|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-577 |
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: 1065.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 48 IPEYFNFAKDVLDQWTNTEKTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMK 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 208 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 288 QGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 368 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLR 447
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 527
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 65301416 528 DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-573 |
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: 628.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSsFGL 248
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 329 QNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 408
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 409 TILPPGQEGDIAVQVlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVE 488
Cdd:cd05972 268 RELPPGEEGDIAIKL---PPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 489 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVK 568
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*
gi 65301416 569 RNELR 573
Cdd:cd05972 423 RVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
45-577 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 607.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 45 KIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKI 124
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRG-----DKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIV---- 191
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 192 SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSD 271
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 272 TGWAKSAWSSVFSPWTQGACVFAH-YLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITSYKFNSLKHCVSA 346
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 347 GEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlp 425
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVI---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 426 DRPF-GLFTHYVDNPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:COG0365 391 KGPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 502 VVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
37-576 |
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: 588.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 37 YESMKHDFKIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTeACSLQRGDR 116
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYP-----DKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD--DTLAPAVDIVAAKCENLHSKLIVSQH 194
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 195 SREGWGNLKEMMKYASDS----HTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIASDVMWNTS 270
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 271 DTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPI 350
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 351 NPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPFG 430
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 431 LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 510
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 511 GEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:cd05970 474 GQVVKATIVLAKGYE--PSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-576 |
4.17e-149 |
|
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: 436.23 E-value: 4.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05974 81 N-----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 250 lSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 329
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 330 NDITSYKFnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGT 409
Cdd:cd05974 193 QDLASFDV-KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 410 ilpPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVES 489
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 490 ALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIeELPKTVSGKVKR 569
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 65301416 570 NELRRKE 576
Cdd:cd05974 426 VELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-576 |
8.43e-148 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 437.79 E-value: 8.43e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 33 NFSNYESMKHDFKI-EIPEYF--------NFAKDVLDQWTNTEKTGKrlsnPAFWWVDGNGKEvRWSFEELGSLSRKFAN 103
Cdd:PRK04319 14 NLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 104 ILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAvdIVAAKCE 183
Cdd:PRK04319 89 VLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLER--KPADDLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 184 NLHSKLIVSQHSREGWG--NLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLI 261
Cdd:PRK04319 166 SLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 262 ASDVMWNTSDTGWAKSAWSSVFSPWTQGA--CVFAhylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITSYK 336
Cdd:PRK04319 245 EDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 337 FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPG 414
Cdd:PRK04319 322 LSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 415 QEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEH 494
Cdd:PRK04319 401 RMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 495 PSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK04319 478 PAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
..
gi 65301416 575 KE 576
Cdd:PRK04319 556 WE 557
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-576 |
3.92e-136 |
|
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: 403.42 E-value: 3.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgL 248
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 329 QNDI---TSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEI 403
Cdd:cd05969 195 KEGDelaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 404 LDENGTILPPGQEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 483
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 484 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTV 563
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE--PSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 65301416 564 SGKVKRNELRRKE 576
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-574 |
2.48e-128 |
|
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: 383.32 E-value: 2.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 83 NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 163 KCIITDDTLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHT 242
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 243 HSsFGLGLSVNGRFWLDLI--ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSA 320
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 321 PTAYRML-IQNDITSYKFNSLKHCVSAGEPINPEVMeQWKKKT-GLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSP 397
Cdd:cd05971 189 PTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELL-GWAREQfGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 398 AFNVEILDENGTILPPGQEGDIAVQvLPDrPFGLFThYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILS 477
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 478 SGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIE 557
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVN 422
|
490
....*....|....*..
gi 65301416 558 ELPKTVSGKVKRNELRR 574
Cdd:cd05971 423 ELPRTATGKIRRRELRA 439
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
86-580 |
4.75e-124 |
|
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: 372.61 E-value: 4.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:COG0318 22 GRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:COG0318 101 VT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FgLGLSVNGRFWLDLIASDVMWNTS----DTGWaksaWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:COG0318 125 L-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 TAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSPA 398
Cdd:COG0318 198 TMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 399 FNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSS 478
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 479 GYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEE 558
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL-DAEELRAFLRERL----ARYKVPRRVEFVDE 427
|
490 500
....*....|....*....|..
gi 65301416 559 LPKTVSGKVKRNELRRKEWTTT 580
Cdd:COG0318 428 LPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-574 |
1.05e-110 |
|
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: 337.95 E-value: 1.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 tlapavdivAAKCENLHSKLIVsqhsregwgnlkeMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05973 80 ---------AANRHKLDSDPFV-------------MM---------------------FTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG-ACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 329 QNDITSYKF--NSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFNVEIL 404
Cdd:cd05973 194 AAGAEVPARpkGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 405 DENGTILPPGQEGDIAVQVlPDRPFGLFTHYVDNPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 484
Cdd:cd05973 274 DDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 485 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 564
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE--GTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
490
....*....|
gi 65301416 565 GKVKRNELRR 574
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
66-573 |
5.43e-107 |
|
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: 329.52 E-value: 5.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 66 EKTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05936 6 EEAARRFPDkTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 145 TTQLTQKDILYRLQSSKSKCIITDDTLApavdivaakcenlhsKLIVSQHSREGWgnlkemmkyasdshtCVDTKHnELM 224
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------DLLAAGAPLGER---------------VALTPE-DVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 225 AIYFTSGTTGPPKMIGHTHSSfglgLSVNgrfwldliASDVMWNTSDTGWAKS------------AWS-SVFSPWTQGAC 291
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRN----LVAN--------ALQIKAWLEDLLEGDDvvlaalplfhvfGLTvALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 292 VFahYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGY 370
Cdd:cd05936 197 IV--LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTL 446
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVrgpQV--------MKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 526
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 65301416 527 hdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05936 427 -----TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-568 |
3.47e-104 |
|
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: 317.69 E-value: 3.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 222 ELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFAHylPRFD 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 302 STSILQTLSKFPITVFCSAPTAYRMLIQND-ITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLI 378
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 379 CGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGY 458
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-----RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 459 MDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQE 538
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 65301416 539 HVKKTTAPYKYPRKIEFIEELPKTVSGKVK 568
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-573 |
5.97e-103 |
|
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: 320.47 E-value: 5.97e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 50 EYFNFAKDVLDQwtnteKTGKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWL 129
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAG---SLTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRE--GWGNLKEMMK 207
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 208 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 288 QGACVFahYLP-RFDSTSILQTLSKFPITVFCSAPTAYR-MLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD 365
Cdd:cd05959 230 VGATTV--LMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 366 IYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 444
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYV-----RGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 524
Cdd:cd05959 382 TFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 65301416 525 KlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05959 462 E--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-573 |
1.40e-96 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 301.70 E-value: 1.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtCVdtkhnelmaIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd05958 88 LCAHALTASDDI-------------------------------------CI---------LAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 326 -MLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIL 404
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 405 DENGTILPPGQEGDIAVQvlpdRPFGLftHYVDNPSKtASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 484
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 485 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 564
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI--PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 65301416 565 GKVKRNELR 573
Cdd:cd05958 431 GKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
88-577 |
5.32e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 294.79 E-value: 5.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK06187 31 RTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 DDTLAPAVDIVAAKCENLHSKLIVSQHSREG----WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWAksawssvFSPWTQGACVFahYLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK06187 190 RNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGAKQV--IPRRFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLIQNDITS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNF-----KGMKIKPG 390
Cdd:PRK06187 260 FAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWTKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 SMGKPSPAFNVEILDENGTILPP--GQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFV 468
Cdd:PRK06187 340 SAGRPLPGVEARIVDDDGDELPPdgGEVGEIIV-----RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYIT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 469 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhdqEQLK-KEIQEHVKKTTAPY 547
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG------ATLDaKELRAFLRGRLAKF 488
|
490 500 510
....*....|....*....|....*....|
gi 65301416 548 KYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
33-573 |
2.18e-88 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 286.07 E-value: 2.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 33 NFSNYESMkHDFKIEIPEYF--NFAKDVLDqWTNTEKTGKRLSNPAF--WWVDG-------------------------- 82
Cdd:TIGR02188 3 NLEQYKEL-YEESIEDPDKFwaKLARELLD-WFKPFTKVLDWSFPPFykWFVGGelnvsyncvdrhlearpdkvaiiweg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 83 --NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDILYRL 157
Cdd:TIGR02188 81 dePGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALADRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 158 QSSKSKCIITDDT---------LAPAVDIVAAKCENLHSKLIVSQH----------SREGWGNlkEMMKYASDSHTCVDT 218
Cdd:TIGR02188 157 NDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRtgnpvvpwveGRDVWWH--DLMAKASAYCEPEPM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 219 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHY-L 297
Cdd:TIGR02188 235 DSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEgV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRFDSTS-ILQTLSKFPITVFCSAPTAYRMLIQ---NDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---IYEGY 370
Cdd:TIGR02188 315 PTYPDPGrFWEIIEKHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTET--VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILP-PGQEGDIAV-QVLPDRPFGLF---THYVDNPSKTA 443
Cdd:TIGR02188 395 WQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIkQPWPGMLRTIYgdhERFVDTYFSPF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 444 StlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 523
Cdd:TIGR02188 475 P----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDG 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 65301416 524 YKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:TIGR02188 551 YEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-573 |
6.98e-86 |
|
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: 273.57 E-value: 6.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 tlapavDIVAakcenlhsklivsqhsregwgnlkemmkYASdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05919 91 ------DDIA----------------------------YLL-----------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPrfDSTSILQTLSKFPITVFCSAPTAY-RML 327
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYaNLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 328 IQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDEN 407
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 408 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEV 487
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 488 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 567
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP--AAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
....*.
gi 65301416 568 KRNELR 573
Cdd:cd05919 431 QRFKLR 436
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-573 |
3.92e-85 |
|
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: 276.75 E-value: 3.92e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 53 NFAKDVLDQwtNTEKTGKRlsnPAFWWvDGN--GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLA 130
Cdd:cd05966 53 NISYNCLDR--HLKERGDK---VAIIW-EGDepDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 131 NVACLRTG---TVLIPGttqLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHsKLIVSQHS--- 195
Cdd:cd05966 126 MLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTgge 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 196 ------REGWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNT 269
Cdd:cd05966 202 vpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 270 SDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQ---NDITSYKFNSLKHCV 344
Cdd:cd05966 280 ADIGWITGHSYIVYGPLANGAtTVMFEGTPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 345 SAGEPINPEVMEQWKKKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQE 416
Cdd:cd05966 360 SVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 417 GDIAVqvlpDRPFglfthyvdnPSkTASTLRGN--------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRI 482
Cdd:cd05966 437 GYLVI----KRPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 483 GPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKT 562
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
570
....*....|.
gi 65301416 563 VSGKVKRNELR 573
Cdd:cd05966 581 RSGKIMRRILR 591
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-567 |
9.11e-84 |
|
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: 267.94 E-value: 9.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17631 18 GRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd17631 97 FDD------------------------------------------------------LALLMYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FgLGLSVNGRFWLDLIASDV------MWNTSDTGwaksawssVFSPWT--QGACVfaHYLPRFDSTSILQTLSKFPITVF 317
Cdd:cd17631 123 L-LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTllRGGTV--VILRKFDPETVLDLIERHRVTSF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGK 394
Cdd:cd17631 192 FLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 395 PSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDV 474
Cdd:cd17631 271 PVFFVEVRIVDPDGREVPPGEVGEIVV-----RGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 475 ILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIE 554
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED-----ELIAHCRERLARYKIPKSVE 420
|
490
....*....|...
gi 65301416 555 FIEELPKTVSGKV 567
Cdd:cd17631 421 FVDALPRNATGKI 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-573 |
2.08e-81 |
|
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: 264.01 E-value: 2.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 50 EYFNFAKDVLDqwTNTEKtgKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWL 129
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVE--GRGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSkLIVSQHSREGWGNLKEMMKYA 209
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 210 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 290 ACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYR-MLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 368
Cdd:TIGR02262 230 ATTVL-MGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 369 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRG 448
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 449 NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhd 528
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 65301416 529 qeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-567 |
4.63e-81 |
|
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: 265.59 E-value: 4.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 53 NFAKDVLDQwtNTEKTGKRLsnpAFWWVDGNGKEVR-WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLAN 131
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 132 VACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVA-AKCENLHSKLIVSqhsREG--- 198
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDDALnPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 199 ------WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 273 GWAKSAWSSVFSPWTQGACVFAHY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITSYKFNSLKHCVSAG 347
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 348 EPINPEVMEQWKKKTGLD---IYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 422
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 423 V-LPDRPFGLFThyvDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:cd17634 444 DpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301416 500 SAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 567
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHG--VEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
71-573 |
1.46e-77 |
|
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: 257.24 E-value: 1.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 71 RLSNPAFWWVDG-NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIPG--- 144
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 145 TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAKcENLHSKLIVSQH------------------SREGWGNLKEMM 206
Cdd:cd05967 143 AKELAS-----RIDDAKPKLIVTASCGIEPGKVVPYK-PLLDKALELSGHkphhvlvlnrpqvpadltKPGRDLDWSELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 207 KYASdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPW 286
Cdd:cd05967 217 AKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 287 TQGAcvfahylprfdsTSIL---------------QTLSKFPITVFCSAPTAYRMLIQND-----ITSYKFNSLKHCVSA 346
Cdd:cd05967 296 LHGA------------TTVLyegkpvgtpdpgafwRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 347 GEPINPEVMEQWKKKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 422
Cdd:cd05967 364 GERLDPPTLEWAENTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 423 vLPDRPFGLFTHYVDNP---SKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:cd05967 444 -LPLPPGCLLTLWKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 500 SAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
66-573 |
2.15e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 253.67 E-value: 2.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 66 EKTGKRL-SNPAFwwVDGngkEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK07656 12 ARAARRFgDKEAY--VFG---DQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 145 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKH 220
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 221 NELMAIYFTSGTTGPPK--MIGHTHSsfglgLSvNGRFW---LDLIASD---------------VMWNTsdtgwaksaws 280
Cdd:PRK07656 166 DDVADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 281 svfsPWTQGACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWK 359
Cdd:PRK07656 229 ----PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 360 KKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHY 435
Cdd:PRK07656 303 SELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 436 VDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 514
Cdd:PRK07656 378 YDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 65301416 515 KAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07656 458 KAYVVLKPGAEL-TEEELIAYCREHL----AKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
76-573 |
3.88e-77 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 256.61 E-value: 3.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 76 AFWWVDGNGKEVR-WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQK 151
Cdd:PRK00174 85 AIIWEGDDPGDSRkITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 152 DILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIVS--------QHSREGWGNlkEMMKYASDSHT 214
Cdd:PRK00174 161 ALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 215 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA 294
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 295 HY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQ---NDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---I 366
Cdd:PRK00174 319 FEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGErcpI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 367 YEGYGQTET--VLIC---GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpDRPFglfthyvdnPS- 440
Cdd:PRK00174 399 VDTWWQTETggIMITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPW---------PGm 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 441 ------------KTA-STLRGNfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPD 507
Cdd:PRK00174 463 mrtiygdherfvKTYfSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 508 PIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
83-567 |
1.50e-76 |
|
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: 250.98 E-value: 1.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 83 NGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05911 7 TGKE--LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 163 KCIITDDTLAPAVdIVAAKCENLHSKLIVSQHSREGWGNLKEMMK---YASDSH--TCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:cd05911 84 KVIFTDPDGLEKV-KEAAKELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 238 MIGHTHSSFGLGL-SVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWtQGACVfaHYLPRFDSTSILQTLSKFPITV 316
Cdd:cd05911 163 GVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATV--IIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGK 394
Cdd:cd05911 240 LYLVPPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 395 PSPAFNVEILDENG-TILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSD 472
Cdd:cd05911 320 LLPNVEAKIVDDDGkDSLGPNEPGEICV-----RGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeqlkKEIQEHVKKTTAPYKYPRK 552
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*.
gi 65301416 553 -IEFIEELPKTVSGKV 567
Cdd:cd05911 470 gVVFVDEIPKSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-577 |
7.19e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 250.65 E-value: 7.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 62 WTNTEKTGKRLSNPAFWWVDGNgkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVL 141
Cdd:PRK08314 13 FHNLEVSARRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 142 IPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVD-----------IVAAKCENLHSK-------LIVSQHSRE-----G 198
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVApavgnlrlrhvIVAQYSDYLPAEpeiavpaWLRAEPPLQalapgG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 199 WGNLKEMMK--YASDSHTcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSD----T 272
Cdd:PRK08314 169 VVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 273 GWAKSAWSSVFSpwtqGACVFahYLPRFDSTSILQTLSKFPITVFCSAPTayrMLI----QNDITSYKFNSLKHCVSAGE 348
Cdd:PRK08314 245 GMVHSMNAPIYA----GATVV--LMPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 349 PINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSpaFNVE--ILD-ENGTILPPGQEGDIAV--- 421
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPT--FGVDarVIDpETLEELPPGEVGEIVVhgp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 422 QVlpdrpfglFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSI 497
Cdd:PRK08314 393 QV--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 498 AESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-478 |
1.45e-75 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 246.07 E-value: 1.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 82 GNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 162 SKCIITDDTL-APAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSH-TCVDTKHNELMAIYFTSGTTGPPKMI 239
Cdd:pfam00501 94 AKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHTH---SSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPIT 315
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 391
Cdd:pfam00501 254 VLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 392 MGKPSPAFNVEILDEN-GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVA 469
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV-----RGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 65301416 470 RSDDVILSS 478
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-572 |
8.33e-75 |
|
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: 244.70 E-value: 8.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 169
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 tlapavdivaakcenlHSKLivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 329
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 330 N-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD-EN 407
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 408 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 483
Cdd:cd05935 270 GRELPPNEVGEIVV-----RGPQIFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 484 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTV 563
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 65301416 564 SGKVKRNEL 572
Cdd:cd05935 422 SGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-573 |
4.17e-73 |
|
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: 239.89 E-value: 4.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 DdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPK--MIGHTHSS 245
Cdd:cd05934 82 D------------------------------------------------------PASILYTSGTTGPPKgvVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FGLGLSVNgrfWLDLIASDVMW--------NTSDTGWAkSAWSSvfspwtQGACVFahyLPRFDSTSILQTLSKFPITVF 317
Cdd:cd05934 108 FAGYYSAR---RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLI-QNDITSYKFNSLKHCVSAgePINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPS 396
Cdd:cd05934 175 NYLGAMLSYLLaQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 397 PAFNVEILDENGTILPPGQEGDIAVQvlPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVIL 476
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 477 SSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHVKKTTAPYKYPRKIEFI 556
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL-DPE----ELFAFCEGQLAYFKVPRYIRFV 405
|
490
....*....|....*..
gi 65301416 557 EELPKTVSGKVKRNELR 573
Cdd:cd05934 406 DDLPKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-574 |
5.34e-73 |
|
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: 240.27 E-value: 5.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIit 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 ddtLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHTHSSfg 247
Cdd:cd05941 89 ---LDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 248 lglsvngrfwldlIASDVMWNTSDTGWAKS--------------AWSSVFSP-WTQGACVFahyLPRFDSTSILQTLSKF 312
Cdd:cd05941 114 -------------LAANVRALVDAWRWTEDdvllhvlplhhvhgLVNALLCPlFAGASVEF---LPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 313 PITVFCSAPTAYRMLIQ---------NDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGN-F 382
Cdd:cd05941 178 SITVFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 383 KGmKIKPGSMGKPSPAFNVEILDENGT-ILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG-NFYITGDRGYMD 460
Cdd:cd05941 258 DG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQV-----RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 461 EDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKkeiqEH 539
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 65301416 540 VKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
84-576 |
2.67e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 231.08 E-value: 2.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06710 47 GKDI--TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITDDTLAPAVDIV--AAKCENL-----------------------HSKLIV---SQHSREGWGNLKEmmkyasDSHTC 215
Cdd:PRK06710 124 VILCLDLVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVkvsESETIHLWNSVEK------EVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 216 VDT---KHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLdliasdvmWNTSDTGWAKSAWSSVFSPWTQGAC- 291
Cdd:PRK06710 198 VEVpcdPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVm 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 292 ---VFAHY----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDI-TSYKFNSLKHCVSAGEPINPEVMEQWKKKTG 363
Cdd:PRK06710 269 nlsIMQGYkmvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 364 LDIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQVlPDrpfgLFTHYVDNPSK 441
Cdd:PRK06710 349 GKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG-PQ----IMKGYWNKPEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 442 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:PRK06710 424 TAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 522 pdyklHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK06710 504 -----EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
53-573 |
4.94e-68 |
|
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: 231.61 E-value: 4.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 53 NFAKDVLDQWTNTEKTgkrlsNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANV 132
Cdd:cd05968 61 NIVEQLLDKWLADTRT-----RPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 133 ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLhSKLIVSQHSregwGNLK 203
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTV-EKVVVVRHL----GNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 204 EMMKYASDSHTCVDTKH----------NELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTG 273
Cdd:cd05968 210 TPAKGRDLSYDEEKETAgdgaerteseDPLMIIY-TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 274 WAKSAWsSVFSPWTQGACVFAHY-LPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLI---QNDITSYKFNSLKHCVSAGE 348
Cdd:cd05968 289 WMMGPW-LIFGGLILGATMVLYDgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 349 PINPEVMeQWKKKTGLD----IYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPgQEGDIAVQ- 422
Cdd:cd05968 368 PWNPEPW-NWLFETVGKgrnpIINYSGGTEISgGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLa 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 423 VLPDRPFGLF---THYVDnpskTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:cd05968 446 PWPGMTRGFWrdeDRYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 500 SAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
88-573 |
1.33e-65 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 222.44 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 DDTLAPAVDIVAAKCENLHskliVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK--M------- 238
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlshgnll 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 239 -----------------------IGHTHssfGLGLSVNGRfwldLIAsdvmwntsdtgwaksawssvfspwtqGACVFah 295
Cdd:PRK07514 183 snaltlvdywrftpddvlihalpIFHTH---GLFVATNVA----LLA--------------------------GASMI-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 296 YLPRFDSTSILQTLSKfpITVFCSAPTAY-RMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE 374
Cdd:PRK07514 228 FLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 375 TVLICGN-FKGMKIkPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdrpfG--LFTHYVDNPSKTASTLRGN- 449
Cdd:PRK07514 306 TNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADg 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQ 529
Cdd:PRK07514 378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAL-DE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 65301416 530 EQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07514 457 AAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
89-573 |
5.24e-65 |
|
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: 220.65 E-value: 5.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 D----------------TLAPAVDivAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDshtcvdtkhneLMAIYFTSGT 232
Cdd:cd05926 94 KgelgpasraasklglaILELALD--VGVLIRAPSAESLSNLLADKKNAKSEGVPLPDD-----------LALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 233 TGPPKMIGHTHssfgLGLSVNGRFwldlIASDVMWNTSDT-----------GWAKSAWSSVFSpwtQGACVFAhylPRFD 301
Cdd:cd05926 161 TGRPKGVPLTH----RNLAASATN----ITNTYKLTPDDRtlvvmplfhvhGLVASLLSTLAA---GGSVVLP---PRFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 302 STSILQTLSKFPITVFCSAPTAYRMLIQNDITSY--KFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV--L 377
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 378 ICGNFKGMKIKPGSMGKPspaFNVE--ILDENGTILPPGQEGDIAVQ---VlpdrpfglfTH-YVDNPSKTA-STLRGNF 450
Cdd:cd05926 307 TSNPLPPGPRKPGSVGKP---VGVEvrILDEDGEILPPGVVGEICLRgpnV---------TRgYLNNPEANAeAAFKDGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 530
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV---- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 65301416 531 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05926 451 -TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
85-573 |
9.19e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 217.88 E-value: 9.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 85 KEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IITDDTLAPAVDIVAAKCENLHSKLIVS---QHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 242 THSSFgLGLSVNGRFWLDLIASDVMWNtsdtgwA----KSAWSSVF-SPWTQ-GACVfaHYLPRFDSTSILQTLSKFPIT 315
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRMLIQN-DITSYKFNSLKHCVSaGEPINP-EVMEQWKKK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 387
Cdd:PRK08316 263 SFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 388 KPGSMGKPspAFNVE--ILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYF 465
Cdd:PRK08316 339 RPGSAGRP--VLNVEtrVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 466 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTA 545
Cdd:PRK08316 412 TVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATV-----TEDELIAHCRARLA 486
|
490 500
....*....|....*....|....*...
gi 65301416 546 PYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
73-572 |
5.04e-62 |
|
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: 212.87 E-value: 5.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 73 SNPAFwwVDG-NGKEVrwSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQK 151
Cdd:cd05904 20 SRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 152 DILYRLQSSKSKCIITDDTLAPavdivaaKCENLHSKLI-VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTS 230
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAE-------KLASLALPVVlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 231 GTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDLIASDVMwntsdtGWAKSAWSSVFSpwtqGACVFAhyLPR 299
Cdd:cd05904 168 GTTGRSKgvMLTHrnliamvaqFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATVVV--MPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT-SYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTET-- 375
Cdd:cd05904 236 FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTEStg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 376 -VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI- 452
Cdd:cd05904 316 vVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATIDKEGWLh 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 453 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQl 532
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL--TED- 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 65301416 533 kkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd05904 468 --EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-577 |
5.34e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 210.15 E-value: 5.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGNGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 160 SKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKE----MMKYASDSHTCVDtkhneLMAiyFTSGTTGP 235
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEalaaQPDTPIADETAGA-----DML--YSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 236 PKMI------GHTHSSFGLGLSVNGRFwldliasdvMWNTSDTGWAKSA--WSSVFSPWTQGACVFAH---YLPRFDSTS 304
Cdd:PRK08276 155 PKGIkrplpgLDPDEAPGMMLALLGFG---------MYGGPDSVYLSPAplYHTAPLRFGMSALALGGtvvVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 305 ILQTLSKFPITVFCSAPTAY-RML-IQNDI-TSYKFNSLKHCVSAGEPINPEVMEQ----WkkktGLDIYEGYGQTE--- 374
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLkLPEEVrARYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEggg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 375 -TVLICGNFKGmkiKPGSMGKPSPAfNVEILDENGTILPPGQEGDIAVQvLPDRPFglftHYVDNPSKTASTLRGNFYIT 453
Cdd:PRK08276 302 vTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 454 -GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQL 532
Cdd:PRK08276 373 vGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDAL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 65301416 533 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:PRK08276 451 AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYW 495
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-574 |
3.69e-59 |
|
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: 202.58 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEEL----GSLSRKFANILTeacslQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05912 2 YTFAELfeevSRLAEHLAALGV-----RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 iitDDTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHT-- 242
Cdd:cd05912 77 ---DDI-----------------------------------------------------ATIMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 243 -H------SSFGLGLSVNGRfWLDLIAsdvMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTLSKFPIT 315
Cdd:cd05912 101 nHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRMLIQNDITSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 393
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 394 KPSPAFNVEILDENGtilPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 470
Cdd:cd05912 246 KPLFPVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDR 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 471 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKttapYKYP 550
Cdd:cd05912 315 RSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKVP 387
|
490 500
....*....|....*....|....
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05912 388 KKIYFVDELPRTASGKLLRHELKQ 411
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
70-574 |
2.62e-57 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 202.87 E-value: 2.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 70 KRLSNPAFWWVDGN-GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPG- 144
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 145 -TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAK------CENLHSK----LIVSQhsregwgNLKEMMK------ 207
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSRGGKVVPYKplldeaIALAQHKprhvLLVDR-------GLAPMARvagrdv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 208 -YAS------DSHT-CVDTKHNELMAIYFTSGTTGPPKMI-----GHThssFGLGLSVNGRFwlDLIASDVMWNTSDTGW 274
Cdd:PRK10524 212 dYATlraqhlGARVpVEWLESNEPSYILYTSGTTGKPKGVqrdtgGYA---VALATSMDTIF--GGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 275 AKSAWSSVFSPWTQG-ACVFAHYLP-RFDSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITSYKFNSLKHCVSAGEP 349
Cdd:PRK10524 287 VVGHSYIVYAPLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 350 INpEVMEQWKKKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDEN-GTILPPGQEGDIAVQV 423
Cdd:PRK10524 367 LD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 424 -LPdrPFGLFTHYVDNP---SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:PRK10524 446 pLP--PGCMQTVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301416 500 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQ---LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVkrneLRR 574
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRR 597
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-574 |
3.96e-57 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 199.70 E-value: 3.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSqhsregwgnLKEMMKYASDShtCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSFGLGlSVNGRFWLDLIASDV------MWNTSDTGWAksawssVFSPWTQGACVFahyLP-RFDSTSILQTLSKFPITV 316
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVII---VPrKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET-----VLICGNFKGmkiKPG 390
Cdd:PRK06839 242 VMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 470
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLI-----RGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 471 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL-----IEKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|....
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-580 |
6.15e-57 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 199.98 E-value: 6.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 242 THSSFglglsvngrFW--------LDLIASDVMWNTSDTgWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFP 313
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 314 ITVFCSAPTAYRMLIQNDIT-SYKFNSLKHCVSAGEPinPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 392
Cdd:PRK06155 269 ATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 GKPSPAFNVEILDENGTILPPGQEGDIAVQVlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 472
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRK 552
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV-----ALVRHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|....*...
gi 65301416 553 IEFIEELPKTVSGKVKRNELRRKEWTTT 580
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
80-576 |
2.34e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 197.11 E-value: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGNGKevrWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK03640 22 EFEEKK---VTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 160 SKSKCIITDDTLApavdivaakcenlhSKLIVSQHSRegwgnLKEMMKYASDSHTCVDTKH-NELMAIYFTSGTTGPPKM 238
Cdd:PRK03640 98 AEVKCLITDDDFE--------------AKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 239 I-----GHTHSSFG----LGLSVNGRfWLdliASDVMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTL 309
Cdd:PRK03640 159 ViqtygNHWWSAVGsalnLGLTEDDC-WL---AAVPIFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 310 SKFPITVFCSAPTAY-RMLIQNDITSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICG-NFKGMK 386
Cdd:PRK03640 226 QTGGVTIISVVSTMLqRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 387 IKPGSMGKPspAFNVEI-LDENGTILPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDED 462
Cdd:PRK03640 304 TKLGSAGKP--LFPCELkIEKDGVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDGWFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 463 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpDYKLhDQEQLKKEIQEHVkk 542
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEV-TEEELRHFCEEKL-- 448
|
490 500 510
....*....|....*....|....*....|....
gi 65301416 543 ttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK03640 449 --AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
90-572 |
1.38e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 196.80 E-value: 1.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK06178 60 TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVAAKCEnLHSKLIVSQH--------------------SREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT 229
Cdd:PRK06178 139 QLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 230 SGTTGPPKMIGHTH-------SSFGlGLSVNGRfwldliASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDS 302
Cdd:PRK06178 218 GGTTGMPKGCEHTQrdmvytaAAAY-AVAVVGG------EDSVFLSFLPEFWIAGENFGLLFPLFSGATLV--LLARWDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 303 TSILQTLSKFPITVfcsapTAyrMLIQN--------DITSYKFNSLKH--CVSAGEPINPEVMEQWKKKTGLDIYEG-YG 371
Cdd:PRK06178 289 VAFMAAVERYRVTR-----TV--MLVDNavelmdhpRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTETvLICGNF-KGM-------KIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKT 442
Cdd:PRK06178 362 MTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVV-----RTPSLLKGYWNKPEAT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 443 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 522
Cdd:PRK06178 436 AEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 65301416 523 DYKLhDQEQLKKEIQEHVkkttAPYKYPrKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK06178 516 GADL-TAAALQAWCRENM----AVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
297-569 |
7.39e-55 |
|
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: 188.63 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 297 LPRFDSTSILQTLSKFPITVFCS-APTAYRMLIQNDITSYKFNSLKHcVSAGEpiNPEVMEQWKKKTGLDIYEGYGQTET 375
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 376 ---VLICGNFKgmkiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI 452
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 453 TGDRGYMDEDGYFWFVARS--DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqe 530
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT--- 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 65301416 531 qlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:cd17637 297 --ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-573 |
5.83e-54 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 192.16 E-value: 5.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVD-----------IVAAKCENLHSK-LIVSQHSRegwgNLKEMM----------------KYASDSHTCVDTKHN 221
Cdd:PRK07059 129 NFATTVQqvlaktavkhvVVASMGDLLGFKgHIVNFVVR----RVKKMVpawslpghvrfndalaEGARQTFKPVKLGPD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 222 ELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSdtgWAKSAWSS---VFSPWTQGAC----VFA 294
Cdd:PRK07059 205 DVAFLQYTGGTTGVSKGATLLHRN---------------IVANVLQMEA---WLQPAFEKkprPDQLNFVCALplyhIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 295 ---HYL--------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVME 356
Cdd:PRK07059 267 ltvCGLlgmrtggrnilipnPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 357 QWKKKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfgl 431
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIrgpQVMAG----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 432 fthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 510
Cdd:PRK07059 420 ---YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 65301416 511 GEVVKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07059 497 GEAVKLFVVKK------DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-572 |
1.14e-53 |
|
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: 188.89 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGNGkevRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05930 7 VDGDQ---SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 160 SKSKCIITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 239
Cdd:cd05930 83 SGAKLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKF 312
Cdd:cd05930 112 MVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 313 PITVFCSAPTAYRMLIQNDITSyKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF--KGMKIKP 389
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYrvPPDDEED 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 390 GSM--GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMD 460
Cdd:cd05930 263 GRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI-----GGAGLARGYLNRPELTAERFVPNpfgpgerMYRTGDLVRWL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 461 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHV 540
Cdd:cd05930 338 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD-----EEELRAHL 412
|
490 500 510
....*....|....*....|....*....|..
gi 65301416 541 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd05930 413 AERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-573 |
1.50e-53 |
|
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: 189.43 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLApavdivaakcenlHSKLIVSQHSREGWgnlkemmKYASDSHtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12118 106 FVDREFE-------------YEDLLAEGDPDFEW-------IPPADEW--------DPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FglglsvngrfWLDLIASDVMWNTSD-------------TGWAksawssvfSPWTQGACVFAHY-LPRFDSTSILQTLSK 311
Cdd:cd12118 158 A----------YLNALANILEWEMKQhpvylwtlpmfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 312 FPITVFCSAPTAYRMLIQ-NDITSYKFNSLKHCVSAGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICgnfkgmKI 387
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVC------AW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 388 KPGSMGKPSP---------------AFNVEILDENGTILPP--GQE-GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 449
Cdd:cd12118 293 KPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPrdGKTiGEIVF-----RGNIVMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQ 529
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 65301416 530 eqlkkEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELR 573
Cdd:cd12118 448 -----EIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLR 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
57-573 |
3.65e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 190.60 E-value: 3.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 57 DVLDQwtNTEKTGKRlsnPAFWWVdgnGKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK05605 36 DLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 137 TGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP---------------AVDIVAA------------------KCE 183
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAAmpllqrlalrlpipalrkARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 184 NLHSKL-------IVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSsfglGLSVN--- 253
Cdd:PRK05605 185 ALTGPApgtvpweTLVDAAIGGDGSDVSHPRPTPDD----------VALILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 254 GRFWLDLIASD----------------VMWNTsdtgwaksawssvFSPWTQGACVFahyLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLIQN------DITSYKfNSLkhcvSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPG 390
Cdd:PRK05605 315 PGVPPLYEKIAEAaeergvDLSGVR-NAF----SGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 SMGKPSPAFNVEILD-EN-GTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYF 465
Cdd:PRK05605 390 YVGVPFPDTEVRIVDpEDpDETMPDGEEGELLVrgpQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 466 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTA 545
Cdd:PRK05605 462 RIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL-DPEGLR----AYCREHLT 536
|
570 580
....*....|....*....|....*...
gi 65301416 546 PYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK05605 537 RYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-578 |
7.09e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 188.66 E-value: 7.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 73 SNPAFWWVDGngkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIP-GTTQl 148
Cdd:PRK06188 27 DRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 149 tqkDILYRLQSSKSKCIITDDT--LAPAVDIvAAKCENLHSKLIVSQhSREGWGNLKEMMKYASDSHTCVDTkHNELMAI 226
Cdd:PRK06188 100 ---DHAYVLEDAGISTLIVDPApfVERALAL-LARVPSLKHVLTLGP-VPDGVDLLAAAAKFGPAPLVAAAL-PPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 227 YFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF----------AHY 296
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRS---------------IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFflptllrggtVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 297 LPRFDSTSILQTLSKFPITVFCSAPTA-YRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE- 374
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMiYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 375 ----TVLICGNFKGMKIKP-GSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 449
Cdd:PRK06188 319 pmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlHDQ 529
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAA-VDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 65301416 530 EqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWT 578
Cdd:PRK06188 473 A----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
84-575 |
1.32e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 188.45 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVRWSfeELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSfglglsVNGRFwLDLIASDVMWNTSDTGWAKS------AWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPIT-V 316
Cdd:PRK07786 197 AN------LTGQA-MTCLRTNGADINSDVGFVGVplfhiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCsAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKGMKIkpGS 391
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEmspvTCMLLGEDAIRKL--GS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 392 MGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 471
Cdd:PRK07786 347 VGKVIPTVAARVVDENMNDVPVGEVGEIVY-----RAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 472 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVkkttAPYKYPR 551
Cdd:PRK07786 422 KDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----ARYKHPK 497
|
490 500
....*....|....*....|....
gi 65301416 552 KIEFIEELPKTVSGKVKRNELRRK 575
Cdd:PRK07786 498 ALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-576 |
1.47e-52 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 188.72 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVAAKCENLHSKL--IVSQHSReGWGNL--------KEMM-KY---ASDSHTCV------------DTKHNEL 223
Cdd:PRK08974 130 NFAHTLEKVVFKTPVKHVILtrMGDQLST-AKGTLvnfvvkyiKRLVpKYhlpDAISFRSAlhkgrrmqyvkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 224 MAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWntsdtgwAKSAWSSVFSPWTQGAC-------VFAHY 296
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN---------------MLANLEQ-------AKAAYGPLLHPGKELVVtalplyhIFALT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 297 L-----------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQW 358
Cdd:PRK08974 267 VncllfielggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNeEFQELDFSSLKLSVGGGMAVQQAVAERW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 359 KKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLpdrpfglfTH 434
Cdd:PRK08974 346 VKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVkgpQVM--------LG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 435 YVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 514
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 515 KAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK08974 498 KIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
67-573 |
4.90e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 186.40 E-value: 4.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 67 KTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 145
Cdd:PRK07470 15 QAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 146 TQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKL-IVSQHSREGWGNLkeMMKYASDSHTCVDTKHNELM 224
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVaIGGARAGLDYEAL--VARHLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 225 AIYFTSGTTGPPKMIGHTHSSfgLGLSVNGRFwldliaSDVMWNTSDTGWaksawSSVFSPWTQGACVfaHYL------- 297
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL------ADLMPGTTEQDA-----SLVVAPLSHGAGI--HQLcqvarga 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 -------PRFDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEG 369
Cdd:PRK07470 232 atvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 370 YGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYVDNPSK 441
Cdd:PRK07470 312 FGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 442 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:PRK07470 387 NAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 65301416 522 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07470 467 DGAPVDEA-----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
81-573 |
2.04e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.50 E-value: 2.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 81 DGNGKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEW---WLAnVACLrtGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK08008 30 SSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMVPINARLLREESAWIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 158 QSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSqhsREGWGNLKEMMKYAS--DSHTCVDTKHNELMA-----IYFTS 230
Cdd:PRK08008 106 QNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT---RVALPADDGVSSFTQlkAQQPATLCYAPPLSTddtaeILFTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 231 GTTGPPKMIGHTHSsfglglsvNGRF------W-LDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDST 303
Cdd:PRK08008 183 GTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL--LEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 304 SILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNslkHCVSagepinpEVM------EQWK----KKTGLDIYEGYGQT 373
Cdd:PRK08008 253 AFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ---HCLR-------EVMfylnlsDQEKdafeERFGVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 374 ETVL-ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPfgLFTHYVDNPSKTASTLRGNFYI 452
Cdd:PRK08008 323 ETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYLDPKATAKVLEADGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 453 -TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeq 531
Cdd:PRK08008 401 hTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE-- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 65301416 532 lkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK08008 479 ---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
88-573 |
2.59e-51 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 182.20 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKipeWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPN---WWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IITDDTlapavdivaakcenlhsklivsqhsregWGNlkemMKYASDShtcvdtkhNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 SfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:cd05903 117 T----LSASIRQYAERLGlgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 TayrmLIQNDITSYKF-----NSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNfkgmkIKPG------ 390
Cdd:cd05903 191 P----FLTDLLNAVEEageplSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrl 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 -SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 469
Cdd:cd05903 262 yTDGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 470 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV-KKTTAPYK 548
Cdd:cd05903 337 RSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL-TFD----ELVAYLdRQGVAKQY 411
|
490 500
....*....|....*....|....*
gi 65301416 549 YPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05903 412 WPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
90-573 |
1.76e-50 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 182.77 E-value: 1.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVAAKCE---------------------NL---HSKLIVSQHSREGWGNLKEMMKYASdSHTC--VDTKHNEL 223
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 224 MAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRfWLD-----------LIASDVMWNTsdtgWAKSAWSSVFSPWtqGACV 292
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAgtgkleegcevVITALPLYHI----FALTANGLVFMKI--GGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 293 FAHYLPRfDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 371
Cdd:PRK08751 284 HLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLR 447
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIkgpQVMKG--------YWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykl 526
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK----- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 65301416 527 hDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK08751 510 -DPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-573 |
2.01e-50 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 177.47 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSFglglsVNGRFwldlIASDVMWNTSDT------------GWAKSAWSSVfspwTQGA-CV 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI-----VNNGY----FIGERLGLTEQDrlcipvplfhcfGSVLGVLACL----THGAtMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 293 FAHylPRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGY 370
Cdd:cd05917 74 FPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETVLICgnFKGMKIKP-----GSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 444
Cdd:cd05917 152 GMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCI-----RGYSVMKGYWNDPEKTAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLRG-NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 523
Cdd:cd05917 225 AIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 65301416 524 YKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05917 305 AELTEE-----DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-573 |
2.58e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 182.28 E-value: 2.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 I------TDDTLAPAVDIV---------AAKCENL-HSKLIVSQHSRE-----GWGNLKEMMKYASDSHTCVDT---KHN 221
Cdd:PRK12583 122 IcadafkTSDYHAMLQELLpglaegqpgALACERLpELRGVVSLAPAPppgflAWHELQARGETVSREALAERQaslDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 222 ELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRF---WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahyLP 298
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV---YP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 R--FDSTSILQTLSKFPITVFCSAPTayrMLIQN----DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYG 371
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPT---MFIAEldhpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTET---VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG 448
Cdd:PRK12583 352 MTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT-----RGYSVMKGYWNNPEATAESIDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 449 NFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 527
Cdd:PRK12583 427 DGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 65301416 528 DQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK12583 507 EE-----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-576 |
4.63e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 182.85 E-value: 4.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 87 VRWSFEELgsLSR--KFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVlIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:PRK07529 57 ETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IIT-----DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLK--------------------EMMKYASDSHTCVDTK 219
Cdd:PRK07529 133 LVTlgpfpGTDIWQKVAEVLAALPEL--RTVVEVDLARYLPGPKrlavplirrkaharildfdaELARQPGDRLFSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 220 HNELMAIYF-TSGTTGPPKMIGHTHSsfglGLSVNGrfWLdlIASDVMWNTSDTGWA-------KSAWSSVFSPWTQGA- 290
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WL--GALLLGLGPGDTVFCglplfhvNALLVTGLAPLARGAh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 291 CVFA--------HYLPRFdsTSILQtlsKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKT 362
Cdd:PRK07529 283 VVLAtpqgyrgpGVIANF--WKIVE---RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 363 GLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEI--LDENGTIL---PPGQEGDIAVQvlpdRPfGLFTHYV 436
Cdd:PRK07529 358 GVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIA----GP-NVFSGYL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 437 DNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 516
Cdd:PRK07529 433 EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 517 FIVLNPDYKLhDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK07529 513 YVQLKPGASA-TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
88-577 |
1.21e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 177.63 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 D-------------------DTLAPAVDIVAAKCEnlHSKLIVSQhsregwgnlkEMMKYASDSHTCvDTKHNELMAIYF 228
Cdd:PRK06087 128 PtlfkqtrpvdlilplqnqlPQLQQIVGVDKLAPA--TSSLSLSQ----------IIADYEPLTTAI-TTHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPKMIGHTHSSFGLG-LSVNGRfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDSTSILQ 307
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 308 TLSKFPITVFCSA-PTAYRMLIQNDITSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETV--LICGNFKG 384
Cdd:PRK06087 271 LLEQQRCTCMLGAtPFIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNLDDP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 385 MKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTL--RGNFYiTGDRGYMDED 462
Cdd:PRK06087 350 LSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRMDEA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 463 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEqlkkEIQEHV-K 541
Cdd:PRK06087 424 GYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLE----EVVAFFsR 499
|
490 500 510
....*....|....*....|....*....|....*.
gi 65301416 542 KTTAPYKYPRKIEFIEELPKTVSGKVKRNELrRKEW 577
Cdd:PRK06087 500 KRVAKYKYPEHIVVIDKLPRTASGKIQKFLL-RKDI 534
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-573 |
1.21e-48 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 175.71 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 111 LQRGDRVMVILPKIPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYrlqsskskcIITDdtLAPAVDIVAAKCENlH 186
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRY---------LVAD--AGGRIVLADAGAAD-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 187 SKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRfwLDLIASDV 265
Cdd:cd05922 83 LRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 266 MWNTSDTGWAkSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVS 345
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 346 AGEPINPEVMEQWKKK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQE 416
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 417 GDIAVQvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPS 496
Cdd:cd05922 313 GEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 497 IAESAVVSSPDPIrGEVVKAFIVLNPDYKLHDqeqlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05922 389 IIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-573 |
1.36e-48 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 176.67 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 81 DGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILpkipeW--------WLAnVAClrTGTVLIPGTTQLTQKD 152
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA-----WnthrhlelYYA-VPG--MGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 153 ILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSR------EGWGNLKEMMKYASDSHTCVDTKHNELMAI 226
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRFWLDLIASDV------MWNTSdtgwaksAWSSVFSPWTQGACvfaHYLP- 298
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAK---LVLPg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 -RFDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET- 375
Cdd:cd12119 239 pYLDPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 376 -VLICGnfkgmKIKPG--------------SMGKPSPAFNVEILDENGTILP--PGQEGDIAVQvlpdRPFgLFTHYVDN 438
Cdd:cd12119 318 pLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVR----GPW-VTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 439 PSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 518
Cdd:cd12119 388 DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 519 VLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd12119 468 VLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
90-578 |
1.65e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 176.42 E-value: 1.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVAAKCENLHSKLIVSQH-SREGWGNLKEMMKYASDshTCVDTKhNELMAIYFTSGTTGPPKMIGHTHSSFGL 248
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDgELEGFVGYAEAVAGLPA--TPIADE-SLGTDMLYSSGTTGRPKGIKRPLPEQPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 249 GLSVNgrfWLDLIASdvMWN-TSDTGW---------AKSAWSSVfspwTQ--GACVFAhyLPRFDSTSILQTLSKFPITV 316
Cdd:PRK13391 182 DTPLP---LTAFLQR--LWGfRSDMVYlspaplyhsAPQRAVML----VIrlGGTVIV--MEHFDAEQYLALIEEYGVTH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCSAPTAY-RML-IQNDI-TSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICG-NFKGMKIKPGSM 392
Cdd:PRK13391 251 TQLVPTMFsRMLkLPEEVrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 GKPSPAfNVEILDENGTILPPGQEGDIAVQvlPDRPFglftHYVDNPSKTASTL--RGNFYITGDRGYMDEDGYFWFVAR 470
Cdd:PRK13391 331 GRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 471 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PRK13391 404 AAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD--GVDPGPALAAELIAFCRQRLSRQKCP 481
|
490 500
....*....|....*....|....*...
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELRRKEWT 578
Cdd:PRK13391 482 RSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-576 |
1.56e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 174.57 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 53 NFAKDV----------LDQWTNT----EKTGKRLSN-PAFWWVdgnGKEVRWSfeELGSLSRKFANILTEACSLQRGDRV 117
Cdd:PRK05677 4 NFWKDKypagiaaeinPDEYPNIqavlKQSCQRFADkPAFSNL---GKTLTYG--ELYKLSGAFAAWLQQHTDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 118 MVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLA-------PAVDI---VAAKCENLHS 187
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAhlaekvlPKTGVkhvIVTEVADMLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 188 ---------------KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsfglglsv 252
Cdd:PRK05677 159 plkrllinavvkhvkKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 253 ngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSP--------WTQGaCVF-----AHYL----PRfDSTSILQTLSKFPIT 315
Cdd:PRK05677 231 ------NLVANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFH-CMAmmligNHNIlisnPR-DLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMG 393
Cdd:PRK05677 303 GFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 394 KPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVA 469
Cdd:PRK05677 382 IPVPSTLCKVIDDDGNELPLGEVGELCVkgpQVMKG--------YWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 470 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTAPYKY 549
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETL-TKEQVM----EHMRANLTGYKV 528
|
570 580
....*....|....*....|....*..
gi 65301416 550 PRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-573 |
2.70e-47 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 172.89 E-value: 2.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 169
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 tlAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvDTKHNELMaiYFTSGTTGPPKMI-----GHTHS 244
Cdd:PRK13390 103 --SAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT--EQPCGAVM--LYSSGTTGFPKGIqpdlpGRDVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKS-AWSSVFSPwTQGACVFAHylpRFDSTSILQTLSKFPITVFCSAPTA 323
Cdd:PRK13390 177 APGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVTQMVPTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 324 Y-RMLIQND--ITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVLICGNFKGmkiKPGSMGKpS 396
Cdd:PRK13390 253 FvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPGSVGR-S 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 397 PAFNVEILDENGTILPPGQEGDIAVQvlPDR-PFglftHYVDNPSKTASTLRGN--FYIT-GDRGYMDEDGYFWFVARSD 472
Cdd:PRK13390 329 VLGDLHICDDDGNELPAGRIGTVYFE--RDRlPF----RYLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYLYLADRKS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRK 552
Cdd:PRK13390 403 FMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEG--IRGSDELARELIDYTRSRIAHYKAPRS 480
|
490 500
....*....|....*....|.
gi 65301416 553 IEFIEELPKTVSGKVKRNELR 573
Cdd:PRK13390 481 VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
226-575 |
3.84e-47 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 173.02 E-value: 3.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKmiGHTHSSFGlGLSVngrfwldliASDVMwntSDTGWAKSAWSSVFSP----WTQGACVFAHYLP--- 298
Cdd:PRK13382 201 ILLTSGTTGTPK--GARRSGPG-GIGT---------LKAIL---DRTPWRAEEPTVIVAPmfhaWGFSQLVLAASLActi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 ----RFDSTSILQTLSKFPITVFCSAPTAYRMLIQ---NDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 371
Cdd:PRK13382 266 vtrrRFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVdnPSKTASTLRGnF 450
Cdd:PRK13382 346 ATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-F 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 530
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASA---- 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 65301416 531 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 575
Cdd:PRK13382 494 -TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
75-572 |
7.63e-47 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 170.51 E-value: 7.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 75 PAFWWvdgngKEVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKdil 154
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 155 yRLQSskskcIItdDTLAPAVDIVAAkcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTG 234
Cdd:cd05945 79 -RIRE-----IL--DAAKPALLIADG----------------------------------------DDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 235 PPKMIGHTHS---SFGLGLsvNGRFwlDLIASDVMWNTSDtgwaksaWS---SVFS---PWTQGACVFAhyLPR---FDS 302
Cdd:cd05945 111 RPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VPRdatADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 303 TSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVLICg 380
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAV- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 381 nfKGMKIKPGSM--------GKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTLRGN 449
Cdd:cd05945 257 --TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVIsgpSV--------SKGYLNNPEKTAAAFFPD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 F----YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyk 525
Cdd:cd05945 327 EgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP--- 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 65301416 526 lHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd05945 404 -GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
76-574 |
9.47e-47 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 174.32 E-value: 9.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 76 AFWWvDGN--GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDI 153
Cdd:PLN02654 107 AIYW-EGNepGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 154 LYRLQSSKSKCIITDDTLAPAV------DIV-AAKCENLHSKLIV---------SQHSREG--WGNLKEMM------KYA 209
Cdd:PLN02654 185 AQRIVDCKPKVVITCNAVKRGPktinlkDIVdAALDESAKNGVSVgicltyenqLAMKREDtkWQEGRDVWwqdvvpNYP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 210 SDSHTCVDTKHNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:PLN02654 265 TKCEVEWVDAEDPLFLLY-TSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 290 ACVFA-HYLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITSYKFNSLKHCVSAGEPINPEVMEQWKKKTG- 363
Cdd:PLN02654 344 ATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGd 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 364 --LDIYEGYGQTETvlicGNFKGMKI------KPGSmgKPSPAFNVE--ILDENGTILPPGQEGDIAVQvlPDRPFGLFT 433
Cdd:PLN02654 424 srCPISDTWWQTET----GGFMITPLpgawpqKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLCVK--KSWPGAFRT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 434 HYVDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRG 511
Cdd:PLN02654 496 LYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKG 575
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 65301416 512 EVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PLN02654 576 QGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-574 |
2.43e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 166.50 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 220 HNELMAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRFWLDliasDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAH 295
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEvynAWMLALNSLFDPD----DVLLCGLPLFHVNGSVVTLLTPLASGAhVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 296 YLPRFDST---SILQTLSKFPITVFCSAPTAYRMLIQNDITSyKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQ 372
Cdd:cd05944 77 PAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 373 TE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGT---ILP--PGQEGDIAVQvlpdRPfGLFTHYVDNPSKTASTL 446
Cdd:cd05944 156 TEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrlLRDcaPDEVGEICVA----GP-GVFGGYLYTEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 526
Cdd:cd05944 231 ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 65301416 527 hDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05944 311 -EEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-576 |
4.30e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 170.49 E-value: 4.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMViLPKIPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKSK 163
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVAV-LARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITDDTLAPAVDIVAAKCENLHSkLIVS----QHSREGWGNLKEMMKYASDSHTCVDTKHNELmaIYFTSGTTGPPKMI 239
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRA-WGGNpdddEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHTHSSfglGLSVNGRFwLDLI---ASDVMWNTS----DTGWAKSAWSsvfspWTQGACVFAHYlpRFDSTSILQTLSKF 312
Cdd:PRK07788 226 PRPEPS---PLAPLAGL-LSRVpfrAGETTLLPApmfhATGWAHLTLA-----MALGSTVVLRR--RFDPEATLEDIAKH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 313 PITVFCSAPTAY-RML--IQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVlicGNFKGM 385
Cdd:PRK07788 295 KATALVVVPVMLsRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 386 KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKtaSTLRGnFYITGDRGYMDEDGYf 465
Cdd:PRK07788 372 AEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 466 WFVA-RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVKKTT 544
Cdd:PRK07788 443 LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD-----EDAIKDYVRDNL 517
|
490 500 510
....*....|....*....|....*....|..
gi 65301416 545 APYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-575 |
1.25e-45 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 169.01 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 66 EKTGKRLSNPAFwwVDGNGKEVrWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 145
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 146 TQLTQKDILYRLQSSKSKCIITddtLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA 225
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSsfGLGLSV---------NgrfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhy 296
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 297 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT-SYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY-EGYGQTE 374
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVeKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 375 --TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-R 447
Cdd:PLN02246 336 agPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 527
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 65301416 528 DQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 575
Cdd:PLN02246 491 ED-----EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
298-577 |
2.39e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 167.57 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITSYKFN--SLKHCVSAGEPINPEV----MEQWkkktGLDIYEGY 370
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLKLPEEVRAKYDvsSLRHVIHAAAPCPADVkramIEWW----GPVIYEYY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTET--VLICGNFKGMKiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQV--LPDrpfglFThYVDNPSKTASTL 446
Cdd:PRK12406 304 GSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIagNPD-----FT-YHNKPEKRAEID 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 526
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 65301416 527 hDQEqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:PRK12406 457 -DEA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-573 |
1.57e-44 |
|
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: 165.78 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKceNLHSKLIVSQHSREGWGNLKEMMKYASdSHTCVD-----------TKHNELMAIYFTSGTTG 234
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTFIT-QNLPPGfneydfkppsfDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 235 PPKMIGHTHSSFGLGLSVngrfwldliASDVMWntsdtGWAKSAWSSVFS--PWTQG---------ACVFAH--YLPRFD 301
Cdd:cd17642 198 LPKGVQLTHKNIVARFSH---------ARDPIF-----GNQIIPDTAILTviPFHHGfgmfttlgyLICGFRvvLMYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 302 STSILQTLSKFPITVFCSAPTAYRMLIQNDITS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTET---V 376
Cdd:cd17642 264 EELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 377 LICGNfkgMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TG 454
Cdd:cd17642 344 LITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 455 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklHDQEQLKK 534
Cdd:cd17642 416 DIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE-----AGKTMTEK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 65301416 535 EIQEHVKKTTAPYKYPR-KIEFIEELPKTVSGKVKRNELR 573
Cdd:cd17642 491 EVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
90-573 |
1.93e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 164.67 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK06145 29 SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVaakcenlHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTkhnELMAIYFTSGTTGPPKMIGHTHSSF--- 246
Cdd:PRK06145 108 EFDAIVALE-------TPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPT---DLVRLMYTSGTTDRPKGVMHSYGNLhwk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 247 ------GLGLSVNGRFW----------LDLIASDVMWntsdtgwaksawssvfspwtQGACVFAHYlpRFDSTSILQTLS 310
Cdd:PRK06145 178 sidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------VGGTLRIHR--EFDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 311 KFPITVFCSAPTAY-RMLIQNDITSYKFNSLKHCVSAGEPiNPE--VMEQWKKKTGLDIYEGYGQTETvliCGNFKGMKI 387
Cdd:PRK06145 236 RHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSGDTLMEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 388 -----KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDED 462
Cdd:PRK06145 312 greieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM-----RGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 463 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVKK 542
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT-----LEALDRHCRQ 461
|
490 500 510
....*....|....*....|....*....|.
gi 65301416 543 TTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK06145 462 RLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-573 |
2.12e-44 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 164.09 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 225 AIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIasdvmwntsdtGWakSAWSSVFSPWT------QGACVFAHYL- 297
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLP-GGPPDNDTLMAAALGF-----------GP--GADSVYLSPAPlyhaapFRWSMTALFMg 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 ------PRFDSTSILQTLSKFPITVFCSAPTAY-RM--LIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 368
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 369 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfNVEILDENGTILPPGQEGDiaVQVLPDRPFglftHYVDNPSKTA-STL 446
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGE--VYFANGPGF----EYTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAfiVLNPDYKL 526
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 65301416 527 HDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
81-574 |
2.72e-44 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 165.23 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 81 DGNGKEVRWSFEELGSLSRKFANILTEaCSLQRGDrvmVILPKIPEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 158 QSSKSKCIItddtlAPAV----DIvAAKCENLHSKLIVSQH----SREGWGNLKEMM-----KYASDSHTCVDTKH---N 221
Cdd:PRK13295 124 KHAESKVLV-----VPKTfrgfDH-AAMARRLRPELPALRHvvvvGGDGADSFEALLitpawEQEPDAPAILARLRpgpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 222 ELMAIYFTSGTTGPPKMIGHTHSS-FGLGLSVNGRfwLDLIASDVMWNTS----DTGWAKSAwssvFSPWTQGACVFahY 296
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 297 LPRFDSTSILQTLSKFPITvFCSAPTAYRMLIQN--DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE 374
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVT-FTMASTPFLTDLTRavKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 375 TVLICGnfkgmkIKPG--------SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL 446
Cdd:PRK13295 349 NGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV-----RGCSNFGGYLKRPQLNGTDA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 526
Cdd:PRK13295 418 DG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSL 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 65301416 527 hDQEQLKKEIQEHvkKTTAPYkYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK13295 497 -DFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-502 |
9.34e-44 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 160.89 E-value: 9.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKS 162
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 163 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRegwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHT 242
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 243 HSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHY--LPRFDSTSILQTLSKFPITVFCSA 320
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPedEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 321 PTAYRMLIQNDITSykFNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGnfkgMKIKPGSM------- 392
Cdd:TIGR01733 220 PSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDaprespv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 --GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA---------STLRGNFYITGDRGYMDE 461
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYLP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 65301416 462 DGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV 502
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
89-580 |
8.23e-43 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 161.30 E-value: 8.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DTlapavdiVAAKCENLHSKLIV-SQHSREGWGNLKEMMKyASDShtCVDTKHNE------LMAIYFTSGTTGPPKMIGH 241
Cdd:PLN02330 135 DT-------NYGKVKGLGLPVIVlGEEKIEGAVNWKELLE-AADR--AGDTSDNEeilqtdLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 242 TH---------SSFGLGLSVNGRF-WLDLIASDVMWNTSDTGWAKSAwssvfspwTQGACVFahyLPRFDSTSILQTLSK 311
Cdd:PLN02330 205 THrnlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYGITGICCATLR--------NKGKVVV---MSRFELRTFLNALIT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 312 FPITVFCSAPTAYRMLIQN------DITSYKfnsLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF-- 382
Cdd:PLN02330 274 QEVSFAPIVPPIILNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgd 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 383 --KGMKI-KPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRG 457
Cdd:PLN02330 351 peKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 458 YMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdqeQLKKEIQ 537
Cdd:PLN02330 426 YIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK-----ESEEDIL 500
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 65301416 538 EHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 580
Cdd:PLN02330 501 NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-574 |
9.65e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 156.69 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKmighthssfGLGLSVNGrfwldlIASDVmwntsdTGWAKsAWSsvfspWTqGACVFAHYLP------- 298
Cdd:PRK07787 133 IVYTSGTTGPPK---------GVVLSRRA------IAADL------DALAE-AWQ-----WT-ADDVLVHGLPlfhvhgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 ------------------RFDSTSILQTLSkFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKK 360
Cdd:PRK07787 185 vlgvlgplrignrfvhtgRPTPEAYAQALS-EGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 361 KTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlpdRPFGLFTHYVDNPS 440
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 441 KTASTLRGN-FYITGDRGYMDEDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 518
Cdd:PRK07787 341 ATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 519 VLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK07787 421 VGADDVAA-------DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
64-575 |
2.96e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 154.87 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 64 NTEKTGKRlsnPAFWWVDgNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP 143
Cdd:COG1022 20 RAARFPDR---VALREKE-DGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 144 GTTQLTQKDILYRLQSSKSKCIIT-DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWG-----NLKEMMKYASDSHT--- 214
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 215 ----CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWaksawsSVFS 284
Cdd:COG1022 173 learRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 285 pWTQGACVfaHYLPRFDStsILQTLSKFPITVFCSAPtayRML--IQNDI--------------------TSYKFNS--- 339
Cdd:COG1022 246 -LAAGATV--AFAESPDT--LAEDLREVKPTFMLAVP---RVWekVYAGIqakaeeagglkrklfrwalaVGRRYARarl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 340 -------------------------------LKHCVSAGEPINPEV------MeqwkkktGLDIYEGYGQTET-VLICGN 381
Cdd:COG1022 318 agkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELarffraL-------GIPVLEGYGLTETsPVITVN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 382 FKGmKIKPGSMGKPSPafNVEI-LDENGTIL---PpgqegdiavqvlpdrpfGLFTHYVDNPSKTASTLR--GNFYiTGD 455
Cdd:COG1022 391 RPG-DNRIGTVGPPLP--GVEVkIAEDGEILvrgP-----------------NVMKGYYKNPEATAEAFDadGWLH-TGD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 456 RGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpirGE----VVkAFIVLNPDY------ 524
Cdd:COG1022 450 IGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEAlgewae 521
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 525 ----------KLHDQEQLKKEIQEHVKKTT---APYKYPRKIEFI--------EELpkTVSGKVKRNELRRK 575
Cdd:COG1022 522 englpytsyaELAQDPEVRALIQEEVDRANaglSRAEQIKRFRLLpkeftienGEL--TPTLKLKRKVILEK 591
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-574 |
7.90e-40 |
|
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: 151.72 E-value: 7.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 215 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 294 AHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQNdITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQT 373
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 374 ETV-LICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFY 451
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLV-----RGPNVMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 452 ITGDRGYMDEDGYFWFVARsddviLSSGYRIG----PFE-VESALIEH-PSIAESAVVSSPDPIRGEVVKAFivlnpdYK 525
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------TT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 65301416 526 LHDQEQLkkEIQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05909 441 TTDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-575 |
9.36e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 152.41 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIY--FTSGTTGPPKM 238
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAflasgDPDFAWTLPADEWDAIAlnYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 239 IGHTHSSFGLGLSVNGRFWlDLIASDV-MW-------NtsdtGWAksawssvFsPWT----QGACVFahyLPRFDSTSIL 306
Cdd:PRK08162 200 VVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTvaarAGTNVC---LRKVDPKLIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 307 QTLSKFPITVFCSAPTAYRMLIqNDITSYKfNSLKHCVS---AGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICG 380
Cdd:PRK08162 264 DLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAAPPAAVIAK-MEEIGFDLTHVYGLTETygpATVCA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 381 NFKGMKIKP--------GSMGKPSPAFN-VEILD-ENGTILPPGQE--GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG 448
Cdd:PRK08162 341 WQPEWDALPlderaqlkARQGVRYPLQEgVTVLDpDTMQPVPADGEtiGEIMF-----RGNIVMKGYLKNPKATEEAFAG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 449 NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhD 528
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD-----G 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 65301416 529 QEQLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 575
Cdd:PRK08162 491 ASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-573 |
1.95e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 151.89 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 87 VRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 166
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 167 TDD------------TLAP------AVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHtcvDTKHNELMA--- 225
Cdd:PRK08315 121 AADgfkdsdyvamlyELAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 ------IYFTSGTTGPPKmiGHTHSSFGLGLsvNGRF---WLDLIASD--------------VMWNTSDTgwaksawssv 282
Cdd:PRK08315 198 pddpinIQYTSGTTGFPK--GATLTHRNILN--NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNLACV---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 283 fspwTQGAC-VFAhyLPRFDSTSILQTLSKFPITVFCSAPTayrMLI----QNDITSYKFNSLKHCVSAGEPINPEVMEQ 357
Cdd:PRK08315 264 ----THGATmVYP--GEGFDPLATLAAVEEERCTALYGVPT---MFIaeldHPDFARFDLSSLRTGIMAGSPCPIEVMKR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 358 WKKKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFNVEILD-ENGTILPPGQEGDIA 420
Cdd:PRK08315 335 VIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGELC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 421 VqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 499
Cdd:PRK08315 403 T-----RGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 500 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-569 |
6.52e-39 |
|
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: 145.87 E-value: 6.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 225 AIYFTSGTTGPPKMIGHTHSSFGLGLSVngrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYL-----PR 299
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 FDSTSILQTLSKFPITVFCSAPTAYrmliqNDITSYKFNSLKHC-------VSAGEPINPEV-MEQWKKKTglDIYEGYG 371
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLL-----SKLVSELKSANATVpslrligYGGSRAIAADVrFIEATGLT--NTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRGNF 450
Cdd:cd17635 151 LSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhDQE 530
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 65301416 531 QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:cd17635 302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-567 |
1.19e-38 |
|
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: 144.75 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 289 GACVFahyLPRFDSTSILQTLSKFPIT-VFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGE--PINPEVMEQWKKKTGld 365
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 366 iyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 444
Cdd:cd17636 142 ---GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 524
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 65301416 525 KLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 567
Cdd:cd17636 293 SVTEA-----ELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-573 |
2.05e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 148.82 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 66 EKTGKRLSN-PAFwwvdgNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK12492 31 ERSCKKFADrPAF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 145 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLH---SKLIVSQHSREGW------GNLKEMMKY------- 208
Cdd:PRK12492 106 NPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 209 ---------ASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDliASDVMWn 268
Cdd:PRK12492 186 pfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKgaMLTHgnlvanmlqVRACLSQLGPDGQPLMKE--GQEVMI- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 269 tsdtgwAKSAWSSVFSPWTQGACVFA---HYL----PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSL 340
Cdd:PRK12492 263 ------APLPLYHIYAFTANCMCMMVsgnHNVlitnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 341 KHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDI 419
Cdd:PRK12492 336 KLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 420 AV---QVLPDrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHP 495
Cdd:PRK12492 416 CIkgpQVMKG--------YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301416 496 SIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-569 |
1.90e-37 |
|
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: 141.48 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPK--MIGHTHSsfgLGLSVNgrfWldliaSDVMWNTSDTGWA-----------KSAWSSVFspwTQGACV 292
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 293 FAHYLprFDSTSILQTLSKFPITVFCSAPTAYR-MLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGY 370
Cdd:cd17638 71 VPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTE--TVLICGNFKGMKIKPGSMGKPSPAFNVEILDEngtilppgqeGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG 448
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLV-----RGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 449 NFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLh 527
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 65301416 528 DQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-573 |
2.15e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.95 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANIL-TEACSlqRGDRVMViLPKIPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLrRRGCV--DGERLAV-LARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLApavdivAAKCENLHSKLIVSQhsregwgnlkemmkyaSDSHTCVDTKH---NELMAIYFTSGTTGPPK--MIG 240
Cdd:PRK09088 99 LGDDAVA------AGRTDVEDLAAFIAS----------------ADALEPADTPSippERVSLILFTSGTSGQPKgvMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 241 -----HTHSSFGLGLSVNGR--FWLDLiasdVMWNTsdTGWAksawSSVFSPWTQGACVFAHylPRFDSTSILQTLSKFP 313
Cdd:PRK09088 157 ernlqQTAHNFGVLGRVDAHssFLCDA----PMFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 314 ITV---FCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTE--TVLicgnfkGMKI- 387
Cdd:PRK09088 225 LGIthyFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSEagTVF------GMSVd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 388 ------KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMD 460
Cdd:PRK09088 298 cdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLL-----RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 461 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV 540
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHL 447
|
490 500 510
....*....|....*....|....*....|...
gi 65301416 541 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK09088 448 STRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
80-574 |
2.98e-37 |
|
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: 145.29 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGngkEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGtvLIPGTT--QLTQKDILYRL 157
Cdd:COG1021 45 VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFAlpAHRRAEISHFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 158 QSSKSKCIITDDT-----LAPAVDIVAAKCENLHSKLIVsqHSREGWGNLKEMmkYASDSHTCVDTKHNELMAIYFTS-G 231
Cdd:COG1021 119 EQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDAL--LAAPADLSEPRPDPDDVAFFQLSgG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 232 TTGPPKMIGHTH---------SSFGLGLSVNGRFwldLIASDVMWNtsdtgwakSAWSS--VFSPWTQGAC-VFAhylPR 299
Cdd:COG1021 195 TTGLPKLIPRTHddylysvraSAEICGLDADTVY---LAALPAAHN--------FPLSSpgVLGVLYAGGTvVLA---PD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQ-NDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG------- 371
Cdd:COG1021 261 PSPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvn 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QT------ETVLicgnfkgmkikpGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 444
Cdd:COG1021 341 YTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLT-----RGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 --TLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnp 522
Cdd:COG1021 404 afTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 65301416 523 dyklhDQEQLK-KEIQEHVK-KTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:COG1021 481 -----RGEPLTlAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
111-573 |
3.31e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.10 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD----DTLAPAVDIVAAKcenlh 186
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 187 sklIVSQHSREGWGNLKEMMKYASDSHTcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVM 266
Cdd:PRK06060 127 ---LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 267 WNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRfdSTSILQTLS-KFPITVFCSAPTAYRMLIqNDITSYKFNSLKHCVS 345
Cdd:PRK06060 191 LCSARMYFAYGLGNSVWFPLATGGSAVINSAPV--TPEAAAILSaRFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 346 AGEPINPEVMEQWKKK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV 421
Cdd:PRK06060 268 AGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 422 qvlpdRPFGLFTHYVDNPSKTASTlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:PRK06060 345 -----RGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 502 VVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK06060 418 VVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
89-572 |
8.79e-37 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 142.35 E-value: 8.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgl 248
Cdd:cd05907 85 DP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 249 glsvngrfwldliasdvMWN--TSDTGWAKSA--WSSVFSP-WTQGACVFAHYLP-------RF--DSTSILQTLSKFPI 314
Cdd:cd05907 113 -----------------LSNalALAERLPATEgdRHLSFLPlAHVFERRAGLYVPllagariYFasSAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 315 TVFCSAPTAYRMLI----QNDITSYK--------FNSLKHCVSAGEPINPEVMEQWKKkTGLDIYEGYGQTETV-LICGN 381
Cdd:cd05907 176 TVFLAVPRVWEKVYaaikVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 382 FKGmKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA-STLRGNFYITGDRGYMD 460
Cdd:cd05907 255 PPG-DNRIGTVGKPLPGVEVRI----------ADDGEILV-----RGPNVMLGYYKNPEATAeALDADGWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 461 EDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPirgeVVKAFIVLNPDY--------------- 524
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaeehgiaytdv 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 65301416 525 -KLHDQEQLKKEIQEHVK---KTTAPYKYPRKIEFIEElPKTV-------SGKVKRNEL 572
Cdd:cd05907 395 aELAANPAVRAEIEAAVEaanARLSRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
216-569 |
1.97e-36 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 144.11 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 216 VDTKHNelMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAksAWSSVFSPWTQGACVFAH 295
Cdd:PTZ00237 251 VESSHP--LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV--SFHGFLYGSLSLGNTFVM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 296 Y-----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQND-----ITS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGL 364
Cdd:PTZ00237 327 FeggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSkYDLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 365 DIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvLPDRPFGLFTHYV-DNPSKT 442
Cdd:PTZ00237 407 KSSRGYGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKnDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 443 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 522
Cdd:PTZ00237 486 LFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 65301416 523 DYKLH--DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:PTZ00237 566 DQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
90-573 |
2.02e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 142.23 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEACSLQRgdRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPavDIVAAKCEnlhsklIVSqhsregWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:PRK07638 106 YKLN--DLPDEEGR------VIE------IDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 250 LSVNGR-FWLD-----LIASDVMwntsdtgwaksawSSVF-----SPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFC 318
Cdd:PRK07638 172 FDCNVHdFHMKredsvLIAGTLV-------------HSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 319 SAPTAYRMLIQndITSYKFNSLKhCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPGSMG 393
Cdd:PRK07638 237 TVPTMLESLYK--ENRVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPNSVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 394 KPSPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVdNPSKTASTLRGNFYIT-GDRGYMDEDGYFWFVARSD 472
Cdd:PRK07638 311 RPFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVGREK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyklhDQEQLKKEIQEHVKKTTAPYKYPRK 552
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|.
gi 65301416 553 IEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEAK 476
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-572 |
4.69e-36 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 140.93 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 160 SKSKCIITDDTLAPaVDIVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 239
Cdd:cd05920 111 AEAVAYIVPDRHAG-FDHRALARELAES--------------------------------IPEVALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHTHSSFGLGLSVngrfwldliASDVMWNTSDT----------GWAKSAWSSVFSPWTQGACVFAhylPRFDSTSILQTL 309
Cdd:cd05920 158 PRTHNDYAYNVRA---------SAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 310 SKFPITVFCSAPTAYRMLIQNDITS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLicgNFKGM--- 385
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRrADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 386 -KIKPGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdrpfGLFT--HYVDNPSKTASTLRGN-FYITGDRGYMD 460
Cdd:cd05920 303 dEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEGELLTR-------GPYTirGYYRAPEHNARAFTPDgFYRTGDLVRRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 461 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEhv 540
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPP--SAAQLRRFLRE-- 451
|
490 500 510
....*....|....*....|....*....|..
gi 65301416 541 kKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd05920 452 -RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-569 |
6.67e-36 |
|
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: 136.77 E-value: 6.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfWldlIASDVMwntSDTGWAKSAWSSVFSPWTQG------ACVFAHYLPR 299
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------W---IESFVC---NEDLFNISGEDAILAPGPLShslflyGAISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 -------FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITSykfNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYG 371
Cdd:cd17633 68 tfigqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGtilppGQEGDIAVQvlpdRPFgLFTHYVDNPSKTAstlrGNFY 451
Cdd:cd17633 145 TSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK----SEM-VFSGYVRGGFSNP----DGWM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 452 ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklhdqEQ 531
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------KL 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 65301416 532 LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:cd17633 283 TYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
111-572 |
7.51e-36 |
|
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: 140.72 E-value: 7.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKSKCIITDDTLAPAVDIVAAKcenlhskli 190
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA--------IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIA 262
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKGAVIPQRA---------------AE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 263 SDVMWNTSDTGWAKSAWSSVFS--PWTQGACVFA-----------HYLPR-FDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05923 177 SRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAvlvaalaldgtYVVVEeFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 329 QN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPspAFN-----V 401
Cdd:cd05923 257 AAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRP--GFFsevriV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 402 EILDENGTILPPGQEGDIAVQVLPDRPFglfTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYR 481
Cdd:cd05923 331 RIGGSPDEALANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 482 IGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQLKKEIQEHVKKTT--APYKYPRKIEFIEEL 559
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-------GTLSADELDQFCRASelADFKRPRRYFFLDEL 480
|
490
....*....|...
gi 65301416 560 PKTVSGKVKRNEL 572
Cdd:cd05923 481 PKNAMNKVLRRQL 493
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
219-574 |
7.78e-36 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 141.52 E-value: 7.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 219 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWldliASDVMWNTSDTGWAksAWSSVFSPWtqGACVFAHYL- 297
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFE----ASQYEYPGSDNVYL--AALPMFHIY--GLSLFVVGLl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 ---------PRFDSTSILQTLSKFPITVFCSAPTAYRMLIQN--DITSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLD 365
Cdd:PLN02574 268 slgstivvmRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlPHVD 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 366 IYEGYGQTETVLICG---NFKGMKiKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdRPfGLFTHYVDNPSK 441
Cdd:PLN02574 348 FIQGYGMTESTAVGTrgfNTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKA 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 442 TASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 520
Cdd:PLN02574 422 TQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 65301416 521 NPDYKLhDQEQlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PLN02574 502 RQGSTL-SQEA----VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-569 |
1.21e-35 |
|
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: 139.50 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05914 82 AIFV--------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSfgLGLSVNGRFWLDLI-ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFdSTSILQTLSKFPITVFCSAPT 322
Cdd:cd05914 112 RN--IVSNVDGVKEVVLLgKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 323 A------YRMLIQNDITSYKF--------------------------NSLKHCVSAGEPINPEVmEQWKKKTGLDIYEGY 370
Cdd:cd05914 187 PlviekiFKMDIIPKLTLKKFkfklakkinnrkirklafkkvheafgGNIKEFVIGGAKINPDV-EEFLRTIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETV-LICGNFKGmKIKPGSMGKPSPAFNVEILDENgtilPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS--TLR 447
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV-----RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GNFYiTGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAFIVLNPDY-- 524
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 65301416 525 -----KLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFI-EELPKTVSGKVKR 569
Cdd:cd05914 410 vkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-575 |
3.31e-35 |
|
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: 135.15 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 228 FTSGTTGPPKMIGHT-----HSSFG----LGLSVNGRFWLDLIASDV-----MWNtsdtgWAKSAWSSVFSPWTQGAcvf 293
Cdd:cd17630 7 LTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDSWLLSLPLYHVgglaiLVR-----SLLAGAELVLLERNQAL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 294 ahylprfdstsiLQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQT 373
Cdd:cd17630 79 ------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 374 ETV-LICGNFKGMKiKPGSMGKPSPAFNVEIlDENGTILPPGQegdiavqvlpdrpfGLFTHYVDNPSKTASTLRGNFYi 452
Cdd:cd17630 146 ETAsQVATKRPDGF-GRGGVGVLLPGRELRI-VEDGEIWVGGA--------------SLAMGYLRGQLVPEFNEDGWFT- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 453 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQL 532
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG-------PAD 281
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 65301416 533 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 575
Cdd:cd17630 282 PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
211-573 |
3.99e-35 |
|
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: 137.50 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 211 DS-HTCVDTKHNELMA-IYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFwLDLIASDVMWNTSDTGWaKSAWSSVFSPWTQ 288
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 289 GACVFAHYLPRFDSTSILQTL-SKFPITVFcSAPTAY-RMLIQ--NDITSYKFNSLKHCVSAGEPINPEVMEQWKKkTGL 364
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVL-DLPPAYlQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWLK-APV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 365 DIYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFNVEILDENGTILPPGQEGD--IAVQvlpdrpfGLFTHYVD 437
Cdd:cd17649 238 RLFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 438 NPSKTASTL--------RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 509
Cdd:cd17649 311 RPELTAERFvpdpfgapGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 510 RGEVVkAFIVLNPDYKlhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd17649 391 GKQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
86-573 |
4.70e-35 |
|
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: 138.25 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAkcenlhsklIVSQHSREGWGNLkemmkyASDSHTCVDTKHNELMAIYfTSGTTGPPKmighthss 245
Cdd:cd17651 97 LTHPALAGELAVELV---------AVTLLDQPGAAAG------ADAEPDPALDADDLAYVIY-TSGSTGRPK-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 fglGLSVNGRFWLDLIAsdvmWNT----SDTGWAKSAWSS---------VFSPWTQGACVfaHYLP---RFDSTSILQTL 309
Cdd:cd17651 153 ---GVVMPHRSLANLVA----WQArassLGPGARTLQFAGlgfdvsvqeIFSTLCAGATL--VLPPeevRTDPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 310 SKFPITVfCSAPTAY-RMLIQN-DITSYKFNSLKHCVSAGEP--INPEVMEQWKKKTGLDIYEGYGQTE----TVLICGN 381
Cdd:cd17651 224 DEQRISR-VFLPTVAlRALAEHgRPLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 382 FKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL-------RGNFYITG 454
Cdd:cd17651 303 DPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAERFvpdpfvpGARMYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 455 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKK 534
Cdd:cd17651 378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV-DAAELRA 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 65301416 535 EIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:cd17651 457 ALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
90-572 |
6.02e-35 |
|
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: 137.84 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd17655 24 TYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIvAAKCENLHSKLIVSQHSRegwgNLKemmkyasdshtcVDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFG 247
Cdd:cd17655 103 HLQPPIAF-IGLIDLLDEDTIYHEESE----NLE------------PVSKSDDLAYVIYTSGSTGKPKgvMIEH-RGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 248 LGLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPTAY 324
Cdd:cd17655 165 LVEWANKVIYQG--EHLRVALFASISFDASVTE-IFASLLSGNTL--YIVRKetvLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 325 RMLIQNDITSykFNSLKHCVSAGEPINPEVMEQWKKKTGL--DIYEGYGQTETVLIC--GNFKGMKIKPGS--MGKPSPA 398
Cdd:cd17655 240 KLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 399 FNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARS 471
Cdd:cd17655 318 TRIYILDQYGRPQPVGVAGELYIG-----GEGVARGYLNRPELTAEKFVDDpfvpgerMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 472 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYPR 551
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV-------AQLREFLARELPDYMIPS 465
|
490 500
....*....|....*....|.
gi 65301416 552 KIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17655 466 YFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
87-575 |
7.62e-35 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 138.82 E-value: 7.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 87 VRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 166
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 167 TDD---TLAP-AVDIVAAKCENLHSK--LIVSQHSREGWGNLKEMM-KYASDSHTCVDTKHNEL-----------MAIYF 228
Cdd:PLN02479 123 VDQeffTLAEeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALgKGAIEYEKFLETGDPEFawkppadewqsIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPK-MIGHTHSSFGLGLSvNGRFWLDLIASDVMWNTSD---TGWAksawssvfSPWTQGA-CVFAHYLPRFDST 303
Cdd:PLN02479 203 TSGTTASPKgVVLHHRGAYLMALS-NALIWGMNEGAVYLWTLPMfhcNGWC--------FTWTLAAlCGTNICLRQVTAK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 304 SILQTLSKFPITVFCSAPTAYRMLIqNDITSYKFNSLKHCV---SAGEPINPEVMEQWKKKtGLDIYEGYGQTETV---L 377
Cdd:PLN02479 274 AIYSAIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETYgpsT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 378 ICG----------------------NFKGMK----IKPGSMgKPSPAfnveildeNGTILppgqeGDIAVqvlpdRPFGL 431
Cdd:PLN02479 352 VCAwkpewdslppeeqarlnarqgvRYIGLEgldvVDTKTM-KPVPA--------DGKTM-----GEIVM-----RGNMV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 432 FTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRG 511
Cdd:PLN02479 413 MKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 512 EVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 575
Cdd:PLN02479 493 ESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-572 |
1.96e-33 |
|
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: 133.48 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDivaakceNLHSKLIVSQHSREGwgnlkemmkYASDSHTCVDTKHneLMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12117 99 LTDRSLAGRAG-------GLEVAVVIDEALDAG---------PAGNPAVPVSPDD--LAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FgLGLsVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITV-FCSAP 321
Cdd:cd12117 161 V-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARL--VLAPKgtlLDPDALGALIAEEGVTVlWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 TaYRMLIQNDITSykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKPS 396
Cdd:cd12117 236 L-FNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 397 PAFNVEILDENGTILPPGQEGDIAVqvLPDrpfGLFTHYVDNPSKTAS-------TLRGNFYITGDRGYMDEDGYFWFVA 469
Cdd:cd12117 313 ANTRVYVLDEDGRPVPPGVPGELYV--GGD---GLALGYLNRPALTAErfvadpfGPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 470 RSDDVILSSGYRIGPFEVESALIEHPSIAESAV-VSSPDPIRGEVVkAFIVlnPDYKLHDQeqlkkEIQEHVKKTTAPYK 548
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVV--AEGALDAA-----ELRAFLRERLPAYM 459
|
490 500
....*....|....*....|....
gi 65301416 549 YPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd12117 460 VPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
90-572 |
4.26e-33 |
|
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: 132.40 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLA---PAVDIVAAKCENLHSKLIVSQHSREgwgnlkemmkYASDSHTCVdtkhnelmaIYfTSGTTGPPK--MIGHThs 244
Cdd:cd17646 104 DLAarlPAGGDVALLGDEALAAPPATPPLVP----------PRPDNLAYV---------IY-TSGSTGRPKgvMVTHA-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 sfglGLsVNGRFWL----DLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCS 319
Cdd:cd17646 162 ----GI-VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 320 APTAYRMLIQnDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKPS 396
Cdd:cd17646 236 VPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVPIGRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 397 PAFNVEILDENGTILPPGQEGDI---AVQVlpdrPFGlfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFW 466
Cdd:cd17646 315 PNTRLYVLDDALRPVPVGVPGELylgGVQL----ARG----YLGRPALTAERFVPDpfgpgsrMYRTGDLARWRPDGALE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 467 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLkkeiQEHVKKTTAP 546
Cdd:cd17646 387 FLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERLPE 462
|
490 500
....*....|....*....|....*.
gi 65301416 547 YKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17646 463 YMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
74-580 |
7.08e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 132.50 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 74 NPAFWWVDGngkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIpGTTQLTQKDI 153
Cdd:PRK07867 19 DRGLYFEDS-----FTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV-GLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 154 LYR-LQSSKSKCIITDDTLAPAVDIVAAKCEnlhsklIVSQHSREgWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGT 232
Cdd:PRK07867 93 LARdIAHADCQLVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 233 TGPPKMIGHTHSSF-GLGLSVNGRFwlDLIASDVMWntsdtgwaksawssVFSPWTQGACVFAHYLP------------R 299
Cdd:PRK07867 164 SGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasialrrK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 FDSTSILQTLSKFPITVF--CSAPTAYrMLIQNDITSYKFNSLKhcVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETvl 377
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSY-VLATPERPDDADNPLR--IVYGNEGAPGDIARFARRFGCVVVDGFGSTEG-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 378 icgnfkGMKIK------PGSMGKPSPafNVEILD-ENGTILPPGQ-------EGDIAVQVL--PDRPfGLFTHYVDNPSK 441
Cdd:PRK07867 303 ------GVAITrtpdtpPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIGELvnTAGP-GGFEGYYNDPEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 442 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 65301416 522 PDYKLhDQEQLKKEIqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 580
Cdd:PRK07867 454 PGAKF-DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
226-572 |
2.70e-32 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 129.35 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYfTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTS 304
Cdd:cd17643 99 IY-TSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrLVVVPYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 305 ILQTLSKFPITVFCSAPTAYRMLIQNDITSYK-FNSLKHCVSAGEPINPEVMEQWKKKTGL---DIYEGYGQTET-VLIc 379
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRdPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 380 gNFKGMK---IKPGSM---GKPSPAFNVEILDENGTILPPGQEGDIAV---QVLP---DRPFGLFTHYVDNPsKTASTLR 447
Cdd:cd17643 255 -TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GnfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklH 527
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 65301416 528 DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
84-574 |
9.82e-32 |
|
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: 127.43 E-value: 9.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdilyrlqssksk 163
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP-------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 ciitDDTLAPAVDIVAAkCENLHSKLIVSqhsregwgnlkemmkyasdshtcvDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd17653 77 ----LDAKLPSARIQAI-LRTSGATLLLT------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHylPRFDSTSILQTLSKFPITvfcsaPT 322
Cdd:cd17653 128 RGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGGTlVLAD--PSDPFAHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 323 AYRMLIQNDitsykFNSLKHCVSAGEPINPEVMEQWKKktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVE 402
Cdd:cd17653 199 ILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 403 ILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSD 472
Cdd:cd17653 272 ILDADLQPVPEGVVGEICIsgvQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdpIRGEVVkAFIVlnPDYKlhDQEQLKKEIQEHVkkttAPYKYPRK 552
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PETV--DVDGLRSELAKHL----PSYAVPDR 411
|
490 500
....*....|....*....|..
gi 65301416 553 IEFIEELPKTVSGKVKRNELRR 574
Cdd:cd17653 412 IIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
226-574 |
1.06e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 129.53 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGrfwLDLIA------SDVMWNTS---DTGWAKSAWSSVFSpwtqGAC-VFah 295
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSA----LIVQS---LAKIAivgygeDDVYLHTAplcHIGGLSSALAMLMV----GAChVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 296 yLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI---QNDITSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYG 371
Cdd:PLN02860 244 -LPKFDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFNVEI-LDEngtilpPGQEGDIAVqvlpdR 427
Cdd:PLN02860 323 MTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRILT-----R 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 428 PFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSP 506
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 65301416 507 DPIRGEVVKAFIVLNPDYKLHDQE--------QLKKEIQEH--VKKTTAPYKYPRKIEFIEE-LPKTVSGKVKRNELRR 574
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGWIWSDNEkenakknlTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRR 550
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
213-579 |
1.23e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 128.99 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 213 HTCVDTKHNELMaiYFTSGTTGPPKMIGHTHSSFG-LGLSVNGRFwlDLIASDVMW--------NTSDTGWAKSAwssvf 283
Cdd:PRK13388 144 HREVDAMDPFML--IFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 284 spwTQGACVFAHylPRFDSTSILQTLSKFPITVF--CSAPTAYRMLI---QNDITsykfNSLKhcVSAGEPINPEVMEQW 358
Cdd:PRK13388 215 ---ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAYILATperPDDAD----NPLR--VAFGNEASPRDIAEF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 359 KKKTGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafNVEI-------------LDENGTILPPgqegDIAVQVLP 425
Cdd:PRK13388 284 SRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIynpetltecavarFDAHGALLNA----DEAIGELV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 426 DRP-FGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 504
Cdd:PRK13388 356 NTAgAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 505 SPDPIRGEVVKAFIVLNPDYK---------LHDQEQLkkeiqehvkkttAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 575
Cdd:PRK13388 436 VPDERVGDQVMAALVLRDGATfdpdafaafLAAQPDL------------GTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
....
gi 65301416 576 EWTT 579
Cdd:PRK13388 504 GWAT 507
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-567 |
6.89e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.50 E-value: 6.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 217 DTKHNELMAIYFTSGTTGPPK--MIGHT----------------------------HSsfgLGLSVNgrFWLDLIasdvm 266
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWLPLL----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 267 wntsdtgwaksawssvfspwtQGACVFAHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQND-ITSYKFNSLKHCVS 345
Cdd:PRK08633 848 ---------------------EGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 346 AGEPINPEVMEQWKKKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPG 414
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPG 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 415 QEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLR----GNFYITGDRGYMDEDGYFWFVARsddviLSSGYRIG---- 483
Cdd:PRK08633 986 EDGLILIggpQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemv 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 484 PF-EVESALIE--HPSIAESAVVSSPDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAP--YKyPRKIEFIE 557
Cdd:PRK08633 1053 PLgAVEEELAKalGGEEVVFAVTAVPDEKKGEK----LVV-----LHTCGAEDVEeLKRAIKESGLPnlWK-PSRYFKVE 1122
|
410
....*....|
gi 65301416 558 ELPKTVSGKV 567
Cdd:PRK08633 1123 ALPLLGSGKL 1132
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
110-573 |
1.23e-30 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 126.29 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 110 SLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP----AVDIVAAKCENL 185
Cdd:PLN03102 60 NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlareVLHLLSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 186 HSKLIV------------SQHSREGWGNLKEMMKYASDSHTCVDTKHNELmAIYFTSGTTGPPK--MIGHTHSSFGLGLS 251
Cdd:PLN03102 140 NLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKgvVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 252 VNGrfWLDLIASDVMWNTSD---TGWAKSaWSSVFSPWTQgACVFAHYLPRfdstsILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:PLN03102 219 IIG--WEMGTCPVYLWTLPMfhcNGWTFT-WGTAARGGTS-VCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 329 QNDITSYKFNSLK-HCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTET---VLICG---------NFKGMKIKPGSMGKP 395
Cdd:PLN03102 290 KGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKARQGVSI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 396 SPAFNVEILDENGTILPPgQEGDIAVQVLPdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI 475
Cdd:PLN03102 369 LGLADVDVKNKETQESVP-RDGKTMGEIVI-KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 476 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLK-----KEIQEHVKKTTAPYKYP 550
Cdd:PLN03102 447 ISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtreRDLIEYCRENLPHFMCP 526
|
490 500
....*....|....*....|...
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELR 573
Cdd:PLN03102 527 RKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-566 |
1.45e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 125.77 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYfTSGTTGPPK--MI 239
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHT---HSSFGLGLSVNGRFWLD----------------LIASDVMWNTSDtgWAksAWSSVFSpwtqGACVFAHYLPRF 300
Cdd:PRK07798 184 RQEdifRVLLGGRDFATGEPIEDeeelakraaagpgmrrFPAPPLMHGAGQ--WA--AFAALFS----GQTVVLLPDVRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 301 DSTSILQTLSKFPITVFCSAPTAY-RMLIQ--NDITSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYEGYGQTETv 376
Cdd:PRK07798 256 DADEVWRTIEREKVNVITIVGDAMaRPLLDalEARGPYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSET- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 377 licgNFKGMKI-KPGSMGKPSPAFN----VEILDENGTILPPGQE--GDIAvqvlpdR----PFGlfthYVDNPSKTAST 445
Cdd:PRK07798 335 ----GFGGSGTvAKGAVHTGGPRFTigprTVVLDEDGNPVEPGSGeiGWIA------RrghiPLG----YYKDPEKTAET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 446 LR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 521
Cdd:PRK07798 401 FPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 65301416 522 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 566
Cdd:PRK07798 481 EGARPDLA-----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
90-573 |
7.44e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 123.70 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIItdd 169
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 tLAPA---VDIVAAKCENLHSKLIVSQ--------------HSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT-SG 231
Cdd:PRK06164 113 -VWPGfkgIDFAAILAAVPPDALPPLRaiavvddaadatpaPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 232 TTGPPKMIGHTHSSF---------GLGLSVNGRFWLDLIASDVMwntsdtgwaksAWSSVFSPWTQGACVfaHYLPRFDS 302
Cdd:PRK06164 192 TTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVFDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 303 TSILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHC-VSAGEPINPEVMeQWKKKTGLDIYEGYGQTE--TVLIC 379
Cdd:PRK06164 259 ARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFgFASFAPALGELA-ALARARGVPLTGLYGSSEvqALVAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 380 GNFK---GMKIKPGsmGKP-SPAFNVEILD-ENGTILPPGQEGDIAVQVlpdrPfGLFTHYVDNPSKTASTLRGN-FYIT 453
Cdd:PRK06164 338 QPATdpvSVRIEGG--GRPaSPEARVRARDpQDGALLPDGESGEIEIRA----P-SLMRGYLDNPDATARALTDDgYFRT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 454 GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdPIRGE-VVKAFIVLNPDYKLhDQEQL 532
Cdd:PRK06164 411 GDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASP-DEAGL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 65301416 533 KKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSG---KVKRNELR 573
Cdd:PRK06164 488 MA----ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
86-572 |
1.09e-29 |
|
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: 122.40 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLA-------PAVDIVAAKCENLHSKLIVSQHSregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKM 238
Cdd:cd12116 89 LTDDALPdrlpaglPVLLLALAAAAAAPAAPRTPVSP----DDLAYVI---------------------YTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 239 IGHTHSSF-GLGLSVNGRfwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITV 316
Cdd:cd12116 144 VVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCSAPTAYRMLIQNDITsyKFNSLkHCVSAGEPINPEVMEQWKKKTGlDIYEGYGQTETVL------ICGNFKGMKIkpg 390
Cdd:cd12116 221 MQATPATWRMLLDAGWQ--GRAGL-TALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 smGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPD---RPFGLFTHYVDNPSKTAstlRGNFYITGDRGYMDEDGY 464
Cdd:cd12116 294 --GRPLANTQVYVLDAALRPVPPGVPGELYIggdGVAQGylgRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 465 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLnPDYKLHDQEQLKkeiqEHVKKTT 544
Cdd:cd12116 369 LEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALR----AHLRATL 442
|
490 500
....*....|....*....|....*...
gi 65301416 545 APYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
218-572 |
3.50e-29 |
|
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: 120.62 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 218 TKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFwlDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGAC-VFA 294
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 295 HYLPRFDSTSILQTLSKFPITVFcSAPTAYRMLIQNDITSYKF---NSLKHCVSAGEPINPEVMEQWKKKTGLDI--YEG 369
Cdd:cd17644 179 PEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 370 YGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTAS 444
Cdd:cd17644 258 YGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLRGN---------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 515
Cdd:cd17644 333 KFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 516 AFIVlnPDYklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17644 413 AYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-566 |
1.43e-28 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 108.40 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 486 EVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhdqEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSG 565
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 65301416 566 K 566
Cdd:pfam13193 76 K 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-572 |
2.66e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 121.22 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEacslqRG----DRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIA-----RGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSG 4648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 162 SKCIITDDTLAPAVDIVAAkcenLHSKLIVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12316 4649 AALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGFPAHDPAVRLHPDN----------LAYVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 242 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:PRK12316 4715 SHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 TAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MGKP 395
Cdd:PRK12316 4793 VYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGTP 4872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 396 SPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL--------RGNFYITGDRGYMDEDGYFWF 467
Cdd:PRK12316 4873 LGNRSGYVLDGQLNPLPVGVAGELYLG-----GEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVIDY 4947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 468 VARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLNpDYKLHD----QEQLKKEIQEHVKKT 543
Cdd:PRK12316 4948 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQ-DPALADadeaQAELRDELKAALRER 5025
|
490 500
....*....|....*....|....*....
gi 65301416 544 TAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK12316 5026 LPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-580 |
2.97e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 120.73 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKCENLhSKLIVSQHSregwgnlkemmkyASDSHTCVDTKHneLMAIYFTSGTTGPPK--MIghTH 243
Cdd:COG1020 578 LTQSALAARLPELGVPVLAL-DALALAAEP-------------ATNPPVPVTPDD--LAYVIYTSGSTGRPKgvMV--EH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSFG-LGLSVNGRFWLDliASDVM-WNTS---DTgwakSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVF 317
Cdd:COG1020 640 RALVnLLAWMQRRYGLG--PGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLIQNDITSykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM-- 392
Cdd:COG1020 713 NLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSVpi 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 GKPSPAFNVEILDENGTILPPGQEGDIAV---QV----LpDRPfGL----FthyVDNPSKTASTlRgnFYITGDRGYMDE 461
Cdd:COG1020 791 GRPIANTRVYVLDAHLQPVPVGVPGELYIggaGLargyL-NRP-ELtaerF---VADPFGFPGA-R--LYRTGDLARWLP 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 462 DGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVK 541
Cdd:COG1020 863 DGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GAAAAAALLRLALA 937
|
490 500 510
....*....|....*....|....*....|....*....
gi 65301416 542 KTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 580
Cdd:COG1020 938 LLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
340-572 |
5.86e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 117.79 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 340 LKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGD 418
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 419 IAV--QVLPDRpfglfthYVDNPSKtaSTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPS 496
Cdd:PRK13383 374 IFVggELAGTR-------YTDGGGK--AVVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 497 IAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPGSGV-DAAQLRDYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
107-572 |
6.72e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 6.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 107 EACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIlyrlqssKSKCIITDdtlaPAVDIVAAKC---- 182
Cdd:PRK05857 59 RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAI-------ERFCQITD----PAAALVAPGSkmas 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 183 ----ENLHSKLIVSQHSREGWGNLKEMMKYASDShTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG---LSVNGR 255
Cdd:PRK05857 128 savpEALHSIPVIAVDIAAVTRESEHSLDAASLA-GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 256 FWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYlprfDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITS 334
Cdd:PRK05857 207 NWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 335 YKFNSLKHCVSAG-EPINPEVmeQWKKKTGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 408
Cdd:PRK05857 283 ATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 409 TilppgqeGDIAVQVLPDRPFGLF--------THYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGY 480
Cdd:PRK05857 361 I-------GPTAPGAGPSASFGTLwikspanmLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 481 RIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELP 560
Cdd:PRK05857 434 NIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIP 513
|
490
....*....|..
gi 65301416 561 KTVSGKVKRNEL 572
Cdd:PRK05857 514 RTQSGKVMRASL 525
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
90-569 |
1.15e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 116.91 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLKEMMKYASDSHTCVDT----KHNELMaIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 fgLGLSVNGrfwldLIAS----------DVMWNTSDTGWAKSAWSSVFSpwtqGACVFAHYLPRFDSTSILQTLSKFPIT 315
Cdd:PRK05852 201 --IASSVRA-----IITGyrlsprdatvAVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRMLIQNDITSY---KFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--------VLICGNFKG 384
Cdd:PRK05852 270 WYTAVPTIHQILLERAATEPsgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 385 MKIKPGSMGKpSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGY 464
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 465 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQlkkEIQEHVKKTT 544
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERL 498
|
490 500
....*....|....*....|....*
gi 65301416 545 APYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:PRK05852 499 AAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-566 |
6.31e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 112.48 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSFGLGLS-----VNGRFWLDLIASDVMWNTSDTGW--------AKSAWSSVFSPWTQGACV 292
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 293 FAHylPRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQ--NDITSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYE 368
Cdd:cd05924 88 LPD--DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 369 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafNVEILDENGTILPPGQEGdiaVQVLPDR---PFGlfthYVDNPSKTAS 444
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGG---VGWIARRghiPLG----YYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 520
Cdd:cd05924 237 TFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 65301416 521 NPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 566
Cdd:cd05924 317 REGAGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-572 |
2.74e-26 |
|
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: 111.88 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 DDtlapavdivaakcenlhsklivsqhsregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 248 lglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKFPITV-FCS 319
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPserRLDLDALNDYFNQEGITIsFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 320 APTAYR-MLIQNditsykfNSLKHCVSAGEPINPevmeqwKKKTGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPSP 397
Cdd:cd17645 203 TGAAEQfMQLDN-------QSLRVLLTGGDKLKK------IERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPID 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 398 AFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVAR 470
Cdd:cd17645 270 NTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 471 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdyklhDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:cd17645 345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMIP 417
|
490 500
....*....|....*....|..
gi 65301416 551 RKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17645 418 TYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
83-575 |
3.49e-26 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 112.18 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 83 NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 163 KCIIT---DD--TLAPAVDivaakcENLHSkLIVSQHS----REGWGNLKEMMKYASDSHTcvdTKHNELMAIYFTSGTT 233
Cdd:cd05932 80 KALFVgklDDwkAMAPGVP------EGLIS-ISLPPPSaancQYQWDDLIAQHPPLEERPT---RFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 234 GPPKMIGHTHSSFG---------LGLSVNGRF--WLDL--IASDVMwntsdtgwaksawssVFSPWTQGACV--FAHYLP 298
Cdd:cd05932 150 GQPKGVMLTFGSFAwaaqagiehIGTEENDRMlsYLPLahVTERVF---------------VEGGSLYGGVLvaFAESLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 RFdstsiLQTLSKFPITVFCSAP---TAYRMLIQNDITSYKFNSL----------KHCVSAG-------------EPINP 352
Cdd:cd05932 215 TF-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 353 EVMEqWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGLF 432
Cdd:cd05932 290 ALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 433 THYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSS-GYRIGPFEVESALIEHPSIAESAVVSS--PDP 508
Cdd:cd05932 354 MGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAP 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 509 IRGEVVKAFIVLNPDYKlhDQEQLKKEIQEH---VKKTTAPYKYPRKIEFIEElPKTVSG-------KVKRNELRRK 575
Cdd:cd05932 434 LALVVLSEEARLRADAF--ARAELEASLRAHlarVNSTLDSHEQLAGIVVVKD-PWSIDNgiltptlKIKRNVLEKA 507
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-523 |
3.90e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 112.68 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKSKCII 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 167 TddtlapavdIVAA---------KCENLHSKLIVSQhsREGWGN--LKEMM-KYASDSHTCVDTKHNELMAIYFTSGTTG 234
Cdd:PRK09274 119 G---------IPKAhlarrlfgwGKPSVRRLVTVGG--RLLWGGttLATLLrDGAAAPFPMADLAPDDMAAILFTSGSTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 235 PPKMIGHTHSSF---------GLGLSVNGRfwlDLIASDVMwntsdtgwaksawsSVFSPwtqgACVFAHYLPRFDST-- 303
Cdd:PRK09274 188 TPKGVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGP----ALGMTSVIPDMDPTrp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 304 ------SILQTLSKFPITVFCSAPtAY-----RMLIQNDItsyKFNSLKHCVSAGEPINPEVMEQWKK--KTGLDIYEGY 370
Cdd:PRK09274 247 atvdpaKLFAAIERYGVTNLFGSP-ALlerlgRYGEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETVLICgnfkgmKIkpGS------------------MGKPSPAFNVEILD---------ENGTILPPGQEGDIAVQ- 422
Cdd:PRK09274 323 GATEALPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAg 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 423 --VLPDrpfglfthYVDNPSKTA-----STLRGNFYITGDRGYMDEDGYFWFVAR-SDDVILSSGyRIGPFEVESALIEH 494
Cdd:PRK09274 395 pmVTRS--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTH 465
|
490 500 510
....*....|....*....|....*....|
gi 65301416 495 PSIAESAVVSSPDPirGEVVKAFIV-LNPD 523
Cdd:PRK09274 466 PGVKRSALVGVGVP--GAQRPVLCVeLEPG 493
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-572 |
6.60e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.51 E-value: 6.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDiVAAKCENL---HSKLIVSQHSREgwgNLKemmkyasdshTCVDTKHneLMAIYFTSGTTGPPKMIGHT 242
Cdd:PRK12316 613 LSQSHLGRKLP-LAAGVQVLdldRPAAWLEGYSEE---NPG----------TELNPEN--LAYVIYTSGSTGKPKGAGNR 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 243 HSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK12316 677 HRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 318 CSAPTAYRMLIQN-DITSykFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MG 393
Cdd:PRK12316 751 HFVPSMLQAFLQDeDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvpIG 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 394 KPSPAFNVEILDENGTILPPGQEGDIavqVLPDRpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFW 466
Cdd:PRK12316 829 RPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGVIE 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 467 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNpdyklHDQEQLKKEIQEHVKKTTAP 546
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-----SEGGDWREALKAHLAASLPE 974
|
490 500
....*....|....*....|....*.
gi 65301416 547 YKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK12316 975 YMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-576 |
7.62e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.33 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILteacsLQRG---DR-VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRL-----IAIGvgpDVlVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 162 SKCIITDDTLAPAVDIVAAkcenLHSkLIVSQHSREGWgnlkemmkyaSDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12467 3193 VKLLLTQAHLLEQLPAPAG----DTA-LTLDRLDLNGY----------SENNPSTRVMGENLAYVIYTSGSTGKPKGVGV 3257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 242 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:PRK12467 3258 RHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPP 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 TAYRMLIQN-DITSYkfNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSMGK 394
Cdd:PRK12467 3336 AYLQQFAEDaGGADC--ASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGR 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 395 PSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFW 466
Cdd:PRK12467 3414 PVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIE 3488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 467 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAP 546
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASLPD 3562
|
490 500 510
....*....|....*....|....*....|
gi 65301416 547 YKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK12467 3563 YMVPAQLLVLAAMPLGPNGKVDRKALPDPD 3592
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
88-574 |
8.66e-26 |
|
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: 110.71 E-value: 8.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP-GTTQLTQkdilyRLQSskskciI 166
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPlDPSHPLQ-----RLQE------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 167 TDDTLAPAVdivaakcenlhsklIVSQHSregwgnlkemmkyasdshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSF 246
Cdd:cd05918 92 LQDTGAKVV--------------LTSSPS--------------------------DAAYVIFTSGSTGKPKGVVIEHRAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 247 ---------GLGLSVNGRfWLDL--IASDVMWNtsdtgwaksawsSVFSPWTQGACV-----------FAHYLPRFDSTS 304
Cdd:cd05918 132 stsalahgrALGLTSESR-VLQFasYTFDVSIL------------EIFTTLAAGGCLcipseedrlndLAGFINRLRVTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 305 ILQTlskfpitvfcsaPTAYRMLIQNDITSykfnsLKHCVSAGEPINPEVMEQWKKKTGLdiYEGYGQTE-TVLICGNFK 383
Cdd:cd05918 199 AFLT------------PSVARLLDPEDVPS-----LRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATVSPV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 384 GMKIKPGSMGKPSPAfNVEILDENGT--ILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTA--------------S 444
Cdd:cd05918 260 VPSTDPRNIGRPLGA-TCWVVDPDNHdrLVPIGAVGELLIegpILARG--------YLNDPEKTAaafiedpawlkqegS 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 445 TLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK---AFIVLN 521
Cdd:cd05918 331 GRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVLD 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 522 PDYKLHDQEQ------------LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05918 411 GSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
214-572 |
9.00e-26 |
|
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: 110.03 E-value: 9.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 214 TCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGlGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVf 293
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 294 aHYLPRFDSTS---ILQTLSKFPITVFCSAPTAYRMLIQNDITSykfnsLKHCVSAGEPINPEVMEQWKKktGLDIYEGY 370
Cdd:cd17652 163 -VLAPAEELLPgepLADLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVDRWAP--GRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETVL---ICGNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA---- 443
Cdd:cd17652 235 GPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAerfv 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 444 ----STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 519
Cdd:cd17652 308 adpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 65301416 520 LNPDYKLhDQEQLKkeiqEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17652 388 PAPGAAP-TAAELR----AHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
86-574 |
1.49e-25 |
|
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: 110.60 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPavdiVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCV-DTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05915 101 LFDPNLLP----LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPvRVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAY 324
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPAS-LVELFDGEGVTFTAGVPTVW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 325 RMLIQ-NDITSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTET------VLICGNFKGMKIKPGSMGKPSP 397
Cdd:cd05915 256 LALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETspvvvqNFVKSHLESLSEEEKLTLKAKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 398 AFN-----VEILDENGTILPpgQEGDiAVQVLPDRPFGLFTHYV-DNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARS 471
Cdd:cd05915 335 GLPiplvrLRVADEEGRPVP--KDGK-ALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 472 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyKLHDQEQLKKEIQEHVKKTTAPYKY-P 550
Cdd:cd05915 412 KDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV------VPRGEKPTPEELNEHLLKAGFAKWQlP 485
|
490 500
....*....|....*....|....
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05915 486 DAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
218-572 |
1.77e-25 |
|
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: 109.33 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 218 TKHNELMAIYFTSGTTGPPKMIGHTHSSfglglSVNGRFWldliasdvmwntSDTGWAKSAWSSV--------------- 282
Cdd:cd12115 102 TDPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAFLQW------------AAAAFSAEELAGVlastsicfdlsvfel 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 283 FSPWTQGACVF----AHYL---PRFDSTSILQTLskfpitvfcsaPTAYRMLIQNDI--TSYKFNSLkhcvsAGEPINPE 353
Cdd:cd12115 165 FGPLATGGKVVladnVLALpdlPAAAEVTLINTV-----------PSAAAELLRHDAlpASVRVVNL-----AGEPLPRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 354 -VMEQWKKKTGLDIYEGYGQTE-----TVLICGnfKGMKIKPgSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdr 427
Cdd:cd12115 229 lVQRLYARLQVERVVNLYGPSEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 428 PFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 500
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 501 AVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-572 |
1.95e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.18 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKcenlhSKLIVSQHSREGWGnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12467 614 LTQSHLLAQLPVPAGL-----RSLCLDEPADLLCG--------YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FGLGLSVNGRfWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPT 322
Cdd:PRK12467 681 LANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPS 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 323 AYRMLIQnDITSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMGKPSP 397
Cdd:PRK12467 757 HLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 398 AFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVA 469
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIG-----GAGLARGYHRRPALTAerfvpdpfGADGGRLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 470 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVlnPDYKLHDQEQ--LKKEIQEHVKKTTAPY 547
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHqaTRDELKAQLRQVLPDY 987
|
490 500
....*....|....*....|....*
gi 65301416 548 KYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-574 |
2.20e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.89 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLA-PAVDIVAAKCenlhsklivsqhsregwgnLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLD-------------------LDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 SFGLGLSVNGRFwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDS-TSILQTLSKFPITVFCSAPTA 323
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 324 YRMLIQnDITSYKFNSLKHCVSAGEPINPEVMEQWKkkTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFNV 401
Cdd:PRK12316 3298 LQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRAC 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 402 EILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDV 474
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDpfvpgerLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 475 ILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIE 554
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPED-----EAGDLREALKAHLKASLPEYMVPAHLL 3520
|
490 500
....*....|....*....|
gi 65301416 555 FIEELPKTVSGKVKRNELRR 574
Cdd:PRK12316 3521 FLERMPLTPNGKLDRKALPR 3540
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-573 |
3.66e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 106.37 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 84 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKY------ASDSHTCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:PRK06018 114 VVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiaeADGDFAWKTFDENTAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 238 MIGHTHSSFGL-GLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFahyLP--RFDSTSILQTLSKFPI 314
Cdd:PRK06018 194 GVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 315 TVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETVLIcgnfkgmkikpGSMG 393
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPL-----------GTLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 394 KPSPAFNVEILDENGTIL-----PP-GQEGDI---AVQVLP--DRPFGLFThyVDNPSKTASTLRGN--------FYITG 454
Cdd:PRK06018 338 ALKPPFSKLPGDARLDVLqkqgyPPfGVEMKItddAGKELPwdGKTFGRLK--VRGPAVAAAYYRVDgeildddgFFDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 455 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKK 534
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATRE 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 65301416 535 EIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK06018 491 EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-573 |
4.18e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 106.33 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVIlpkipEW-----WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALA-ALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 163 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNL-----KEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 238 MIGHTHSS-----FGLGLSVNgrfwLDLIASDV------MWNTSdtgwaksAWSSVFS-PWTQGACVFAHylPRFDSTSI 305
Cdd:PRK07008 193 GALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSaPLTGAKLVLPG--PDLDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 306 LQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLIcGNFKG 384
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 385 MKIKPGSMGKPS----------PAFNVE--ILDENGTILP-PGQE-GDIAVQ---VLpDRPFGlfthyvdnpsKTASTLR 447
Cdd:PRK07008 339 LKWKHSQLPLDEqrkllekqgrVIYGVDmkIVGDDGRELPwDGKAfGDLQVRgpwVI-DRYFR----------GDASPLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 527
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 65301416 528 DQEQLKkeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07008 488 REELLA-----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-574 |
9.73e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 105.06 E-value: 9.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 80 VDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPK----IPEWWlanvACLRTGTVLIPGTTQLTQKDILY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 156 RLQSSK-------SKCIITDDTLAPAVDIVAAKCENLHSKLIVSQhsregwgnlkEMMKYASDSHTcVDTKHNELMAIYF 228
Cdd:cd05906 106 RLRKLRhiwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHDL-PQSRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPKMIGHTHSSF---GLGLSVNGRF--------W--LDLIASDVMWNTSDtgwaksawssVFSPWTQGACVFAH 295
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNIlarSAGKIQHNGLtpqdvflnWvpLDHVGGLVELHLRA----------VYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 296 YLPrfDSTSILQTLSKFPITV-FcsAPT-AYRMLIQ--NDITSYKFN--SLKHCVSAGEPINPEVMEQWK---KKTGLD- 365
Cdd:cd05906 245 ILA--DPLRWLDLIDRYRVTItW--APNfAFALLNDllEEIEDGTWDlsSLRYLVNAGEAVVAKTIRRLLrllEPYGLPp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 366 --IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYV 436
Cdd:cd05906 321 daIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV-----VTKGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 437 DNPSKTASTLR-GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES--AVVSSPDPIRGEV 513
Cdd:cd05906 396 NNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETE 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 514 VKAfIVLNPDYKLHDQ-EQLKKEIQEHV-KKTTAPYKY----PRkiefiEELPKTVSGKVKRNELRR 574
Cdd:cd05906 475 ELA-IFFVPEYDLQDAlSETLRAIRSVVsREVGVSPAYliplPK-----EEIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
89-572 |
1.02e-23 |
|
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: 104.48 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DTLApavdiVAAKCENLHSKLIVSQHSREGWGNLKemMKYASDshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSFGL 248
Cdd:cd17656 93 RHLK-----SKLSFNKSTILLEDPSISQEDTSNID--YINNSD----------DLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 249 GLSVNGRFWLDLIASDVMWNTSDTgwAKSAWSSVFSPWTQGACVF-AHYLPRFDSTSILQTLSKFPITVFcSAPTAYRML 327
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 328 IQNDITSYK--FNSLKHCVSAGEP--INPEVMEQWKKKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------MGKPS 396
Cdd:cd17656 233 IFSEREFINrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeipelppIGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 397 PAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVA 469
Cdd:cd17656 308 SNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 470 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDqEQLKKEIQEHVKKttapYKY 549
Cdd:cd17656 383 RADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLREYLAKQLPE----YMI 455
|
490 500
....*....|....*....|...
gi 65301416 550 PRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17656 456 PSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-573 |
3.68e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 103.15 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV------------LIPGTTQLTQKdi 153
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrseLNAYASQIEPA-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 154 lyRLQSSKSKCIITDDTLapaVDIVAAKCENLhskLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTT 233
Cdd:PRK10946 123 --LLIADRQHALFSDDDF---LNTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 234 GPPKMIGHTHSSFGL---------GLSVNGRFWLDLIASDvmwntsdtgwaKSAWSS-----VFspWTQGACVFAhylPR 299
Cdd:PRK10946 195 GTPKLIPRTHNDYYYsvrrsveicGFTPQTRYLCALPAAH-----------NYPMSSpgalgVF--LAGGTVVLA---PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 376
Cdd:PRK10946 259 PSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSrAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 377 LicgNFKGMKIKP----GSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN-F 450
Cdd:PRK10946 339 V---NYTRLDDSDerifTTQGRPmSPDDEVWVADADGNPLPQGEVGRLMTR----GPY-TFRGYYKSPQHNASAFDANgF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdQE 530
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK---AV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 65301416 531 QLKKEIQEHvkkTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK10946 488 QLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
81-574 |
8.25e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 102.55 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 81 DGNGKEVRwSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQ 158
Cdd:PRK05620 32 GGAEQEQT-TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 159 SSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHS-REGWGNLKEMMKYAS-----DSHTCV----DTKHNELMAIYF 228
Cdd:PRK05620 109 HAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPKMIGHTHSSFGLGLsvngrfwLDLIASDVMWNTSDTG-------WAKSAWSSVFSPWTQGACVFahyLPRFD 301
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESflccvpiYHVLSWGVPLAAFMSGTPLV---FPGPD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 302 STSilQTLSKFPIT----VFCSAPTAYRMLIQNDI-TSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 376
Cdd:PRK05620 259 LSA--PTLAKIIATamprVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 377 LIcgnfkGMKIKPG-------------SMGKPSPAFNVEILDEnGTILPPG--QEGDIAVqvlpdRPFGLFTHYVDNPSK 441
Cdd:PRK05620 337 PV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTdrNEGEIQV-----RGNWVTASYYHSPTE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 442 T----ASTLRGN-------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 504
Cdd:PRK05620 406 EgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 505 SPDPIRGEVVKAFIVLNPDYKLHDQ--EQLKKEIQEHVKKTTAPYKYprkiEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-572 |
1.14e-22 |
|
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: 101.19 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAkcenLHSKLIVSQHsregwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd12114 89 LTDGPDAQLDVAVFD----VLILDLDALA--------------APAPPPPVDVAPDDLAYVIFTSGSTGTPKgvMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 244 SSFGLgLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCSAPT 322
Cdd:cd12114 151 ALNTI-LDINRRFAVG--PDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 323 AYRMLI----QNDITSykfNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM----- 392
Cdd:cd12114 227 LLEMLLdvleAAQALL---PSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsi 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 --GKPSPAFNVEILDENGTILPPGQEGDIavqvlpdrpF----GLFTHYVDNPSKTAS-----TLRGNFYITGDRGYMDE 461
Cdd:cd12114 301 pyGRPLANQRYRVLDPRGRDCPDWVPGEL---------WiggrGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 462 DGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYklhdQEQLKKEIQEHVK 541
Cdd:cd12114 372 DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG----TPIAPDALRAFLA 446
|
490 500 510
....*....|....*....|....*....|.
gi 65301416 542 KTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd12114 447 QTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
210-576 |
1.21e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.32 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 210 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQG 289
Cdd:PRK12467 1707 SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLING 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 290 A-CVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTG-LDIY 367
Cdd:PRK12467 1785 ArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLF 1864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 368 EGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPS 440
Cdd:PRK12467 1865 NLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLGGV-----GLARGYLNRPA 1937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 441 KTA--------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGE 512
Cdd:PRK12467 1938 LTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGK 2016
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 513 VVKAFIVLNPDYKLHD---QEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 576
Cdd:PRK12467 2017 QLVAYVVPTDPGLVDDdeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD 2083
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
226-569 |
1.46e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 101.13 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSS-----------FGLGlsvNGRFWL-------DLiasDVMwntsdtgwaksawsSVFSPWT 287
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNlvsftnwmledFALP---EGPQFLnqapysfDL---SVM--------------DLYPTLA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 288 QGACVFAhyLPRfDSTS----ILQTLSKFPITVFCSAPTAYRM-LIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKK- 361
Cdd:PRK04813 208 SGGTLVA--LPK-DMTAnfkqLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERf 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 362 TGLDIYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQEGDI-----AVQVlpdr 427
Cdd:PRK04813 285 PSATIYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIvisgpSVSK---- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 428 pfGlfthYVDNPSKTAS---TLRGN-FYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVV 503
Cdd:PRK04813 357 --G----YLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 65301416 504 sspdPI-RGEVVK---AFIVLNPdyklHDQE---QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 569
Cdd:PRK04813 430 ----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
226-579 |
1.51e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 100.11 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFWLD-----LIASDVmwnTSDTGWAksawSSVFSPWTQGA--CVFAHYL 297
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeAYNEALNCEqdetpIVACPV---THSYGLI----CGVLAALTRGSkpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRFdstsILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLkhcVSAGEPINPEVMEQWKKKTgLDIYEGYGQTET-- 375
Cdd:PRK08308 179 PKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGCSEAgc 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 376 VLICGNFKgmkiKPGSMGKPSPAFNVEI-LDENgtilppgqegdiavqvlpdrpfglfthyvdNPSKTASTLRGNFYITG 454
Cdd:PRK08308 251 VSICPDMK----SHLDLGNPLPHVSVSAgSDEN------------------------------APEEIVVKMGDKEIFTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 455 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKK 534
Cdd:PRK08308 297 DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI---DPVQLRE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 65301416 535 EIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 579
Cdd:PRK08308 374 WCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-574 |
2.87e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAkcenlhskLIVSQHSREGWgnlkemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12316 2105 LTQRHLLERLPLPAG--------VARLPLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYR 325
Cdd:PRK12316 2171 LVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQ 2248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 326 MLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETVLICGNFKGMKIKPGS-----MGKPSPAF 399
Cdd:PRK12316 2249 QLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNR 2328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 400 NVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVARS 471
Cdd:PRK12316 2329 RAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRI 2403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 472 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVlnPDyklHDQEQLKKEIQEHVKKTTAPYKYPR 551
Cdd:PRK12316 2404 DHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPAYMVPA 2477
|
490 500
....*....|....*....|...
gi 65301416 552 KIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK12316 2478 HWVVLERLPLNPNGKLDRKALPK 2500
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
75-574 |
7.47e-22 |
|
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: 99.24 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 75 PAFWWVD-GNGKEVRWSFEELGSLSRKFANILTEACslQRGDRVMVILPKIPEWWLANVACLRTGTV---LIPGTTQLTQ 150
Cdd:cd05931 10 PAYTFLDdEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPPTPGRHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 151 KDILYRLQSSKSKCIITDDTLAPAV-DIVAAKCENLHSKLIVSQHSREGwgnlkemmkyASDSHTCVDTKHNELMAIYFT 229
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAAVrAFAASRPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 230 SGTTGPPK--MIGHthssfgLGLSVNgrfwLDLIASDVMWNTSDTGwakSAW----------SSVFSPWTQGA-CVF--- 293
Cdd:cd05931 158 SGSTGTPKgvVVTH------RNLLAN----VRQIRRAYGLDPGDVV---VSWlplyhdmgliGGLLTPLYSGGpSVLmsp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 294 AHYL--P-RFdstsiLQTLSKFPITvFCSAPT-AYRMLIQ----NDITSYKFNSLKHCVSAGEPINPEVMEQWKKK---T 362
Cdd:cd05931 225 AAFLrrPlRW-----LRLISRYRAT-ISAAPNfAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 363 GLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFNVEILDENG-TILP 412
Cdd:cd05931 299 GFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDPETgRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 413 PGQEGDIAVQ---VLPdrpfGlfthYVDNPSKTASTLR-------GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRI 482
Cdd:cd05931 379 DGEVGEIWVRgpsVAS----G----YWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 483 GPFEVESALIE-HPSIAES--AVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQ-----EH-VKkttapykyPRKI 553
Cdd:cd05931 450 YPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLVVVAEVERGADPA-DLAAIAAAIRaavarEHgVA--------PADV 520
|
570 580
....*....|....*....|...
gi 65301416 554 EFIE--ELPKTVSGKVKRNELRR 574
Cdd:cd05931 521 VLVRpgSIPRTSSGKIQRRACRA 543
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-538 |
8.86e-22 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 98.59 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ItddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd17640 82 V-------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 246 FGLGLSvngRFW--LDLIASDVMWntsdtgwaksawsSVFSPW--TQGAC---VFA-----HYlprfdsTSI---LQTLS 310
Cdd:cd17640 113 LLHQIR---SLSdiVPPQPGDRFL-------------SILPIWhsYERSAeyfIFAcgcsqAY------TSIrtlKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 311 KFPITVFCSAPTAYRML---IQNDITSYKF------------NSLKHCVSAGEPINPEVmEQWKKKTGLDIYEGYGQTET 375
Cdd:cd17640 171 RVKPHYIVSVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 376 --VLICGNFKGMKIkpGSMGKPSPAFNVEILDENG-TILPPGQEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLRGN 449
Cdd:cd17640 250 spVVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVrgpQVM--------KGYYKNPEATSKVLDSD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 -FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIaESAVVSSPDPIRgevVKAFIVlnPDYklh 527
Cdd:cd17640 320 gWFNTGDLGWLTCGGELVLTGRAKDTIvLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIV--PNF--- 390
|
490
....*....|.
gi 65301416 528 dqEQLKKEIQE 538
Cdd:cd17640 391 --EELEKWAKE 399
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
347-573 |
6.93e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 95.45 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 347 GEPINPEVMEQwKKKTGLDIYEGYGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFNVEIldengtilPPGQEGD 418
Cdd:PRK07445 239 GAPAWPSLLEQ-ARQLQLRLAPTYGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITI--------PANQTGN 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 419 IAVQVlPDRPFGLFTHYVDNPsktastlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIA 498
Cdd:PRK07445 304 ITIQA-QSLALGYYPQILDSQ---------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQ 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 499 ESAVVSSPDPIRGEVVKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PRK07445 374 DVCVLGLPDPHWGEVVTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-572 |
8.88e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 93.96 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 170 TLAPAVDIVaakcenlhSKLIVSQHSREGWGNLKEMMKYASDSHTCVdtkhnelmaIYFTSGTTGPPK--MIGHThssfg 247
Cdd:PRK10252 564 DQLPRFADV--------PDLTSLCYNAPLAPQGAAPLQLSQPHHTAY---------IIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 248 lgLSVNGRFWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF-----AHYlprfDSTSILQTLSKFPITV-- 316
Cdd:PRK10252 622 --AIVNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTth 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 --------FCSAPTayrmliqNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVL------ICG-- 380
Cdd:PRK10252 695 fvpsmlaaFVASLT-------PEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGee 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 381 --NFKGMKIKPGSmgkpsPAFN--VEILDENGTILPPGQEGDI---AVQvlpdrpfgLFTHYVDNPSKTASTLRGN---- 449
Cdd:PRK10252 768 laAVRGSSVPIGY-----PVWNtgLRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfap 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 450 ---FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA----VVSSPDPIRGEVVK--AFIVL 520
Cdd:PRK10252 835 gerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDARQlvGYLVS 914
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 65301416 521 NPDYKLhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK10252 915 QSGLPL-DTSAL----QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
216-572 |
1.82e-19 |
|
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: 91.31 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 216 VDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFWLDLIASDVMwntsdtgwaksawsSVFSPWtqgacVF 293
Cdd:cd17648 89 VITNSTDLAYAIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAV--------------LFFSNY-----VF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 294 AHYLPRFdSTSIL--QTLSKFPITVFCSAPTAYRMLIQNDIT----------SYKF---NSLKHCVSAGEPINPEVMEQW 358
Cdd:cd17648 149 DFFVEQM-TLALLngQKLVVPPDEMRFDPDRFYAYINREKVTylsgtpsvlqQYDLarlPHLKRVDAAGEEFTAPVFEKL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 359 KKKTGLDIYEGYGQTETVL--ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGD-------IAVQVLpDRPF 429
Cdd:cd17648 228 RSRFAGLIINAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGElylggdgVARGYL-NRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 430 GLFTHYVDNPSKTAS-TLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 505
Cdd:cd17648 307 LTAERFLPNPFQTEQeRARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 65301416 506 PDP-IRGEVVKAFIVlnpDYKLHDQEQL-KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17648 387 EDAsQAQSRIQKYLV---GYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-569 |
3.99e-18 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 87.86 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 89 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 169 DTlaPAVDIVAAKCENLHS--KLIVS--------QHSREGW-GNLKEMMKYASDSHTCV------DTKHNELMAIYFTSG 231
Cdd:cd17641 91 DE--EQVDKLLEIADRIPSvrYVIYCdprgmrkyDDPRLISfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 232 TTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACV-FAHylprfDSTSILQTLS 310
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnFPE-----EPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 311 KFPITVFCSAP------------------------------TAYRMLIQN---------DITSYK--------------- 336
Cdd:cd17641 243 EIGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGkrgrpvslwLRLASWladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 337 FNSLKHCVSAGEPINPEVMeQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIlDENGTILPPGQe 416
Cdd:cd17641 323 FSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEILVRSP- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 417 gdiavqvlpdrpfGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDV-ILSSGYRIGPFEVESALIEH 494
Cdd:cd17641 400 -------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 495 PSIAESAVVSSPDPIrgevVKAFIVLNP---------------DYK-LHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEE 558
Cdd:cd17641 467 PYIAEAVVLGAGRPY----LTAFICIDYaivgkwaeqrgiaftTYTdLASRPEVYELIRKEVEKVNASLPEAQRIRRFLL 542
|
570 580
....*....|....*....|
gi 65301416 559 LPK---------TVSGKVKR 569
Cdd:cd17641 543 LYKeldaddgelTRTRKVRR 562
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-574 |
1.79e-17 |
|
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: 85.17 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IITDdtlapavdivaakcenlHSKLIVSQHSREgwgnlkemmkyasdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05939 79 LIFN-----------------LLDPLLTQSSTE--------------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 SFgLGLSVNGRFWLDLIASDVMWNTsdtgwaKSAWSSVFSPWTQGACVFahylprFDSTSILQtlSKFPITVFCSAPTAY 324
Cdd:cd05939 128 RY-YRIAAGAYYAFGMRPEDVVYDC------LPLYHSAGGIMGVGQALL------HGSTVVIR--KKFSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 325 RMLIQNDI---------TSYKFNSLKHCV--SAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKG-------- 384
Cdd:cd05939 193 NCTIVQYIgeicryllaQPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 385 ----MKIKPGSMGKPSPAFNVEILDENGTILP--PGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNF------YI 452
Cdd:cd05939 273 srilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 453 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVlNPDYKLhDQE 530
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DPERKV-DLD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 65301416 531 QLKKEIQehvkKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05939 430 RFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
51-573 |
1.79e-17 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 86.29 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 51 YFNFAKDVLdqwtnTEKTGKRLSNPAFWWVD--GNGKEV-RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW 127
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDegSDDLPVnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL-----------------APAVDIVAAKCENLHSKLi 190
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 191 vsqhsREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLIASDV 265
Cdd:PLN03052 326 -----REGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 266 M-WNTsDTGWAKSAWsSVFSPWTQGACvfahyLPRFDSTSILQTLSKF----PITVFCSAPTAYRMLIQNDITS-YKFNS 339
Cdd:PLN03052 400 VcWPT-NLGWMMGPW-LVYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAgLDWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 340 LKHCVSAGEPINPE----VMEQWKKKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFNVEILDENGTIL 411
Cdd:PLN03052 473 IRCFGSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 412 PPGQEGDIAVqvlpdrpfGLFTHYVDNPSKTASTLRGNFYITGD--------RGYMDE-----DGYFWFVARSDDVIlss 478
Cdd:PLN03052 547 PDDAPCTGEL--------ALFPLMFGASSTLLNADHYKVYFKGMpvfngkilRRHGDIfertsGGYYRAHGRADDTM--- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 479 gyRIGPFEVESALIE------HPSIAESAVVSSPDPIRG--EVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYP 550
Cdd:PLN03052 616 --NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKV 693
|
570 580
....*....|....*....|...
gi 65301416 551 RKIEFIEELPKTVSGKVKRNELR 573
Cdd:PLN03052 694 SAVVIVPSFPRTASNKVMRRVLR 716
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
45-566 |
4.15e-17 |
|
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: 84.63 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 45 KIEIPEYF-----NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMV 119
Cdd:cd05943 58 IMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 120 ILPKIPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDDT---------LAPAVDIVAAKCENLHS 187
Cdd:cd05943 129 YLPNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 188 KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNEL----------MAIYFTSGTTGPPKMIghTHSSFGLGLSVNGRFW 257
Cdd:cd05943 206 VVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPKCI--VHGAGGTLLQHLKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 258 L--DLIASDVM-WNTSdTGWAksAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTL-SKFPITVFCSAPTAYRMLIQNDI 332
Cdd:cd05943 284 LhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGAtIVLYDGSPFYPDTNALWDLaDEEGITVFGTSAKYLDALEKAGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 333 ---TSYKFNSLKHCVSAGEPINPE----VMEQWKKktGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFNV 401
Cdd:cd05943 361 kpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 402 EILDENGTILPpGQEGD-IAVQVLPDRPfglfTHYVDNPSktASTLRGNFYIT-------GDRGYMDEDGYFWFVARSDD 473
Cdd:cd05943 436 EAFDEEGKPVW-GEKGElVCTKPFPSMP----VGFWNDPD--GSRYRAAYFAKypgvwahGDWIEITPRGGVVILGRSDG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 474 VILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKI 553
Cdd:cd05943 509 TLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEL--DDELRKRIRSTIRSALSPRHVPAKI 586
|
570
....*....|...
gi 65301416 554 EFIEELPKTVSGK 566
Cdd:cd05943 587 IAVPDIPRTLSGK 599
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
218-572 |
5.25e-17 |
|
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: 83.67 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 218 TKHNELMAIYFTSGTTGPPK--MIGH---THSSFGL-------GLSVN----GRFWLDLIASDvmwntsdtgWAKSAWS- 280
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHrnvAHAAHAWrreyeldSFPVRllqmASFSFDVFAGD---------FARSLLNg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 281 SVFSPWTQGAcvfahylpRFDSTSILQTLSKFPITVFCSAPTAYRMLIQN-DITSYKFNSLKHCVSAGEpinpEVMEQWK 359
Cdd:cd17650 161 GTLVICPDEV--------KLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSD----GCKAQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 360 K------KTGLDIYEGYGQTETVLICGNFK-GMKIKPGS----MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrP 428
Cdd:cd17650 229 KtlaarfGQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 429 FGLFTHYVDNPSKTASTLR-------GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:cd17650 304 AGVARGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAV 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 502 VVSSPDPiRGEV-VKAFIVlnPDYKLHdqeqlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17650 384 VAVREDK-GGEArLCAYVV--AAATLN-----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
88-507 |
1.71e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 82.61 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIpgTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK08279 62 SISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLL--NTQQRGAVLAHSLNLVDAKHL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 166 ITDDTLAPAVDIVAAKCENLHSKLIVSQ---HSREGWGNLKEMMKyASDSHTCVDTKH--NELMAIY-FTSGTTGPPKMI 239
Cdd:PRK08279 139 IVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAA-GAPTTNPASRSGvtAKDTAFYiYTSGTTGLPKAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 240 GHTH-----SSFGLGLSvngrfwLDLIASDVMWNT----SDTGwAKSAWSSVFSPwtqGACVFAHylPRFDSTSILQTLS 310
Cdd:PRK08279 218 VMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWSSVLAA---GATLALR--RKFSASRFWDDVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 311 KFPITVFCsaptaY-----RMLIQNDITSY-KFNSLKHCVSAGepINPEVMEQWKKKTGLD-IYEGYGQTE--TVLIcgN 381
Cdd:PRK08279 286 RYRATAFQ-----YigelcRYLLNQPPKPTdRDHRLRLMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEgnVGFI--N 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 382 FKGmkiKPGSMGKpSPAFN------VEILDENGTIL----------PPGQEGDIAVQVLPDRPfglFTHYVDnPSKT-AS 444
Cdd:PRK08279 357 VFN---FDGTVGR-VPLWLahpyaiVKYDVDTGEPVrdadgrcikvKPGEVGLLIGRITDRGP---FDGYTD-PEASeKK 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 65301416 445 TLRGNF------YITGDRGYMDEDGYFWFVARSDDVilssgYR-----IGPFEVESALIEHPSIAESAV--VSSPD 507
Cdd:PRK08279 429 ILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-573 |
2.95e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 81.79 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 121 LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL----------------APAVDIV-AAKCE 183
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplyskvveaAPAKAIVlPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 184 NLHSKLivsqhsREGWGNLKEMMKYASDSHtCVDTKHNE--------LMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGR 255
Cdd:PLN03051 81 PVAVPL------REQDLSWCDFLGVAAAQG-SVGGNEYSpvyapvesVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 256 FWLDLIASDVM-WNTSdTGWAKSAWsSVFSPWTQGACVfAHYLPRFDSTSILQTLSKFPITVFCSAPT---AYRMLIQND 331
Cdd:PLN03051 153 AHMDIQPGDVVcWPTN-LGWMMGPW-LLYSAFLNGATL-ALYGGAPLGRGFGKFVQDAGVTVLGLVPSivkAWRHTGAFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 332 ITSYKFNSLKHCVSAGEPINPE------VMEQWKKKT-----GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFN 400
Cdd:PLN03051 230 MEGLDWSKLRVFASTGEASAVDdvlwlsSVRGYYKPVieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 401 VEILDENGTILPPGQE--GDIAVQVL----PDRpfgLF------THYVDNP--SKTASTLRGNfyitGDRGYMDEDGYFW 466
Cdd:PLN03051 302 FVLLNDNGVPYPDDQPcvGEVALAPPmlgaSDR---LLnadhdkVYYKGMPmyGSKGMPLRRH----GDIMKRTPGGYFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 467 FVARSDDVILSSGYRIGPFEVESALIE-HPSIAESAVVSSPDPIRGE----VVKAFIVLNPDYKLHDQEQLKKEIQEHVK 541
Cdd:PLN03051 375 VQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQ 454
|
490 500 510
....*....|....*....|....*....|..
gi 65301416 542 KTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 573
Cdd:PLN03051 455 TNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-572 |
2.99e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.91 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 221 NELMAIYFTSGTTGPPKmighthssfglGLSVNGRF----------WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTqGA 290
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLF-GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 291 CV------FAHylprfDSTSILQTLSKFPITVFCSAPT-AYRMLIQNDITsykFNSLKHCVSAGEPINPEVMEQW-KKKT 362
Cdd:PRK05691 3937 RVeivpnaIAH-----DPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWlQRYP 4008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 363 GLDIYEGYGQTETVLICGNFK-GMKIKPGS---MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDN 438
Cdd:PRK05691 4009 QIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGD 4083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 439 PSKTASTLRGN--------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiR 510
Cdd:PRK05691 4084 PLRTALAFVPHpfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-N 4162
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 65301416 511 GEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK05691 4163 GKHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-503 |
1.10e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 79.81 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 218 TKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLsvngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSPwtqgACVFAHYL 297
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--------DALRQLYGIRPGEVDLATFPLFALFGP----ALGLTSVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRFDSTS--------ILQTLSKFPITVFCSAPTAYRML----IQNDITsykFNSLKHCVSAGEPINPEVMEQWKK--KTG 363
Cdd:cd05910 150 PDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVarycAQHGIT---LPSLRRVLSAGAPVPIALAARLRKmlSDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 364 LDIYEGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFNVEILD---------ENGTILPPGQEGDIAV--- 421
Cdd:cd05910 227 AEILTPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVtgp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 422 QVLPDrpfglfthYVDNPSKTA----STLRGNF-YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPS 496
Cdd:cd05910 307 TVTPT--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPG 378
|
....*..
gi 65301416 497 IAESAVV 503
Cdd:cd05910 379 VRRSALV 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-572 |
1.62e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.60 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYfTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWaKSAWSSVFSPWTQGACVFAHYLPRFDSTS 304
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 305 ILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETV---LICG 380
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACL 2494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 381 NFKGMKIKPGS--MGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNF 450
Cdd:PRK05691 2495 APEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRL 2569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP----IRGEVVKAFIVLNPDykl 526
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqLAGYLVSAVAGQDDE--- 2646
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 65301416 527 hDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:PRK05691 2647 -AQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
81-572 |
1.74e-15 |
|
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: 79.05 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 81 DGNGKEVRWSFEELGSLSRKFANILTEacSLQRGDRVMVI-LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd17654 9 DQTTSDTTVSYADLAEKISNLSNFLRK--KFQTEERAIGLrCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 160 SKSKCIITDdtlapavdivaakCENLHSKLivsqhsregwgnlkemmkYASDSHTCVDTKHNELMA-IYFTSGTTGPPKM 238
Cdd:cd17654 87 CHVSYLLQN-------------KELDNAPL------------------SFTPEHRHFNIRTDECLAyVIHTSGTTGTPKI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 239 IGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGACVFAHYLPRFDSTSILQTL--SKFPITV 316
Cdd:cd17654 136 VAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 317 FCSAPTAYRMLIQNDITSY---KFNSLKHCVSAGEPInPE--VMEQWKKK-TGLDIYEGYGQTETVlICGNFKGMKIK-- 388
Cdd:cd17654 214 LQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPF-PSlvILSSWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEds 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 389 PGSMGKPSPAFNVEILDENGTiLPPGQ---EGDIAVQVLPDrpfglfthYVDNPsktastlRGNFYITGDRGYMdEDGYF 465
Cdd:cd17654 292 PVQLGSPLLGTVIEVRDQNGS-EGTGQvflGGLNRVCILDD--------EVTVP-------KGTMRATGDFVTV-KDGEL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 466 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDpirgEVVKAFIVLnpdyklhdqEQLKKEIQEHVKKTT- 544
Cdd:cd17654 355 FFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVG---------ESSSSRIHKELQLTLl 421
|
490 500
....*....|....*....|....*...
gi 65301416 545 APYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17654 422 SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
220-579 |
2.37e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 220 HNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSvngrfWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFA 294
Cdd:PRK05691 1273 DNLAYVIY-TSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGCrLVLA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 295 HYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITSyKFNSLKHCVSAGEPINPE----VMEQWKkktGLDIYEGY 370
Cdd:PRK05691 1346 GPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAElrnrVLQRLP---QVQLHNRY 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 371 GQTETVL-----ICGNFKGMKikpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA-- 443
Cdd:PRK05691 1422 GPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAer 1493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 444 ------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAF 517
Cdd:PRK05691 1494 fvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQ 1568
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 518 IV--LNPDYKLHDQ-EQLKKEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 579
Cdd:PRK05691 1569 LVgyYTGEAGQEAEaERLKAALAAELPE----YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
221-575 |
5.20e-15 |
|
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: 77.91 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 221 NELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRfwldLIASDVMWNTSDT--GWAksawssvfsPWTQG--------A 290
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHEN----LVHNMF----AILNSTEWKTKDRilSWM---------PLTHDmgliafhlA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 291 CVFAHYLPRFDSTSI--------LQTLSKFPITVFCSAPTAYRMLIQ--NDITSYKFN--SLKHCVSAGEPINPEVMEQW 358
Cdd:cd05908 169 PLIAGMNQYLMPTRLfirrpilwLKKASEHKATIVSSPNFGYKYFLKtlKPEKANDWDlsSIRMILNGAEPIDYELCHEF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 359 KK---KTGLD---IYEGYGQTE-TVLICGNFKGMKIKPG---------------------------SMGKPSPAFNVEIL 404
Cdd:cd05908 249 LDhmsKYGLKrnaILPVYGLAEaSVGASLPKAQSPFKTItlgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRIC 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 405 DENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMdEDGYFWFVARSDDVILSSGYRIG 483
Cdd:cd05908 329 DEDNKILPDGYIGHIQI-----RGKNVTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVY 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 484 PFEVESALIEHPSIAESAVVS---SPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTApyKYPRKIEFIEELP 560
Cdd:cd05908 403 PHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIP 478
|
410
....*....|....*
gi 65301416 561 KTVSGKVKRNELRRK 575
Cdd:cd05908 479 KTTSGKVKRYELAQR 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
88-562 |
1.19e-14 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 76.95 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSKSKC 164
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IITDDTLAPAVDIV--AAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELM---AIY-FTSGTTGPPK- 237
Cdd:cd05938 82 LVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIkspALYiYTSGTTGLPKa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 238 -MIGHTHSSFGLG-LSVNGrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAhylPRFDSTSILQTLSKFPI 314
Cdd:cd05938 162 aRISHLRVLQCSGfLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGAtCVLK---PKFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 315 TVFCSAPTAYRMLIQndiTSYKFNSLKHCV--SAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGNFKGmkiKPGS 391
Cdd:cd05938 234 TVIQYIGELLRYLCN---QPQSPNDRDHKVrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYTG---KIGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 392 MGKPS-------P----AFNVE----ILDENGTILP--PGQEGDIAVQVLPDRPfglFTHYVDNPSKTASTL------RG 448
Cdd:cd05938 308 VGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP---FLGYAGDKEQTEKKLlrdvfkKG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 449 NFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVLNPDYK 525
Cdd:cd05938 385 DVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKLKPGHE 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 65301416 526 LhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKT 562
Cdd:cd05938 464 F-DGKKL----YQHVREYLPAYARPRFLRIQDSLEIT 495
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-567 |
1.94e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.93 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 225 AIYFTSGTTGPPKMIGHTHSSFglgLS----VNGRfwLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRF 300
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 301 DS---TS--ILQTLSKFPITVFCSaPTAYR----MLIQNDIT-----------------SYKFNSLKHCVSAGEPINPEV 354
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeLIYDTNATilfgtdtflngyaryahPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 355 MEQWKKKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFN-----VEILDENGTILPPGqegdiavqvlPDR 427
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEyrlepVPGIDEGGRLFVRG----------PNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 428 PFGlfthYV--DNPSkTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 505
Cdd:PRK06814 992 MLG----YLraENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI 1066
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 506 PDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKV 567
Cdd:PRK06814 1067 PDARKGER----IIL-----LTTASDATRAaFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-574 |
4.94e-14 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 74.31 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 88 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLtqkdilyRLQSskskciit 167
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL-------RGES-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 168 ddtLAPAVDIVAAKcenlhsklivsqhsregwgnlkemmkyasdsHTCVDTkhneLMAIYfTSGTTGPPKMIGHTHSSFG 247
Cdd:cd05940 67 ---LAHCLNVSSAK-------------------------------HLVVDA----ALYIY-TSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 248 LGLSVNGrFWLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRFDSTSILQTLS-------------KFPI 314
Cdd:cd05940 108 RGGAFFA-GSGGALPSDVLYTC---------------------------LPLYHSTALIVGWSaclasgatlvirkKFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 315 TVFCSAPTAYR-MLIQ--NDITSYKFNS------LKHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNF 382
Cdd:cd05940 160 SNFWDDIRKYQaTIFQyiGELCRYLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 383 KGmkiKPGSMG-------KPSPAFNVEILDENGTIL----------PPGQEGDIAVQVLPDRPFglfTHYVDNPSKTAST 445
Cdd:cd05940 240 FG---KPGAIGrnpsllrKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPF---DGYTDPAATEKKI 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 446 LRGNF------YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAF 517
Cdd:cd05940 314 LRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 65301416 518 IVLNPDYKLhDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:cd05940 393 IVLQPNEEF-DLSALAA----HLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
451-574 |
7.13e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.16 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 451 YITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklHDQE 530
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDG----GPAP 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 65301416 531 QLkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 574
Cdd:PRK07824 311 TL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-569 |
1.10e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 70.59 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 53 NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEwwlANV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 133 ACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDD------TLAPAVDIVAAKCENLHS--KLIVSQHSREG--- 198
Cdd:PRK03584 155 AMLATaslGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggKAFDRRAKVAELRAALPSleHVVVVPYLGPAaaa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 199 --------WGNLkeMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfG---------LGLSvngrfwLDLI 261
Cdd:PRK03584 235 aalpgallWEDF--LAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---GgillehlkeLGLH------CDLG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 262 ASD-VMWNTSdTGWAksAWSSVFSPWTQGACVfahYL----PRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQNDIT-- 333
Cdd:PRK03584 304 PGDrFFWYTT-CGWM--MWNWLVSGLLVGATL---VLydgsPFYPDPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVpg 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 334 -SYKFNSLKHCVSAGEPINPE----VMEQWKKktglDIY--EGYGQTEtvlICGNFKG----MKIKPGSMGKPSPAFNVE 402
Cdd:PRK03584 378 eTHDLSALRTIGSTGSPLPPEgfdwVYEHVKA----DVWlaSISGGTD---ICSCFVGgnplLPVYRGEIQCRGLGMAVE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 403 ILDENGTilpP--GQEGDIAV-QVLPDRPFGlFTHYVDNpsktaSTLRGNFYIT-------GDRGYMDEDGYFWFVARSD 472
Cdd:PRK03584 451 AWDEDGR---PvvGEVGELVCtKPFPSMPLG-FWNDPDG-----SRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGRSD 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqLKKEIQEHVKKTTAPYKYPRK 552
Cdd:PRK03584 522 ATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA--LRARIRTTIRTNLSPRHVPDK 599
|
570 580
....*....|....*....|..
gi 65301416 553 IEFIEELPKTVSGK-----VKR 569
Cdd:PRK03584 600 IIAVPDIPRTLSGKkvelpVKK 621
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-574 |
1.83e-12 |
|
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: 69.94 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTlapaVDIVAakcenlhsklivsqhsregwgnLKE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAG----VKVYS----------------------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 205 MMK-YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVmwntsdtgwaksawSSVF 283
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGN---------------IVSNV--------------AGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 284 SPWTQGACVFAH-----YLP-----------------------RFDSTSILQTLSKFPITVFCSAPTAY-RML--IQNDI 332
Cdd:cd05927 148 KILEILNKINPTdvyisYLPlahifervvealflyhgakigfySGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkIFNKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 333 --------------TSYKFNSLKH---------------------------CVSAGEPINPEVMEQWKKKTGLDIYEGYG 371
Cdd:cd05927 228 qakgplkrklfnfaLNYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 372 QTETV-LICGNFKGMKIkPGSMGKPSPAFNVEILD--E-NGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLR 447
Cdd:cd05927 308 QTECTaGATLTLPGDTS-VGHVGGPLPCAEVKLVDvpEmNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 448 GN-FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVvsspdpiRGEVVKAF----IVLN 521
Cdd:cd05927 382 EDgWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 522 PDY-------KLHDQ---------EQLKKEIQEHVKKTTA-----PYKYPRKI-----EFIEE---LpkTVSGKVKRNEL 572
Cdd:cd05927 455 PDVlkewaasKGGGTgsfeelcknPEVKKAILEDLVRLGKenglkGFEQVKAIhlepePFSVEnglL--TPTFKLKRPQL 532
|
..
gi 65301416 573 RR 574
Cdd:cd05927 533 KK 534
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
209-569 |
2.83e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 69.25 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 209 ASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfglglsvnGRFWLDL----------IASDVMwntsdtgwakSA 278
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITH----------GNLYANAeamfvaaefdVETDVM----------VS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 279 WSSVF----------SPWTQGACVF----AHYLPrfDSTSILQTLSKFPITV-----FCSAPTAYRMLIQNDITSYKFNS 339
Cdd:PRK07768 200 WLPLFhdmgmvgfltVPMYFGAELVkvtpMDFLR--DPLLWAELISKYRGTMtaapnFAYALLARRLRRQAKPGAFDLSS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 340 LKHCVSAGEPINPEVMEQW---KKKTGLD---IYEGYGQTETVLI-----CGNfkGMKI------------------KPG 390
Cdd:PRK07768 278 LRFALNGAEPIDPADVEDLldaGARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 391 -----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQ---VLPdrpfglftHYVDNPSKTASTLRGNFYITGDRGYMDED 462
Cdd:PRK07768 356 trrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRgesVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 463 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYKLHDQE---QLKKEIQEH 539
Cdd:PRK07768 428 GEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAevrRIRHQVAHE 506
|
410 420 430
....*....|....*....|....*....|..
gi 65301416 540 VKKTTApyKYPRKIEFIE--ELPKTVSGKVKR 569
Cdd:PRK07768 507 VVAEVG--VRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
226-566 |
5.41e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.42 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA-----HY--LP 298
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplHYriVP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 299 R----------FDSTSILQTLSKFpitvfcSAPtayrmliqnditsYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 368
Cdd:PRK08043 449 ElvydrnctvlFGTSTFLGNYARF------ANP-------------YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 369 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD----ENGTIL----PPGQEGDIAVQvlpdRPFGLFTHYVDNPs 440
Cdd:PRK08043 510 GYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNGYLRVE----KPGVLEVPTAENA- 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 441 ktASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVES-ALIEHPSiAESAVVSSPDPIRGEvvkAFIV 519
Cdd:PRK08043 585 --RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDASKGE---ALVL 658
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 65301416 520 LNPDYKLHdQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGK 566
Cdd:PRK08043 659 FTTDSELT-REKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGK 701
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
393-573 |
2.94e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 393 GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMdEDGYFWFVARSD 472
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 473 DVILSSGYRIGPFEVESALIEHPSI--AESAVVSSPDPiRGEVVKAFI---VLNPDyklhDQEQLKKEIQEHVKKTTApy 547
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*...
gi 65301416 548 kYPRKIEFI--EELPKTVSGKVKRNELR 573
Cdd:PRK09192 535 -VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-503 |
3.37e-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: 59.68 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDtlAPAVDIVAAKCENL-HSKLIVsQHSRE------ 197
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKILQIQDKLpHLKAII-QYKEPlkekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 198 ---GWGNLKEMMKYASDS--HTCVDT-KHNELMAIYFTSGTTGPPK--MIGHTHSSF-GLGLSVNGRF------------ 256
Cdd:cd05933 121 nlySWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLrpatvgqesvvs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 257 WLDL--IASDVMwntsdtgwaksawsSVFSPWTQGACVfahYLPRFDST--SILQTLSKFPITVFCSAP----------- 321
Cdd:cd05933 201 YLPLshIAAQIL--------------DIWLPIKVGGQV---YFAQPDALkgTLVKTLREVRPTAFMGVPrvwekiqekmk 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 322 ------TAYRMLI-------------------QNDITSYK---------------FNSLKHCVSAGEPINPEVMEQWkkk 361
Cdd:cd05933 264 avgaksGTLKRKIaswakgvgletnlklmggeSPSPLFYRlakklvfkkvrkalgLDRCQKFFTGAAPISRETLEFF--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 362 TGLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFNVEILDEN----GTILPPGQEgdiavqvlpdrpfg 430
Cdd:cd05933 341 LSLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDadgiGEICFWGRH-------------- 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 65301416 431 LFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDD-VILSSGYRIGPFEVESALIEHPSIAESAVV 503
Cdd:cd05933 402 VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKKELPIISNAML 476
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
341-577 |
1.19e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 57.44 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 341 KHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP---------AFNVEILDENG 408
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfenqVVLVKMDPETD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 409 TIL-----------PPGQEGDIAVQVLPDrPFGLFTHYVDNPSKTASTL------RGN-FYITGDRGYMDEDGYFWFVAR 470
Cdd:cd05937 281 DPIrdpktgfcvraPVGEPGEMLGRVPFK-NREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 471 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP-IRGEVVKAFIVLNPDYKLHDQEQlKKEIQEHVKKTTAPYKY 549
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFT-KSLLASLARKNLPSYAV 438
|
250 260
....*....|....*....|....*...
gi 65301416 550 PRKIEFIEELPKTVSGKVKRNELRRKEW 577
Cdd:cd05937 439 PLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
229-575 |
1.11e-07 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 54.17 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPKMIGHTHSSFglglsvngRFWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGACvfAHY-L 297
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL--------DVWAELVArcldaagvtpGDRVQNA--YG---------YGLFTGGLG--FHYgA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRFDSTSI----------LQTLSKFPITVFCSAPT--------AYRMLIqnditSYKFNSLKHCVSAGEPINPEVMEQWK 359
Cdd:cd05913 145 ERLGALVIpagggnterqLQLIKDFGPTVLCCTPSyalylaeeAEEEGI-----DPRELSLKVGIFGAEPWTEEMRKRIE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 360 KKTGLDIYEGYGQTE-----TVLICGNFKGMKIKpgsmgkpSPAFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLFT 433
Cdd:cd05913 220 RRLGIKAYDIYGLTEiigpgVAFECEEKDGLHIW-------EDHFIPEIIDpETGEPVPPGEVGEL-----------VFT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 434 HYvdnpSKTASTLRgnFYITGD------------RGYMDEDGyfwFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 501
Cdd:cd05913 282 TL----TKEAMPLI--RYRTRDitrllpgpcpcgRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 502 --VVSSPDP-----IRGEVVKAFIVLNPDyklhdqEQLKKEIQEHVKKTTA--PykyprKIEFIE--ELPKTvSGKVKRN 570
Cdd:cd05913 353 qlILTRQEHldeltIKVEVRPEADDDEKL------EALKQRLERHIKSVLGvtV-----EVELVEpgSLPRS-EGKAKRV 420
|
....*
gi 65301416 571 ELRRK 575
Cdd:cd05913 421 IDKRK 425
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
226-494 |
2.26e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.67 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPrFDS 302
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTHAN----LLANQRACLKFFSpkeDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNP-LYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 303 TSILQTLSKFPITVFCSAPTAYRMLIQndiTSYKFN----SLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE-TV 376
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFDYILK---TAKKQEsclpSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTEcSP 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 377 LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTI-LPPGQEGDIAVqvlpdRPFGLFTHYVDN-PSKTASTLRG-NFYIT 453
Cdd:PRK06334 340 VITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLT-----RGTSLFSGYLGEdFGQGFVELGGeTWYVT 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 65301416 454 GDRGYMDEDGYFWFVARsddviLSSGYRIGPFEV-----ESALIEH 494
Cdd:PRK06334 415 GDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
229-569 |
6.91e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 51.69 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 229 TSGTTGPPKMIGHTHSSFGLglsvngrfWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGacVFAHY-L 297
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDR--------WAELFArslraagvrpGDRVQNA--FG---------YGLFTGG--LGLHYgA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 298 PRF----------DSTSILQTLSKFPITVFCSAPT--------AYRMLIqnDITSYkfnSLKHCVSAGEPInPEVMEQW- 358
Cdd:COG1541 150 ERLgatvipagggNTERQLRLMQDFGPTVLVGTPSyllylaevAEEEGI--DPRDL---SLKKGIFGGEPW-SEEMRKEi 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 359 KKKTGLDIYEGYGQTET-VLI---CGNFKGMKIKPGSmgkpspaFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLFT 433
Cdd:COG1541 224 EERWGIKAYDIYGLTEVgPGVayeCEAQDGLHIWEDH-------FLVEIIDpETGEPVPEGEEGEL-----------VVT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 434 HYvdnpSKTASTL-RgnfYITGDRGYMDED---------------GyfwfvaRSDDVILSSGYRIGPFEVESALIEHPSI 497
Cdd:COG1541 286 TL----TKEAMPLiR---YRTGDLTRLLPEpcpcgrthprigrilG------RADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 65301416 498 AESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKTTapyKYPRKIEFIE--ELPKTVsGKVKR 569
Cdd:COG1541 353 GPEYQIVVDREGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL---GLRAEVELVEpgSLPRSE-GKAKR 419
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-572 |
1.55e-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: 51.06 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 217 DTKHNELMAIYFTSGTTGPPKMIGHTHSSF-----GLGLSVNGRFW--------------LDLIASDV--MWNT------ 269
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLvagiaGLGDRVPELLGpddrylaylplahiFELAAENVclYRGGtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 270 ----SDTGWAKSAWS-SVFSPwTQGACVfahylPR-FDST-----SILQTLSKFPITVFCSAPTAYRMLIQNDITSYKFN 338
Cdd:cd17639 164 prtlTDKSKRGCKGDlTEFKP-TLMVGV-----PAiWDTIrkgvlAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 339 S-------------LKHCVSAGEPINPEVMEqWKKKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFN 400
Cdd:cd17639 238 ElvfkkvraalggrLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 401 VEILD--ENG--TILPPGQeGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN--FYiTGDRGYMDEDGYFWFVARSDD- 473
Cdd:cd17639 312 IKLVDweEGGysTDKPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDl 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 474 VILSSGYRIGPFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLN------------------PDYkLHDQEQLK-- 533
Cdd:cd17639 385 VKLQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPNekhltklaekhgvinsewEEL-CEDKKLQKav 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 65301416 534 -KEIQEHVKKTT-APYKYPRKIEFIEEL--PK----TVSGKVKRNEL 572
Cdd:cd17639 461 lKSLAETARAAGlEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
111-516 |
2.32e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.48 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdiLY-RLQSSKSKCIITDDTLApAVDIVAAKCENLHS-- 187
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVA-AIFCVPQTLNTLLScl 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 188 ------KLIV----------SQHSREGwgnlKEMMKYA-------SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHs 244
Cdd:PLN02736 169 seipsvRLIVvvggadeplpSLPSGTG----VEIVTYSkllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 245 sfglglsvngrfwLDLIAS------DVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRF---DSTSILQTLSKFPIT 315
Cdd:PLN02736 244 -------------GNLIANvagsslSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFyqgDNLKLMDDLAALRPT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 316 VFCSAPTAYRML---IQNDI------------TSYK--------------------FNSLK--------HCVSAGEPINP 352
Cdd:PLN02736 311 IFCSVPRLYNRIydgITNAVkesgglkerlfnAAYNakkqalengknpspmwdrlvFNKIKaklggrvrFMSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 353 EVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFNVEILDengtiLP---------PGQEGDIAVq 422
Cdd:PLN02736 391 DVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVD-----VPemnytsedqPYPRGEICV- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 423 vlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAES 500
Cdd:PLN02736 464 ----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQC 539
|
490 500
....*....|....*....|....*..
gi 65301416 501 AV-----------VSSPDPirgEVVKA 516
Cdd:PLN02736 540 FVygdslnsslvaVVVVDP---EVLKA 563
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
447-572 |
7.55e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 48.67 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES------------AVVS--SPDPIRGE 512
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 65301416 513 VVKAFIVLNPDYKLHDQ--------EQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 572
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
447-574 |
3.47e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.68 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 447 RGNFYITGDRGYMDEDGYFwFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGevVKAFIVLNPDYKL 526
Cdd:PRK05851 394 PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRG 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 65301416 527 HDQEQLKKEIQEHVKKTTApyKYPRKIEFIE--ELPKTVSGKVKRNELRR 574
Cdd:PRK05851 471 PDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
344-557 |
3.79e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 46.73 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 344 VSAGEPINPEVMEQWKKKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPspafnveilDEN---GTILPPGQEGDIA 420
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFP---------DEMcmlGTVGAPAVYNELR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 421 VQVLPD---RPFG-------------LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIG 483
Cdd:PLN02430 449 LEEVPEmgyDPLGepprgeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 484 PFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNPD---------------YKLHDQEQLKKEIQEHVKKTTAPYK 548
Cdd:PLN02430 529 LEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEEntnkwakdngftgsfEELCSLPELKEHILSELKSTAEKNK 605
|
....*....
gi 65301416 549 YpRKIEFIE 557
Cdd:PLN02430 606 L-RGFEYIK 613
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
368-477 |
3.39e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.47 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 368 EGYGQTETVLICGNFKGMKIkpGSMGKPSP--------AFNVE----ILDENGTIlppgQEGDIA-VQVLPDRPFGLFTh 434
Cdd:PRK07868 749 EFFATTDGQAVLANVSGAKI--GSKGRPLPgagrvelaAYDPEhdliLEDDRGFV----RRAEVNeVGVLLARARGPID- 821
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 65301416 435 yvdnpsKTASTLRGNFyITGDR----GYM---DEDGYFWFVARSDDVILS 477
Cdd:PRK07868 822 ------PTASVKRGVF-APADTwistEYLfrrDDDGDYWLVDRRGSVIRT 864
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-261 |
3.43e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 40.34 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 65301416 165 IITDDTLAPAVDIvaakcenlHSKLIVSqhsregWGNLKEMMKYASDSHTC-VDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PTZ00216 221 IIYLDSLPASVDT--------EGCRLVA------WTDVVAKGHSAGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
90
....*....|....*....
gi 65301416 244 SSFGLG-LSVNGRFwLDLI 261
Cdd:PTZ00216 287 GSLTAGiLALEDRL-NDLI 304
|
|
| |
