDSHTCVKTKHNEIMAMF 233
Cdd:PRK07867 94 ARDIA------HADCqlVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSF-GLGLSVNGRFwlDLTPSDVMWntsdtgwaksawssVFSPWIQGACVFAHHLP-------- 304
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasi 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 305 ----RFEPTSVLQTLSKYPITvfcsaatvYrmlvqndmASYKFKSLKHCVSA---------------GEPITPDVTEKWR 365
Cdd:PRK07867 223 alrrKFSASGFLPDVRRYGAT--------Y--------ANYVGKPLSYVLATperpddadnplrivyGNEGAPGDIARFA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 366 NKTGLDIYEGYGQTETvlicgnfkGMKIK------PGSMGKPSPafDVKIVDVN-GNVLPPGQEGD---------IGIQV 429
Cdd:PRK07867 287 RRFGCVVVDGFGSTEG--------GVAITrtpdtpPGALGPLPP--GVAIVDPDtGTECPPAEDADgrllnadeaIGELV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 430 LPNRPfGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK07867 357 NTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVY 435
|
490 500
....*....|....*....|
gi 967501916 510 SSPDPIRGEVVKAFIVLNPD 529
Cdd:PRK07867 436 AVPDPVVGDQVMAALVLAPG 455
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
74-556 |
7.12e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 111.90 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAFWWINgkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK05852 26 ATRLPEAPALVVTA---DRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 154 LTQKDILYRLQSSKANCIITnDVLAPAvDAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVKT----KHNEI 229
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLI-DADGPH-DRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 230 MAMFfTSGTSGYPKMTAHTHSSfgLGLSVNGRFW-LDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiqGACVFAHHLP 304
Cdd:PRK05852 180 MIMF-TGGTTGLPKMVPWTHAN--IASSVRAIITgYRLSPRDatvaVMPLYHGHGLIAALLATLAS----GGAVLLPARG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 305 RFEPTSVLQTLSKYPITVFCSAATVYRMLVQ---NDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 382 --------VLICGNFKGMKIKPGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLR 453
Cdd:PRK05852 333 thqvtttqIEGIGQTENPVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnPDYKSH 533
Cdd:PRK05852 407 DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAP 484
|
490 500
....*....|....*....|...
gi 967501916 534 DQEQlikEIQEHVKKTTAPYKYP 556
Cdd:PRK05852 485 PTAE---ELVQFCRERLAAFEIP 504
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
91-545 |
9.13e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 110.84 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNDVLAPAVDAIAPkcenlhSKLIVSENSREGWGNLKEMMKCASDSHtcvktkhneimaMFFTSGTSGYPKMTAHTHS 250
Cdd:cd12116 88 VLTDDALPDRLPAGLP------VLLLALAAAAAAPAAPRTPVSPDDLAY------------VIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SF-GLGLSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd12116 150 NLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQNDmasykFKSLKH----CvsAGEPITPDVTEKWRNKTGlDIYEGYGQTETVL------ICGNFKGMKIkpgsm 398
Cdd:cd12116 227 TWRMLLDAG-----WQGRAGltalC--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTAstlRGNFYITGDRGYMDEDGYFW 472
Cdd:cd12116 294 GRPLANTQVYVLDAALRPVPPGVPGELyigGDGVAQgylGRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADGRLE 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967501916 473 FVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFIVLnPDYKSHDQEQLIKEIQEH 545
Cdd:cd12116 371 YLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
72-556 |
9.59e-26 |
|
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: 110.88 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPA--FwwingkgEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP 149
Cdd:cd17655 5 EQAEKTPDHTAvvF-------EDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDaiapkcenlHSKLIVSENSREGWGNLKEMMKCASDShtcvktkhNEI 229
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIA---------FIGLIDLLDEDTIYHEESENLEPVSKS--------DDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 230 MAMFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF-AHHLP 304
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGV-----VNLVEWANkviyQGEHLRVALFASISFDASVTE-IFASLLSGNTLYiVRKET 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 305 RFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASykFKSLKHCVSAGEPITPDVTEKW--RNKTGLDIYEGYGQTETV 382
Cdd:cd17655 214 VLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 383 LIC--GNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFAHYADDPSKTAstl 452
Cdd:cd17655 292 VDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRPELTAEKFVDDPFVPG--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 rGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKs 532
Cdd:cd17655 369 -ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP- 446
|
490 500
....*....|....*....|....
gi 967501916 533 hdqeqlIKEIQEHVKKTTAPYKYP 556
Cdd:cd17655 447 ------VAQLREFLARELPDYMIP 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-556 |
1.36e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.74 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFwwingKGEEVRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 4559 ERARMTPDAVAV-----VFDEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaiaPKCENLHSKLIVSENSREGWgnlkemmkcaSDSHTCVKTKHN 227
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL----PIPDGLASLALDRDEDWEGF----------PAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFE 307
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMK-IKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFAHYADDPSKTASTL------- 452
Cdd:PRK12316 4853 LWKARDgDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGElyLGGE-------GVARGYLERPALTAERFvpdpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 -RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYK 531
Cdd:PRK12316 4926 pGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALA 5005
|
490 500
....*....|....*....|....*..
gi 967501916 532 SHDQEQ--LIKEIQEHVKKTTAPYKYP 556
Cdd:PRK12316 5006 DADEAQaeLRDELKAALRERLPEYMVP 5032
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
93-559 |
2.33e-25 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 110.32 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 93 VRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 173 TNDVLAP----AVDAIAPKCENLHSK--LIVSENSREGWGNLKEMM-KCASDSHTCVKTKHNEI-----------MAMFF 234
Cdd:PLN02479 123 VDQEFFTlaeeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALgKGAIEYEKFLETGDPEFawkppadewqsIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 235 TSGTSGYPKmtahthssfGLGLSVNGRFWLDLTpSDVMWNTSD-------------TGWAKSaWSsvfspwIQGACVFAH 301
Cdd:PLN02479 203 TSGTTASPK---------GVVLHHRGAYLMALS-NALIWGMNEgavylwtlpmfhcNGWCFT-WT------LAALCGTNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 302 HLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVqNDMASYKFKSLKHCV---SAGEPITPDVTEKWrNKTGLDIYEGYGQ 378
Cdd:PLN02479 266 CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAM-SEKGFRVTHTYGL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 379 TETVlicgnfkgmkiKPGSMGKPSPAFD-----------------------VKIVDVNGNVLPPGQEGDIGIQVLpnRPF 435
Cdd:PLN02479 344 SETY-----------GPSTVCAWKPEWDslppeeqarlnarqgvryiglegLDVVDTKTMKPVPADGKTMGEIVM--RGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 436 GLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PLN02479 411 MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 967501916 516 RGEVVKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PLN02479 491 WGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSV 534
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
90-546 |
2.65e-25 |
|
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: 108.94 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDvlapAVDAIApkcenlhskLIVsensregwgnlkemmkcasdshtcvktkhneimamfFTSGTSGYPKMTAHTH 249
Cdd:cd17653 97 LLLTTD----SPDDLA---------YII------------------------------------FTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRFepTSVLQTLSKYPITvfcsaAT 328
Cdd:cd17653 128 RGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGGTlVLADPSDPF--AHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQNDmasykFKSLKHCVSAGEPITPDVTEKWRNktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVK 408
Cdd:cd17653 199 ILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 409 IVDVNGNVLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSD 478
Cdd:cd17653 272 ILDADLQPVPEGVVGEIcisGVQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 479 DIILSSGYRIGPFEVENALNEHPSVAESAVVSSpdpIRGEVVkAFIVlnPDykSHDQEQLIKEIQEHV 546
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL 403
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
232-567 |
3.98e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 110.22 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKsawssvFSPWIQGACVFAHHLPRFE---- 307
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 -----PTSVLQTLSKYPITVFCSAATVYRMLVQND------MASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:PTZ00237 333 knkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRP-FGLFAHYADDPSKTASTLRG 454
Cdd:PTZ00237 413 GQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPsFATTFYKNDEKFKQLFSKFP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKSH- 533
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQs 571
|
330 340 350
....*....|....*....|....*....|....*
gi 967501916 534 -DQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 567
Cdd:PTZ00237 572 iDLNKLKNEINNIITQDIESLAVLRK--IIIVNQL 604
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-559 |
6.89e-25 |
|
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: 106.31 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSFGLGLS-----VNGRFWLDLTPSDVMWNTSDTGW--------AKSAWSSVFSPWIQGACV 298
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 299 FahHLPRFEPTSVLQTLSKYPITVFCSAATVY-RMLVQ--NDMASYKFKSLKHCVSAGEPITPDVTEKW-RNKTGLDIYE 374
Cdd:cd05924 88 L--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfahYADDPSKTASTLR 453
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARRGHIPLG----YYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 ---GNFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPD 529
Cdd:cd05924 240 evdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350
....*....|....*....|....*....|
gi 967501916 530 YKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05924 320 AGVDLE-----ELREHCRTRIARYKLPKQV 344
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
96-545 |
2.16e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 107.29 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKANCII 172
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 173 TNDvLAPAVDAIAP-KCENLHSKLIVSenSREGWGN--LKEMMKCASD-SHTCVKTKHNEIMAMFFTSGTSGYPKMTAHT 248
Cdd:PRK09274 119 GIP-KAHLARRLFGwGKPSVRRLVTVG--GRLLWGGttLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGVVYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSSF---------GLGLSVNGRfwlDLTPSDVMwntsdtgwaksawsSVFSPWIQGACVfahhLPRFEPT--------SV 311
Cdd:PRK09274 196 HGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGPALGMTSV----IPDMDPTrpatvdpaKL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 312 LQTLSKYPIT-VFCSAA---TVYRMLVQNDMasyKFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIYEGYGQTETVLIC 385
Cdd:PRK09274 255 FAAIERYGVTnLFGSPAlleRLGRYGEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 gnfkgmKIkpGS------------------MGKPSPAFDVKIVDVNGN---------VLPPGQEGDI---GIQVLP---N 432
Cdd:PRK09274 332 ------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAISDApipewddalRLATGEIGEIvvaGPMVTRsyyN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 433 RPfglfahYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSP 512
Cdd:PRK09274 404 RP------EATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
490 500 510
....*....|....*....|....*....|....
gi 967501916 513 DPirGEVVKAFIV-LNPDyKSHDQEQLIKEIQEH 545
Cdd:PRK09274 478 VP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
289-552 |
2.34e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 289 FSPWIQGACVFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEKWRNK 367
Cdd:PRK08633 843 WLPLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHpLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 368 TGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GIQVLpnr 433
Cdd:PRK08633 922 FGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLIligGPQVM--- 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 434 pfglfAHYADDPSKTASTLR----GNFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PF-EVENALNE--HPS 502
Cdd:PRK08633 999 -----KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalGGE 1068
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 967501916 503 VAESAVVSSPDPIRGEVVkafIVLnpdyksHDQEQL-IKEIQEHVKKTTAP 552
Cdd:PRK08633 1069 EVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLP 1110
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
234-557 |
6.80e-24 |
|
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: 104.70 E-value: 6.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA--CVFAHHLPRfEPTSV 311
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrlVVVPYEVAR-SPEDF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 312 LQTLSKYPITVFCSAATVYRMLVQNDMASYKFK-SLKHCVSAGEPITPDVTEKWRNKTGL---DIYEGYGQTET-VLIcg 386
Cdd:cd17643 177 ARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV-- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMK---IKPGSM---GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPfGLFA-HYADDPsKTASTLR 453
Cdd:cd17643 255 TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELyvsGAGVARgylGRP-ELTAeRFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GnfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdyksH 533
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340
....*....|....*....|....
gi 967501916 534 DQEQLIKEIQEHVKKTTAPYKYPR 557
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPA 429
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
63-556 |
7.13e-24 |
|
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: 105.61 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDQWtnmekAGKKPSNPAFwwINGkgeEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG1021 29 DLLRRR-----AERHPDRIAV--VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGtvLIPGTT--QLTQKDILYRLQSSKANCIITNDV-----LAPAVDAIAPKCENLhsKLIVSENSREGWGNLKEMmkCA 215
Cdd:COG1021 98 AG--AIPVFAlpAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSL--RHVLVVGDAGEFTSLDAL--LA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 216 SDSHTCVKTKHNEIMAMFFTS-GTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMW-------NtsdtgwakSAWSS 287
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVYLaalpaahN--------FPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 288 --VFSPWIQGAC-VFAhhlPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQ-NDMASYKFKSLKHCVSAGEPITPDVTEK 363
Cdd:COG1021 243 pgVLGVLYAGGTvVLA---PDPSPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 364 WRNKTGLDIYEGYG-------QT------ETVLicgnfkgmkikpGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiqV 429
Cdd:COG1021 320 VRPALGCTLQQVFGmaeglvnYTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVG-----E 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 430 LPNRPFGLFAHYADDPSKTAS--TLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARafTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 967501916 508 VVSSPDPIRGEVVKAFIVLNpdykshDQEQLIKEIQEHVK-KTTAPYKYP 556
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVPR------GEPLTLAELRRFLReRGLAAFKLP 505
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
234-557 |
1.65e-23 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 104.50 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSF---GLG-LSVNGrfwldLTPSDVMWNTS---DTGwaksAWSSVFSPWIQGAC-VFahhLPR 305
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALivqSLAkIAIVG-----YGEDDVYLHTAplcHIG----GLSSALAMLMVGAChVL---LPK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 306 FEPTSVLQTLSKYPITVFCSAATVYRMLV---QNDMASYKFKSLKHCVSAGEPIT----PDVTEKWRNKtglDIYEGYGQ 378
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSsrllPDAKKLFPNA---KLFSAYGM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 379 TET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFDVKIvdvngnvlppGQEGDIGIQVLPNRPF 435
Cdd:PLN02860 324 TEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKI----------GLDESSRVGRILTRGP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 436 GLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 514
Cdd:PLN02860 394 HVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 967501916 515 IRGEVVKAFIVLNPDYK-SHDQEQLIK--------EIQEHV-KKTTAPYKYPR 557
Cdd:PLN02860 474 RLTEMVVACVRLRDGWIwSDNEKENAKknltlsseTLRHHCrEKNLSRFKIPK 526
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-559 |
6.97e-23 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 102.79 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 105 RKFANILSeaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP----A 180
Cdd:PLN03102 51 RLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlareV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 181 VDAIAPKCENLHSKLIV------------SENSREGWGNLKEMMKCASDSHTCVKTKHNEImAMFFTSGTSGYPKMTAHT 248
Cdd:PLN03102 129 LHLLSSEDSNLNLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKGVVIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 249 HSSFGL-GLSVNGRFWLDLTPSdVMWNTSD---TGWAKSaWSSVFSpwiQGACVFAHHLPRFEptsVLQTLSKYPITVFC 324
Cdd:PLN03102 208 HRGAYLsTLSAIIGWEMGTCPV-YLWTLPMfhcNGWTFT-WGTAAR---GGTSVCMRHVTAPE---IYKNIEMHNVTHMC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 325 SAATVYRMLVQNDMASYKFKSLK-HCVSAGEPiTPDVTEKWRNKTGLDIYEGYGQTET---VLIC-----------GNFK 389
Cdd:PLN03102 280 CVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlpeNQQM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 390 GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDED 468
Cdd:PLN03102 359 ELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVI-----KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 469 GYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVL--NPDYKSHDQEQLI---KEIQ 543
Cdd:PLN03102 434 GHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLI 513
|
490
....*....|....*.
gi 967501916 544 EHVKKTTAPYKYPRKV 559
Cdd:PLN03102 514 EYCRENLPHFMCPRKV 529
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
90-546 |
8.91e-23 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 102.36 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPR----VPEWWlanvACLRTGTVLIPGTTQLTqkdilYRLQS 165
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----YDEPN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 166 SKAN------------CIITNDVLAPAVDAIAPKCENLHSKLIVSENSREgwgnlkemmkCASDSHTCVKTKhNEIMAMF 233
Cdd:cd05906 105 ARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLD----------TAADHDLPQSRP-DDLALLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSF---GLGLSVNGRFwldlTPSDVMWNtsdtgwaksawssvfspWIQ----GACVFAHHLPRF 306
Cdd:cd05906 174 LTSGSTGFPKAVPLTHRNIlarSAGKIQHNGL----TPQDVFLN-----------------WVPldhvGGLVELHLRAVY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 307 ---------------EPTSVLQTLSKYPITVFCSAATVYRMLVQ----NDMASYKFKSLKHCVSAGEPITPDVTEKWRN- 366
Cdd:cd05906 233 lgcqqvhvpteeilaDPLRWLDLIDRYRVTITWAPNFAFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 367 --KTGLD---IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPnrp 434
Cdd:cd05906 313 lePYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 435 fgLFAHYADDPSKTASTLR-GNFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAES--AVVSS 511
Cdd:cd05906 390 --VTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAV 466
|
490 500 510
....*....|....*....|....*....|....*.
gi 967501916 512 PDPIRGEVVKAfIVLNPDYKSHDQ-EQLIKEIQEHV 546
Cdd:cd05906 467 RDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVV 501
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
346-562 |
1.11e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.00 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 346 LKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGD 424
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 425 I--GIQVLPNRpfglfahYADDPSKtaSTLRGnFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPS 502
Cdd:PRK13383 374 IfvGGELAGTR-------YTDGGGK--AVVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 503 VAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQlikeIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDRVSRFEQPRDINIV 498
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-513 |
2.08e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 101.49 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 63 DVLDQWtnmekAGKKPSNPAFwwingKGEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK08279 41 DVFEEA-----AARHPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 143 TGTV--LIpgTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAIAPkCENLHSKLIV----SENSREGWGNLkemMKCAS 216
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARA-DLARPPRLWVaggdTLDDPEGYEDL---AAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 217 DSHTCVKTKHNEIMA-----MFFTSGTSGYPKMTAHTH-----SSFGLGLSvngrfwLDLTPSDVMWNT----SDTGwAK 282
Cdd:PRK08279 184 GAPTTNPASRSGVTAkdtafYIYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 283 SAWSSVFSPwiqGACV-----FAhhLPRFEPTSVlqtlsKYPITVFCSAATVYRMLV-QNDMASYKFKSLKHCVSAGepI 356
Cdd:PRK08279 257 VAWSSVLAA---GATLalrrkFS--ASRFWDDVR-----RYRATAFQYIGELCRYLLnQPPKPTDRDHRLRLMIGNG--L 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 357 TPDVTEKWRNKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFDVK---IV-----------DVNGNVLP- 418
Cdd:PRK08279 325 RPDIWDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLAHpyaIVkydvdtgepvrDADGRCIKv 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 419 -PGQEGD-IGiQVLPNRPF-GlfahYAdDPSKT-ASTLRGNF------YITGDRGYMDEDGYFWFVARSDDIilssgYR- 487
Cdd:PRK08279 399 kPGEVGLlIG-RITDRGPFdG----YT-DPEASeKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRw 467
|
490 500 510
....*....|....*....|....*....|..
gi 967501916 488 ----IGPFEVENALNEHPSVAESAV--VSSPD 513
Cdd:PRK08279 468 kgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
92-509 |
3.28e-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: 99.74 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKanci 171
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 itndvlapavdaiapkcenlhSKLIVSENSregwgnlkemmkcasdshtcvktkHNEIMAMFFTSGTSGYPKMTAHTHSS 251
Cdd:cd17640 78 ---------------------SVALVVEND------------------------SDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 252 FGLGLSvngRFW--LDLTPSDVMWntsdtgwaksawsSVFSPW-----------IQGACVFAHHLPRFeptsVLQTLSKY 318
Cdd:cd17640 113 LLHQIR---SLSdiVPPQPGDRFL-------------SILPIWhsyersaeyfiFACGCSQAYTSIRT----LKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 319 PITVFCSAATVYRMLVQN------DMASYKFKSLKHCVSAGE---PIT-----PDVTEKWRNKTGLDIYEGYGQTET--V 382
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGiqkqvsKSSPIKQFLFLFFLSGGIfkfGISgggalPPHVDTFFEAIGIEVLNGYGLTETspV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 383 LICGNFKGMKIkpGSMGKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVLPNrpfglfahYADDPSKTASTLRGN-FY 457
Cdd:cd17640 253 VSARRLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVwvrGPQVMKG--------YYKNPEATSKVLDSDgWF 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 967501916 458 ITGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd17640 323 NTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
90-562 |
1.41e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 98.66 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIitndVLAPA---------VDAIAPKC-ENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEIMA-------- 231
Cdd:PRK06164 110 WL----VVWPGfkgidfaaiLAAVPPDAlPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAadpdagal 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFWLDLTPSDVMwntsdtgwaksAWSSVFSPWIQGACVfaHH 302
Cdd:PRK06164 186 LFTTSGTTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 303 LPRFEPTSVLQTLSKYPIT-VFCSAATVYRMLVQNDmASYKFKSLKHC-VSAGEPITPDVTEkWRNKTGLDIYEGYGQTE 380
Cdd:PRK06164 253 EPVFDAARTARALRRHRVThTFGNDEMLRRILDTAG-ERADFPSARLFgFASFAPALGELAA-LARARGVPLTGLYGSSE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 381 --TVLICGNFK---GMKIKPGsmGKP-SPAFDVKIVDV-NGNVLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLR 453
Cdd:PRK06164 331 vqALVALQPATdpvSVRIEGG--GRPaSPEARVRARDPqDGALLPDGESGEIEIRA-PS----LMRGYLDNPDATARALT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpdPIRGEVVKAFIVLNPDYKS 532
Cdd:PRK06164 404 DDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPTDGAS 481
|
490 500 510
....*....|....*....|....*....|
gi 967501916 533 HDQEQLIKeiqeHVKKTTAPYKYPRKVGIL 562
Cdd:PRK06164 482 PDEAGLMA----ACREALAGFKVPARVQVV 507
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-552 |
7.66e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.39 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 NDVLAPAVDAIAPKCENLHSKLIVSENS-REGWGNLKEMMKCAS-----DSHTCV----KTKHNEIMAMFFTSGTSGYPK 243
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 244 MTAHTHSSFGL---------GLSV-NGRFWLDLTPsdvMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHLPRFEPTSVLQ 313
Cdd:PRK05620 198 GVVYSHRSLYLqslslrttdSLAVtHGESFLCCVP---IYHVLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 314 TLSKYPiTVFCSaatvyrMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLIcgnfkGMKI 393
Cdd:PRK05620 275 VAHGVP-TLWIQ------LMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----GTVA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 394 KPG-------------SMGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVLPNRpfgLFAHYADDPSKT----ASTLRGN- 455
Cdd:PRK05620 343 RPPsgvsgearwayrvSQGRFPASLEYRIVN-DGQVMESTDRNEGEIQVRGNW---VTASYYHSPTEEgggaASTFRGEd 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 456 ------------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:PRK05620 419 vedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510
....*....|....*....|....*....|.
gi 967501916 524 IVLNPDYKSHDQ--EQLIKEIQEHVKKTTAP 552
Cdd:PRK05620 499 TVLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
71-567 |
1.15e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 95.85 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 71 MEKAGKKPSNPAFWWINGKGEevrWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 151 TTQLTQKDIlyrlqssKANCIITNdvlaPAVDAIAPKC--------ENLHSKLIVSENSREGWGNlkemMKCASDSH--- 219
Cdd:PRK05857 97 DGNLPIAAI-------ERFCQITD----PAAALVAPGSkmassavpEALHSIPVIAVDIAAVTRE----SEHSLDAAsla 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 220 TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLG---LSVNGRFWLDltpsdvmWNTSDTGWAKSAWSSVFSPW---- 292
Cdd:PRK05857 162 GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVT-------WVVGETTYSPLPATHIGGLWwilt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 293 --IQGA-CVFAHHlprfEPTSVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAG-EPITPDVteKWRNK 367
Cdd:PRK05857 235 clMHGGlCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADV--RFIEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 368 TGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG---NVLPPGQEGDIGIQVLPNrPFGLFA 439
Cdd:PRK05857 309 TGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSASFGTLWIKS-PANMLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 440 hYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 519
Cdd:PRK05857 388 -YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 967501916 520 VKAFIVLNPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 567
Cdd:PRK05857 467 VGLAVVASAELDESAARALKHTIAARFRRESEPMARPST--IVIVTDI 512
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
229-529 |
1.75e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 95.09 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 229 IMAMFFTSGTSGYPKMTAHTHSSFG-LGLSVNGRFwlDLTPSDVMW--------NTSDTGWAKSAwssvfspwIQGACVF 299
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV--------ASGAAVA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 AHhlPRFEPTSVLQTLSKYPITVFcsaATVYRMLvqndmaSYKFKSLKHCVSAGEPIT--------PDVTEKWRNKTGLD 371
Cdd:PRK13388 222 LP--AKFSASGFLDDVRRYGATYF---NYVGKPL------AYILATPERPDDADNPLRvafgneasPRDIAEFSRRFGCQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 372 IYEGYGQTETVLICGNFKGMKikPGSMGKPSPafDVKIVDV-------------NGNVLPPgqegDIGIQVLPNRP-FGL 437
Cdd:PRK13388 291 VEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIYNPetltecavarfdaHGALLNA----DEAIGELVNTAgAGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 438 FAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:PRK13388 363 FEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
330
....*....|..
gi 967501916 518 EVVKAFIVLNPD 529
Cdd:PRK13388 443 DQVMAALVLRDG 454
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
91-556 |
1.99e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.38 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITNdvlaPAVDAIAPKCENLHSkLIVSENSREGWGnlkemmkcASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:PRK12467 613 LLTQ----SHLLAQLPVPAGLRS-LCLDEPADLLCG--------YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLPR---FEPTSVLQTLSKYPITVFCSAA 327
Cdd:PRK12467 680 ALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 328 TVYRMLVQnDMASYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMGKPS 402
Cdd:PRK12467 756 SHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 403 PAFDVKIVDVNGNVLPPGQEGD--IGIQVLPN----RPfGLFAHY-ADDPSKTAStlrGNFYITGDRGYMDEDGYFWFVA 475
Cdd:PRK12467 835 ANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRP-ALTAERfVPDPFGADG---GRLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFIVlnPDYKSHDQEQLIK--EIQEHVKKTTAPY 553
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHQATrdELKAQLRQVLPDY 987
|
...
gi 967501916 554 KYP 556
Cdd:PRK12467 988 MVP 990
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
492-559 |
6.64e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 84.13 E-value: 6.64e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYkshdqEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEV 63
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
96-562 |
1.42e-19 |
|
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: 91.55 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd17652 14 TYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 vlapavdaiapKCENLhsklivsensregwgnlkemmkcasdshtcvktkhneiMAMFFTSGTSGYPKMTAHTHSSFGlG 255
Cdd:cd17652 91 -----------TPDNL--------------------------------------AYVIYTSGSTGRPKGVVVTHRGLA-N 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfahHLPrfePTSVLQ-------TLSKYPITVFCSAAT 328
Cdd:cd17652 121 LAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL---VLA---PAEELLpgepladLLREHRITHVTLPPA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQNDMASykfksLKHCVSAGEPITPDVTEKWrnKTGLDIYEGYGQTETVL---ICGNFKGMKIKPgsMGKPSPAF 405
Cdd:cd17652 194 ALAALPPDDLPD-----LRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVcatMAGPLPGGGVPP--IGRPVPGT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 406 DVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTA--------STLRGNFYITGDRGYMDEDGYFWFV 474
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELyiaGA--------GLARGYLNRPGLTAerfvadpfGAPGSRMYRTGDLARWRADGQLEFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 475 ARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLikeiQEHVKKTTAPYK 554
Cdd:cd17652 337 GRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG-AAPTAAEL----RAHLAERLPGYM 411
|
....*...
gi 967501916 555 YPRKVGIL 562
Cdd:cd17652 412 VPAAFVVL 419
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-528 |
1.84e-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: 92.10 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 175 DvlAPAVDAIAPKCENLHS--KLIVSE-----NSREGW----GNLKEMMKCASDSHTCV------KTKHNEIMAMFFTSG 237
Cdd:cd17641 91 D--EEQVDKLLEIADRIPSvrYVIYCDprgmrKYDDPRlisfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 238 TSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfahHLPRfEPTSVLQTLSK 317
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPE-EPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 318 YPITVFCSAATV------------------------------YRMLVQN---------DMASYK---------------F 343
Cdd:cd17641 244 IGPTFVLLPPRVwegiaadvrarmmdatpfkrfmfelgmklgLRALDRGkrgrpvslwLRLASWladallfrplrdrlgF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 344 KSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVnGNVLPPGQeg 423
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-GEILVRSP-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 424 digiqvlpnrpfGLFAHYADDPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDI-ILSSGYRIGPFEVENALNEHP 501
Cdd:cd17641 400 ------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSP 467
|
490 500
....*....|....*....|....*..
gi 967501916 502 SVAESAVVSSPDPIrgevVKAFIVLNP 528
Cdd:cd17641 468 YIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
92-538 |
3.40e-18 |
|
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: 87.71 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12114 10 DGTLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLAPAVDAIAPKcenlhskLIVSENSREGWgnlKEMMKCASDSHTcvktkhneiMA-MFFTSGTSGYPKMTAHTHS 250
Cdd:cd12114 89 LTDGPDAQLDVAVFDV-------LILDLDALAAP---APPPPVDVAPDD---------LAyVIFTSGSTGTPKGVMISHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 S-FGLGLSVNGRFwlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd12114 150 AaLNTILDINRRF--AVGPDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQNDMASYKFK-SLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 399
Cdd:cd12114 227 LLEMLLDVLEAAQALLpSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 400 KPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTAS-----TLRGNFYITGDRGYMDEDGYF 471
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGELwigGR--------GVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967501916 472 WFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAFIVLNPDYKSHDQEQL 538
Cdd:cd12114 376 EFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDAL 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
96-509 |
4.35e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 88.56 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 176 VLA---PAVDAIAPKCENlhSKLIVSENSREGWGnlkemmkcaSDSHTCVktkhneimaMFFTSGTSGYPKMTAHTHSSF 252
Cdd:PRK10252 564 DQLprfADVPDLTSLCYN--APLAPQGAAPLQLS---------QPHHTAY---------IIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 253 glglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF-----AHHlprfEPTSVLQTLSKYPITV- 322
Cdd:PRK10252 624 -----VNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTt 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 323 ---------FCSAATVyrmlvqnDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMK 392
Cdd:PRK10252 694 hfvpsmlaaFVASLTP-------EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 393 IKPGSMGKPSP-AFDV-----KIVDVNGNVLPPGQEGDI---GIQvlpnrpfgLFAHYADDPSKTASTLRGN-------F 456
Cdd:PRK10252 767 ELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfapgerM 838
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 967501916 457 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK10252 839 YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
74-546 |
6.75e-18 |
|
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: 86.91 E-value: 6.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 74 AGKKPSNPAF-WWINGKGEEVRWSFEELGSLSRKFANILSEACslQRGDRVILILPRVPEWWLANVACLRTGTV---LIP 149
Cdd:cd05931 3 AAARPDRPAYtFLDDEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDA-IAPKCENLHSKLIVSENSREGwgnlkemmkcASDSHTCVKTKHNE 228
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAfAASRPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 229 IMAMFFTSGTSGYPK--MTAHT--HSSFGLGLSVngrfwLDLTPSDVMWNtsdtgwaksaW----------SSVFSPWIQ 294
Cdd:cd05931 151 IAYLQYTSGSTGTPKgvVVTHRnlLANVRQIRRA-----YGLDPGDVVVS----------WlplyhdmgliGGLLTPLYS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 295 GA-CVFAHhlPR-F--EPTSVLQTLSKYPITvfCSAAT--VYRMLVQ----NDMASYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:cd05931 216 GGpSVLMS--PAaFlrRPLRWLRLISRYRAT--ISAAPnfAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 365 RNK---TGLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFDVKIVDV 412
Cdd:cd05931 292 AEAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 413 NGN-VLPPGQEGDIGIQVlPNrpfgLFAHYADDPSKTASTLR-------GNFYITGDRGYMDeDGYFWFVARSDDIILSS 484
Cdd:cd05931 372 ETGrELPDGEVGEIWVRG-PS----VASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVR 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967501916 485 GYRIGPFEVENAL-NEHPSVAES--AVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLIKEIQEHV 546
Cdd:cd05931 446 GRNHYPQDIEATAeEAHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAV 509
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
94-556 |
9.70e-18 |
|
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: 86.07 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 NDvlapavdaiapkcenlhsklivsensregwGNLKEMMkcasdshtcvktkhneimamfFTSGTSGYPKMTAHTHSSFg 253
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 254 lglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfaHHLPRfEPTSVLQTLSKY------PITVF 323
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPS-ERRLDLDALNDYfnqegiTISFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 324 CSAATVYRMLVQNdmasykfKSLKHCVSAGepitpDVTEKWRNKtGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPS 402
Cdd:cd17645 202 PTGAAEQFMQLDN-------QSLRVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 403 PAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVA 475
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLIKEIQEHVKKTTAPYKY 555
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMI 416
|
.
gi 967501916 556 P 556
Cdd:cd17645 417 P 417
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
234-562 |
1.77e-17 |
|
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: 85.06 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSfglglSVNGRFWLDLT-PSD----VMWNTSdTGWAKSAWSsVFSPWIQGACVF----AHHL- 303
Cdd:cd12115 112 YTSGSTGRPKGVAIEHRN-----AAAFLQWAAAAfSAEelagVLASTS-ICFDLSVFE-LFGPLATGGKVVladnVLALp 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 304 --PRFEPTSVLQTLskyPitvfcSAAtvyRMLVQNDMASykfKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQTE 380
Cdd:cd12115 185 dlPAAAEVTLINTV---P-----SAA---AELLRHDALP---ASVRVVNLAGEPLPRDlVQRLYARLQVERVVNLYGPSE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 381 -----TVLICGnfKGMKIKPgSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFAHYADDPSKTASTL 452
Cdd:cd12115 251 dttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELyigGA--------GVARGYLGRPGLTAERF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 RGN-------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIV 525
Cdd:cd12115 320 LPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV 399
|
330 340 350
....*....|....*....|....*....|....*..
gi 967501916 526 LNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd12115 400 AEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRL 431
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
399-562 |
2.40e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 85.43 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVLPNR-PFgLFAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFVA 475
Cdd:PRK10946 356 GRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 476 RSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDYKS-----HDQEQLIkeiqehvkktt 550
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAvqlrrFLREQGI----------- 498
|
170
....*....|..
gi 967501916 551 APYKYPRKVGIL 562
Cdd:PRK10946 499 AEFKLPDRVECV 510
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
208-553 |
2.77e-17 |
|
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: 84.90 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 208 LKEMMKcASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPS-----------DVMWNts 276
Cdd:cd05918 88 LQEILQ-DTGAKVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA-LGLTSEsrvlqfasytfDVSIL-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 277 dtgwaksawsSVFSPWIQGACVFA-------HHLPRFeptsvlqtLSKYPITVFCSAATVYRMLVQNDmasykFKSLKHC 349
Cdd:cd05918 164 ----------EIFTTLAAGGCLCIpseedrlNDLAGF--------INRLRVTWAFLTPSVARLLDPED-----VPSLRTL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 350 VSAGEPITPDVTEKWRNKTGLdiYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFdVKIVDVNGN--VLPPGQEGDI- 425
Cdd:cd05918 221 VLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHdrLVPIGAVGELl 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 426 --GIQVLPnrpfGlfahYADDPSKTA--------------STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 489
Cdd:cd05918 298 ieGPILAR----G----YLNDPEKTAaafiedpawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVE 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVK---AFIVLNPDYKSHDQEQ------------LIKEIQEHVKKTTAPY 553
Cdd:cd05918 370 LGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSY 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-562 |
4.22e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 2011 EQAARAPEAIAVVF----GDQ-HLSYAELDSRANRLAHRL-----RARGvgpeVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLApavdAIAPKCENLHSKLIVSENSREGWgnlkemmkcaSDSHTCVKTKHN 227
Cdd:PRK12316 2081 VPLDPNYPAERLAYMLEDSGAALLLTQRHLL----ERLPLPAGVARLPLDRDAEWADY----------PDTAPAVQLAGE 2146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFE 307
Cdd:PRK12316 2147 NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWD 2224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETVLICG 386
Cdd:PRK12316 2225 PEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPL 2304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMKIKPGS-----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFAHYADDPSKTA--------ST 451
Cdd:PRK12316 2305 LWKCRPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGElyLGGE-------GLARGYLNRPGLTAerfvpdpfSA 2377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 452 LRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFIVlnPDyk 531
Cdd:PRK12316 2378 SGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD-- 2452
|
490 500 510
....*....|....*....|....*....|.
gi 967501916 532 sHDQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK12316 2453 -DAAEDLLAELRAWLAARLPAYMVPAHWVVL 2482
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
224-556 |
4.64e-17 |
|
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: 84.02 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 224 TKHNEIMAMFFTSGTSGYPKMTAHTHSS---FGLGLSVNgrfwLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VF 299
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSlvnLSHGLIKE----YGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 300 AHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVqNDMASYKF---KSLKHCVSAGEPITPDVTEKWRNKTGLDI--YE 374
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLV-LELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA 449
Cdd:cd17644 257 VYGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 450 STLRGN---------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVV 520
Cdd:cd17644 332 EKFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350
....*....|....*....|....*....|....*.
gi 967501916 521 KAFIVlnPDYkshDQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17644 412 VAYIV--PHY---EESPSTVELRQFLKAKLPDYMIP 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-558 |
5.37e-17 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 84.06 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSeaCSLQRGDRVILI-LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLR--EKGVKKDSIVAImMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 170 CIITNDVLApavdaIAPKCENLHSKLIVSENSREgwgnlkemmkcaSDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTH 249
Cdd:cd17656 88 VVLTQRHLK-----SKLSFNKSTILLEDPSISQE------------DTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 250 SSFGLGLSVNGRFWLDLTPSDVMWNTSDTgwAKSAWSSVFSPWIQGACVF-AHHLPRFEPTSVLQTLSKYPI-TVFCSAA 327
Cdd:cd17656 151 KNMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIeVVFLPVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 328 TVYRMLVQNDMASYKFKSLKHCVSAGEP--ITPDVTEKWRNKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------M 398
Cdd:cd17656 229 FLKFIFSEREFINRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeipelppI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV---LPNRPFGLFAHYADDPSKTASTLrgnfYITGDRGYMDEDGYFW 472
Cdd:cd17656 304 GKPISNTWIYILDQEQQLQPQGIVGELyisGASVargYLNRQELTAEKFFPDPFDPNERM----YRTGDLARYLPDGNIE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 473 FVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLIKEIQEHVKKTTAP 552
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNISQLREYLAKQLPE 452
|
....*.
gi 967501916 553 YKYPRK 558
Cdd:cd17656 453 YMIPSF 458
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-557 |
5.89e-17 |
|
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: 84.27 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 91 EEVRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 167
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 168 ANCIITNDVLAPAVDAIAP--KCENLHSKLIVSENSREGWGNLKEMMKCASD--------SHTCVKTKhneimAMF-FTS 236
Cdd:cd05938 79 AKVLVVAPELQEAVEEVLPalRADGVSVWYLSHTSNTEGVISLLDKVDAASDepvpaslrAHVTIKSP-----ALYiYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 237 GTSGYPKMTAHTHSSFglgLSVNGRFWL-DLTPSDVMWNTSDTgWAKSAWSSVFSPWIQ-GA-CVFAhhlPRFEPTSVLQ 313
Cdd:cd05938 154 GTTGLPKAARISHLRV---LQCSGFLSLcGVTADDVIYITLPL-YHSSGFLLGIGGCIElGAtCVLK---PKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 314 TLSKYPITVFCSAATVYRMLVQ-----NDMAsykfkslkHCV--SAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLIC 385
Cdd:cd05938 227 DCRKHNVTVIQYIGELLRYLCNqpqspNDRD--------HKVrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 386 GNFKGmkiKPGSMGKPS-------P----AFDVK----IVDVNGNVLP--PGQEGDIGIQVLPNRPF-GlfahYADDPSK 447
Cdd:cd05938 299 FNYTG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSPFlG----YAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 448 TASTL------RGNFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpIRGE 518
Cdd:cd05938 372 TEKKLlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGR 450
|
490 500 510
....*....|....*....|....*....|....*....
gi 967501916 519 VVKAFIVLNPDYkSHDQEQLIkeiqEHVKKTTAPYKYPR 557
Cdd:cd05938 451 IGMAAVKLKPGH-EFDGKKLY----QHVREYLPAYARPR 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-526 |
9.99e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 9.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFWWingkGEEvRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK12316 519 EQVERTPEAPALAF----GEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 152 TQLTQKDILYRLQSSKANCIITNDVLAPAVDaIAPKCENLHSKLIVSENSREGWGNLKemmkcasdshTCVktkHNEIMA 231
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYSEENPG----------TEL---NPENLA 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 -MFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAHHLPR 305
Cdd:PRK12316 659 yVIYTSGSTGKPKGAGNRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDH 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 306 FEPTSVLQTLSKYPITVFCSAATVYRMLVQnDMASYKFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETVLI 384
Cdd:PRK12316 733 RDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAID 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 385 CGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqVLPNRpfGLFAHYADDPSKTASTLRGN------- 455
Cdd:PRK12316 812 VTHWTCVEEGGDSvpIGRPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvager 886
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967501916 456 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFIVL 526
Cdd:PRK12316 887 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL 953
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
234-562 |
9.99e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.44 E-value: 9.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFAHHLPRFEPTSVLQ 313
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQ 3321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 314 TLSKYPITVFCSAATVYRMLVQN-DMASYKfkSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLI-----CG 386
Cdd:PRK12467 3322 AIHAHRISIACFPPAYLQQFAEDaGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCG 3399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA--------STLRGNFYI 458
Cdd:PRK12467 3400 GDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYR 3474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFIVLNPdykshDQEQL 538
Cdd:PRK12467 3475 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDW 3548
|
330 340
....*....|....*....|....
gi 967501916 539 IKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK12467 3549 RETLRDHLAASLPDYMVPAQLLVL 3572
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
122-556 |
1.81e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.67 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 122 RVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaiaPKCENLHSKLIVSENs 201
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQED- 1700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 202 regwgnlkEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWA 281
Cdd:PRK12467 1701 --------DWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFD 1771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 282 KSAWSsVFSPWIQGA-CVFAHHLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDV 360
Cdd:PRK12467 1772 VSVWE-LFWPLINGArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEA 1850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 361 TEKWRNKTG-LDIYEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqv 429
Cdd:PRK12467 1851 LRPWLERLPdTGLFNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELylgGV-- 1926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 430 lpnrpfGLFAHYADDPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHP 501
Cdd:PRK12467 1927 ------GLARGYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQG 2000
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 502 SVAESAVVSSpDPIRGEVVKAFIV-LNPDYKSHDQEQ--LIKEIQEHVKKTTAPYKYP 556
Cdd:PRK12467 2001 GVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAQvaLRAILKNHLKASLPEYMVP 2057
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-509 |
1.98e-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: 82.12 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 224 TKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWLDLTPSDVMWntsdtgwAKSAWSSVFSPWIQGACVFA--- 300
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEVDL-------ATFPLFALFGPALGLTSVIPdmd 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 301 HHLP-RFEPTSVLQTLSKYPIT-VFCSAA---TVYRMLVQNDMasyKFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIY 373
Cdd:cd05910 154 PTRPaRADPQKLVGAIRQYGVSiVFGSPAlleRVARYCAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 374 EGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKIVDVN---------GNVLPPGQEGDI---GIQVLP 431
Cdd:cd05910 231 TPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEIDdepiaewddTLELPRGEIGEItvtGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 432 ---NRPFGLFAHYADDPSKtastlrGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:cd05910 311 tyvNRPVATALAKIDDNSE------GFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
.
gi 967501916 509 V 509
Cdd:cd05910 385 V 385
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-556 |
2.26e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLA-PAVDAIAPKCENLHSKLIVSENSRegwgnlkemmkcasdshtcVKTKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLDLDRGDENYAEANPA-------------------IRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFGLGLSVNGRFwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACV-FAHHLPRFEPTSVLQTLSKYPITVFCSAATV 329
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVvLAGPEDWRDPALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 330 YRMLVQNDMASyKFKSLKHCVSAGEPITPDVTEKWrnKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFDV 407
Cdd:PRK12316 3298 LQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRAC 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 408 KIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDI 480
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDpfvpgerLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 481 ILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFIVLnpdykSHDQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP-----EDEAGDLREALKAHLKASLPEYMVP 3516
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
178-514 |
9.98e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.14 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 178 APAVDAIAPKCENLHSKLIVSENSREGWGNL-----KEMMKCASDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSS- 251
Cdd:PRK07008 122 LPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSt 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 252 ----FGLGLSVNgrfwLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQGA-CVFAHhlPRFEPTSVLQTLSKYPI 320
Cdd:PRK07008 202 vlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSAPLTGAkLVLPG--PDLDGKSLYELIEAERV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 321 TVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLIcGNFKGMKIKPGSM- 398
Cdd:PRK07008 269 TFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCKLKWKHSQLp 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 -----------GKPSPAFDVKIVDVNGNVLP-PGQE-GDIgiqvLPNRPFGLFAHYADDpsktASTLRGNFYITGDRGYM 465
Cdd:PRK07008 348 ldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDL----QVRGPWVIDRYFRGD----ASPLVDGWFPTGDVATI 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 967501916 466 DEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 514
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
376-558 |
1.36e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 79.27 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 376 YGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFDVKIVdvngnvlpPGQEGDIGIQVlPNRPFGLFAHYADDPsk 447
Cdd:PRK07445 261 YGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITIP--------ANQTGNITIQA-QSLALGYYPQILDSQ-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 448 tastlrgNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVln 527
Cdd:PRK07445 324 -------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV-- 394
|
170 180 190
....*....|....*....|....*....|.
gi 967501916 528 PDYKSHDQEqlikEIQEHVKKTTAPYKYPRK 558
Cdd:PRK07445 395 PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
313-558 |
4.81e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.01 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 313 QTLSKYPITVFCSAATVYRM-LVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE-TVLIcgnfK 389
Cdd:PRK04813 228 ETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERfPSATIYNTYGPTEaTVAV----T 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 390 GMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqVLPNRPFGlfahYADDPSKTAS---TLRGN-FY 457
Cdd:PRK04813 304 SIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGPSVSKG----YLNNPEKTAEaffTFDGQpAY 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 458 ITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVsspdPI-RGEVVK---AFIVLNPdyksH 533
Cdd:PRK04813 379 HTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----E 449
|
250 260
....*....|....*....|....*...
gi 967501916 534 DQE---QLIKEIQEHVKKTTAPYKYPRK 558
Cdd:PRK04813 450 DFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
92-559 |
1.15e-14 |
|
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: 76.70 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 92 EVRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 172 ITNDVLApavdAIAPKCENLHSKLIVSENSREGWGNLKEMMKCASDSHTCVK-TKHNEIMAMFFTSGTSGYPKMTAHTHS 250
Cdd:cd05915 101 LFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFGLGLSVNGRF-WLDLTPSDVMWNTSDTgWAKSAWSSVFS-PWIQGACVFAHHLPRFEptSVLQTLSKYPITVFCSAAT 328
Cdd:cd05915 177 ALVLHSLAASLVdGTALSEKDVVLPVVPM-FHVNAWCLPYAaTLVGAKQVLPGPRLDPA--SLVELFDGEGVTFTAGVPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQ-NDMASYKFKSLKHCVSAGEPiTPDVTEKWRNKTGLDIYEGYGQTETVLI------------CGNFKGMKIK- 394
Cdd:cd05915 254 VWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVvvqnfvkshlesLSEEEKLTLKa 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 395 ---------------PGSMGKPSPAFDVKIVDVNGNVLPPGqegdigiqvlpnrpfglfaHYADDPSKTASTLRGNFYIT 459
Cdd:cd05915 333 ktglpiplvrlrvadEEGRPVPKDGKALGEVQLKGPWITGG-------------------YYGNEEATRSALTPDGFFRT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 460 GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNpdykshDQEQLI 539
Cdd:cd05915 394 GDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------GEKPTP 467
|
490 500
....*....|....*....|.
gi 967501916 540 KEIQEHVKKTTAPYKY-PRKV 559
Cdd:cd05915 468 EELNEHLLKAGFAKWQlPDAY 488
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
90-518 |
2.30e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 90 GEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILI---LPRVPEWWLAnvaCLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQAL-DRDGIKLGDRVATIawnTWRHLEAWYG---IMGIGAICHTVNPRLFPEQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 167 KANCIITNDVLAPAVDAIAPKCENLHSKLIVSENSREGWGNLK------EMMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:PRK06018 111 EDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKnavayeEWIAEADGDFAWKTFDENTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 241 YPKMTAHTHSSFGL-GLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFahhLP--RFEPTSVLQTLSK 317
Cdd:PRK06018 191 DPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 318 YPITVFCSAATVYRMLVQN-DMASYKFKSLKHCVSAGEPItPDVTEKWRNKTGLDIYEGYGQTETVLI--CGNFKG---- 390
Cdd:PRK06018 267 EKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgtLAALKPpfsk 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 391 ------MKIKPgSMGKPSPAFDVKIVDVNGNVLPpgQEGDIGIQVLPNRP------FGLFAHYADDpsktastlRGnFYI 458
Cdd:PRK06018 346 lpgdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDGKTFGRLKVRGPavaaayYRVDGEILDD--------DG-FFD 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 518
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
234-559 |
1.39e-13 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.20 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPK--MTAHtHSSFGLGLSVNGRFWLDLTPSDVMWNTSdtgwaksawSSVFSPWIQGAC--VFAHH----LP- 304
Cdd:cd17648 101 YTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS---------NYVFDFFVEQMTlaLLNGQklvvPPd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 305 --RFEPTSVLQTLSKYPITVFCSAATVyrmLVQNDMASykFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV 382
Cdd:cd17648 171 emRFDPDRFYAYINREKVTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 383 L--ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFAHYADDPSKTAS-TLR 453
Cdd:cd17648 246 VtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELylgGDGVARgylNRPELTAERFLPNPFQTEQeRAR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 454 GNF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP-IRGEVVKAFIVlnpD 529
Cdd:cd17648 326 GRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---G 402
|
330 340 350
....*....|....*....|....*....|.
gi 967501916 530 YKSHDQEQLIK-EIQEHVKKTTAPYKYPRKV 559
Cdd:cd17648 403 YYLPEPGHVPEsDLLSFLRAKLPRYMVPARL 433
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
131-530 |
1.82e-13 |
|
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: 73.02 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapaVDaiapKCENLHSklivsensregWGNLKE 210
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF--------CD----AGVKVYS-----------LEEFEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 211 MMKcaSDSHTCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLtpsdVMWNTSDTGWAKSAWSSVFS 290
Cdd:cd05927 100 LGK--KNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYISYLPLAHIFE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 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 967501916 347 KH---------------------------CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIkPGSM 398
Cdd:cd05927 250 RSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTS-VGHV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDV---NGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGN-FYITGDRGYMDEDGYFWFV 474
Cdd:cd05927 329 GGPLPCAEVKLVDVpemNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKII 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967501916 475 ARSDDII-LSSGYRIGPFEVENALNEHPSVAESAVvsspdpiRGEVVKAF----IVLNPDY 530
Cdd:cd05927 404 DRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDV 457
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
94-508 |
3.95e-13 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 71.69 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKANC 170
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 171 IITN--DVLAPAVDAIAPKCE--NLHSKLIvsensregwgnlkemmkcasdshtcvktkhneimaMFFTSGTSGYPKMTA 246
Cdd:cd05939 79 LIFNllDPLLTQSSTEPPSQDdvNFRDKLF-----------------------------------YIYTSGTTGLPKAAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 247 HTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSA 326
Cdd:cd05939 124 IVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRK--KFSASNFWDDCVKYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 327 ATVYRMLVQndmASYKFKSLKHCV--SAGEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKG------------M 391
Cdd:cd05939 201 GEICRYLLA---QPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfnsrilP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 392 KIKPGSMGKPSPAFDVKIVDVNGNVLP--PGQEGDIGIQVLPNRPFGLFAHYADDPSKTASTLRGNF------YITGDRG 463
Cdd:cd05939 278 SVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFLSGDVL 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 967501916 464 YMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:cd05939 358 VMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVV 402
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
459-556 |
8.64e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.45 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 459 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnpdykSHDQEQL 538
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHEEIDP 368
|
90
....*....|....*...
gi 967501916 539 IkEIQEHVKKTTAPYKYP 556
Cdd:PRK08308 369 V-QLREWCIQHLAPYQVP 385
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
51-564 |
6.46e-12 |
|
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: 68.45 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 51 KLEIPEYF-----NFAKDVLdqwtnmekAGKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVIL 125
Cdd:cd05943 58 IMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 126 ILPRVPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAIAPKCENLHS 193
Cdd:cd05943 129 YLPNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 194 KLIVSENSREGWGNLKEMMKCASDSHTCVKTKHNEI----------MAMFFTSGTSGYPKmtAHTHSSFGLGLSVNGRFW 263
Cdd:cd05943 206 VVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPK--CIVHGAGGTLLQHLKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 264 L--DLTPSDVM-WNTSdTGWAksAWSSVFSPWIQGA-CVFAHHLPRFEPTSVLQTL-SKYPITVFCSAATVYRMLVQNDM 338
Cdd:cd05943 284 LhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGAtIVLYDGSPFYPDTNALWDLaDEEGITVFGTSAKYLDALEKAGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 339 ---ASYKFKSLKHCVSAGEPITPD----VTEKWrnKTGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFDV 407
Cdd:cd05943 361 kpaETHDLSSLRTILSTGSPLKPEsfdyVYDHI--KPDVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 408 KIVDVNGNVLPpGQEGDIGI-QVLPNRPFGL-------------FAHYaddpsktastlrGNFYITGDRGYMDEDGYFWF 473
Cdd:cd05943 436 EAFDEEGKPVW-GEKGELVCtKPFPSMPVGFwndpdgsryraayFAKY------------PGVWAHGDWIEITPRGGVVI 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 474 VARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQLIKEIQEHVKKTTAPY 553
Cdd:cd05943 503 LGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRSA 576
|
570
....*....|.
gi 967501916 554 KYPRKVGILII 564
Cdd:cd05943 577 LSPRHVPAKII 587
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
234-513 |
2.22e-11 |
|
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: 66.34 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKMTAHTHSSFG-LGLSVNGRFWLDLTPSDVMWNTS---DTGWAKSAWSSVFSpwiqGACVFAHHLPRFEPT 309
Cdd:cd17650 100 YTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQMASfsfDVFAGDFARSLLNG----GTLVICPDEVKLDPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 310 SVLQTLSKYPITVFCSAATVYRMLVQN-DMASYKFKSLKHCV--SAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:cd17650 176 ALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIvgSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDST 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFK-GMKIKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTASTLR-------G 454
Cdd:cd17650 256 YYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----GAGVARGYLNRPELTAERFVenpfapgE 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 967501916 455 NFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 513
Cdd:cd17650 331 RMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED 389
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-509 |
5.61e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.96 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 72 EKAGKKPSNPAFWWINGKgeevrWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05691 1139 EQARQTPERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 152 TQLTQKDILYRLQSSKANCIITNDVL---APAVDAIAPKC-ENLHSklivsensrEGWgnlkemmkcasDSHTCVKTKHN 227
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---------DSW-----------PSQAPGLHLHG 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 228 EIMA-MFFTSGTSGYPKMTAHTHSSFGLGLSvngrfWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFAH 301
Cdd:PRK05691 1273 DNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGCrLVLAG 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 302 HLPRFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMASyKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE 380
Cdd:PRK05691 1347 PGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTE 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 381 TVL-----ICGNFKGMKikpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA------ 449
Cdd:PRK05691 1426 TAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAerfvpd 1497
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967501916 450 --STLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK05691 1498 plGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
94-562 |
1.34e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 63.91 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIt 173
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 174 ndvlapaVDAiapkcenlhsklivsensregwgnlkemmkcasdshtcvktkhneimAMF-FTSGTSGYPKMTAHTHSSF 252
Cdd:cd05940 81 -------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 253 GLGLSVNGrFWLDLTPSDVMWNT----SDTGwAKSAWSSVFspwIQGACVFAHHlpRFEPTSVLQTLSKYPITVFCSAAT 328
Cdd:cd05940 107 WRGGAFFA-GSGGALPSDVLYTClplyHSTA-LIVGWSACL---ASGATLVIRK--KFSASNFWDDIRKYQATIFQYIGE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 329 VYRMLVQndmASYKFKSLKHCVSA--GEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGmkiKPGSMGKPSP-- 403
Cdd:cd05940 180 LCRYLLN---QPPKPTERKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFG---KPGAIGRNPSll 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 404 --AFDVKIV-----------DVNGNV--LPPGQEGDIGIQVLPNRPF-GlfahYADDPSKTASTLRGNF------YITGD 461
Cdd:cd05940 254 rkVAPLALVkydlesgepirDAEGRCikVPRGEPGLLISRINPLEPFdG----YTDPAATEKKILRDVFkkgdawFNTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 462 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpIRGEVVKAFIVLNPDYkSHDQEQLi 539
Cdd:cd05940 330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNE-EFDLSAL- 406
|
490 500
....*....|....*....|...
gi 967501916 540 keiQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05940 407 ---AAHLEKNLPGYARPLFLRLQ 426
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
340-552 |
1.54e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.22 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 340 SYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKIVDVngnvl 417
Cdd:PRK06814 903 PYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLEPV----- 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 418 pPGQEGDIGIQVL-PNRPFGlfahY--ADDPSkTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 494
Cdd:PRK06814 976 -PGIDEGGRLFVRgPNVMLG----YlrAENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 495 NALNEHPSVAESAVVSSPDPIRGEVvkafIVLNPDYKSHDQEqlikEIQEHVKKTTAP 552
Cdd:PRK06814 1050 ELAAELWPDALHAAVSIPDARKGER----IILLTTASDATRA----AFLAHAKAAGAS 1099
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
96-551 |
1.61e-10 |
|
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: 63.65 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 96 SFEELGSLSRKFANILSEacSLQRGDRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17654 18 SYADLAEKISNLSNFLRK--KFQTEERAIgLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 175 dvlapavdaiapkCENLHSKLIVSENSRegwgnlkemmkcasdsHTCVKTKHNeIMAMFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd17654 96 -------------KELDNAPLSFTPEHR----------------HFNIRTDEC-LAYVIHTSGTTGTPKIVAVPHKCI-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VFAHHLPRFEPTSVLQTLSKYP-ITVFCSAATVYRM 332
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATlLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 333 LVQNDMASY---KFKSLKHCVSAGEPITPDVTEK-WRNK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:cd17654 224 FGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSsWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 408 KI--VDVNGNVlPPGQEGDIGIqvlpNRpfglfAHYADDPSKTAstlRGNFYITGDRGYMdEDGYFWFVARSDDIILSSG 485
Cdd:cd17654 303 VIevRDQNGSE-GTGQVFLGGL----NR-----VCILDDEVTVP---KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 486 YRIGPFEVENALNEHPSVAESAVVSSPDpirgEVVKAFIVLNPdykSHDQEQliKEIQEHVKKTTA 551
Cdd:cd17654 369 KRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLSSHA 425
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
222-545 |
4.34e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.81 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 222 VKTKHNEIMAMFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAH 301
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 302 HLP---RFEPTSVLQTlskyPITVFCSAATV---YRMLVQndmaSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEG 375
Cdd:PRK08043 439 PSPlhyRIVPELVYDR----NCTVLFGTSTFlgnYARFAN----PYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEG 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 376 YGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PN---------RPFGLFAHYADDP 445
Cdd:PRK08043 511 YGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV------PGIEQGGRLQLKgPNimngylrveKPGVLEVPTAENA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 446 sktASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEvvkAFIV 525
Cdd:PRK08043 585 ---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVL 658
|
330 340
....*....|....*....|
gi 967501916 526 LNPDyKSHDQEQLIKEIQEH 545
Cdd:PRK08043 659 FTTD-SELTREKLQQYAREH 677
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
127-552 |
5.68e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 61.76 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 127 LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLA------PAVDAIAPKCENLHSKLIVSEN 200
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 201 S-----REGWGNLKEMMKCASDSH-------TCVKTKHNEIMAMFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTP 268
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 269 SDVM-WNTSdTGWAKSAWsSVFSPWIQGACVFAHHlprFEPTS--VLQTLSKYPITVFCSAATV---YRMLVQNDMASYK 342
Cdd:PLN03051 160 GDVVcWPTN-LGWMMGPW-LLYSAFLNGATLALYG---GAPLGrgFGKFVQDAGVTVLGLVPSIvkaWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 343 FKSLKHCVSAGEPITPDvTEKWRNKT------------GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKIV 410
Cdd:PLN03051 235 WSKLRVFASTGEASAVD-DVLWLSSVrgyykpvieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 411 DVNGNVLPPGQE--GDIGIqvlpnRPFGLFA------------HYADDP--SKTASTLRGNfyitGDRGYMDEDGYFWFV 474
Cdd:PLN03051 306 NDNGVPYPDDQPcvGEVAL-----APPMLGAsdrllnadhdkvYYKGMPmyGSKGMPLRRH----GDIMKRTPGGYFCVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 475 ARSDDIILSSGYRIGPFEVENALNE-HPSVAESAVVSSPDPIRGE----VVKAFIVLNPDYKSHDQEQLIKEIQEHVKKT 549
Cdd:PLN03051 377 GRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTN 456
|
...
gi 967501916 550 TAP 552
Cdd:PLN03051 457 LNP 459
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
308-496 |
3.65e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 59.24 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 308 PTSVLQTLSKYPITVFCSAATVY-----RMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRN---KTGLD---IYEGY 376
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAPNFAYallarRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpeaILPAY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 377 GQTETVLI-----CGNfkGMKI------------------KPG-----SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIq 428
Cdd:PRK07768 315 GMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIEL- 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967501916 429 vlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENA 496
Cdd:PRK07768 392 ----RGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
131-499 |
5.57e-09 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 58.91 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN-CIITNDVLAPAVDAIAPKCENLHSKLIVSENSRE------ 203
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANiLVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEkepnly 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 204 GWGNLKEMMKCASDS--HTCVKT-KHNEIMAMFFTSGTSGYPK--MTAHTHSSFGLGLSVNGrfwLDLTPSDVMwntsdt 278
Cdd:cd05933 124 SWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWTAKAASQH---MDLRPATVG------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 279 gwAKSAWS------------SVFSPWIQGACV-FAH----------HLPRFEPTS------VLQTLSKYPITVFCSAATV 329
Cdd:cd05933 195 --QESVVSylplshiaaqilDIWLPIKVGGQVyFAQpdalkgtlvkTLREVRPTAfmgvprVWEKIQEKMKAVGAKSGTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 330 YRMLV-----------QNDMAS-----YKFKSLKH-----------------CVSAGEPITPDVTEKWrnkTGLDI--YE 374
Cdd:cd05933 273 KRKIAswakgvgletnLKLMGGespspLFYRLAKKlvfkkvrkalgldrcqkFFTGAAPISRETLEFF---LSLNIpiME 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 375 GYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIVDVNGNvlppGQeGDIGIqvlpnRPFGLFAHYADDPSKTA 449
Cdd:cd05933 350 LYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDAD----GI-GEICF-----WGRHVFMGYLNMEDKTE 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 967501916 450 STLRGNFYI-TGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVENALNE 499
Cdd:cd05933 415 EAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKK 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-556 |
8.47e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 234 FTSGTSGYPKmtahthssfglGLSVNGRF----------WLDLTPSDVMWNTSDTGWAKSAWSSVFSPwIQGACV----- 298
Cdd:PRK05691 3876 YTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAP-LFGARVeivpn 3943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 299 -FAHHlprfePTSVLQTLSKYPITVFCSAAT-VYRMLVQNDMAsykFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEG 375
Cdd:PRK05691 3944 aIAHD-----PQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNA 4015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 376 YGQTETVLICGNFK-GMKIKPGS---MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFAHYADDPSKTAST 451
Cdd:PRK05691 4016 YGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTALA 4090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 452 LRGN--------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAF 523
Cdd:PRK05691 4091 FVPHpfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGY 4169
|
330 340 350
....*....|....*....|....*....|...
gi 967501916 524 IVlnPDYKSHDQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:PRK05691 4170 LV--PHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
227-550 |
3.16e-08 |
|
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: 56.34 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 227 NEIMAMFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDVMWN--TSDTGWAksawSSVFSPWIQGACVFAHHL 303
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNmFAILNSTEWKTKDRILSWMplTHDMGLI----AFHLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 304 PRF--EPTSVLQTLSKYPITVFCSAATVYRMLVQ----NDMASYKFKSLKHCVSAGEPITPDVTE---KWRNKTGLD--- 371
Cdd:cd05908 182 RLFirRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpEKANDWDLSSIRMILNGAEPIDYELCHeflDHMSKYGLKrna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 372 IYEGYGQTE-TVLICGNFKGMKIKPGSM-------GKPSPAFD--------------------VKIVDVNGNVLPPGQEG 423
Cdd:cd05908 262 ILPVYGLAEaSVGASLPKAQSPFKTITLgrrhvthGEPEPEVDkkdsecltfvevgkpidetdIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 424 DIGIqvlpnRPFGLFAHYADDPSKTASTLRGN-FYITGDRGYMdEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPS 502
Cdd:cd05908 342 HIQI-----RGKNVTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 967501916 503 VAESAVVS---SPDPIRGEVVKAFIVLNpdyKSHDQ-EQLIKEIQEHVKKTT 550
Cdd:cd05908 416 VELGRVVAcgvNNSNTRNEEIFCFIEHR---KSEDDfYPLGKKIKKHLNKRG 464
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
457-562 |
5.93e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 457 YITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFIVlnpdyKSHDQE 536
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPA 309
|
90 100
....*....|....*....|....*.
gi 967501916 537 QLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVV 335
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
350-522 |
8.38e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.11 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 350 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVngnvlP---------P 419
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDV-----PemnytsedqP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 420 GQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVENAL 497
Cdd:PLN02736 456 YPRGEICV-----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVY 530
|
170 180 190
....*....|....*....|....*....|....*.
gi 967501916 498 NEHPSVAESAV-----------VSSPDPirgEVVKA 522
Cdd:PLN02736 531 AKCKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
86-511 |
1.41e-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: 54.28 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 86 INGKGEE-VRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQ 164
Cdd:cd05905 5 LDSKGKEaTTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 165 SSKANCIITNDVLAP----AVDAIAPKCENLHSKLIvsENSREGWGNLKEMMKCASDSHTCVKTKHNEIMAMFFTSGTSG 240
Cdd:cd05905 85 TCKVRVALTVEACLKglpkKLLKSKTAAEIAKKKGW--PKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 241 YPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWN----TSDTGWAKSAWSSVFSpwiqGACV--FAHHLPRFEPTSVLQT 314
Cdd:cd05905 163 SLSGVAVSHSSL-LAHCRALKEACELYESRPLVTvldfKSGLGLWHGCLLSVYS----GHHTilIPPELMKTNPLLWLQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 315 LSKYPI-TVFCSAATVYRMLVQ--NDMASYK-----FKSLKHC-VSAGEPITPDVTEKWRN---KTGL------------ 370
Cdd:cd05905 238 LSQYKVrDAYVKLRTLHWCLKDlsSTLASLKnrdvnLSSLRMCmVPCENRPRISSCDSFLKlfqTLGLspravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 371 ----------------DIY---------------EGYGQTETVLICGnfkgmKIKPGsmgkpspafdVKIVDVNGNVLPP 419
Cdd:cd05905 318 vnpficwqgtsgpepsRVYldmralrhgvvrldeRDKPNSLPLQDSG-----KVLPG----------AQVAIVNPETKGL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 420 GQEGDIG-IQVL-PNRPFGLFA-------HYADDPSKTASTLRGN-FYI-TGDRGY----------MDEDGYFWFVARSD 478
Cdd:cd05905 383 CKDGEIGeIWVNsPANASGYFLldgetndTFKVFPSTRLSTGITNnSYArTGLLGFlrptkctdlnVEEHDLLFVVGSID 462
|
490 500 510
....*....|....*....|....*....|....
gi 967501916 479 DIILSSGYRIGPFEVEN-ALNEHPSVAESAVVSS 511
Cdd:cd05905 463 ETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVFSI 496
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-556 |
1.88e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 232 MFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQGACVFAHHLPRFEPTS 310
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 311 VLQTLSKYPITVFCSAATVYRMLVQNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-IYEGYGQTETV---LICG 386
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACL 2494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 387 NFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFAHYADDPSKTA--------STLRGNF 456
Cdd:PRK05691 2495 APEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRL 2569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 457 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAEsAVVSSPDPIRGEVVKAFIVLNPDYKSHDQE 536
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
330 340
....*....|....*....|.
gi 967501916 537 QLIKE-IQEHVKKTTAPYKYP 556
Cdd:PRK05691 2649 AALREaLKAHLKQQLPDYMVP 2669
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
180-529 |
3.03e-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: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 180 AVDAIAPkcenLHSKLIVSENSREGWGNLKemmkCASDSHTCVKTKHNE---------IMAMFFTSGTSGYPKMTAHTHS 250
Cdd:cd05921 117 ALAAIFP----LGTPLVVSRNAVAGRGAIS----FAELAATPPTAAVDAafaavgpdtVAKFLFTSGSTGLPKAVINTQR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 251 SFGLGLSVNGRFWLDLTPSD-VM-----WNTSDTGwaksawSSVFSPWIQGACVFahHLPRFEPT-----SVLQTLSKYP 319
Cdd:cd05921 189 MLCANQAMLEQTYPFFGEEPpVLvdwlpWNHTFGG------NHNFNLVLYNGGTL--YIDDGKPMpggfeETLRNLREIS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 320 ITVFCSAATVYRMLVQ---NDMASYK--FKSLKHCVSAGEPITPDVTEKWRN----KTGLDI--YEGYGQTETVLICGNF 388
Cdd:cd05921 261 PTVYFNVPAGWEMLVAaleKDEALRRrfFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATFT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 389 KGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqEGDI-GIQVLPNrpfglfahYADDPSKTASTL-RGNFYITGDRGYM- 465
Cdd:cd05921 341 HWPTERSGLIGLPAPGTELKLVPSGGKY-----EVRVkGPNVTPG--------YWRQPELTAQAFdEEGFYCLGDAAKLa 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 466 ---DEDGYFWFVAR-SDDIILSSG--YRIGPFEVEnALNEHPSVAESAVVSSPDpirGEVVKAFIVLNPD 529
Cdd:cd05921 408 dpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAEVGALVFPDLL 473
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
399-547 |
1.09e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.54 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFAHYADDPSKTASTLRGNFYITGDRGYMdEDGYFWFVARSD 478
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967501916 479 DIILSSGYRIGPFEVENALNEHPSV--AESAVVSSPDPiRGEVVKAFI---VLNPDykshDQEQLIKEIQEHVK 547
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVR 530
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
346-549 |
2.65e-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: 50.29 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 346 LKHCVSAGEPITPDvTEKWRNKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFDVKIVDV----NGNV 416
Cdd:cd17639 252 LRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCEIKLVDWeeggYSTD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 417 LPPGQeGDIGIQvlpnRPFgLFAHYADDPSKTASTLRGN--FYiTGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEV 493
Cdd:cd17639 326 KPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKL 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 967501916 494 ENALNEHPSVAESAVVSspDPIRGEVVkAFIVLNpdykshdQEQLIKEIQEHVKKT 549
Cdd:cd17639 399 ESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVIN 444
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
231-509 |
4.57e-06 |
|
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: 49.35 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 231 AMFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFAHHlpRFepts 310
Cdd:cd05937 91 ILIYTSGTTGLPKAAAISWRRTLVTSNLLSH-DLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSR--KF---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 311 vlqTLSKYPITVFCSAAT--VY-----RMLVqNDMASYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTETV 382
Cdd:cd05937 164 ---SASQFWKDVRDSGATiiQYvgelcRYLL-STPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVpEIGEFYAATEGV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 383 LICGNFKGMKIKPGSMGKPSP------AFDVKIVDVNGN--------------VLPPGQEGDIgIQVLPNRPFGLFAHYA 442
Cdd:cd05937 240 FALTNHNVGDFGAGAIGHHGLirrwkfENQVVLVKMDPEtddpirdpktgfcvRAPVGEPGEM-LGRVPFKNREAFQGYL 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967501916 443 DDPSKTASTL------RGN-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd05937 319 HNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
222-500 |
5.23e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.43 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 222 VKTKHNEIMA-MFFTSGTSGYPKMTAHTHSSfglgLSVNGRFWLDL---TPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 297
Cdd:PRK06334 177 VSDKDPEDVAvILFTSGTEKLPKGVPLTHAN----LLANQRACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 298 VFAHHLPrFEPTSVLQTLSKYPITVFCSAATVYRMLVQNDMAS-YKFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEG 375
Cdd:PRK06334 253 VVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQeSCLPSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 376 YGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlpPGQEGDIGIQVLpnRPFGLFAHY-ADDPSKTASTLR 453
Cdd:PRK06334 332 YGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKV--PVSSGETGLVLT--RGTSLFSGYlGEDFGQGFVELG 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 967501916 454 G-NFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIGPFEV-----ENALNEH 500
Cdd:PRK06334 408 GeTWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
350-529 |
5.47e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 46.35 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 350 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPSPAFDVKIVDVNG--NVLPPGQEGDIGI 427
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFPDEMCMLGTVGAPAvyNELRLEEVPEMGY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 428 QVLPNRPFG--------LFAHYADDPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVENALN 498
Cdd:PLN02430 458 DPLGEPPRGeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYG 537
|
170 180 190
....*....|....*....|....*....|.
gi 967501916 499 EHPSVAESAVVSspDPIRGEVVkAFIVLNPD 529
Cdd:PLN02430 538 QNPIVEDIWVYG--DSFKSMLV-AVVVPNEE 565
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
59-143 |
1.37e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.79 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 59 NFAKDVLDQwtnmekagKKPSNPAFWWINGKGEEVRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEwwlANV 138
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
....*
gi 967501916 139 ACLRT 143
Cdd:PRK03584 155 AMLAT 159
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
453-556 |
3.02e-04 |
|
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: 43.66 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967501916 453 RGNFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVENALNEHPSVAES------------AVVS--SPDPIRGE 518
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 967501916 519 VVKAFIVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
|
| |
