|
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: 1092.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 48 LPKNFNFAADVLDQWSQKEKTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 128 WLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSRNGWLSFQELFQ 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 208 FASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWL 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 288 CGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLY 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 368 EGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFCFFSKYVDNPQKTAATIR 447
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 448 GDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSY 527
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 114643324 528 NPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEW 577
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-574 |
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: 602.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 89 WSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVas 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 169 eevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscveTGSQEPMTIYFTSGTTGFPKMAQHSqSSLGI 248
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 249 GFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLV 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 329 QKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENG 408
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 409 NVLPPGKEGEIALRLKPTRPfcfFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVE 488
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPGL---FLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 489 SALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIK 568
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEP--SEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 114643324 569 RNVLRD 574
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
49-577 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 592.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 49 PKNFNFAADVLDQWSQkektgERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWW 128
Cdd:COG0365 5 GGRLNIAYNCLDRHAE-----GRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 129 LVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVA---------PAVESIVLECPDLKTKLLV----SPQS 195
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 196 RNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWV 275
Cdd:COG0365 159 MEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 276 KAAIGSVFSSWLCGACVFVH-------------RMAQFdtdtfldtlttYPITTLCSPPTVYRMLVQKD---LKRYKFKS 339
Cdd:COG0365 239 TGHSYIVYGPLLNGATVVLYegrpdfpdpgrlwELIEK-----------YGVTVFFTAPTAIRALMKAGdepLKKYDLSS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMI-CANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGE 418
Cdd:COG0365 308 LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 419 IALRlkptRPF-CFFSKYVDNPQKTAATIRGDF---YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEH 494
Cdd:COG0365 388 LVIK----GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 495 PAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:COG0365 464 PAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEP--SDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
...
gi 114643324 575 QEW 577
Cdd:COG0365 542 IAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
49-576 |
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: 561.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 49 PKNFNFAADVLDQWSQkektgERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWW 128
Cdd:cd05970 13 PENFNFAYDVVDAMAK-----EYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 129 LVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEE--VAPAVESIVLECPDLKTKLLVSPQSRNGWLSFQELF 206
Cdd:cd05970 87 YSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 207 QFASEE----HSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSsLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSV 282
Cdd:cd05970 167 KNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 283 FSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQT 362
Cdd:cd05970 246 YGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 363 GLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFCFFSKYVDNPQKT 442
Cdd:cd05970 326 GIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 443 AATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAa 522
Cdd:cd05970 406 AEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA- 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 523 pfKSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQE 576
Cdd:cd05970 485 --KGYEPsEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-576 |
8.49e-133 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 399.27 E-value: 8.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 69 GERPANPALWWVNGKGDEvKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGII-------F 141
Cdd:PRK04319 55 GGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNGAIvgplfeaF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 142 MPGTIqltaKDilyRLRASKAKCIVASEEVAPAVesIVLECPDLKTKLLVSPQSRN--GWLSFQELFQFASEEHSCVETG 219
Cdd:PRK04319 133 MEEAV----RD---RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEgpGTLDFNALMEQASDEFDIEWTD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 220 SQEPMTIYFTSGTTGFPK--------MAQHSQSslgigftlcGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGAC 291
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKgvlhvhnaMLQHYQT---------GKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VFV----------HRMAQFdtdtfldtlttYPITTLCSPPTVYRMLVQKD---LKRYKFKSLRHCLTGGEPLNPEVLEQW 358
Cdd:PRK04319 275 NVIdggrfsperwYRILED-----------YKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLNPEVVRWG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 359 RAQTGLDLYEGYGQTEVG--MICaNQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALrlKPTRPfCFFSKYV 436
Cdd:PRK04319 344 MKVFGLPIHDNWWMTETGgiMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 437 DNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKA 516
Cdd:PRK04319 420 NNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKA 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 517 FVVLAApfkSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQE 576
Cdd:PRK04319 500 FVALRP---GYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-576 |
1.77e-129 |
|
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: 386.15 E-value: 1.77e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAkCIVASE 169
Cdd:cd05974 2 SFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscveTGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIG 249
Cdd:cd05974 80 EN----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FtLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQ 329
Cdd:cd05974 114 H-LSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 330 KDLKRYKFKsLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGN 409
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 410 vlpPGKEGEIALRLKPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVES 489
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 490 ALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSyNPEkLTLELQDHVKKSTAPYKYPRKVEFVqELPKTITGKIKR 569
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEP-SPE-TALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 114643324 570 NVLRDQE 576
Cdd:cd05974 426 VELRRRE 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-580 |
2.42e-122 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 368.37 E-value: 2.42e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQkektgERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACI 135
Cdd:COG0318 2 ADLLRRAAA-----RHPDRPALVF-----GGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 136 RTGIIFMPGTIQLTAKDILYRLRASKAKCIVAseevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehsc 215
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 216 vetgsqepMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMS----DTGWVkaaiGSVFSSWLCGAC 291
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLT----VGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VFVHR----------MAQfdtdtfldtlttYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEVLEQWRA 360
Cdd:COG0318 170 LVLLPrfdpervlelIER------------ERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 361 QTGLDLYEGYGQTEVGMICAN--QKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlkptrPFCFFSKYVDN 438
Cdd:COG0318 238 RFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 439 PQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFV 518
Cdd:COG0318 313 PEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFV 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 519 VLAApfksynPEKLTL-ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:COG0318 393 VLRP------GAELDAeELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-576 |
7.46e-118 |
|
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: 356.43 E-value: 7.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 89 WSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVAS 168
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 169 EEVAPavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvETGSQEPMTIYFTSGTTGFPKMAQHSQSSLgI 248
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 249 GFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRmAQFDTDTFLDTLTTYPITTLCSPPTVYRMLV 328
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 329 QKD---LKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMIC-ANQKGQEIKPGSMGKGMLPYDVQII 404
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMiANYPCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 405 DENGNVLPPGKEGEIALrlKPTRPfCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGP 484
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 485 FEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfKSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTI 563
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLK---EGFEPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 114643324 564 TGKIKRNVLRDQE 576
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-574 |
2.36e-115 |
|
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: 349.81 E-value: 2.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 83 KGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKA 162
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVL-KEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 163 KCIVASeevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetGSQEPMTIYFTSGTTGFPKMAQHS 242
Cdd:cd05971 80 SALVTD--------------------------------------------------GSDDPALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 243 QSSLgIGFTLCGRYWLDL--KSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSP 320
Cdd:cd05971 110 HRVL-LGHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 321 PTVYRMLVQ--KDLKRYKFKsLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKG-QEIKPGSMGKGML 397
Cdd:cd05971 189 PTALKMMRQqgEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 398 PYDVQIIDENGNVLPPGKEGEIALRLKptRPFCFFSkYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIIS 477
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEIAVELP--DPVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 478 SGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfkSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFV 556
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNP---GETPsDALAREIQELVKTRLAAHEYPREIEFV 421
|
490
....*....|....*...
gi 114643324 557 QELPKTITGKIKRNVLRD 574
Cdd:cd05971 422 NELPRTATGKIRRRELRA 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-573 |
1.86e-106 |
|
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: 327.17 E-value: 1.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASe 169
Cdd:cd05973 2 TFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 evapavesivlecPDLKTKLlvspqsrngwlsfqelfqfaseehscvetgSQEPMTIYFTSGTTGFPKMAQHSQSSLgIG 249
Cdd:cd05973 80 -------------AANRHKL------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCG-ACVFVHrmAQFDTDTFLDTLTTYPITTLCSPPTVYRML- 327
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLm 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 328 -----VQKDLKrykfKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKG--QEIKPGSMGKGMLPYD 400
Cdd:cd05973 194 aagaeVPARPK----GRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHAleHPVHAGSAGRAMPGWR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 401 VQIIDENGNVLPPGKEGEIALRLKPTrPFCFFSKYVDNPQKTAAtirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGY 480
Cdd:cd05973 270 VAVLDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 481 RIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELP 560
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|...
gi 114643324 561 KTITGKIKRNVLR 573
Cdd:cd05973 424 KTPSGKIQRFLLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
56-573 |
3.89e-103 |
|
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: 319.51 E-value: 3.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQKektgeRPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACI 135
Cdd:cd05936 2 ADLLEEAARR-----FPDKTALIF-----MGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 136 RTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEevapavesivlecpdlktkllvspqsrngwlSFQELFQFASEEHSC 215
Cdd:cd05936 71 KAGAVVVPLNPLYTPRELEHILNDSGAKALIVAV-------------------------------SFTDLLAAGAPLGER 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 216 VETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIwnmsdtgwVKAAI---------GSVFSSW 286
Cdd:cd05936 120 VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDV--------VLAALplfhvfgltVALLLPL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 287 LCGAC-VFVHR---------MAQfdtdtfldtlttYPITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVL 355
Cdd:cd05936 192 ALGATiVLIPRfrpigvlkeIRK------------HRVTIFPGVPTMYIALLNaPEFKKRDFSSLRLCISGGAPLPVEVA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 356 EQWRAQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTRpfcfFSK 434
Cdd:cd05936 260 ERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQV----MKG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 435 YVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVV 514
Cdd:cd05936 335 YWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAV 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 515 KAFVVLAapfksyNPEKLTL-ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd05936 415 KAFVVLK------EGASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
52-573 |
3.28e-99 |
|
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: 310.45 E-value: 3.28e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 52 FNFAADVLDQwsqkeKTGERPANPALWwvngkGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVN 131
Cdd:cd05959 3 YNAATLVDLN-----LNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 132 VACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIV-LECPDLKTKLLVSP-QSRNGWLSFQELFQFA 209
Cdd:cd05959 72 LGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALtKSEHTLVVLIVSGGaGPEAGALLLAELVAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 210 SEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWvkaAIG----SVFSS 285
Cdd:cd05959 152 AEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFF---AYGlgnsLTFPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 286 WLCGACV----------FVHRMAQfdtdtfldtlttYPITTLCSPPTVYR-MLVQKDLKRYKFKSLRHCLTGGEPLNPEV 354
Cdd:cd05959 229 SVGATTVlmperptpaaVFKRIRR------------YRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 355 LEQWRAQTGLDLYEGYGQTEVGMI-CANQKGqEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFcffs 433
Cdd:cd05959 297 GERWKARFGLDILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 434 kYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEV 513
Cdd:cd05959 372 -YWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTK 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 514 VKAFVVLAAPFKSynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd05959 451 PKAFVVLRPGYED--SEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-568 |
7.27e-99 |
|
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: 303.82 E-value: 7.27e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRyWLDLKSSDIIWNMSDTGWVkAAIGSVFSSWLCGACVFVHRMaqFD 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA-SGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK--FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 TDTFLDTLTTYPITTLCSPPTVYRMLVQKDL-KRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVG--MI 378
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 379 CANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLkPTRpfcfFSKYVDNPQKTAATIRGDFYVTGDRGV 458
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRG-PSV----MKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 459 MDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPEKLTL-ELQ 537
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR------PGADLDAeELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 114643324 538 DHVKKSTAPYKYPRKVEFVQELPKTITGKIK 568
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
56-580 |
1.66e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 293.63 E-value: 1.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQKektgeRPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACI 135
Cdd:PRK06187 9 GRILRHGARK-----HPDKEAVYF-----DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 136 RTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSRNG----WLSFQELFQFASE 211
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 212 EHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIwnMSDT------GWvkaaiGSVFSS 285
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAVCAWLKLSRDDVY--LVIVpmfhvhAW-----GLPYLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 286 WLCGA-CVFVHRmaqfdtdtfldtlttYP------------ITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLN 351
Cdd:PRK06187 230 LMAGAkQVIPRR---------------FDpenlldlieterVTFFFAVPTIWQMLLKaPRAYFVDFSSLRLVIYGGAALP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 352 PEVLEQWRAQTGLDLYEGYGQTEVG-MICAN-----QKGQEIKPGSMGKGMLPYDVQIIDENGNVLPP-GKE-GEIALRl 423
Cdd:PRK06187 295 PALLREFKEKFGIDLVQGYGMTETSpVVSVLppedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 424 KPtrpfCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVV 503
Cdd:PRK06187 374 GP----WLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114643324 504 SSPDQIRGEVVKAFVVLaAPFKSYNPEKLTLELQDHVkkstAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK06187 450 GVPDEKWGERPVAVVVL-KPGATLDAKELRAFLRGRL----AKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-573 |
8.34e-85 |
|
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: 270.89 E-value: 8.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRAskakci 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 166 vASEEVAPAVESivlecpdlktkllvspqsrngwlsfqelfqfaseehscvETGSQEPMTIYFTSGTTGFPKMAQHSQSS 245
Cdd:cd05958 82 -ARITVALCAHA---------------------------------------LTASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 246 LGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVhrMAQFDTDTFLDTLTTYPITTLCSPPTVYR 325
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 326 -MLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQII 404
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 405 DENGNVLPPGKEGEIALRlKPTrpfcffsKYVDNPQKTAAT-IRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIG 483
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR-GPT-------GCRYLADKRQRTyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 484 PFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTI 563
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
490
....*....|
gi 114643324 564 TGKIKRNVLR 573
Cdd:cd05958 430 TGKLQRFALR 439
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
66-478 |
3.00e-82 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 263.40 E-value: 3.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANpalwwvnGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGT 145
Cdd:pfam00501 6 ARTPDKTAL-------EVGEGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIVASEE-VAPAVESIVLECPDLKTKLLVSPQS-RNGWLSFQELFQFASEEHSCVETGSQEP 223
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPvLKEEPLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 MTIYFTSGTTGFPKMAQHSQSSL---GIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGA-CVFVHRMAQ 299
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 300 FDTDTFLDTLTTYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMI 378
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 379 CA---NQKGQEIKPGSMGKGMLPYDVQIIDEN-GNVLPPGKEGEIALRlkptRPfCFFSKYVDNPQKTAATI-RGDFYVT 453
Cdd:pfam00501 318 VTtplPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAFdEDGWYRT 392
|
410 420
....*....|....*....|....*
gi 114643324 454 GDRGVMDSDGYFWFVGRADDVIISS 478
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
71-567 |
3.18e-81 |
|
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: 261.39 E-value: 3.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 71 RPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTA 150
Cdd:cd17631 8 HPDRTALVF-----GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KDILYRLRASKAKCIVAseevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqEPMTIYFTS 230
Cdd:cd17631 82 PEVAYILADSGAKVLFD------------------------------------------------------DLALLMYTS 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 231 GTTGFPKMAQHSQSSLGiGFTLCGRYWLDLKSSDI---IWNMSDTGwvkAAIGSVFSSWLCGACVFVHRmaQFDTDTFLD 307
Cdd:cd17631 108 GTTGRPKGAMLTHRNLL-WNAVNALAALDLGPDDVllvVAPLFHIG---GLGVFTLPTLLRGGTVVILR--KFDPETVLD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 308 TLTTYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEVLEQWRAqTGLDLYEGYGQTEVGM-ICANQ-KG 384
Cdd:cd17631 182 LIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPgVTFLSpED 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTRpfcfFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGY 464
Cdd:cd17631 261 HRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPHV----MAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 465 FWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfKSYNPEKLTlELQDHVKKST 544
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVP----RPGAELDED-ELIAHCRERL 410
|
490 500
....*....|....*....|...
gi 114643324 545 APYKYPRKVEFVQELPKTITGKI 567
Cdd:cd17631 411 ARYKIPKSVEFVDALPRNATGKI 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-574 |
1.24e-80 |
|
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: 262.08 E-value: 1.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 50 KNFNFAADVLDqwsqkeKTGERPANPALWWVNgkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWL 129
Cdd:TIGR02262 1 EKYNAAEDLLD------RNVVEGRGGKTAFID---DISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 130 VNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTkLLVSPQSRNGWLSFQELFQFA 209
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 210 SEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCG 289
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 290 ACVFVHRMAQFDTDTFLDTLTTYPiTTLCSPPTVYR-MLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYE 368
Cdd:TIGR02262 230 ATTVLMGERPTPDAVFDRLRRHQP-TIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 369 GYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTRPfcffSKYVDNPQKTAATIRG 448
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-GPSSA----TMYWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 DFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSyn 528
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 114643324 529 pekLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
70-575 |
3.44e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 258.68 E-value: 3.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:PRK07656 17 RFGDKEAYVF-----GDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSP----QSRNGWLSFQELFQFASEEHSCVETGSQEPMT 225
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETeeddPHTEKMKTFTDFLAAGDPAERAPEVDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPK--MAQHSQSslgigfTLCGRYW---LDLKSSD--IIWN-MSDTGWVKAAIGSVFSSwlcGACVFVHrm 297
Cdd:PRK07656 171 ILFTSGTTGRPKgaMLTHRQL------LSNAADWaeyLGLTEGDryLAANpFFHVFGYKAGVNAPLMR---GATILPL-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 298 AQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLD-LYEGYGQTEV 375
Cdd:PRK07656 240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQhPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 376 -GMICANQKGQEIK--PGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlkptrPFCFFSKYVDNPQKTAATIRGDFYV 452
Cdd:PRK07656 320 sGVTTFNRLDDDRKtvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR-----GPNVMKGYYDDPEATAAAIDADGWL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 453 -TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEk 531
Cdd:PRK07656 395 hTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL-KPGAELTEE- 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 114643324 532 ltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK07656 473 ---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
53-574 |
6.50e-79 |
|
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: 261.03 E-value: 6.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 53 NFAADVLDQW--SQKEKTgerpanpALWW-VNGKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWL 129
Cdd:TIGR02188 57 NVSYNCVDRHleARPDKV-------AIIWeGDEPGEVRKITYRELHREVCRFANVL-KSLGVKKGDRVAIYMPMIPEAAI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 130 VNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEV---------APAVESIVLECPDLKTKLLVSP------- 193
Cdd:TIGR02188 129 AMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGlrggkviplKAIVDEALEKCPVSVEHVLVVRrtgnpvv 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 194 ---QSRNGWlsFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMS 270
Cdd:TIGR02188 209 pwvEGRDVW--WHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 271 DTGWVKAAIGSVFSSWLCGACVFVH----------RMAQFDTDtfldtlttYPITTLCSPPTVYRMLVQ---KDLKRYKF 337
Cdd:TIGR02188 287 DVGWITGHSYIVYGPLANGATTVMFegvptypdpgRFWEIIEK--------HKVTIFYTAPTAIRALMRlgdEWVKKHDL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 338 KSLRHCLTGGEPLNPEVLEQWRAQTGLD---LYEGYGQTEVG--MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLP 412
Cdd:TIGR02188 359 SSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTWWQTETGgiMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 413 -PGKEGeiALRLKPTRPFCFFSKYVDnPQKTAATIRGDF---YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVE 488
Cdd:TIGR02188 439 gPGEGG--YLVIKQPWPGMLRTIYGD-HERFVDTYFSPFpgyYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIE 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 489 SALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfKSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKI 567
Cdd:TIGR02188 516 SALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLK---DGYEPdDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKI 592
|
....*..
gi 114643324 568 KRNVLRD 574
Cdd:TIGR02188 593 MRRLLRK 599
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-573 |
8.00e-79 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 255.46 E-value: 8.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAPAvesivlecpdlktkllvspqsrngWLsfqelfqfaseehscvetgsqepmtiyFTSGTTGFPKMAQHSQSSLGIG 249
Cdd:cd05919 91 DDIAY------------------------LL---------------------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPiTTLCSPPTVY-RMLV 328
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRP-TVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 329 QKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENG 408
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 409 NVLPPGKEGEIALRLkPTRpfcfFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVE 488
Cdd:cd05919 279 HTIPPGEEGDLLVRG-PSA----AVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 489 SALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKsyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIK 568
Cdd:cd05919 354 SLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAA--PQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
....*
gi 114643324 569 RNVLR 573
Cdd:cd05919 432 RFKLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-567 |
3.49e-78 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 257.89 E-value: 3.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 31 TPLTLADFEAINRCNRPLPK-NFNFAADVLDQWSQkektgERPANPALWWVNGKGDEVK-WSFRELGSLSRKAANMLtKP 108
Cdd:cd17634 30 QKVKNTSFAPGAPSIKWFEDaTLNLAANALDRHLR-----ENGDRTAIIYEGDDTSQSRtISYRELHREVCRFAGTL-LD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 109 CGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIV-ASEEVAP---------AVESI 178
Cdd:cd17634 104 LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItADGGVRAgrsvplkknVDDAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 179 VLECPDLKTKLLVSpqsRNG---------WLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIG 249
Cdd:cd17634 184 NPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFL--DTLTTYPITTLCSPPTVYRML 327
Cdd:cd17634 261 AATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARmwQVVDKHGVNILYTAPTAIRAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 328 VQKD---LKRYKFKSLRHCLTGGEPLNPEVLE-QWR--AQTGLDLYEGYGQTEVG-MICANQKG-QEIKPGSMGKGMLPY 399
Cdd:cd17634 341 MAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGgFMITPLPGaIELKAGSATRPVFGV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 400 DVQIIDENGNVLPPGKEGEIALRLK-PTRPFCFFSKYVDNPQKTAATIRGdFYVTGDRGVMDSDGYFWFVGRADDVIISS 478
Cdd:cd17634 421 QPAVVDNEGHPQPGGTEGNLVITDPwPGQTRTLFGDHERFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRSDDVINVA 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 479 GYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKsyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQE 558
Cdd:cd17634 500 GHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDS 577
|
....*....
gi 114643324 559 LPKTITGKI 567
Cdd:cd17634 578 LPKTRSGKI 586
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-574 |
3.86e-78 |
|
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: 258.26 E-value: 3.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 53 NFAADVLDQWSqkEKTGERPAnpALWWVNGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNV 132
Cdd:cd05966 53 NISYNCLDRHL--KERGDKVA--IIWEGDEPDQSRTITYRELLREVCRFANVLKS-LGVKKGDRVAIYMPMIPELVIAML 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 133 ACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEV---------APAVESIVLECPDLKTKLLVS--------PQS 195
Cdd:cd05966 128 ACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGyrggkviplKEIVDEALEKCPSVEKVLVVKrtggevpmTEG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 196 RNGWlsFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWV 275
Cdd:cd05966 208 RDLW--WHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 276 KAAIGSVFSSWLCGACVFV----------HRMAQFDTDtfldtlttYPITTLCSPPTVYRMLVQ---KDLKRYKFKSLRH 342
Cdd:cd05966 286 TGHSYIVYGPLANGATTVMfegtptypdpGRYWDIVEK--------HKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 343 CLTGGEPLNPEVLEQWRAQTG---LDLYEGYGQTEVGMIC-ANQKG-QEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEG 417
Cdd:cd05966 358 LGSVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMiTPLPGaTPLKPGSATRPFFGIEPAILDEEGNEVEGEVEG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 418 EIALRlkptRPF----------------CFFSKYvdnpqktaatirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYR 481
Cdd:cd05966 438 YLVIK----RPWpgmartiygdheryedTYFSKF------------PGYYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 482 IGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfkSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELP 560
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKD---GEEPsDELRKELRKHVRKEIGPIATPDKIQFVPGLP 578
|
570
....*....|....
gi 114643324 561 KTITGKIKRNVLRD 574
Cdd:cd05966 579 KTRSGKIMRRILRK 592
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
71-574 |
5.24e-76 |
|
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: 253.01 E-value: 5.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 71 RPANPALWWVNG-KGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGII-------Fm 142
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsvvfggF- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 143 pgtiqlTAKDILYRLRASKAKCIVASE---------EVAPAVES------------IVLECPDLKTKLLVSpqsrNGWLS 201
Cdd:cd05967 142 ------AAKELASRIDDAKPKLIVTAScgiepgkvvPYKPLLDKalelsghkphhvLVLNRPQVPADLTKP----GRDLD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 202 FQELFQFAsEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSqsslgIGFTLCGRYW-----LDLKSSDIIWNMSDTGWVK 276
Cdd:cd05967 212 WSELLAKA-EPVDCVPVAATDPLYILYTSGTTGKPKGVVRD-----NGGHAVALNWsmrniYGIKPGDVWWAASDVGWVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 277 AAIGSVFSSWLCGAC---------------VFVHRMAQfdtdtfldtlttYPITTLCSPPTVYRMLVQKD-----LKRYK 336
Cdd:cd05967 286 GHSYIVYGPLLHGATtvlyegkpvgtpdpgAFWRVIEK------------YQVNALFTAPTAIRAIRKEDpdgkyIKKYD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 337 FKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVG-MICANQKGQE---IKPGSMGKGMLPYDVQIIDENGNVLP 412
Cdd:cd05967 354 LSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwPITANPVGLEplpIKAGSPGKPVPGYQVQVLDEDGEPVG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 413 PGKEGEIALRLkPTRPFCFFSKYVDNP---QKTAATIRGdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVES 489
Cdd:cd05967 434 PNELGNIVIKL-PLPPGCLLTLWKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 490 ALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILR 590
|
....*
gi 114643324 570 NVLRD 574
Cdd:cd05967 591 RTLRK 595
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
87-567 |
9.62e-73 |
|
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: 240.96 E-value: 9.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 87 VKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIV 166
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 167 ASEEVAPAVeSIVLECPDLKTKLLVSPQSRNGWLSFQELFQFASEEHS-----CVETGSQEPMTIYFTSGTTGFPKMAQH 241
Cdd:cd05911 88 TDPDGLEKV-KEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 242 SQSSLGIGFTLCGRYW-LDLKSSDIIWNMSDTGWVKAAIGSVFSSwLCGACVFVHRmaQFDTDTFLDTLTTYPITTLCSP 320
Cdd:cd05911 167 SHRNLIANLSQVQTFLyGNDGSNDVILGFLPLYHIYGLFTTLASL-LNGATVIIMP--KFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 321 PTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGL-DLYEGYGQTEVGMICANQKGQEIKPGSMGKgMLP 398
Cdd:cd05911 244 PPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGR-LLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 399 -YDVQIIDENGN-VLPPGKEGEIALRLkptrPFCFfSKYVDNPQKTAATI-RGDFYVTGDRGVMDSDGYFWFVGRADDVI 475
Cdd:cd05911 323 nVEAKIVDDDGKdSLGPNEPGEICVRG----PQVM-KGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 476 ISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPEKLT-LELQDHVKKSTAPYKYPRK-V 553
Cdd:cd05911 398 KYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK------PGEKLTeKEVKDYVAKKVASYKQLRGgV 471
|
490
....*....|....
gi 114643324 554 EFVQELPKTITGKI 567
Cdd:cd05911 472 VFVDEIPKSASGKI 485
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
72-575 |
3.00e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 237.91 E-value: 3.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWvngkGDEVkWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:PRK08316 25 PDKTALVF----GDRS-WTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSR---NGWLSFQELFQFASEEHSCVETGSQEPMTIYF 228
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGReapGGWLDFADWAEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 229 TSGTTGFPKMAQHSQSSLgigftlCGRYW-----LDLKSSDIIwnmsdtgwVKA------AIGSVF--SSWLCGACVFVh 295
Cdd:PRK08316 179 TSGTESLPKGAMLTHRAL------IAEYVscivaGDMSADDIP--------LHAlplyhcAQLDVFlgPYLYVGATNVI- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 rMAQFDTDTFLDTLTTYPITTLCSPPTVY-RMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQT 373
Cdd:PRK08316 244 -LDAPDPELILRTIEAERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 374 EVG---MIcANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlkpTRPFCffSKYVDNPQKTAATIRGDF 450
Cdd:PRK08316 323 EIAplaTV-LGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLM--LGYWDDPEKTAEAFRGGW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfKSYNPE 530
Cdd:PRK08316 397 FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTED 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 114643324 531 kltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK08316 476 ----ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
85-574 |
1.37e-68 |
|
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: 228.71 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 85 DEVKWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAkc 164
Cdd:cd05941 8 DGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 165 ivaseevapaveSIVLEcpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqePMTIYFTSGTTGFPKMAQHSQS 244
Cdd:cd05941 86 ------------SLVLD-----------------------------------------PALILYTSGTTGRPKGVVLTHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 245 SLGIGFTLCGRYWlDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGA-CVFvhrMAQFDTDTFLDTLTTYPITTLCSPPTV 323
Cdd:cd05941 113 NLAANVRALVDAW-RWTEDDVLLHVLPLHHVHGLVNALLCPLFAGAsVEF---LPKFDPKEVAISRLMPSITVFMGVPTI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 324 YRMLVQ---------KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGK 394
Cdd:cd05941 189 YTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 395 GMLPYDVQIIDENGN-VLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRAD 472
Cdd:cd05941 269 PLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGYYWILGRSS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 473 DVIISS-GYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEkltlELQDHVKKSTAPYKYPR 551
Cdd:cd05941 344 VDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQRLAPYKRPR 419
|
490 500
....*....|....*....|...
gi 114643324 552 KVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
84-574 |
4.72e-68 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 232.34 E-value: 4.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGII-------FmpgtiqlTAKDILYR 156
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggF-------SAEALADR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 157 LRASKAKCIVASEE-------VA--PAVESIVLECPDLKTKLLVSpqsRNG----W-----LSFQELFQFASEEHSCVET 218
Cdd:PRK00174 166 IIDAGAKLVITADEgvrggkpIPlkANVDEALANCPSVEKVIVVR---RTGgdvdWvegrdLWWHELVAGASDECEPEPM 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 219 GSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFV---- 294
Cdd:PRK00174 243 DAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMfegv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 295 ------HRMAQFDTDtfldtlttYPITTLCSPPTVYRMLVQ---KDLKRYKFKSLRhcLTG--GEPLNPEVLEqWraqtg 363
Cdd:PRK00174 323 pnypdpGRFWEVIDK--------HKVTIFYTAPTAIRALMKegdEHPKKYDLSSLR--LLGsvGEPINPEAWE-W----- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 364 ldLYEGYG-----------QTEVG--MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALrlkpTRPF- 429
Cdd:PRK00174 387 --YYKVVGgercpivdtwwQTETGgiMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPWp 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 430 ---------------CFFSKYvdnpqktaatirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEH 494
Cdd:PRK00174 461 gmmrtiygdherfvkTYFSTF------------KGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 495 PAVVESAVVSSPDQIRGEVVKAFVVLAApfkSYNP-EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK00174 529 PKVAEAAVVGRPDDIKGQGIYAFVTLKG---GEEPsDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
.
gi 114643324 574 D 574
Cdd:PRK00174 606 K 606
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-573 |
1.30e-66 |
|
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: 222.55 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:cd05934 3 RWTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 SeevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqePMTIYFTSGTTGFPK--MAQHSQss 245
Cdd:cd05934 82 D------------------------------------------------------PASILYTSGTTGPPKgvVITHAN-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 246 lgigFTLCGRY---WLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGA-CVFVHRMAQFDTDTFLDTLTtypiTTLCS-- 319
Cdd:cd05934 106 ----LTFAGYYsarRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGAtLVLLPRFSASRFWSDVRRYG----ATVTNyl 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 ---PPTVYRMLVQKDLKRYKFKslrhcLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGM 396
Cdd:cd05934 178 gamLSYLLAQPPSPDDRAHRLR-----AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 397 LPYDVQIIDENGNVLPPGKEGEIALRlkPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVII 476
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 477 SSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfKSYNPEkltlELQDHVKKSTAPYKYPRKVEFV 556
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPE----ELFAFCEGQLAYFKVPRYIRFV 405
|
490
....*....|....*..
gi 114643324 557 QELPKTITGKIKRNVLR 573
Cdd:cd05934 406 DDLPKTPTEKVAKAQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
72-574 |
3.05e-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: 221.03 E-value: 3.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALwwVNGKGDEVkWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:cd05926 1 PDAPAL--VVPGSTPA-LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVA-SEEVAPAVES------IVLECPDLKTKLLVSPQsrNGWLSFQElfqfASEEHSCVETGSQEP- 223
Cdd:cd05926 77 EFEFYLADLGSKLVLTpKGELGPASRAasklglAILELALDVGVLIRAPS--AESLSNLL----ADKKNAKSEGVPLPDd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 -MTIYFTSGTTGFPKMAQHSQ-----SSLGIGFTLCgrywldLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACV----- 292
Cdd:cd05926 151 lALILHTSGTTGRPKGVPLTHrnlaaSATNITNTYK------LTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVvlppr 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 -----FVHRMAQfdtdtfldtlttYPITTLCSPPTVYRMLVQ--KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLD 365
Cdd:cd05926 225 fsastFWPDVRD------------YNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 366 LYEGYGQTEVG--MICANQKGQEIKPGSMGKGMLPyDVQIIDENGNVLPPGKEGEIALRLKP-TRpfcffsKYVDNPQKT 442
Cdd:cd05926 293 VLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNvTR------GYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 443 AA-TIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLA 521
Cdd:cd05926 366 AEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 522 ApfksyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd05926 446 E-----GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
72-580 |
1.05e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 220.99 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWVngkGDEVkwSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:PRK08314 24 PDKTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAK-CIVASE---EVAPAVESIVLEC------------------PD-LKTKLLVSPQSRNGWLSFQElfqf 208
Cdd:PRK08314 99 ELAHYVTDSGARvAIVGSElapKVAPAVGNLRLRHvivaqysdylpaepeiavPAwLRAEPPLQALAPGGVVAWKE---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 209 ASEEHSC---VETGSQEPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSS 285
Cdd:PRK08314 175 ALAAGLApppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 286 WLCGACVFVhrMAQFDTDTFLDTLTTYPITTLCSPPTvyrMLV----QKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQ 361
Cdd:PRK08314 254 IYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGGAAMPEAVAERLKEL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 362 TGLDLYEGYGQTE-VGMICANQKGQEiKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNP 439
Cdd:PRK08314 329 TGLDYVEGYGLTEtMAQTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ----VFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 440 QKTAA---TIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVK 515
Cdd:PRK08314 403 EATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 516 AFVVLAAPFKSYNPEKltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK08314 483 AVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
53-573 |
3.51e-62 |
|
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: 215.82 E-value: 3.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 53 NFAADVLDQWsqkekTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNV 132
Cdd:cd05968 61 NIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 133 ACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE---------EVAPAVESIVLECPDLKTKLLVS------PQSRN 197
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVEKVVVVRhlgndfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 198 GWLSFQElfQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVka 277
Cdd:cd05968 215 RDLSYDE--EKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWM-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 278 aIGS--VFSSWLCGACVFVHRMA--QFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKD---LKRYKFKSLRHCLTGGEPL 350
Cdd:cd05968 291 -MGPwlIFGGLILGATMVLYDGApdHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGdapVNAHDLSSLRVLGSTGEPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 351 NPEVLeQWRAQTGLD----LYEGYGQTEV-GMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPgKEGEIALrLKP 425
Cdd:cd05968 370 NPEPW-NWLFETVGKgrnpIINYSGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVL-LAP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 426 ----TRPF---------CFFSKYvdnpqktaatirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALI 492
Cdd:cd05968 447 wpgmTRGFwrdedryleTYWSRF------------DNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 493 EHPAVVESAVVSSPDQIRGEVVKAFVVL--AAPFKSYNPEKLTLELQDHVKKstaPYKyPRKVEFVQELPKTITGKIKRN 570
Cdd:cd05968 515 AHPAVLESAAIGVPHPVKGEAIVCFVVLkpGVTPTEALAEELMERVADELGK---PLS-PERILFVKDLPKTRNAKVMRR 590
|
...
gi 114643324 571 VLR 573
Cdd:cd05968 591 VIR 593
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
89-580 |
5.60e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 212.46 E-value: 5.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 89 WSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVAS 168
Cdd:PRK08276 12 VTYGELEARSNRLAHGL-RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 169 EEVAPAVESIVLECPDLKTKLLVSPQSRNGWLSFQELFQFASEEHSCVET-GSqepmTIYFTSGTTGFPK---------- 237
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETaGA----DMLYSSGTTGRPKgikrplpgld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 238 ---MAQHSQSSLGIGFTLCG--RYwldLKSSDI------IWNMSdtgwVKAAIGSVfsswlcgacVFvhrMAQFDTDTFL 306
Cdd:PRK08276 167 pdeAPGMMLALLGFGMYGGPdsVY---LSPAPLyhtaplRFGMS----ALALGGTV---------VV---MEKFDAEEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 307 DTLTTYPITTLCSPPTVY-RML-----VQKdlkRYKFKSLRHCLTGGEPLNPEV----LEQWraqtGLDLYEGYGQTEVG 376
Cdd:PRK08276 228 ALIERYRVTHSQLVPTMFvRMLklpeeVRA---RYDVSSLRVAIHAAAPCPVEVkramIDWW----GPIIHEYYASSEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 377 MICANQKGQEI-KPGSMGKGMLPyDVQIIDENGNVLPPGKEGEIALRlKPTRPFcffsKYVDNPQKTAATIRGDFYVT-G 454
Cdd:PRK08276 301 GVTVITSEDWLaHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVTvG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 455 DRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynPEKLTL 534
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADA--GDALAA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 114643324 535 ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK08276 453 ELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-573 |
5.66e-62 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 215.59 E-value: 5.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 87 VKWSFRELgsLSR--KAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFmPGTIQLTAKDILYRLRASKAKC 164
Cdd:PRK07529 57 ETWTYAEL--LADvtRTANLLHS-LGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 165 IVA-----SEEVAPAVESIVLECPDLKTKLLV-----------------SPQSRNGWLSF-QELFQFASEEHSCVETGSQ 221
Cdd:PRK07529 133 LVTlgpfpGTDIWQKVAEVLAALPELRTVVEVdlarylpgpkrlavpliRRKAHARILDFdAELARQPGDRLFSGRPIGP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYF-TSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIwnMSDTGW--VKAAIGSVFSSWLCGACV------ 292
Cdd:PRK07529 213 DDVAAYFhTGGTTGMPKLAQHTHGNE-VANAWLGALLLGLGPGDTV--FCGLPLfhVNALLVTGLAPLARGAHVvlatpq 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 -------------FVHRmaqfdtdtfldtlttYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWR 359
Cdd:PRK07529 290 gyrgpgvianfwkIVER---------------YRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTGLDLYEGYGQTEVGMICA-NQKGQEIKPGSMGKgMLPY-DVQII--DENGNVL---PPGKEGEIALRlKPTrpfcFF 432
Cdd:PRK07529 355 AATGVRIVEGYGLTEATCVSSvNPPDGERRIGSVGL-RLPYqRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN----VF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 433 SKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGE 512
Cdd:PRK07529 429 SGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGE 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 513 VVKAFVVLaAPFKSYNPEKLTLELQDHVKKSTApykYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK07529 509 LPVAYVQL-KPGASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-572 |
1.77e-61 |
|
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: 209.26 E-value: 1.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EvapavesivLEcpDLktkllvspqsrngwlsfqelfqfaseehscvetgsqepMTIYFTSGTTGFPKMAQHSQSSLgIG 249
Cdd:cd05935 82 E---------LD--DL--------------------------------------ALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVhrMAQFDTDTFLDTLTTYPIT-TLCSPPTVYRMLV 328
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTfWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 329 QKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIID-EN 407
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 408 GNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAA---TIRG-DFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIG 483
Cdd:cd05935 270 GRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 484 PFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKltlELQDHVKKSTAPYKYPRKVEFVQELPKTI 563
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 114643324 564 TGKIKRNVL 572
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
84-575 |
5.94e-60 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 207.42 E-value: 5.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASEEVAPAVESIVLEC--PDLKTkllvspQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQH 241
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAgaPHVET------LDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 242 SQSSLGI-GFTLcGRYWlDLKSSDIIWNM----------SDTGWVKAAIGSVFssWLCG--ACVFVHRMAQFdtdtfldt 308
Cdd:PRK07514 177 SHGNLLSnALTL-VDYW-RFTPDDVLIHAlpifhthglfVATNVALLAGASMI--FLPKfdPDAVLALMPRA-------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 309 lttypiTTLCSPPTVY-RMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEI 387
Cdd:PRK07514 245 ------TVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 388 KPGSMGKGmLP-YDVQIID-ENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGY 464
Cdd:PRK07514 319 RAGTVGFP-LPgVSLRVTDpETGAELPPGEIGMIEVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 465 FWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAfVVLAAPFKSYNPEKLTLELQDHVkkst 544
Cdd:PRK07514 393 VHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGAALDEAAILAALKGRL---- 467
|
490 500 510
....*....|....*....|....*....|.
gi 114643324 545 APYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK07514 468 ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
46-575 |
1.09e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 207.69 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 46 RPLPKNFNFAADVLDQwsQKEKTGERPanpaLWWVNGKgdevKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIP 125
Cdd:PRK06155 14 DPLPPSERTLPAMLAR--QAERYPDRP----LLVFGGT----RWTYAEAARAAAAAAHALAA-AGVKRGDRVALMCGNRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 126 EWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSRNGW---LSF 202
Cdd:PRK06155 83 EFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagWST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 203 QELFQfASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQ--HSQsslgigFTLCGRYW---LDLKSSDIIWN---MSDTGw 274
Cdd:PRK06155 163 APLPP-LDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCcpHAQ------FYWWGRNSaedLEIGADDVLYTtlpLFHTN- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 275 vkaAIGSVFSSWLCGACV----------FVHRMAQFDTDTFLDTLTTYPITtLCSPPTvyrmlvqkdlKRYKFKSLRHCL 344
Cdd:PRK06155 235 ---ALNAFFQALLAGATYvleprfsasgFWPAVRRHGATVTYLLGAMVSIL-LSQPAR----------ESDRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 345 TGGEPlnPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGqEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLK 424
Cdd:PRK06155 301 GPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHG-SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 425 PtrPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVS 504
Cdd:PRK06155 378 E--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 505 SPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK06155 456 VPSELGEDEVMAAVVL-RDGTALEPV----ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-575 |
5.12e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 202.01 E-value: 5.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASEEVAPAVESIvlecpdlKTKLLVSPQSRNGWLSfqELFQfaSEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQ 243
Cdd:PRK06839 103 VLFVEKTFQNMALSM-------QKVSYVQRVISITSLK--EIED--RKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGfTLCGRYWLDLKSSDIiwnmSDTGWVKAAIGSV----FSSWLCGACVFVHRmaQFDTDTFLDTLTTYPITTLCS 319
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDR----SIVLLPLFHIGGIglfaFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 PPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLnPEVLEQWRAQTGLDLYEGYGQTE----VGMICANQKGQeiKPGSMGK 394
Cdd:PRK06839 245 VPTIHQALINCsKFETTNLQSVRWFYNGGAPC-PEELMREFIDRGFLFGQGFGMTEtsptVFMLSEEDARR--KVGSIGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 395 GMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDV 474
Cdd:PRK06839 322 PVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 475 IISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfKSYNPEKltlELQDHVKKSTAPYKYPRKVE 554
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS--SSVLIEK---DVIEHCRLFLAKYKIPKEIV 471
|
490 500
....*....|....*....|.
gi 114643324 555 FVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK06839 472 FLKELPKNATGKIQKAQLVNQ 492
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
66-572 |
3.23e-57 |
|
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: 199.77 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALwwVNG-KGDEVkwSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPG 144
Cdd:cd05904 13 LFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 145 TIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLecpdlktKLLVSPQSRNGWLSFQELFQFASEEHSCVETGSQ-EP 223
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLAL-------PVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQdDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 MTIYFTSGTTGFPK--MAQH---------------SQSSLGI------------GFTLCGRYWLDLKSSDIIWNMSDTGW 274
Cdd:cd05904 161 AALLYSSGTTGRSKgvMLTHrnliamvaqfvagegSNSDSEDvflcvlpmfhiyGLSSFALGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 275 VKAAIGsvfsswlcgacvfvhrmaqfdtdtfldtltTYPITTL-CSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPE 353
Cdd:cd05904 241 LLAAIE------------------------------RYKVTHLpVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 354 VLEQWRAQ-TGLDLYEGYGQTE---VGMICANQKGQEIKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALRlKPtrp 428
Cdd:cd05904 291 LIEAFRAKfPNVDLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 429 fCFFSKYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPD 507
Cdd:cd05904 367 -SIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPD 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 508 QIRGEVVKAFVVLAApfKSYNPEKltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd05904 446 EEAGEVPMAFVVRKP--GSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
70-569 |
8.31e-57 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 201.72 E-value: 8.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWVNGKGDEVK-WSFREL-GSLSRKAANMltKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGII------- 140
Cdd:PRK10524 65 KRPEQLALIAVSTETDEERtYTFRQLhDEVNRMAAML--RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 141 FMPGTIQLtakdilyRLRASKAKCIVASE------EVAPAV----ESIVLECPDLKTKLLVS----PQSRNGW--LSFQE 204
Cdd:PRK10524 143 FASHSLAA-------RIDDAKPVLIVSADagsrggKVVPYKplldEAIALAQHKPRHVLLVDrglaPMARVAGrdVDYAT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 205 LF-QFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVF 283
Cdd:PRK10524 216 LRaQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 284 SSWLCGACVFVH-------------RMAQFdtdtfldtlttYPITTLCSPPTVYRMLVQKD---LKRYKFKSLRHCLTGG 347
Cdd:PRK10524 296 APLLAGMATIMYeglptrpdagiwwRIVEK-----------YKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 348 EPLNpEVLEQWRAQT-GLDLYEGYGQTEVGM-ICANQKG---QEIKPGSMGKGMLPYDVQIIDEN-GNVLPPGKEGEIAL 421
Cdd:PRK10524 365 EPLD-EPTASWISEAlGVPVIDNYWQTETGWpILAIARGvedRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 422 RlKPTRPFCFFSKYVDNPQ--KTA-ATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVV 498
Cdd:PRK10524 444 E-GPLPPGCMQTVWGDDDRfvKTYwSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114643324 499 ESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPE---KLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:PRK10524 523 EVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-578 |
1.77e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 199.49 E-value: 1.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAPAVES----------IVLECPDLKT--KLLVSP--QSRNGWL----SFQELFQFASEEHSCVETGSQEP-------M 224
Cdd:PRK06710 130 LVFPRVTNvqsatkiehvIVTRIADFLPfpKNLLYPfvQKKQSNLvvkvSESETIHLWNSVEKEVNTGVEVPcdpendlA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 225 TIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLdlkssdiiWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMA------ 298
Cdd:PRK06710 210 LLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQgykmvl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 299 --QFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDL-KRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEV 375
Cdd:PRK06710 281 ipKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 376 GMIC-ANQKGQEIKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVT 453
Cdd:PRK06710 361 SPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWLHT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 454 GDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksyNPEKLT 533
Cdd:PRK06710 436 GDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE-----GTECSE 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 114643324 534 LELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWR 578
Cdd:PRK06710 511 EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
71-575 |
2.57e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 195.77 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 71 RPANPALWWvngKGDEVKWsfRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTA 150
Cdd:PRK07786 30 QPDAPALRF---LGNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTS 230
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 231 GTTGFPKMAQHSQSSLGIGFTLCGRYW-LDLKSsdiiwnmsDTGWVK------AAIGSVFSSWLCGACVFVHRMAQFDTD 303
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTCLRTNgADINS--------DVGFVGvplfhiAGIGSMLPGLLLGAPTVIYPLGAFDPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 304 TFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQTEVGMICANQ 382
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEMSPVTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 383 KGQEI--KPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMD 460
Cdd:PRK07786 336 LGEDAirKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 461 SDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfksynPEKLTL-ELQDH 539
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND-----DAALTLeDLAEF 485
|
490 500 510
....*....|....*....|....*....|....*.
gi 114643324 540 VKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK07786 486 LTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-574 |
7.86e-54 |
|
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: 190.20 E-value: 7.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 166 VASEEVApaVESIVlecpdlktkllvspQSRNGWlsfqELFQFASEEHscvetgsqEPMTIYFTSGTTGFPKmaqhsqss 245
Cdd:cd12118 106 FVDREFE--YEDLL--------------AEGDPD----FEWIPPADEW--------DPIALNYTSGTTGRPK-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 246 lGIGFTLCGRYwLDLKSSDIIWNMSDTG-----------------WVKAAIGsvfsswlcGACVFvhrMAQFDTDTFLDT 308
Cdd:cd12118 150 -GVVYHHRGAY-LNALANILEWEMKQHPvylwtlpmfhcngwcfpWTVAAVG--------GTNVC---LRKVDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 309 LTTYPITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQwRAQTGLDLYEGYGQTEV---GMICANQKG 384
Cdd:cd12118 217 IEKHKVTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAWKPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGS--------MGKGMLPYD-VQIIDENGNVLPP--GKE-GEIALR----LKptrpfcffsKYVDNPQKTAATIRG 448
Cdd:cd12118 296 WDELPTEerarlkarQGVRYVGLEeVDVLDPETMKPVPrdGKTiGEIVFRgnivMK---------GYLKNPEATAEAFRG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 DFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYN 528
Cdd:cd12118 367 GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL-KEGAKVT 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 114643324 529 PEkltlELQDHVKKSTAPYKYPRKVEFVqELPKTITGKIKRNVLRD 574
Cdd:cd12118 446 EE----EIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
88-574 |
3.79e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 188.25 E-value: 3.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 SeevapavesivlecPDLKTKLLVSPQSRngwlsFQELFQFASEEHSCVETGS-QEPMTIYFTSGTTGFPKmaqhsqssl 246
Cdd:PRK03640 106 D--------------DDFEAKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPK--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 247 GIGFTLCGRYWldlkssdiiwnmsdtgwvkAAIGSVFS-------SWLCGACVF-------------------------- 293
Cdd:PRK03640 158 GVIQTYGNHWW-------------------SAVGSALNlglteddCWLAAVPIFhisglsilmrsviygmrvvlvekfda 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 --VHRMAQFDTdtfldtlttypITTLCSPPT-VYRMLVQKDLKRYKfKSLRHCLTGGEPLNPEVLEQWRaQTGLDLYEGY 370
Cdd:PRK03640 219 ekINKLLQTGG-----------VTIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCK-EKGIPVYQSY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 371 GQTEV-GMICA-NQKGQEIKPGSMGKGMLPYDVQIIDeNGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRG 448
Cdd:PRK03640 286 GMTETaSQIVTlSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVK-GPN----VTKGYLNREDATRETFQD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 DFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYn 528
Cdd:PRK03640 360 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEE- 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 114643324 529 pekltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK03640 439 ------ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
72-572 |
3.89e-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: 187.35 E-value: 3.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALwwvngKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWwLVNV-ACIRTGIIFMPGTIQLTA 150
Cdd:cd05930 1 PDAVAV-----VDGDQSLTYAELDARANRLARYL-RERGVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVPLDPSYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KDILYRLRASKAKCIVaseevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscveTGSQEPMTIYFTS 230
Cdd:cd05930 74 ERLAYILEDSGAKLVL---------------------------------------------------TDPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 231 GTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMSDTGWVkAAIGSVFSSWLCGAC-VFVHRMAQFDTDTFLDTL 309
Cdd:cd05930 103 GSTGKPKGVMVEHRGL-VNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATlVVLPEEVRKDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 310 TTYPITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQTEVGMICAnqkGQEIK 388
Cdd:cd05930 181 AEEGITVLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDAT---YYRVP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 389 PGSMGKGMLP-------YDVQIIDENGNVLPPGKEGEIAL------RlkptrpfcffsKYVDNPQKTAATIRGD------ 449
Cdd:cd05930 257 PDDEEDGRVPigrpipnTRVYVLDENLRPVPPGVPGELYIggaglaR-----------GYLNRPELTAERFVPNpfgpge 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 450 -FYVTGDRGVMDSDGYFWFVGRADD-VIIsSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfksy 527
Cdd:cd05930 326 rMYRTGDLVRWLPDGNLEFLGRIDDqVKI-RGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG---- 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 114643324 528 nPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd05930 401 -GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
70-579 |
6.61e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 188.36 E-value: 6.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALwwVNGKGDEVKwSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:PRK13391 9 TTPDKPAV--IMASTGEVV-TYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLV-SPQSRNGWLSFQElfqfaseehsCVETGSQEPMT--- 225
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAE----------AVAGLPATPIAdes 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 ----IYFTSGTTGFPKMAQHSQSSLGIG-----FTLCGRYWLdlKSSDIIWnMSDTGWVKAA----IGSVFSSwlcGACV 292
Cdd:PRK13391 155 lgtdMLYSSGTTGRPKGIKRPLPEQPPDtplplTAFLQRLWG--FRSDMVY-LSPAPLYHSApqraVMLVIRL---GGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 FVhrMAQFDTDTFLDTLTTYPITTLCSPPTVY-RMLVQKD--LKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEG 369
Cdd:PRK13391 229 IV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 370 YGQTE-VGMICANQKGQEIKPGSMGKGMLPyDVQIIDENGNVLPPGKEGEIALrlKPTRPFcffsKYVDNPQKTAAT--I 446
Cdd:PRK13391 307 YAATEgLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWF--EGGRPF----EYLNDPAKTAEArhP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 447 RGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKS 526
Cdd:PRK13391 380 DGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDP 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 527 yNPEkLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRG 579
Cdd:PRK13391 460 -GPA-LAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
90-575 |
9.43e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 189.44 E-value: 9.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:PRK05605 59 TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAP---------AVESIV-----------------LECPDLKTK--LLVSPQSrnGWLSFQELFQFA----SEEHSCVE 217
Cdd:PRK05605 138 KVAPtverlrrttPLETIVsvnmiaampllqrlalrLPIPALRKAraALTGPAP--GTVPWETLVDAAiggdGSDVSHPR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 218 TGSQEPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWL-DLKSSDIIwnmsdtgwVKAA----------IGSVFSSW 286
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNL-FANAAQGKAWVpGLGDGPER--------VLAAlpmfhaygltLCLTLAVS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 287 LCGACVFVHR------MAQFDTDtfldtlttyPITTLCSPPTVYRMLVQKDLKR-YKFKSLRHCLTGGEPLNPEVLEQWR 359
Cdd:PRK05605 287 IGGELVLLPApdidliLDAMKKH---------PPTWLPGVPPLYEKIAEAAEERgVDLSGVRNAFSGAMALPVSTVELWE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGkgmLPY---DVQIID-EN-GNVLPPGKEGEIALRlKPTRpfcfFS 433
Cdd:PRK05605 358 KLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVG---VPFpdtEVRIVDpEDpDETMPDGEEGELLVR-GPQV----FK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 434 KYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEV 513
Cdd:PRK05605 430 GYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114643324 514 VKAFVVLaAPFKSYNPEKltleLQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK05605 510 VVAAVVL-EPGAALDPEG----LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-574 |
1.90e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 188.06 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFREL-GSLSRKAANMLTKpcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKC 164
Cdd:PRK12583 43 ALRYTWRQLaDAVDRLARGLLAL--GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 165 IV------ASEEVAPAVESI---------VLEC---PDLKTKLLVSPQSRNGWLSFQELFQFA---SEEHSCVETGS--- 220
Cdd:PRK12583 121 VIcadafkTSDYHAMLQELLpglaegqpgALACerlPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQASldr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 221 QEPMTIYFTSGTTGFPKMAQHSQSslgigftlcgrywldlkssdiiwNMSDTGWVKA-------------------AIGS 281
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHH-----------------------NILNNGYFVAeslgltehdrlcvpvplyhCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 282 VFSSWLC---GACVfVHRMAQFDTDTFLDTLTTYPITTLCSPPTVY-RMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQ 357
Cdd:PRK12583 258 VLANLGCmtvGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 358 WRAQTGL-DLYEGYGQTE---VGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAlrlkpTRPFCFFS 433
Cdd:PRK12583 337 VMDEMHMaEVQIAYGMTEtspVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 434 KYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGE 512
Cdd:PRK12583 412 GYWNNPEATAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114643324 513 VVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK12583 492 EIVAWVRL-HPGHAASEE----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
88-574 |
1.79e-51 |
|
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: 182.16 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCiva 167
Cdd:cd05912 1 SYTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 sEEVApavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqepmTIYFTSGTTGFPKMAQHSqsslg 247
Cdd:cd05912 77 -DDIA----------------------------------------------------TIMYTSGTTGKPKGVQQT----- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 248 igftlCGRYWldlkssdiiWNmsdtgwvkaAIGSVFS-------SWLCGACVF--------------------------- 293
Cdd:cd05912 99 -----FGNHW---------WS---------AIGSALNlglteddNWLCALPLFhisglsilmrsviygmtvylvdkfdae 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 -VHRMAQFDTdtfldtlttypITTLCSPPTVYRMLVQKDLKRYKfKSLRHCLTGGEPLNPEVLEQWRaQTGLDLYEGYGQ 372
Cdd:cd05912 156 qVLHLINSGK-----------VTIISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGM 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 373 TEVG--MICANQKGQEIKPGSMGKGMLPYDVQIIDENGnvlPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDF 450
Cdd:cd05912 223 TETCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLK-GPN----VTKGYLNRPDATEESFENGW 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYnpe 530
Cdd:cd05912 295 FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE--- 371
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 114643324 531 kltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd05912 372 ----ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
72-573 |
4.36e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 183.29 E-value: 4.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWwVNGKGDEVkwSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVASeevaPAVESIVLEC-PDLKTKLlvspqsrngwlSFQ-ELFQFASEEHSCVETG---SQEP--M 224
Cdd:PRK13390 87 EADYIVGDSGARVLVAS----AALDGLAAKVgADLPLRL-----------SFGgEIDGFGSFEAALAGAGprlTEQPcgA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 225 TIYFTSGTTGFPK-----MAQHSQSSLGIGFTLCGRYWLDLKSSDI------IWNMSDTGWVkaaiGSVFSswLCGACVF 293
Cdd:PRK13390 152 VMLYSSGTTGFPKgiqpdLPGRDVDAPGDPIVAIARAFYDISESDIyyssapIYHAAPLRWC----SMVHA--LGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 VHRMaqfDTDTFLDTLTTYPITTLCSPPTVY-RML-VQKDLK-RYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGY 370
Cdd:PRK13390 226 AKRF---DAQATLGHVERYRITVTQMVPTMFvRLLkLDADVRtRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 371 GQTEV-GMICANQKGQEIKPGSMGKGMLPyDVQIIDENGNVLPPGKEGEIALRlKPTRPFcffsKYVDNPQKTAATIR-- 447
Cdd:PRK13390 303 SSTEAhGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFE-RDRLPF----RYLNDPEKTAAAQHpa 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 448 GDFYVT-GDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKS 526
Cdd:PRK13390 377 HPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 114643324 527 ynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK13390 457 --SDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-574 |
2.62e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.14 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAPAVESIVLECP----------DL-------------KTKLLVSPQSRNGWLSF-QELFQFASEEHSCVETGSQEPMT 225
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvasmgDLlgfkghivnfvvrRVKKMVPAWSLPGHVRFnDALAEGARQTFKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPKmaqhsqsslgiGFTLCGRywldlkssDIIWNMSDTG-WVKAAIGS-----------------VFSSWL 287
Cdd:PRK07059 209 LQYTGGTTGVSK-----------GATLLHR--------NIVANVLQMEaWLQPAFEKkprpdqlnfvcalplyhIFALTV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 288 C-------GAC-----------VFVHRMAQfdtdtfldtlttYPITTLCSPPTVYR-MLVQKDLKRYKFKSLRHCLTGGE 348
Cdd:PRK07059 270 CgllgmrtGGRnilipnprdipGFIKELKK------------YQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 349 PLNPEVLEQWRAQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTr 427
Cdd:PRK07059 338 AVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQ- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 428 pfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSP 506
Cdd:PRK07059 416 ---VMAGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114643324 507 DQIRGEVVKAFVVLAAPfksynpeKLTLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK07059 493 DEHSGEAVKLFVVKKDP-------ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-580 |
3.38e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 181.34 E-value: 3.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 71 RPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMP----GTI 146
Cdd:PRK06188 25 YPDRPALVL-----GDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAlhplGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 147 QltakDILYRLRASKAKCIVAseEVAPAVE---SIVLECPDLKTKLLVSPQsrNGWLSFqeLFQFASEEHSCVETGSQ-- 221
Cdd:PRK06188 99 D----DHAYVLEDAGISTLIV--DPAPFVEralALLARVPSLKHVLTLGPV--PDGVDL--LAAAAKFGPAPLVAAALpp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSLGiGFTlcgrywldlkssdiIWNMSDTGWVK------------AAIGSVFSSWLCG 289
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHRSIA-TMA--------------QIQLAEWEWPAdprflmctplshAGGAFFLPTLLRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 290 ACVFVHRmaQFDTDTFLDTLTTYPIT-TLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYE 368
Cdd:PRK06188 234 GTVIVLA--KFDPAEVLRAIEEQRITaTFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 369 GYGQTEVGM-ICANQKGQEIKP-----GSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlkptRPFcFFSKYVDNPQKT 442
Cdd:PRK06188 312 YYGQTEAPMvITYLRKRDHDPDdpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 443 AATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaA 522
Cdd:PRK06188 387 AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL-R 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 114643324 523 PFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK06188 466 PGAAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGR 519
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
57-572 |
8.84e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 181.01 E-value: 8.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 57 DVLDQWSQkektgERPANPALWWVngkGDEVkwSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIR 136
Cdd:PRK06178 37 EYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 137 TGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPdLKTKLLVS--------------------PQSR 196
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETS-LRHVIVTSladvlpaeptlplpdslrapRLAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 197 NGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSslgigftlcgrywldlkssDIIWNMSDTGWVK 276
Cdd:PRK06178 185 AGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR-------------------DMVYTAAAAYAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 277 AAIG--SVFSSWL-----------------CGACVFVhrMAQFDTDTFLDTLTTYPITTLCSP-PTVYRMLVQKDLKRYK 336
Cdd:PRK06178 246 VVGGedSVFLSFLpefwiagenfgllfplfSGATLVL--LARWDAVAFMAAVERYRVTRTVMLvDNAVELMDHPRFAEYD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 337 FKSLRH--CLTGGEPLNPEVLEQWRAQTGLDLYEG-YGQTE--------VGMicanQKGQE---IKPGSMGkgmLPY--- 399
Cdd:PRK06178 324 LSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTEthtcdtftAGF----QDDDFdllSQPVFVG---LPVpgt 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 400 DVQIID-ENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISS 478
Cdd:PRK06178 397 EFKICDfETGELLPLGAEGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 479 GYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPrKVEFVQE 558
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQL-KPGADLTAA----ALQAWCRENMAVYKVP-EIRIVDA 545
|
570
....*....|....
gi 114643324 559 LPKTITGKIKRNVL 572
Cdd:PRK06178 546 LPMTATGKVRKQDL 559
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
72-579 |
1.57e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 179.47 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWvngkGDEVkWSFRELGS-LSRKAANMLTKpcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTA 150
Cdd:PRK07470 21 PDRIALVW----GDRS-WTWREIDArVDALAAALAAR--GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KDILYRLRASKAK---CIVASEEVAPAVESivlECPDLKTKLLVSpqSRNGWLSFQELF-QFASEEHSCVETGSQEPMTI 226
Cdd:PRK07470 94 DEVAYLAEASGARamiCHADFPEHAAAVRA---ASPDLTHVVAIG--GARAGLDYEALVaRHLGARVANAAVDHDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 227 YFTSGTTGFPKMA--QHSQSSLGIGFTLCgrywlDLkssdiiwnMSDTGWVKAAIgsVFSSWLCGACVfvHRMAQFD--- 301
Cdd:PRK07470 169 FFTSGTTGRPKAAvlTHGQMAFVITNHLA-----DL--------MPGTTEQDASL--VVAPLSHGAGI--HQLCQVArga 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 -----------TDTFLDTLTTYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEvlEQWRAQTGLD--LY 367
Cdd:PRK07470 232 atvllpserfdPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRA--DQKRALAKLGkvLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 368 EGYGQTEV-GMIC-------ANQKGQEIKPGSMG---KGMlpyDVQIIDENGNVLPPGKEGEIALRLKPTrpfcfFSKYV 436
Cdd:PRK07470 310 QYFGLGEVtGNITvlppalhDAEDGPDARIGTCGferTGM---EVQIQDDEGRELPPGETGEICVIGPAV-----FAGYY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 437 DNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKA 516
Cdd:PRK07470 382 NNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114643324 517 FVVLAAPfKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ-EWRG 579
Cdd:PRK07470 462 VCVARDG-APVDEA----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREElEERG 520
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-573 |
2.10e-49 |
|
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: 174.77 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSS-LGIGFTLCGRywLDLKSSDIIwnmsdtgwvkaAI--------GSVFSSWLC---- 288
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNiVNNGYFIGER--LGLTEQDRL-----------CIpvplfhcfGSVLGVLAClthg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 GACVFVHRMAQFDTDTFLDTLTTypITTLCSPPTVY-RMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGL-DL 366
Cdd:cd05917 70 ATMVFPSPSFDPLAVLEAIEKEK--CTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 367 YEGYGQTEVGMICANQK---GQEIKPGSMGKGMLPYDVQIIDENGNVLPP-GKEGEIAlrlkpTRPFCFFSKYVDNPQKT 442
Cdd:cd05917 148 TIAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELC-----IRGYSVMKGYWNDPEKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 443 AATIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLa 521
Cdd:cd05917 223 AEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 114643324 522 APFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd05917 302 KEGAELTEE----DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
56-575 |
4.39e-49 |
|
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: 178.42 E-value: 4.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQkektgERPANPALwwVNGkgdEVKWSFRELGSLS-RKAANMLTKpcGLQRGDRVAVILPPIPEWWLVNVAC 134
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDG---ERRLSYAELDRRAdRLAAGLLAL--GLRPGDRVVVQLPNVAEFVIVFFAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 135 IRTGII---FMPGTIQLtakDILYRLRASKAKCIVASEEVA-----PAVESIVLECPDLKTKLLVSPQSrnGWLSFQELF 206
Cdd:COG1021 96 FRAGAIpvfALPAHRRA---EISHFAEQSEAVAYIIPDRHRgfdyrALARELQAEVPSLRHVLVVGDAG--EFTSLDALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 207 QfASEEHSCVETGSQEPMTIYFTSGTTGFPKmaqhsqsslgigftLCGR----YWLDLKSSDIIWNMsDTGWV------- 275
Cdd:COG1021 171 A-APADLSEPRPDPDDVAFFQLSGGTTGLPK--------------LIPRthddYLYSVRASAEICGL-DADTVylaalpa 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 276 --KAAIGS--VFSSWLCGACVFV---------------HRmaqfdtdtfldtlttypIT-TLCSPPTVYRMLVQKDLKRY 335
Cdd:COG1021 235 ahNFPLSSpgVLGVLYAGGTVVLapdpspdtafplierER-----------------VTvTALVPPLALLWLDAAERSRY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 336 KFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEvGMICANQKG--QEIKPGSMGKGMLPYD-VQIIDENGNVLP 412
Cdd:COG1021 298 DLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYTRLDdpEEVILTTQGRPISPDDeVRIVDEDGNPVP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 413 PGKEGEIAlrlkpTR-PFCFfSKYVDNPQ--KTAATIRGdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVES 489
Cdd:COG1021 377 PGEVGELL-----TRgPYTI-RGYYRAPEhnARAFTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 490 ALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfksyNPEKLTL-ELQDHVK-KSTAPYKYPRKVEFVQELPKTITGKI 567
Cdd:COG1021 450 LLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-------RGEPLTLaELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKI 522
|
....*...
gi 114643324 568 KRNVLRDQ 575
Cdd:COG1021 523 DKKALRAA 530
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
73-573 |
7.54e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 177.57 E-value: 7.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 73 ANPALWWVNGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEW---WLvNVACIrtGIIFMPGTIQLT 149
Cdd:PRK08008 22 HKTALIFESSGGVVRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFifcWF-GLAKI--GAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEVAPAVESIVLECPD-LKTKLLVSPQSR--NGWLSFQELF-QFASEEHSCVETGSQEPMT 225
Cdd:PRK08008 98 REESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPadDGVSSFTQLKaQQPATLCYAPPLSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPKmaqhsqsslGIGFTLC-----GRY--W-LDLKSSDIIWNMSDTGWVK---AAIGSVFSSwlcGACVFV 294
Cdd:PRK08008 178 ILFTSGTTSRPK---------GVVITHYnlrfaGYYsaWqCALRDDDVYLTVMPAFHIDcqcTAAMAAFSA---GATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 295 hrMAQFDTDTFLDTLTTYPIT-TLCSPPTVYRMLVQKDLKRYKfkslRHCLTggeplnpEVL----------EQWRAQTG 363
Cdd:PRK08008 246 --LEKYSARAFWGQVCKYRATiTECIPMMIRTLMVQPPSANDR----QHCLR-------EVMfylnlsdqekDAFEERFG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 364 LDLYEGYGQTE--VGMIcANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRpfCFFSKYVDNPQK 441
Cdd:PRK08008 313 VRLLTSYGMTEtiVGII-GDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYYLDPKA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 442 TAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVL 520
Cdd:PRK08008 390 TAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 114643324 521 AApfksynPEKLTLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK08008 470 NE------GETLSEEeFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
320-569 |
1.39e-48 |
|
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: 172.07 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 PPTVYRMLVQKDLKRYKFKSLRHcLTGGEplNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEiKPGSMGKGMLPY 399
Cdd:cd17637 96 PPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 400 DVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGR--ADDVIIS 477
Cdd:cd17637 172 RVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 478 SGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQ 557
Cdd:cd17637 247 GGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVL-KPGATLTAD----ELIEFVGSRIARYKKPRYVVFVE 321
|
250
....*....|..
gi 114643324 558 ELPKTITGKIKR 569
Cdd:cd17637 322 ALPKTADGSIDR 333
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
89-580 |
1.39e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 177.25 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 89 WSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVAS 168
Cdd:PRK06087 50 YTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 169 EEVA-----PAVESIVLECPDLKTKLLV---SPQSRNgwLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPK--M 238
Cdd:PRK06087 129 TLFKqtrpvDLILPLQNQLPQLQQIVGVdklAPATSS--LSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvM 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 239 AQHSQsslgIGFT---LCGRywLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQfdtdtfldtlttyPIT 315
Cdd:PRK06087 207 LTHNN----ILASeraYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT-------------PDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 316 TL---------CS---PPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLnPEVLEQWRAQTGLDLYEGYGQTE-VGMICAN- 381
Cdd:PRK06087 268 CLalleqqrctCMlgaTPFIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTEsSPHAVVNl 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 382 QKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMD 460
Cdd:PRK06087 347 DDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR-GPN----VFMGYLDEPELTARALDEEgWYYSGDLCRMD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 461 SDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQdhv 540
Cdd:PRK06087 422 EAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFS--- 498
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 114643324 541 KKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRdQEWRGR 580
Cdd:PRK06087 499 RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR-KDIMRR 537
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
312-576 |
2.97e-47 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 173.70 E-value: 2.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 312 YPITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVG-MICANQKGQEIKP 389
Cdd:PRK08974 298 YPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 390 GSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVG 469
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQ----VMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 470 RADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfksyNPEKLTL-ELQDHVKKSTAPYK 548
Cdd:PRK08974 453 RKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVK-------KDPSLTEeELITHCRRHLTGYK 525
|
250 260
....*....|....*....|....*...
gi 114643324 549 YPRKVEFVQELPKTITGKIKRNVLRDQE 576
Cdd:PRK08974 526 VPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
77-573 |
7.20e-47 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 174.70 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 77 LWWVNGKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYR 156
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 157 LRASKAKCIVASEEVAPAVESIVLEcpDLKTKLLVSpQSRNGW-----LSFQELFQFASEEH------------------ 213
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLK--DIVDAALDE-SAKNGVsvgicLTYENQLAMKREDTkwqegrdvwwqdvvpnyp 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 214 -SC-VE-TGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGA 290
Cdd:PLN02654 265 tKCeVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 291 CVFVHRMAQFDTDTFL--DTLTTYPITTLCSPPTVYRMLVQKD---LKRYKFKSLRHCLTGGEPLNPEVleqWR------ 359
Cdd:PLN02654 345 TVLVFEGAPNYPDSGRcwDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRwffnvv 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTGLDLYEGYGQTEVG--MICANQKGQEIKPGSmgkGMLPY-DVQ--IIDENGNVLppgkEGEIA--LRLKPTRPFCFF 432
Cdd:PLN02654 422 GDSRCPISDTWWQTETGgfMITPLPGAWPQKPGS---ATFPFfGVQpvIVDEKGKEI----EGECSgyLCVKKSWPGAFR 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 433 SKYVDNPQKTAATIR--GDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIR 510
Cdd:PLN02654 495 TLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 511 GEVVKAFVVL--AAPFKsynpEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PLN02654 575 GQGIYAFVTLveGVPYS----EELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
157-574 |
8.05e-47 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 172.25 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 157 LRASKAKCIVASEEVAPAVESIVLECPDlKTKLLVSPQSRNGWLSfqELFQFASEEHSCVETGSQEpMTIYFTSGTTGFP 236
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCPQ-ATRIVAWTDEDHDLTV--EVLIAAHAGQRPEPTGRKG-RVILLTSGTTGTP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 237 KMAQHSQSSlGIGftlcgrywlDLKSSdiiwnMSDTGW------VKAAigSVFSSW--------LCGACVFVHRMaQFDT 302
Cdd:PRK13382 212 KGARRSGPG-GIG---------TLKAI-----LDRTPWraeeptVIVA--PMFHAWgfsqlvlaASLACTIVTRR-RFDP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 303 DTFLDTLTTYPITTLCSPPTVYRM---LVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMIC 379
Cdd:PRK13382 274 EATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 380 -ANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKptrpfCFFSKYVdnPQKTAATIRGdFYVTGDRGV 458
Cdd:PRK13382 354 tATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGYT--SGSTKDFHDG-FMASGDVGY 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 459 MDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQD 538
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL-KPGASATPE----TLKQ 500
|
410 420 430
....*....|....*....|....*....|....*.
gi 114643324 539 HVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK13382 501 HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
84-572 |
1.72e-46 |
|
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: 170.20 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGII---FMPGTIQLtakDILYRLRAS 160
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRG-LGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPSHRRS---ELSAFCAHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 161 KAKCIVASEevapavesivlecpdlktkllvspqsRNGWLSFQELFQfasEEHSCVetgsQEPMTIYFTSGTTGFPKMAQ 240
Cdd:cd05920 112 EAVAYIVPD--------------------------RHAGFDHRALAR---ELAESI----PEVALFLLSGGTTGTPKLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 241 HSQSSLGIGFTlcgrywldlKSSDIIWNMSDTGWVKA---------AIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTT 311
Cdd:cd05920 159 RTHNDYAYNVR---------ASAEVCGLDQDTVYLAVlpaahnfplACPGVLGTLLAGGRVVLAPDPSPDAAFPLIEREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 312 YPITTLCsPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEvGMICANQKG--QEIKP 389
Cdd:cd05920 230 VTVTALV-PALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTRLDdpDEVII 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 390 GSMGKGMLPYD-VQIIDENGNVLPPGKEGEIALRLKPTrpfcfFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWF 467
Cdd:cd05920 308 HTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 468 VGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPEKLTLELQDHVKK-STAP 546
Cdd:cd05920 383 EGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRErGLAA 456
|
490 500
....*....|....*....|....*.
gi 114643324 547 YKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd05920 457 YKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
90-573 |
1.85e-46 |
|
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: 169.10 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:cd05903 3 TYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVapavesivlecpdlktkllvspqsrnGWLSFQELfqfaseehscvetgSQEPMTIYFTSGTTGFPKMAQHSQSSLGIG 249
Cdd:cd05903 82 RF--------------------------RQFDPAAM--------------PDAVALLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FT-LCGRYWLDlkSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITtLCSPPTVYRMLV 328
Cdd:cd05903 122 IRqYAERLGLG--PGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFM-MGATPFLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 329 QKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANqkgqeIKPGSMGKGM-------LPYDV 401
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPAPEDRRLytdgrplPGVEI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 402 QIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYR 481
Cdd:cd05903 274 KVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 482 IGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksynPEKLTLE-LQDHV-KKSTAPYKYPRKVEFVQEL 559
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS------GALLTFDeLVAYLdRQGVAKQYWPERLVHVDDL 422
|
490
....*....|....
gi 114643324 560 PKTITGKIKRNVLR 573
Cdd:cd05903 423 PRTPSGKVQKFRLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-574 |
2.07e-46 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 170.89 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 81 NGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILppipeW--------WLVnVACIrtGIIFMPGTIQLTAKD 152
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRR-LGVKPGDRVATLA-----WnthrhlelYYA-VPGM--GAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 153 ILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVS------PQSRNGWLSFQELFQFASEEHSCVETGSQEPMTI 226
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 227 YFTSGTTGFPKMAQHSQSSLGIG-FTLCGRYWLDLKSSDIIwnMSDT------GWvkaaiGSVFSSWLCGAC-VFVHRMA 298
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVV--LPVVpmfhvnAW-----GLPYAAAMVGAKlVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 299 QFDTDTFLDTLttYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQtGLDLYEGYGQTE--- 374
Cdd:cd12119 242 DPASLAELIER--EGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTEtsp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMICANQKGQEIKPGSMG------KGMLPYDVQ--IIDENGNVLP-PGKE-GEIALRlKPTRPfcffSKYVDNPQKTAA 444
Cdd:cd12119 319 LGTVARPPSEHSNLSEDEQlalrakQGRPVPGVElrIVDDDGRELPwDGKAvGELQVR-GPWVT----KSYYKNDEESEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 445 TIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPF 524
Cdd:cd12119 394 LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL-KEG 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 114643324 525 KSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd12119 473 ATVTAE----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
72-575 |
2.67e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 170.07 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWvngKGDEVkwSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:PRK06145 16 PDRAALVY---RDQEI--SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVASEEVAPAVEsivlecpdlktklLVSPQSRNGWLSFQELFQFASEEHSCVETGSQEP---MTIYF 228
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEFDAIVA-------------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPtdlVRLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 229 TSGTTGFPKMAQHSQSSLgigftlcgrYWldlKSSDIIWNMSDTGWVKA-AIGSVFSSWLC----------GACVFVHRM 297
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNL---------HW---KSIDHVIALGLTASERLlVVGPLYHVGAFdlpgiavlwvGGTLRIHRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 298 AQFDTDTFLDTLTTYPITTLcSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPlNPE--VLEQWRAQTGLDLYEGYGQTE- 374
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWM-APVMLSRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTEt 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMICANQKGQEI-KPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALR-LKPTRpfcffsKYVDNPQKTAATIRGDFYV 452
Cdd:PRK06145 303 CSGDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTK------GYWKDPEKTAEAFYGDWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 453 TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksynPEKL 532
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP------GATL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 114643324 533 TLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK06145 451 TLEaLDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-575 |
4.95e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 169.22 E-value: 4.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 SEEVApAVESIVLECPDlktkllvspqsrngwlsfqelFQFASEEHSCVETGS---QEPMTIYFTSGTTGFPKMAQHSQS 244
Cdd:PRK09088 101 DDAVA-AGRTDVEDLAA---------------------FIASADALEPADTPSippERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 245 SL---GIGFTLCGRywLDLKSSDIIwnmsDTGW--VKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCS 319
Cdd:PRK09088 159 NLqqtAHNFGVLGR--VDAHSSFLC----DAPMfhIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 PPTVYRML-VQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQtGLDLYEGYGQTEVGMICANQKGQEI---KPGSMGKG 395
Cdd:PRK09088 233 VPQMAQAFrAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 396 MLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDV 474
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKKDM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 475 IISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlAAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVE 554
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIV-PADGAPLDLE----RIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|.
gi 114643324 555 FVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRDA 482
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
90-576 |
2.40e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 168.79 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA-- 167
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCla 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 -----SEEVAP--AVES-IVLECPDL--------------KTKLLVSPQSRNGWLSFQE-LFQFASEEHSCVETGSQEPM 224
Cdd:PRK05677 131 nmahlAEKVLPktGVKHvIVTEVADMlpplkrllinavvkHVKKMVPAYHLPQAVKFNDaLAKGAGQPVTEANPQADDVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 225 TIYFTSGTTGFPK------------MAQHSQ---SSLGIG---------------FTL-CGRYWLDLKSSDIIWNMSD-T 272
Cdd:PRK05677 211 VLQYTGGTTGVAKgamlthrnlvanMLQCRAlmgSNLNEGceiliaplplyhiyaFTFhCMAMMLIGNHNILISNPRDlP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 273 GWVKAAIGSVFSSWLCGACVFVhrmaqfdtdtfldtlttypitTLCSpptvyrmlvQKDLKRYKFKSLRHCLTGGEPLNP 352
Cdd:PRK05677 291 AMVKELGKWKFSGFVGLNTLFV---------------------ALCN---------NEAFRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 353 EVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFF 432
Cdd:PRK05677 341 ATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQ----VM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 433 SKYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRG 511
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 512 EVVKAFVVlAAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQE 576
Cdd:PRK05677 496 EAIKVFVV-VKPGETLTKE----QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
321-574 |
3.23e-45 |
|
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: 166.40 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 321 PTVY-RML----VQKDlkRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTE-VGMICANqkGQE--IKPGSM 392
Cdd:cd05929 224 PTMFvRLLklpeAVRN--AYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgQGLTIIN--GEEwlTHPGSV 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 393 GKGMLPyDVQIIDENGNVLPPGKEGEIALRLKPTrpfcffSKYVDNPQKTAATIRGDFYVT-GDRGVMDSDGYFWFVGRA 471
Cdd:cd05929 300 GRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 472 DDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAfVVLAAPFKSYNPEkLTLELQDHVKKSTAPYKYPR 551
Cdd:cd05929 373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA-VVQPAPGADAGTA-LAEELIAFLRDRLSRYKCPR 450
|
250 260
....*....|....*....|...
gi 114643324 552 KVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd05929 451 SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-575 |
8.00e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 166.66 E-value: 8.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCI 165
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 166 VASEEVAPAVESIVLECPDLKtkLLV--------SPQSRNGWLSFQELFQFASEEHSCVETGSQ-EPMTIYFTSGTTGFP 236
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPK--PLVidvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 237 KmaqhsqsslGIGFTLCGRYwLDLKSSDIIWNMSD-------------TGW-----VKAAIG-SVFSSWLCGACVF---- 293
Cdd:PRK08162 198 K---------GVVYHHRGAY-LNALSNILAWGMPKhpvylwtlpmfhcNGWcfpwtVAARAGtNVCLRKVDPKLIFdlir 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 VHRmaqfdtdtfldtlttypITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQwRAQTGLDLYEGYGQ 372
Cdd:PRK08162 268 EHG-----------------VTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 373 TEV---GMICANQKGQEIKPGS-----MGKGMLPYDVQiidENGNVLPP---------GKE-GEIALR----LKptrpfc 430
Cdd:PRK08162 330 TETygpATVCAWQPEWDALPLDeraqlKARQGVRYPLQ---EGVTVLDPdtmqpvpadGETiGEIMFRgnivMK------ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 431 ffsKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIR 510
Cdd:PRK08162 401 ---GYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKW 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 511 GEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFvQELPKTITGKIKRNVLRDQ 575
Cdd:PRK08162 478 GEVPCAFVEL-KDGASATEE----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-503 |
9.27e-45 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 163.59 E-value: 9.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAPAVESIVLECPDLKTKLLVSPQSRNgwlsfqelfqfaSEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIG 249
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAP------------APPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 FTLCGRYWlDLKSSDIIWNMS----DtgwvkAAIGSVFSSWLCGACVFV--HRMAQFDTDTFLDTLTTYPITTLCSPPTV 323
Cdd:TIGR01733 149 LAWLARRY-GLDPDDRVLQFAslsfD-----ASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 324 YRMLVqkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTG-LDLYEGYGQTE-----VGMICANQKGQEIKPGSMGKGML 397
Cdd:TIGR01733 223 LALLA--AALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTEttvwsTATLVDPDDAPRESPVPIGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 398 PYDVQIIDENGNVLPPGKEGEIALRLKptrpfCFFSKYVDNPQKTAA---------TIRGDFYVTGDRGVMDSDGYFWFV 468
Cdd:TIGR01733 301 NTRLYVLDDDLRPVPVGVVGELYIGGP-----GVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNLEFL 375
|
410 420 430
....*....|....*....|....*....|....*
gi 114643324 469 GRADDVIISSGYRIGPFEVESALIEHPAvVESAVV 503
Cdd:TIGR01733 376 GRIDDQVKIRGYRIELGEIEAALLRHPG-VREAVV 409
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-573 |
1.33e-44 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 165.92 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALwwVNGKGDEVkWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGT 145
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLHK-LGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIVASeevAPAVESIVLECPDLKTKLLVSPQSRNGWLSFQELFQFASEEHSCVETGSQEPMT 225
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQ---SCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPK--MAQHSQSSLGIGFTLCGRY-WLDLKSSDIIW---NMSDtgwvkaaIGSVFSSWLC----GACVFVh 295
Cdd:PLN02246 184 LPYSSGTTGLPKgvMLTHKGLVTSVAQQVDGENpNLYFHSDDVILcvlPMFH-------IYSLNSVLLCglrvGAAILI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 rMAQFDTDTFLDTLTTYPITTLC-SPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQT 373
Cdd:PLN02246 256 -MPKFEIGALLELIQRHKVTIAPfVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKlPNAVLGQGYGMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 374 EVG----MICANQKGQ-EIKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALR----LKptrpfcffsKYVDNPQKTA 443
Cdd:PLN02246 335 EAGpvlaMCLAFAKEPfPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRgpqiMK---------GYLNDPEATA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 444 ATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAA 522
Cdd:PLN02246 406 NTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSN 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 114643324 523 PFksynpeKLTL-ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PLN02246 486 GS------EITEdEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
85-574 |
2.19e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 164.01 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 85 DEVKWSFRELGSLSRKAANmltkpcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKC 164
Cdd:PRK07787 22 GGRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 165 IVASEEVAPAvesivlECPDLKtkllVSPQSRnGWlsfqelfqfaseeHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQS 244
Cdd:PRK07787 96 WLGPAPDDPA------GLPHVP----VRLHAR-SW-------------HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 245 SLGIGFTLCGRYWLdlkssdiiWNMSDT-----------GWVKAAIGS--VFSSwlcgacvFVH-------RMAQFDTDT 304
Cdd:PRK07787 152 AIAADLDALAEAWQ--------WTADDVlvhglplfhvhGLVLGVLGPlrIGNR-------FVHtgrptpeAYAQALSEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 305 FldtlttypiTTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKG 384
Cdd:PRK07787 217 G---------TLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGSMGKGMLPYDVQIIDENGNVLPPGKE--GEIALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDS 461
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLNRPDATAAAFTADgWFRTGDVAVVDP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 462 DGYFWFVGR-ADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFksyNPEkltlELQDHV 540
Cdd:PRK07787 363 DGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV---AAD----ELIDFV 435
|
490 500 510
....*....|....*....|....*....|....*
gi 114643324 541 KKSTAPYKYPRKVEFVQELPKTITGKI-KRNVLRD 574
Cdd:PRK07787 436 AQQLSVHKRPREVRFVDALPRNAMGKVlKKQLLSE 470
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-576 |
2.18e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 162.79 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPcGLQRGDRVAV--------ILPpipewwlvNVACIRTG--IIFM----PGTiQLtaKDILY 155
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVAVlarnhrgfVLA--------LYAAGKVGarIILLntgfSGP-QL--AEVAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 156 RLrasKAKCIVASEEVAPAVESIVLECPDLKTKLLVS---PQSRNGWLSFQELFqfASEEHSCVETGSQEPMTIYFTSGT 232
Cdd:PRK07788 144 RE---GVKALVYDDEFTDLLSALPPDLGRLRAWGGNPdddEPSGSTDETLDDLI--AGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 233 TGFPKMAQHSQSSlgiGFTLCGRYWldlksSDIIWNMSDT-----------GWVKAAIGSVFsswlcGACVFVHR----- 296
Cdd:PRK07788 219 TGTPKGAPRPEPS---PLAPLAGLL-----SRVPFRAGETtllpapmfhatGWAHLTLAMAL-----GSTVVLRRrfdpe 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 297 --MAqfdtdtfldTLTTYPITTLCSPPT-VYRML--VQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYG 371
Cdd:PRK07788 286 atLE---------DIAKHKATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 372 QTEVGmICANQKGQEIK--PGSMGKGMLPYDVQIIDENGNVLPPGKEGEIalrlkptrpFCF----FSKYVDNPQKtaAT 445
Cdd:PRK07788 357 STEVA-FATIATPEDLAeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRI---------FVGngfpFEGYTDGRDK--QI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 446 IRGdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFK 525
Cdd:PRK07788 425 IDG-LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVK-APGA 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 114643324 526 SYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQE 576
Cdd:PRK07788 503 ALDED----AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
70-575 |
7.12e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 161.37 E-value: 7.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWVN-GKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPpipEWW---LVNVACIRTGIIFMPGT 145
Cdd:PRK13295 36 SCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLP---NWWeftVLYLACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIVASEEV-----APAVESIVLECPDLKTKLLVSPQSRNGWLSF-----QELFQFASEEHSC 215
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALlitpaWEQEPDAPAILAR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 216 VETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYwLDLKSSDIIWNMS----DTGWVKAAIGSVfsswLCGAC 291
Cdd:PRK13295 192 LRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDVILMASpmahQTGFMYGLMMPV----MLGAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VFVH------RMAQFDTDTFldtlttypIT-TLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGL 364
Cdd:PRK13295 267 AVLQdiwdpaRAAELIRTEG--------VTfTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 365 DLYEGYGQTEVGMICANQKGQEIKPGSMGKGM-LP-YDVQIIDENGNVLPPGKEGEIALRLkptrpfCF-FSKYVDNPQK 441
Cdd:PRK13295 339 KIVSAWGMTENGAVTLTKLDDPDERASTTDGCpLPgVEVRVVDADGAPLPAGQIGRLQVRG------CSnFGGYLKRPQL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 442 TAATIRGdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLa 521
Cdd:PRK13295 413 NGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVP- 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 114643324 522 APFKSYNPEKLTLELQDHvkKSTAPYkYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK13295 491 RPGQSLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
84-579 |
9.02e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.25 E-value: 9.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKwSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:PRK12406 8 GDRRR-SFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVA--------SEEVAPAVESIVLECP-DLKTKLLVSPQSR---------NGWLSfqelfQFASEEHSCVEtgsqEPMT 225
Cdd:PRK12406 86 VLIAhadllhglASALPAGVTVLSVPTPpEIAAAYRISPALLtppagaidwEGWLA-----QQEPYDGPPVP----QPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPK------------MAQHSQSSLGIGFTLCGRYWLdlkssdiiwnmsdTGWVKAAIGSVF---SSWLCGA 290
Cdd:PRK12406 157 MIYTSGTTGHPKgvrraaptpeqaAAAEQMRALIYGLKPGIRALL-------------TGPLYHSAPNAYglrAGRLGGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 291 CVFvhrMAQFDTDTFLDTLTTYPITTLCSPPTVY-RMLvqkDL-----KRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGL 364
Cdd:PRK12406 224 LVL---QPRFDPEELLQLIERHRITHMHMVPTMFiRLL---KLpeevrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 365 DLYEGYGQTEVGMIC-ANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFcffsKYVDNPQKTA 443
Cdd:PRK12406 298 VIYEYYGSTESGAVTfATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDF----TYHNKPEKRA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 444 ATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAfVVLAAP 523
Cdd:PRK12406 374 EIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMA-VVEPQP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 114643324 524 FKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRG 579
Cdd:PRK12406 453 GATLDEA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWAN 504
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
227-573 |
2.07e-42 |
|
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: 156.10 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 227 YF-TSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMA----QFD 301
Cdd:cd05944 7 YFhTGGTTGTPKLAQHTHSNE-VYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAgyrnPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 TDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRyKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICA- 380
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 381 NQKGQEIKPGSMGKGMlPYD---VQIIDENGNVL---PPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTG 454
Cdd:cd05944 165 NPPDGPKRPGSVGLRL-PYArvrIKVLDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 455 DRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEKLTL 534
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL-KPGAVVEEEELLA 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 114643324 535 ELQDHVKKSTApykYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd05944 318 WARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-575 |
2.12e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 160.36 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 87 VKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMpgTIQlTA---KDILYRLRASKAK 163
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TIN-PAyrlSELEYALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASE------------EVAP--------AVESIVLecPDLKTKLLVSPQSRNGWLSFQELFQFASEEHS--CVETGSQ 221
Cdd:PRK08315 118 ALIAADgfkdsdyvamlyELAPelatcepgQLQSARL--PELRRVIFLGDEKHPGMLNFDELLALGRAVDDaeLAARQAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 ----EPMTIYFTSGTTGFPKmaqhsqsslgiGFTLCGRywldlkssdiiwNMSDTG-WVKAAI----------------- 279
Cdd:PRK08315 196 ldpdDPINIQYTSGTTGFPK-----------GATLTHR------------NILNNGyFIGEAMklteedrlcipvplyhc 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 280 -GSVFSSWLC---GAC-VFvhrMAQFDTdtfldtlttyPITTL-------CSP----PTVY-RMLVQKDLKRYKFKSLRh 342
Cdd:PRK08315 253 fGMVLGNLACvthGATmVY---PGEGFD----------PLATLaaveeerCTAlygvPTMFiAELDHPDFARFDLSSLR- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 343 clTG---GEPLNPEVLEqwRAQTGLDLYE---GYGQTE---VGMICANQKGQEIKPGSMGKGMLPYDVQIID-ENGNVLP 412
Cdd:PRK08315 319 --TGimaGSPCPIEVMK--RVIDKMHMSEvtiAYGMTEtspVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDpETGETVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 413 PGKEGEIAlrlkpTRPFCFFSKYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESAL 491
Cdd:PRK08315 395 RGEQGELC-----TRGYSVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 492 IEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNV 571
Cdd:PRK08315 470 YTHPKIQDVQVVGVPDEKYGEEVCAWIIL-RPGATLTEE----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFK 544
|
....
gi 114643324 572 LRDQ 575
Cdd:PRK08315 545 MREM 548
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
90-574 |
1.17e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 158.12 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EVAPAVESIVLECP----------DL--------------KTKLLVSPQSRNGWLSFQELFQFASEeHScVETGSQEPMT 225
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgDMlgfpkaalvnfvvkYVKKLVPEYRINGAIRFREALALGRK-HS-MPTLQIEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYF---TSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDI--------------IWNMSDTGWVKAAIGSvfsswlC 288
Cdd:PRK08751 210 IAFlqyTGGTTGVAKGAMLTHRNL-VANMQQAHQWLAGTGKLEegcevvitalplyhIFALTANGLVFMKIGG------C 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 GACV--------FVHRMAQfdtdtfldtlttYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLNPEVLEQWR 359
Cdd:PRK08751 283 NHLIsnprdmpgFVKELKK------------TRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDN 438
Cdd:PRK08751 351 QVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQ----VMKGYWKR 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 439 PQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAF 517
Cdd:PRK08751 426 PEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVV 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 114643324 518 VVLAAPfksynpeKLTLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK08751 506 IVKKDP-------ALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-569 |
2.31e-41 |
|
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: 152.27 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPK--MAQHSQS-SLGIGFTLCGrywlDLKSSD---IIWNMSDTGWVKAAIgsvFSSWLCGACVFVHrmAQ 299
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQTlRAAAAWADCA----DLTEDDrylIINPFFHTFGYKAGI---VACLLTGATVVPV--AV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 300 FDTDTFLDTLTTYPITTLCSPPTVYR-MLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLD-LYEGYGQTEVGM 377
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 378 --ICANQKGQEIKPGSMGKGMLPYDVQIIDEngnvlppgkeGEIALRlkptrPFCFFSKYVDNPQKTAATIRGDFYV-TG 454
Cdd:cd17638 156 atMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVR-----GYNVMQGYLDDPEATAEAIDADGWLhTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 455 DRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfksynpekLTL 534
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG--------VTL 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 114643324 535 ELQDHV---KKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd17638 293 TEEDVIawcRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
110-573 |
4.30e-41 |
|
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: 154.52 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAVILPPIPEW-WL---VNVACIRTGIIFMPGTIQLTAKDILYRlraskakcivaseeVAPAVESIVLECPDL 185
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRYL--------------VADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 186 KTKL-LVSPQSRNG--WLSFQELfqfASEEHSC--VETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYwLDL 260
Cdd:cd05922 80 ADRLrDALPASPDPgtVLDADGI---RAARASApaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY-LGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 261 KSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRMAqFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSL 340
Cdd:cd05922 156 TADDRALTVLPLSY-DYGLSVLNTHLLRGATLVLTNDG-VLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 341 RHCLTGGEPLNPEVLEQWR-AQTGLDLYEGYGQTEVGMICANQKGQEI--KPGSMGKGMLPYDVQIIDENGNVLPPGKEG 417
Cdd:cd05922 234 RYLTQAGGRLPQETIARLReLLPGAQVYVMYGQTEATRRMTYLPPERIleKPGSIGLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 418 EIAlrlkPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAV 497
Cdd:cd05922 314 EIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114643324 498 VESAVVSSPDQIrGEVVKAFVVLaapfksynPEKLTL-ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd05922 390 IEAAAVGLPDPL-GEKLALFVTA--------PDKIDPkDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
222-574 |
1.85e-40 |
|
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: 149.79 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSL---------GIGFTLCGRYWLDLKSSDIiwnmsdtgwvkAAIGSVFSSWLCGACV 292
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLlasaaglhsRLGFGGGDSWLLSLPLYHV-----------GGLAILVRSLLAGAEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 FVHRMAQFDTDTFLDtlttYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQtGLDLYEGYGQ 372
Cdd:cd17630 70 VLLERNQALAEDLAP----PGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 373 TE-VGMICANQKGqEIKPGSMGKgMLPYdVQI-IDENGNVLPPGKegeialrlkptrpfCFFSKYVDNPQKTAATIRGDF 450
Cdd:cd17630 145 TEtASQVATKRPD-GFGRGGVGV-LLPG-RELrIVEDGEIWVGGA--------------SLAMGYLRGQLVPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YvTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlaapfksYNPE 530
Cdd:cd17630 208 T-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV-------GRGP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 114643324 531 KLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-503 |
5.53e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 154.10 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWVNGkGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:COG1022 23 RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAK-CIVASEEVAPAVESIVLECPDLKTKLLVSP---QSRNGWLSFQELFQFASE-------EHSCVET 218
Cdd:COG1022 101 AEEVAYILNDSGAKvLFVEDQEQLDKLLEVRDELPSLRHIVVLDPrglRDDPRLLSLDELLALGREvadpaelEARRAAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 219 GSQEPMTIYFTSGTTGFPKMAQHSQSSL---------GIGF-----TLC--------GRYWL------------------ 258
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLlsnaralleRLPLgpgdrTLSflplahvfERTVSyyalaagatvafaespdt 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 259 ---DLKS-----------------SDIIWNMSDTGWVKAAIgsvFSsWLCGACVFVHRMAQFDTDTFLDTLTTYPIttlc 318
Cdd:COG1022 261 laeDLREvkptfmlavprvwekvyAGIQAKAEEAGGLKRKL---FR-WALAVGRRYARARLAGKSPSLLLRLKHAL---- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 319 spptvYRMLVQKDLKRyKFKS-LRHCLTGGEPLNPEVLEQWRAqTGLDLYEGYGQTEV-GMICANQKGqEIKPGSMGKGM 396
Cdd:COG1022 333 -----ADKLVFSKLRE-ALGGrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 397 LPYDVQIidengnvlppGKEGEIALRlKPtrpfCFFSKYVDNPQKTAATIRGD--FYvTGDRGVMDSDGYFWFVGRADDV 474
Cdd:COG1022 405 PGVEVKI----------AEDGEILVR-GP----NVMKGYYKNPEATAEAFDADgwLH-TGDIGELDEDGFLRITGRKKDL 468
|
490 500 510
....*....|....*....|....*....|
gi 114643324 475 II-SSGYRIGPFEVESALIEHPaVVESAVV 503
Cdd:COG1022 469 IVtSGGKNVAPQPIENALKASP-LIEQAVV 497
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-574 |
9.67e-39 |
|
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: 149.60 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCI 165
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 166 VASEEVAPAVESIVLECPDLKTKLLVSpqSRNGWLSFQELFQFASE---------EHSCVETGSQEPMT-IYFTSGTTGF 235
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILD--SKEDYKGYQCLYTFITQnlppgfneyDFKPPSFDRDEQVAlIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 236 PKMAQHSQSSLGIGFTLCgrywldlKSSDIIWNMSDTGWVKAAIG--------SVFSSWLCGA-CVFVHRMAQFDTDTFL 306
Cdd:cd17642 199 PKGVQLTHKNIVARFSHA-------RDPIFGNQIIPDTAILTVIPfhhgfgmfTTLGYLICGFrVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 307 DTlttYPITTLCSPPTVYRMLVQKDL-KRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLD-LYEGYGQTEVGMICANQKG 384
Cdd:cd17642 272 QD---YKVQSALLVPTLFAFFAKSTLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIalrlkptrpfCF-----FSKYVDNPQKTAATIRGDFYV-TGDRG 457
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGEL----------CVkgpmiMKGYVNNPEATKALIDKDGWLhSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 458 VMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfKSYNPEKltlELQ 537
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEA--GKTMTEK---EVM 493
|
490 500 510
....*....|....*....|....*....|....*...
gi 114643324 538 DHVKKSTAPYKYPR-KVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd17642 494 DYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-573 |
1.71e-38 |
|
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: 147.13 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 217 ETGSQEPMTIYfTSGTTGFPK--------MAQHSQSSLGIgftlcgrywLDLKSSDIIWNMSDTGwVKAAIGSVFSSWLC 288
Cdd:cd17649 91 HHPRQLAYVIY-TSGSTGTPKgvavshgpLAAHCQATAER---------YGLTPGDRELQFASFN-FDGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 GACVFVHRMAQ-FDTDTFLDTLTTYPITTLCSPPTVYRMLVQ--KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRaQTGLD 365
Cdd:cd17649 160 GACVVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 366 LYEGYGQTE---VGMICANQKGQEIKPGSM--GKGMLPYDVQIIDENGNVLPPGKEGEIALRLKptrpfCFFSKYVDNPQ 440
Cdd:cd17649 239 LFNAYGPTEatvTPLVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 441 KTAATIRGD--------FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGE 512
Cdd:cd17649 314 LTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQ 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 513 VVkAFVVLAAPFKSynpEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd17649 394 LV-AYVVLRAAAAQ---PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
84-572 |
2.71e-38 |
|
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: 146.59 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASEevapavesivlecPDlktkllvspqsrngwlsfqelfqfaseehscvetgsqEPMTIYFTSGTTGFPKMAQHSQ 243
Cdd:cd05907 80 ALFVED-------------PD-------------------------------------DLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGFTLCGRYwLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACV-FVHRMAQFDTDTFLDTlttyPiTTLCSPPT 322
Cdd:cd05907 110 RNILSNALALAER-LPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIyFASSAETLLDDLSEVR----P-TVFLAVPR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 323 VYRMLVQK-------DLKRYKFK-----SLRHCLTGGEPLNPEVLEQWRAqTGLDLYEGYGQTEVGMICANQKGQEIKPG 390
Cdd:cd05907 184 VWEKVYAAikvkavpGLKRKLFDlavggRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 391 SMGKGMLPYDVQIidengnvlppGKEGEIALRLKPTrpfcfFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVG 469
Cdd:cd05907 263 TVGKPLPGVEVRI----------ADDGEILVRGPNV-----MLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHITG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 470 RADDVII-SSGYRIGPFEVESALIEHPAVVESAVVSspDQiRGEVVkAFVVLAAPF-----KSYNPEKLTL--------- 534
Cdd:cd05907 328 RKKDLIItSGGKNISPEPIENALKASPLISQAVVIG--DG-RPFLV-ALIVPDPEAleawaEEHGIAYTDVaelaanpav 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 114643324 535 --ELQDHVK---KSTAPYKYPRKVEFVQElPKTI-------TGKIKRNVL 572
Cdd:cd05907 404 raEIEAAVEaanARLSRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
70-573 |
2.81e-38 |
|
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: 147.49 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:cd17651 7 RTPDAPALVA-----EGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEVAPAVEsivlecpdlktkllvsPQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFT 229
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELA----------------VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 230 SGTTGFPKMAQHSQSSLGigfTLCGryWLD----LKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRMAQFDTDTF 305
Cdd:cd17651 145 SGSTGRPKGVVMPHRSLA---NLVA--WQArassLGPGARTLQFAGLGF-DVSVQEIFSTLCAGATLVLPPEEVRTDPPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 306 -LDTLTTYPITTLCSPPTVYRMLVQkDLKRYKFKS--LRHCLTGGEPL--NPEVLEQWRAQTGLDLYEGYGQTEVGMICA 380
Cdd:cd17651 219 lAAWLDEQRISRVFLPTVALRALAE-HGRPLGVRLaaLRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTETHVVTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 381 NQKGQEIK----PGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAATIrgdf 450
Cdd:cd17651 298 LSLPGDPAawpaPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIggaglaRGYLNRPELTAERFVPDPFVPGARM---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlAAPFKSYNPE 530
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV-GDPEAPVDAA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 114643324 531 KLTLELQDHVkkstAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:cd17651 453 ELRAALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
70-569 |
4.10e-38 |
|
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: 146.24 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:cd05945 3 ANPDRPAVVE-----GGRTLTYRELKERADALAAALAS-LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEvapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqEPMTIYFT 229
Cdd:cd05945 77 AERIREILDAAKPALLIADGD---------------------------------------------------DNAYIIFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 230 SGTTGFPKMAQHSQSSLgIGFT--LCGRYwlDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVF-VHRMAQFDTDTFL 306
Cdd:cd05945 106 SGSTGRPKGVQISHDNL-VSFTnwMLSDF--PLGPGDVFLNQAPFSF-DLSVMDLYPALASGATLVpVPRDATADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 307 DTLTTYPITTLCSPPTVYRMLVQ-KDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQT-GLDLYEGYGQTEVGMICAnqkG 384
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVT---Y 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGSMGK-GMLPY-------DVQIIDENGNVLPPGKEGEIALRLKptrpfCFFSKYVDNPQKTAATIRGDF----YV 452
Cdd:cd05945 259 IEVTPEVLDGyDRLPIgyakpgaKLVILDEDGRPVPPGEKGELVISGP-----SVSKGYLNNPEKTAAAFFPDEgqraYR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 453 TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFksynPEKL 532
Cdd:cd05945 334 TGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA----EAGL 409
|
490 500 510
....*....|....*....|....*....|....*..
gi 114643324 533 TLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd05945 410 TKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
110-575 |
2.45e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.49 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVapavesivleCPDLKTKL 189
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL----------RDRFQPSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 190 LVSPQsrngwlsfqELFQFASEehscVETGSQEPMT------IYFTSGTTGFPKMAQHSQSSLgigFT----LCgRYWLD 259
Cdd:PRK06060 121 VAEAA---------ELMSEAAR----VAPGGYEPMGgdalayATYTSGTTGPPKAAIHRHADP---LTfvdaMC-RKALR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 260 LKSSDI---------IWNMSDTGWVKAAIGS--VFSSWLCGACVFVHRMAQFDTDTFLDTLTTYP-ITTLCSPPTvyrml 327
Cdd:PRK06060 184 LTPEDTglcsarmyfAYGLGNSVWFPLATGGsaVINSAPVTPEAAAILSARFGPSVLYGVPNFFArVIDSCSPDS----- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 328 vqkdlkrykFKSLRHCLTGGEPLNPEVLEQW-RAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDE 406
Cdd:PRK06060 259 ---------FRSLRCVVSAGEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 407 NGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFE 486
Cdd:PRK06060 330 DGTTAGPGVEGDLWVR-GPA----IAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 487 VESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGK 566
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATS--GATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGK 480
|
....*....
gi 114643324 567 IKRNVLRDQ 575
Cdd:PRK06060 481 LVRGALRKQ 489
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
80-575 |
1.06e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 143.97 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 80 VNGKGdevkWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRA 159
Cdd:PLN02330 51 VTGKA----VTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 160 SKAKCIVASEEVAPAVESivLECPdlktKLLVSPQSRNGWLSFQELFQFASEehsCVETGSQEPM------TIYFTSGTT 233
Cdd:PLN02330 126 AGAKLIVTNDTNYGKVKG--LGLP----VIVLGEEKIEGAVNWKELLEAADR---AGDTSDNEEIlqtdlcALPFSSGTT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 234 GFPK--MAQHSQ------SSL-GIGFTLCGRY-WLDLKSSDIIWNMsdTGWVKAAI---GSVFSSWLCGACVFVHRMAQF 300
Cdd:PLN02330 197 GISKgvMLTHRNlvanlcSSLfSVGPEMIGQVvTLGLIPFFHIYGI--TGICCATLrnkGKVVVMSRFELRTFLNALITQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 301 DTDTFldtlttyPITtlcsPPTVYRM----LVQK-DLKRYKFKSLrhcLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQTE 374
Cdd:PLN02330 275 EVSFA-------PIV----PPIILNLvknpIVEEfDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMICAN----QKGQEI-KPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALRLKptrpfCFFSKYVDNPQKTAATIRG 448
Cdd:PLN02330 341 HSCITLThgdpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 DFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfksy 527
Cdd:PLN02330 416 DGWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI------- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 114643324 528 NPEKLTLE--LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PLN02330 489 NPKAKESEedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
87-574 |
1.14e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 143.81 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 87 VKWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIV 166
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 167 ASEEVAPAVESIvleCPDLKTKLLVSPQ------SRNGWL---------------------SF-QELFQFASEEHSCVET 218
Cdd:PRK12492 128 YLNMFGKLVQEV---LPDTGIEYLIEAKmgdllpAAKGWLvntvvdkvkkmvpayhlpqavPFkQALRQGRGLSLKPVPV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 219 GSQEPMTIYFTSGTTGFPK-------------------MAQHSQSSLGI------------------GFTL-CGRYWLDL 260
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKgamlthgnlvanmlqvracLSQLGPDGQPLmkegqevmiaplplyhiyAFTAnCMCMMVSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 261 KSSDIIWNMSDT-GWVKAAIGSVFSSWLCGACVFVHRMAqfdtdtfldtlttYPittlcspptvyrmlvqkDLKRYKFKS 339
Cdd:PRK12492 285 NHNVLITNPRDIpGFIKELGKWRFSALLGLNTLFVALMD-------------HP-----------------GFKDLDFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGE 418
Cdd:PRK12492 335 LKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 419 IALRlKPTrpfcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAV 497
Cdd:PRK12492 415 LCIK-GPQ----VMKGYWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114643324 498 VESAVVSSPDQIRGEVVKAFVVLAAPFKSYNpekltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK12492 490 ANCAAIGVPDERSGEAVKLFVVARDPGLSVE------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
70-572 |
4.03e-36 |
|
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: 141.18 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWvngkGDEVkWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:cd12117 9 RTPDAVAVVY----GDRS-LTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVASEEVAPAVesivlecPDLKTKLLVSPQSRngwlsfqelFQFASEEHSCVETGSqePMTIYFT 229
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRA-------GGLEVAVVIDEALD---------AGPAGNPAVPVSPDD--LAYVMYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 230 SGTTGFPK--MAQHSqsslGIGFTLCGRYWLDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVH---------RMA 298
Cdd:cd12117 145 SGSTGRPKgvAVTHR----GVVRLVKNTNYVTLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLApkgtlldpdALG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 299 QFDTDTFldtlttypITTLCSPPTVYRMLVQKDLKRykFKSLRHCLTGGEPLNPEVLEQWRAQT-GLDLYEGYGQTEvGM 377
Cdd:cd12117 220 ALIAEEG--------VTVLWLTAALFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTE-NT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 378 ICANQkgQEIKPGSMGKGMLPY-------DVQIIDENGNVLPPGKEGEI-------ALrlkptrpfcffsKYVDNPQKTA 443
Cdd:cd12117 289 TFTTS--HVVTELDEVAGSIPIgrpiantRVYVLDEDGRPVPPGVPGELyvggdglAL------------GYLNRPALTA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 444 A-------TIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKA 516
Cdd:cd12117 355 ErfvadpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 114643324 517 FVVLAAPFksyNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd12117 435 YVVAEGAL---DAA----ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
110-572 |
4.28e-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: 141.11 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAkCIVASEEVAPAVESIVLECPDLktkL 189
Cdd:cd05923 49 GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM-TAAVIAVDAQVMDAIFQSGVRV---L 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 190 LVSPQSRNGWL-SFQELFQFASEEhscvetgSQEPMTIYFTSGTTGFPK---------------MAQHSQSSLGIGFTLC 253
Cdd:cd05923 125 ALSDLVGLGEPeSAGPLIEDPPRE-------PEQPAFVFYTSGTTGLPKgavipqraaesrvlfMSTQAGLRHGRHNVVL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 254 GRYWLdlkssdiiwnmsdtgwvKAAIGsVFSswlcgacVFVHRMA---------QFDTDTFLDTLTTYPITTLCSPPTVY 324
Cdd:cd05923 198 GLMPL-----------------YHVIG-FFA-------VLVAALAldgtyvvveEFDPADALKLIEQERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 325 RMLVQKDLKR-YKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQkgqEIKPGSMGKGMLPYDVQI 403
Cdd:cd05923 253 DALAAAAEFAgLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMR---DARTGTEMRPGFFSEVRI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 404 IDENGNV---LPPGKEGEIALRLKPTRPFcffSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGY 480
Cdd:cd05923 330 VRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 481 RIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfksyNPEKLTLELQDHVKKST--APYKYPRKVEFVQE 558
Cdd:cd05923 407 NIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVP-------REGTLSADELDQFCRASelADFKRPRRYFFLDE 479
|
490
....*....|....
gi 114643324 559 LPKTITGKIKRNVL 572
Cdd:cd05923 480 LPKNAMNKVLRRQL 493
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
70-580 |
5.38e-35 |
|
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: 141.53 E-value: 5.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWwLVNV-ACIRTGIIFMPgtiqL 148
Cdd:COG1020 488 RTPDAVAVVF-----GDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVP----L 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 149 takDILY---RLRA----SKAKCIVASEEVAPAVesivlecPDLKTKLLVspqsrngwLSFQELFQFASEEHScVETGSQ 221
Cdd:COG1020 557 ---DPAYpaeRLAYmledAGARLVLTQSALAARL-------PELGVPVLA--------LDALALAAEPATNPP-VPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDII---WNMS-DtgwvkAAIGSVFSSWLCGACV----- 292
Cdd:COG1020 618 DLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRYGLGPGDRVlqfASLSfD-----ASVWEIFGALLSGATLvlapp 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 --------FVHRMAQfdtdtfldtlttYPITTLCSPPTVYRMLVQKDLKRykFKSLRHCLTGGEPLNPEVLEQWRAQT-G 363
Cdd:COG1020 692 earrdpaaLAELLAR------------HRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpG 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 364 LDLYEGYGQTEVGmICANqkGQEIKPGSMGKGMLPY-------DVQIIDENGNVLPPGKEGEIAL------Rlkptrpfc 430
Cdd:COG1020 758 ARLVNLYGPTETT-VDST--YYEVTPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELYIggaglaR-------- 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 431 ffsKYVDNPQKTAA-------TIRGD-FYVTGDRGVMDSDGYFWFVGRADD-VIIsSGYRIGPFEVESALIEHPAVVESA 501
Cdd:COG1020 827 ---GYLNRPELTAErfvadpfGFPGArLYRTGDLARWLPDGNLEFLGRADDqVKI-RGFRIELGEIEAALLQHPGVREAV 902
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114643324 502 VVSSPDQIRGEVVKAFVVLAAPfksynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:COG1020 903 VVAREDAPGDKRLVAYVVPEAG-----AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
99-574 |
1.43e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 138.23 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 99 RKAANMLTkpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESI 178
Cdd:PLN03102 51 RLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 179 VLECPDLKTKL------------LVSPQSRNgwLSFQELFQFASEEHSCVET-----GSQEPMTIYFTSGTTGFPKmaqh 241
Cdd:PLN03102 129 LHLLSSEDSNLnlpvifiheidfPKRPSSEE--LDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPK---- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 242 sqsslGIGFTLCGRYwLDLKSSDIIWNMSD-------------TGWV----KAAIGSVfsswlcGACvfvhrMAQFDTDT 304
Cdd:PLN03102 203 -----GVVISHRGAY-LSTLSAIIGWEMGTcpvylwtlpmfhcNGWTftwgTAARGGT------SVC-----MRHVTAPE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 305 FLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLR-HCLTGGEPlNPEVLEQWRAQTGLDLYEGYGQTEVG---MICA 380
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATgpvLFCE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 381 NQ-------KGQEI----KPGSMGKGMLPYDVQIIDENGNVLPPGKE-GEIALRLKptrpfCFFSKYVDNPQKTAATIRG 448
Cdd:PLN03102 345 WQdewnrlpENQQMelkaRQGVSILGLADVDVKNKETQESVPRDGKTmGEIVIKGS-----SIMKGYLKNPKATSEAFKH 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 DFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYN 528
Cdd:PLN03102 420 GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKE 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 114643324 529 PEKLTL-----ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PLN03102 500 DRVDKLvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
221-569 |
5.91e-34 |
|
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: 132.00 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 221 QEPMTIYFTSGTTGFPKMAQHSQSSLgigFTLCgrywLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVF-----VH 295
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTF---FAVP----DILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhgglcVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 RMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQ--KDLKRYKfKSLRHCLTGGE-PLNPEV-LEQWRAQTglDLYEGYG 371
Cdd:cd17635 74 GGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSelKSANATV-PSLRLIGYGGSrAIAADVrFIEATGLT--NTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 372 QTEVGMICANQKGQEIKP-GSMGKGMLPYDVQIIDENGNVLPPGKEGEIALrlKPTRpfcFFSKYVDNPQKTAATIRGDF 450
Cdd:cd17635 151 LSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPA---NMLGYWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksYNPE 530
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA----ELDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 114643324 531 KLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd17635 302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
66-572 |
1.47e-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: 133.94 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGT 145
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIV--ASEEVAPAVESIVLECPDLktkllvspqsrngwlsfqelfQFASEEHS--CVETGSQ 221
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLttADLAARLPAGGDVALLGDE---------------------ALAAPPATppLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPK--MAQHSqsslGIG---FTLCGRYWLDlkssdiiwnMSDTGWVKAAIGSVFSSW------LCGA 290
Cdd:cd17646 139 NLAYVIYTSGSTGRPKgvMVTHA----GIVnrlLWMQDEYPLG---------PGDRVLQKTPLSFDVSVWelfwplVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 291 CVFV-----HRMAqfdtDTFLDTLTTYPITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLD 365
Cdd:cd17646 206 RLVVarpggHRDP----AYLAALIREHGVTTCHFVPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLALPGAE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 366 LYEGYGQTE--VGMI-CANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYV 436
Cdd:cd17646 281 LHNLYGPTEaaIDVThWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLggvqlaRGYLGRPALTAERFV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 437 DNPQKTAATIrgdfYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKA 516
Cdd:cd17646 361 PDPFGPGSRM----YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 114643324 517 FVVLAAPfksyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17646 437 YVVPAAG----AAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
223-569 |
1.79e-33 |
|
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: 130.22 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 223 PMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIwnmsdtgwvkAAIGSVFSSWLCGACVF-------VH 295
Cdd:cd17633 2 PFYIGFTSGTTGLPKAYYRSERSW-IESFVCNEDLFNISGEDAI----------LAPGPLSHSLFLYGAISalylggtFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 RMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLrhcLTGGEPLNPEVLEQWRAQT-GLDLYEGYGQTE 374
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGnvlppGKEGEIALRLKptrpfCFFSKYVDNPQKTAatirGDFYVTG 454
Cdd:cd17633 148 LSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE-----MVFSGYVRGGFSNP----DGWMSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 455 DRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaapfksynpEKLTL 534
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG---------DKLTY 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 114643324 535 -ELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd17633 285 kQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
97-567 |
3.40e-33 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 132.84 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 97 LSRKAANMlTKPcglqrGDRVAVILPPIPEWWLVNVACIRTGIIfmPGTIQLTA--KDILYRLRASKAKCIVAS------ 168
Cdd:cd05909 20 LARKLAKM-TKE-----GENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAglRELRACIKLAGIKTVLTSkqfiek 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 169 ------EEVAPAVESIVLEcpDLKTKLLVSPQSRNG----WLSFQELFQFAseehsCVETGSQEPMTIYFTSGTTGFPKM 238
Cdd:cd05909 92 lklhhlFDVEYDARIVYLE--DLRAKISKADKCKAFlagkFPPKWLLRIFG-----VAPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 239 AQHSQSSLGIGFTLCGRYwLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAqFDTDTFLDTLTTYPITTLC 318
Cdd:cd05909 165 VVLSHKNLLANVEQITAI-FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNP-LDYKKIPELIYDKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 319 SPPTVYRMLVqKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGK--- 394
Cdd:cd05909 243 GTPTFLRGYA-RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRplp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 395 GMlpyDVQIIDENGNV-LPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADD 473
Cdd:cd05909 322 GM---EVKIVSVETHEeVPIGEGGLLLVR-GPN----VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 474 VIISSGYRIGPFEVESALIEH-PAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynpekltlELQDHVKKSTAPYKY-PR 551
Cdd:cd05909 394 FAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPS--------SLNDILKNAGISNLAkPS 465
|
490
....*....|....*.
gi 114643324 552 KVEFVQELPKTITGKI 567
Cdd:cd05909 466 YIHQVEEIPLLGTGKP 481
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-569 |
4.79e-33 |
|
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: 131.80 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELgslSRKAANM--LTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASK 161
Cdd:cd05914 3 YGGEPLTYKDL---ADNIAKFalLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 162 AKCIVASEEvapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsQEPMTIYFTSGTTGFPKMAQH 241
Cdd:cd05914 80 AKAIFVSDE--------------------------------------------------DDVALINYTSGTTGNSKGVML 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 242 SQSSLGIGFTLCGRYWLdLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGA-CVFVHRMAqfdtDTFLDTLTTYPITTLCSP 320
Cdd:cd05914 110 TYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAhVVFLDKIP----SAKIIALAFAQVTPTLGV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 321 PTVYRM--------LVQKDLKRYKFK------------------------SLRHCLTGGEPLNPEVLEQWRaQTGLDLYE 368
Cdd:cd05914 185 PVPLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 369 GYGQTEVG-MICANQKGqEIKPGSMGKGMLPYDVQIIDENgnvlPPGKEGEIALRLKPTrpfcfFSKYVDNPQKTAA--T 445
Cdd:cd05914 264 GYGMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNV-----MKGYYKNPEATAEafD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 446 IRGDFYvTGDRGVMDSDGYFWFVGRADDVII-SSGYRIGPFEVESALIEHPAVVESAVVSSPDQirgEVVKAFVVLAAPF 524
Cdd:cd05914 334 KDGWFH-TGDLGKIDAEGYLYIRGRKKEMIVlSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK---LVALAYIDPDFLD 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 114643324 525 KSY-----NPEKLTLELQDHVKKSTAPYKYPRKVEFV-QELPKTITGKIKR 569
Cdd:cd05914 410 VKAlkqrnIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
70-575 |
6.88e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 132.56 E-value: 6.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPALwwvngKGDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLT 149
Cdd:PRK06164 22 ARPDAVAL-----IDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 AKDILYRLRASKAKCIVaseeVAPAVESIVL----------ECPDLKTKLLVSPQS-------RNGWLsfqELFQFASEE 212
Cdd:PRK06164 96 SHEVAHILGRGRARWLV----VWPGFKGIDFaailaavppdALPPLRAIAVVDDAAdatpapaPGARV---QLFALPDPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 213 HSCVETGSQE----PMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYwLDLKSSDIIWNMSDtgwVKAAIGsvFSSWLC 288
Cdd:PRK06164 169 PPAAAGERAAdpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARA-YGYDPGAVLLAALP---FCGVFG--FSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 G--ACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCltGGEPLNPEV--LEQWRAQTGL 364
Cdd:PRK06164 243 AlaGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPALgeLAALARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 365 DLYEGYGQTEVGMICANQK-----GQEIKPGsmGKGMLP-YDVQIID-ENGNVLPPGKEGEIALRlKPTRpfcfFSKYVD 437
Cdd:PRK06164 321 PLTGLYGSSEVQALVALQPatdpvSVRIEGG--GRPASPeARVRARDpQDGALLPDGESGEIEIR-APSL----MRGYLD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 438 NPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSpdQIRGEVVKA 516
Cdd:PRK06164 394 NPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPV 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114643324 517 FVVLAAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITG---KIKRNVLRDQ 575
Cdd:PRK06164 472 AFVIPTDGASPDEA----GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
320-565 |
1.56e-32 |
|
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: 127.80 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 PPTVYRMLVQKDLKRYKFKSLRHCLT--GGEPLNPEVLEQWRAQTGldlyeGYGQTEV-GMICANQKGQEIKpGSMGKGM 396
Cdd:cd17636 96 PPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG-----GYGQTEVmGLATFAALGGGAI-GGAGRPS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 397 LPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVII 476
Cdd:cd17636 170 PLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 477 SSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFV 556
Cdd:cd17636 245 SGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVL-KPGASVTEA----ELIEHCRARIASYKKPKSVEFA 319
|
....*....
gi 114643324 557 QELPKTITG 565
Cdd:cd17636 320 DALPRTAGG 328
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
64-572 |
2.09e-32 |
|
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: 130.53 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 64 QKEKTgerPANPALWWvngkGDEvKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMP 143
Cdd:cd17655 6 QAEKT---PDHTAVVF----EDQ-TLTYRELNERANQLARTL-REKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 144 GTIQLTAKDILYRLRASKAKCIVASEEVAPAVEsivlecpDLKTKLLVSPQsrngwlsfqelfQFASEEHSCVETGSQEP 223
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIA-------FIGLIDLLDED------------TIYHEESENLEPVSKSD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 MTIY--FTSGTTGFPK--MAQHSQ-SSLGIGFTlcGRYWLDLKS-----SDIIWNmsdtgwvkAAIGSVFSSWLCGACVF 293
Cdd:cd17655 138 DLAYviYTSGSTGKPKgvMIEHRGvVNLVEWAN--KVIYQGEHLrvalfASISFD--------ASVTEIFASLLSGNTLY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 VHRMAQFDTDTF-LDTLTTYPITTLCSPPTVYRMLVQKDLKryKFKSLRHCLTGGEPLNPEVLEQW--RAQTGLDLYEGY 370
Cdd:cd17655 208 IVRKETVLDGQAlTQYIRQNRITIIDLTPAHLKLLDAADDS--EGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 371 GQTE--VG-MI--CANQKGQEIKPgSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNP 439
Cdd:cd17655 286 GPTEttVDaSIyqYEPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRPELTAEKFVDDP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 440 QKTAatirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVV 519
Cdd:cd17655 365 FVPG----ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 520 LAAPFKsynpeklTLELQDHVKKSTAPYKYPRKveFVQ--ELPKTITGKIKRNVL 572
Cdd:cd17655 441 SEKELP-------VAQLREFLARELPDYMIPSY--FIKldEIPLTPNGKVDRKAL 486
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
72-566 |
2.67e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 130.78 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWvngkGDEVkWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:PRK07798 17 PDRVALVC----GDRR-LTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLV----SPQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIY 227
Cdd:PRK07798 91 ELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 228 fTSGTTGFPK--MAQHSQ---SSLGigftlcGRywlDLKSSDIIwnMSDTGWVKAAIGSVFSSWLCgACVFVHRMAQFDT 302
Cdd:PRK07798 171 -TGGTTGMPKgvMWRQEDifrVLLG------GR---DFATGEPI--EDEEELAKRAAAGPGMRRFP-APPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 303 DTFL---DTLTTYPITTLcSPPTVYR---------MLVQKD------------LKRYKFKSLRHCLTGGEPLNPEVLEQW 358
Cdd:PRK07798 238 FAALfsgQTVVLLPDVRF-DADEVWRtierekvnvITIVGDamarplldaleaRGPYDLSSLFAIASGGALFSPSVKEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 359 RAQ-TGLDLYEGYGQTEVG--MICANQKGQEiKPGSMGKGMLPyDVQIIDENGNVLPPG--------KEGEIALRlkptr 427
Cdd:PRK07798 317 LELlPNVVLTDSIGSSETGfgGSGTVAKGAV-HTGGPRFTIGP-RTVVLDEDGNPVEPGsgeigwiaRRGHIPLG----- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 428 pfcffskYVDNPQKTAAT---IRGDFY-VTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVV 503
Cdd:PRK07798 390 -------YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 504 SSPDQIRGEVVKAfVVLAAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGK 566
Cdd:PRK07798 463 GVPDERWGQEVVA-VVQLREGARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
337-574 |
3.56e-32 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 130.73 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 337 FKSLRHCLTGGEPLNPEVLEQW-RAQTGLDLYEGYGQTE---VGMICANQKgQEIKPGSMGKGMLPYDVQIID-ENGNVL 411
Cdd:PLN02574 318 LKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEstaVGTRGFNTE-KLSKYSSVGLLAPNMQAKVVDwSTGCLL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 412 PPGKEGEIALRlKPTrpfcFFSKYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESA 490
Cdd:PLN02574 397 PPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 491 LIEHPAVVESAVVSSPDQIRGEVVKAFVVlaapfkSYNPEKLTLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:PLN02574 472 LISHPEIIDAAVTAVPDKECGEIPVAFVV------RRQGSTLSQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
....*
gi 114643324 570 NVLRD 574
Cdd:PLN02574 546 RELKR 550
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
72-572 |
4.78e-32 |
|
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: 129.33 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALwwvngKGDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:cd12116 1 PDATAV-----RDDDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVASEEVAPAVESIVLecpdlkTKLLVSPQSRNGwlsfqelfqfaseeHSCVETGSQEPMTIY--FT 229
Cdd:cd12116 75 RLRYILEDAEPALVLTDDALPDRLPAGLP------VLLLALAAAAAA--------------PAAPRTPVSPDDLAYviYT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 230 SGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIgSVFSSWLCGA-CVFVHRMAQFDTDTFLDT 308
Cdd:cd12116 135 SGSTGRPKGVVVSHRNL-VNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGArVVIAPRETQRDPEALARL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 309 LTTYPITTLCSPPTVYRMLVQKDLKryKFKSLRhCLTGGEPLNPEVLEQWRAQTGlDLYEGYGQTE------VGMICAnq 382
Cdd:cd12116 213 IEAHSITVMQATPATWRMLLDAGWQ--GRAGLT-ALCGGEALPPDLAARLLSRVG-SLWNLYGPTEttiwstAARVTA-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 383 kgqEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAATirgDFYVTGDR 456
Cdd:cd12116 287 ---AAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIggdgvaQGYLGRPALTAERFVPDPFAGPGS---RLYRTGDL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 457 GVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVkAFVVLAAPfKSYNPEkltlEL 536
Cdd:cd12116 361 VRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG-AAPDAA----AL 434
|
490 500 510
....*....|....*....|....*....|....*.
gi 114643324 537 QDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd12116 435 RAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
56-575 |
8.77e-32 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 129.24 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQKektgeRPANPALWWVNgkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACI 135
Cdd:PRK05852 19 ADLVEVAATR-----LPEAPALVVTA---DRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 136 RTGIIFMPGTIQLTAKDILYRLRASKAKCIVA-----SEEVAPAVesivlecPDLKTKLLVSPQSRNGWLSFQELFQFAS 210
Cdd:PRK05852 90 RADLVVVPLDPALPIAEQRVRSQAAGARVVLIdadgpHDRAEPTT-------RWWPLTVNVGGDSGPSGGTLSVHLDAAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 211 EEHSCVET----GSQEPMtIYFTSGTTGFPKMAQHSQSSLGIGF-TLCGRYWLDLKSSDIIWNMSDTGwvKAAIGSVFSS 285
Cdd:PRK05852 163 EPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHANIASSVrAIITGYRLSPRDATVAVMPLYHG--HGLIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 286 WLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQK------DLKRYKFKSLRHCltgGEPLNPEVLEQWR 359
Cdd:PRK05852 240 LASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatepsGRKPAALRFIRSC---SAPLTAETAQALQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTGLDLYEGYGQTE----VGMICANQKGQEIKP----GSMGKGMLPyDVQIIDENGNVLPPGKEGEIALRlKPTrpfcF 431
Cdd:PRK05852 317 TEFAAPVVCAFGMTEathqVTTTQIEGIGQTENPvvstGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLR-GTT----V 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 432 FSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRG 511
Cdd:PRK05852 391 VRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYG 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114643324 512 EVVKAFVVlaaPFKSYNPEKltLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK05852 471 EAVAAVIV---PRESAPPTA--EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
87-575 |
3.19e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 128.04 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 87 VKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIV 166
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 167 ASEEVAPAVESIVLECPDLKTK------LLVSPQSRNGWLSFQE-LFQFASEEHSCVETGSQE-----------PMTIYF 228
Cdd:PLN02479 123 VDQEFFTLAEEALKILAEKKKSsfkpplLIVIGDPTCDPKSLQYaLGKGAIEYEKFLETGDPEfawkppadewqSIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 229 TSGTTGFPKmaqhsqsslGIGFTLCGRYWLDLkSSDIIWNMSD-------------TGWVkaaigsvfSSW----LCGAC 291
Cdd:PLN02479 203 TSGTTASPK---------GVVLHHRGAYLMAL-SNALIWGMNEgavylwtlpmfhcNGWC--------FTWtlaaLCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VFvhrMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQ--KDLKRYKFKSLRHCLTGGEPLNPEVLEQWrAQTGLDLYEG 369
Cdd:PLN02479 265 IC---LRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 370 YGQTEV---GMICA-----------NQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKE-GEIALRLKPTrpfcfFSK 434
Cdd:PLN02479 341 YGLSETygpSTVCAwkpewdslppeEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGKTmGEIVMRGNMV-----MKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 435 YVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVV 514
Cdd:PLN02479 416 YLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESP 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 515 KAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFvQELPKTITGKIKRNVLRDQ 575
Cdd:PLN02479 496 CAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
72-572 |
1.42e-30 |
|
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: 124.73 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAK 151
Cdd:cd17643 1 PEAVAVVD-----EDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 152 DILYRLRASKAKCIVaseevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscveTGSQEPMTIYFTSG 231
Cdd:cd17643 75 RIAFILADSGPSLLL---------------------------------------------------TDPDDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 232 TTGFPKMAQHSQSSLGIGFTLCGRyWLDLKSSDIiWnmsdtgWVKAAIGSVFSSW-LCGA------CVFVHRMAQFDTDT 304
Cdd:cd17643 104 STGRPKGVVVSHANVLALFAATQR-WFGFNEDDV-W------TLFHSYAFDFSVWeIWGAllhggrLVVVPYEVARSPED 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 305 FLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFK-SLRHCLTGGEPLNPEVLEQWRAQTGL---DLYEGYGQTEVG---- 376
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTvhvt 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 377 ---MICANQKGQEIKPgsMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPqKTAATIR 447
Cdd:cd17643 256 frpLDAADLPAAAASP--IGRPLPGLRVYVLDADGRPVPPGVVGELYVsgagvaRGYLGRPELTAERFVANP-FGGPGSR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 448 GdfYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksy 527
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD----- 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 114643324 528 NPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-573 |
1.64e-30 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 125.49 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 86 EVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGI-----IFMPGTIQLT--AKDILYRLR 158
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVapvnaLFSHQRSELNayASQIEPALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 159 -ASKAKCIVASEEVapaVESIVLECPDLKTKLLvspQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPK 237
Cdd:PRK10946 125 iADRQHALFSDDDF---LNTLVAEHSSLRVVLL---LNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 238 MA--QHS------QSSLGI-GFTLCGRYWLDLKSSDiiwN--MSDTGwvkaAIGsVFsswLCGACVFvhrMAQFdtdtfl 306
Cdd:PRK10946 199 LIprTHNdyyysvRRSVEIcGFTPQTRYLCALPAAH---NypMSSPG----ALG-VF---LAGGTVV---LAPD------ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 307 dtlttyPITTLC--------------SPPTVYRML--VQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGY 370
Cdd:PRK10946 259 ------PSATLCfpliekhqvnvtalVPPAVSLWLqaIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 371 GQTEvGMICANQ--KGQEIKPGSMGKGMLPYD-VQIIDENGNVLPPGKEGEIALRLKPTrpfcfFSKYVDNPQKTAATIR 447
Cdd:PRK10946 333 GMAE-GLVNYTRldDSDERIFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAFD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 448 GD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKS 526
Cdd:PRK10946 407 ANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKA 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 114643324 527 ynpekltLELQDHVK-KSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK10946 487 -------VQLRRFLReQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
204-578 |
1.77e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 125.52 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 204 ELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLG-IGFTLCGRYwlDLKSSDIIW--------NMSDTGW 274
Cdd:PRK13388 133 ELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGW 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 275 VkAAIGSvfsswlcGAcvfvhrmaqfdtdtfldtlttypitTLCSPPT--VYRMLvqKDLKRYKF-------KSLRHCLT 345
Cdd:PRK13388 211 A-PAVAS-------GA-------------------------AVALPAKfsASGFL--DDVRRYGAtyfnyvgKPLAYILA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 346 GGE-------PL--------NPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQeiKPGSMGK---GMLPYD------- 400
Cdd:PRK13388 256 TPErpddadnPLrvafgneaSPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGT--PPGSIGRgapGVAIYNpetltec 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 401 -VQIIDENGNVLPPGKE-GEIAlrlkPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISS 478
Cdd:PRK13388 334 aVARFDAHGALLNADEAiGELV----NTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 479 GYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfKSYNPEKLT--LELQDHVkkstAPYKYPRKVEFV 556
Cdd:PRK13388 410 GENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAafLAAQPDL----GTKAWPRYVRIA 484
|
410 420
....*....|....*....|..
gi 114643324 557 QELPKTITGKIKRNVLRDQEWR 578
Cdd:PRK13388 485 ADLPSTATNKVLKRELIAQGWA 506
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
85-572 |
1.00e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 123.18 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 85 DEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKC 164
Cdd:PRK13383 57 DDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHIST 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 165 IVASEE----VAPAVESIvlecpdlktkLLVSPQSrngwlsfqelfqfASEEHSCVETGSQEPMTI-YFTSGTTGFPK-- 237
Cdd:PRK13383 136 VVADNEfaerIAGADDAV----------AVIDPAT-------------AGAEESGGRPAVAAPGRIvLLTSGTTGKPKgv 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 238 -MAQHSQSSLGIGFTLCGRYWLDLKSSdiiWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITT 316
Cdd:PRK13383 193 pRAPQLRSAVGVWVTILDRTRLRTGSR---ISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 317 LCsPPTVYRMLVQKDLKRYK--FKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGmICANQKGQEIK--PGSM 392
Cdd:PRK13383 270 AV-PVVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG-IGALATPADLRdaPETV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 393 GKGMLPYDVQIIDENGNVLPPGKEGEIAL--RLKPTRpfcffskYVDNPQKtaATIRGdFYVTGDRGVMDSDGYFWFVGR 470
Cdd:PRK13383 348 GKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGK--AVVDG-MTSTGDMGYLDNAGRLFIVGR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 471 ADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlAAPFKSYNPEkltlELQDHVKKSTAPYKYP 550
Cdd:PRK13383 418 EDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVV-LHPGSGVDAA----QLRDYLKDRVSRFEQP 492
|
490 500
....*....|....*....|..
gi 114643324 551 RKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK13383 493 RDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
90-572 |
2.79e-29 |
|
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: 120.44 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE 169
Cdd:cd17652 14 TYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 170 EvapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqEPMTIYFTSGTTGFPK--MAQHSqsslG 247
Cdd:cd17652 93 D---------------------------------------------------NLAYVIYTSGSTGRPKgvVVTHR----G 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 248 I-GFTLCGRYWLDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGAC-VFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYR 325
Cdd:cd17652 118 LaNLAAAQIAAFDVGPGSRVLQFASPSF-DASVWELLMALLAGATlVLAPAEELLPGEPLADLLREHRITHVTLPPAALA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 326 MLVQKDLKrykfkSLRHCLTGGEPLNPEVLEQWraQTGLDLYEGYGQTEVgMICANQKGqeikPGSmGKGMLP------- 398
Cdd:cd17652 197 ALPPDDLP-----DLRTLVVAGEACPAELVDRW--APGRRMINAYGPTET-TVCATMAG----PLP-GGGVPPigrpvpg 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 399 YDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAAtirGDFYVTGDRGVMDSDGYFWFVGRAD 472
Cdd:cd17652 264 TRVYVLDARLRPVPPGVPGELYIagaglaRGYLNRPGLTAERFVADPFGAPG---SRMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 473 DVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlAAPFKSYNPEkltlELQDHVKKSTAPYKYPRK 552
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV-PAPGAAPTAA----ELRAHLAERLPGYMVPAA 415
|
490 500
....*....|....*....|
gi 114643324 553 VEFVQELPKTITGKIKRNVL 572
Cdd:cd17652 416 FVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
66-574 |
2.77e-28 |
|
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: 118.41 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALW-WvngKGDevkWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPewWLV--NVACIRTGIIFM 142
Cdd:cd05918 7 ERARSQPDAPAVCaW---DGS---LTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFEKSK--WAVvaMLAVLKAGGAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 143 PGTIQLTAKDILYRLRASKAKCIVASeevapavesivlecpdlktkllvSPQSrngwlsfqelfqfaseehscvetgsqe 222
Cdd:cd05918 78 PLDPSHPLQRLQEILQDTGAKVVLTS-----------------------SPSD--------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 223 PMTIYFTSGTTGFPK--MAQHSQSSLGI-------GFTLCGRyWLDLKS--SDiiwnmsdtgwvkAAIGSVFSSWLCGAC 291
Cdd:cd05918 108 AAYVIFTSGSTGKPKgvVIEHRALSTSAlahgralGLTSESR-VLQFASytFD------------VSILEIFTTLAAGGC 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VFV-------HRMAqfdtdtflDTLTTYPITTLCSPPTVYRMLVQKDlkrykFKSLRHCLTGGEPLNPEVLEQWraQTGL 364
Cdd:cd05918 175 LCIpseedrlNDLA--------GFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 365 DLYEGYGQTEVGMIC-ANQKGQEIKPGSMGKgmlPYDVQ--IID-ENGNVL-PPGKEGEIAL------Rlkptrpfcffs 433
Cdd:cd05918 240 RLINAYGPAECTIAAtVSPVVPSTDPRNIGR---PLGATcwVVDpDNHDRLvPIGAVGELLIegpilaR----------- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 434 KYVDNPQKTAA--------------TIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVE 499
Cdd:cd05918 306 GYLNDPEKTAAafiedpawlkqegsGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAK 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 500 SAVVS----SPDQIRGEVVkAFVVLA----------APFKSYNPEKLTL--ELQDHVKKSTAPYKYPRKVEFVQELPKTI 563
Cdd:cd05918 386 EVVVEvvkpKDGSSSPQLV-AFVVLDgsssgsgdgdSLFLEPSDEFRALvaELRSKLRQRLPSYMVPSVFLPLSHLPLTA 464
|
570
....*....|.
gi 114643324 564 TGKIKRNVLRD 574
Cdd:cd05918 465 SGKIDRRALRE 475
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-574 |
3.41e-28 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 117.41 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 80 VNGKGDEVkwSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRA 159
Cdd:cd17653 16 VESLGGSL--TYGELDAASNALANRL-LQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 160 SKAKcivaseevapavesivlecpdlktkLLVSPqsrngwlsfqelfqfaseehscveTGSQEPMTIYFTSGTTGFPK-- 237
Cdd:cd17653 93 SGAT-------------------------LLLTT------------------------DSPDDLAYIIFTSGSTGIPKgv 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 238 MAQHSQSSLGIGFTlcgRYWLDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDtlttypITTL 317
Cdd:cd17653 124 MVPHRGVLNYVSQP---PARLDVGPGSRVAQVLSIAF-DACIGEIFSTLCNGGTLVLADPSDPFAHVART------VDAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 318 CSPPTVYRMLvqkdlKRYKFKSLRHCLTGGEPLNPEVLEQWRAqtGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKGML 397
Cdd:cd17653 194 MSTPSILSTL-----SPQDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 398 PYDVQIIDENGNVLPPGKEGEIALR-LKPTRpfcffsKYVDNPQKTAATIRGD-------FYVTGDRGVMDSDGYFWFVG 469
Cdd:cd17653 267 NSTCYILDADLQPVPEGVVGEICISgVQVAR------GYLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 470 RADDVIISSGYRIGPFEVESALIEHPAVVESAVVSspdQIRGEVVkAFVVlaapfksynPEKLTLE-LQDHVKKSTAPYK 548
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI---VVNGRLV-AFVT---------PETVDVDgLRSELAKHLPSYA 407
|
490 500
....*....|....*....|....*.
gi 114643324 549 YPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:cd17653 408 VPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
226-572 |
1.74e-27 |
|
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: 115.61 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPK--MAQHsQSSLGIGFTLCGRYwlDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFV--------- 294
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAF-DVAAEEIYVTLLSGATLVLrpeemrssl 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 295 HRMAQFDTDTFldtlttypITTLCSPPTVYRMLVQKDLKRYK--FKSLRHCLTGGEPLNPEVLEQWRAQTG--LDLYEGY 370
Cdd:cd17644 187 EDFVQYIQQWQ--------LTVLSLPPAYWHLLVLELLLSTIdlPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 371 GQTE------VGMICANQKGQEIKPgSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDN 438
Cdd:cd17644 259 GPTEatiaatVCRLTQLTERNITSV-PIGRPIANTQVYILDENLQPVPVGVPGELHIggvglaRGYLNRPELTAEKFISH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 439 PQKTAATIRgdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFV 518
Cdd:cd17644 338 PFNSSESER--LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 114643324 519 VlaapfKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17644 416 V-----PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
74-578 |
9.66e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 114.01 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 74 NPALWWvngkGDEVkWSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIfmPGTIQLT---- 149
Cdd:PRK07867 19 DRGLYF----EDSF-TSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIV--PVGLNPTrrga 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 150 --AKDILY---RLRASKAKCIVASEEVAPAVESIVLECPDlktkllvspqsrngWlsFQELFQFASEEHSCVETGSQEPM 224
Cdd:PRK07867 92 alARDIAHadcQLVLTESAHAELLDGLDPGVRVINVDSPA--------------W--ADELAAHRDAEPPFRVADPDDLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 225 TIYFTSGTTGFPKMAQHSQSSLGI-GFTLCGRYwlDLKSSDIIW--------NMSDTGWVKAAIgsvfsswlCGACVFVH 295
Cdd:PRK07867 156 MLIFTSGTSGDPKAVRCTHRKVASaGVMLAQRF--GLGPDDVCYvsmplfhsNAVMAGWAVALA--------AGASIALR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 RmaqfdtdtfldtltTYPITTLCSpptvyrmlvqkDLKRYKF-------KSLRHCLTGGE-------PLN--------PE 353
Cdd:PRK07867 226 R--------------KFSASGFLP-----------DVRRYGAtyanyvgKPLSYVLATPErpddadnPLRivygnegaPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 354 VLEQWRAQTGLDLYEGYGQTEVGMICANQKGQeiKPGSMGKgmLPYDVQIID-ENGNVLPPGKE------------GEIA 420
Cdd:PRK07867 281 DIARFARRFGCVVVDGFGSTEGGVAITRTPDT--PPGALGP--LPPGVAIVDpDTGTECPPAEDadgrllnadeaiGELV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 421 LRLKPTRpfcfFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVES 500
Cdd:PRK07867 357 NTAGPGG----FEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 501 AVVSSPDQIRGEVVKAFVVLaAPFKSYNPEKLT--LELQDHVkkstAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWR 578
Cdd:PRK07867 433 AVYAVPDPVVGDQVMAALVL-APGAKFDPDAFAefLAAQPDL----GPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD 507
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-566 |
1.32e-26 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 103.01 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 486 EVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksyNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITG 565
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 114643324 566 K 566
Cdd:pfam13193 76 K 76
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
110-575 |
2.55e-26 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 113.36 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAvILPPIPEW---WLVNVACIrtGIIFMPgtiqltakdILYRLRASKAKciVASEEVAPAV----ESIVL-- 180
Cdd:PLN02860 53 GLRNGDVVA-IAALNSDLyleWLLAVACA--GGIVAP---------LNYRWSFEEAK--SAMLLVRPVMlvtdETCSSwy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 181 ------ECPDLKTKLLVSPQSRNGwlsFQELFQFASEEHSCVETGSQEPMT----------IYFTSGTTGFPKMAQHSQS 244
Cdd:PLN02860 119 eelqndRLPSLMWQVFLESPSSSV---FIFLNSFLTTEMLKQRALGTTELDyawapddavlICFTSGTTGRPKGVTISHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 245 SLGIGftlcgrywlDLKSSDIIWNMSDTGWVKAA-------IGSVFSSWLCGAC-VFVHRMaqfDTDTFLDTLTTYPITT 316
Cdd:PLN02860 196 ALIVQ---------SLAKIAIVGYGEDDVYLHTAplchiggLSSALAMLMVGAChVLLPKF---DAKAALQAIKQHNVTS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 317 LCSPPTVYRMLV---QKDLKRYKFKSLRHCLTGGEPLNPEVLEQW-----RAQtgldLYEGYGQTEV------------- 375
Cdd:PLN02860 264 MITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAkklfpNAK----LFSAYGMTEAcssltfmtlhdpt 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 376 --GMICANQKGQEIKPGSMGK------GMLPYDVQI---IDEngnvlpPGKEGEIAlrlkpTRPFCFFSKYVDNPQKTAA 444
Cdd:PLN02860 340 leSPKQTLQTVNQTKSSSVHQpqgvcvGKPAPHVELkigLDE------SSRVGRIL-----TRGPHVMLGYWGQNSETAS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 445 TIRGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAP 523
Cdd:PLN02860 409 VLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDG 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 524 FKSYNPEK------LTL---ELQDHV-KKSTAPYKYPRK-VEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PLN02860 489 WIWSDNEKenakknLTLsseTLRHHCrEKNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
220-572 |
3.26e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 113.30 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 220 SQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFtlcGRYWLDLKSSD---IIWNMSDTGWVkaAIGSVFSSWLCGACVFVhr 296
Cdd:PTZ00237 253 SSHPLYILYTSGTTGNSKAVVRSNGPHLVGL---KYYWRSIIEKDiptVVFSHSSIGWV--SFHGFLYGSLSLGNTFV-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 297 MAQFDTDTFLDTLTT-------YPITTLCSPPTVYRMLVQKD-----LK-RYKFKSLRHCLTGGEPLNPEVLEQWRAQTG 363
Cdd:PTZ00237 326 MFEGGIIKNKHIEDDlwntiekHKVTHTLTLPKTIRYLIKTDpeatiIRsKYDLSNLKEIWCGGEVIEESIPEYIENKLK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 364 LDLYEGYGQTEVGMICANQKGQEIKP-GSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLkPTRPfCFFSKYVDNPQ-- 440
Cdd:PTZ00237 406 IKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkf 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 441 KTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVL 520
Cdd:PTZ00237 484 KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 114643324 521 AAPFKSYNPE--KLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PTZ00237 564 KQDQSNQSIDlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
84-575 |
4.80e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.79 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKwSFRELGSLSRKAANMLTKPCGLQRgdRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:PRK07638 23 NDRVL-TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASEEVAPAVesivlecPDLKTKLLVSPQSRngwlsfqELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQ 243
Cdd:PRK07638 100 MIVTERYKLNDL-------PDEEGRVIEIDEWK-------RMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGFTlCGRYWLDLKSSDIIwnmsdtgwvkAAIGSVFSS-WLCGA--CVF----VHRMAQFDTDTFLDTLTTYPITT 316
Cdd:PRK07638 166 QSWLHSFD-CNVHDFHMKREDSV----------LIAGTLVHSlFLYGAisTLYvgqtVHLMRKFIPNQVLDKLETENISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 317 LCSPPTVYRMLVQkdLKRYKFKSLRhCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQTEVGMICANQKGQ-EIKPGSMGK 394
Cdd:PRK07638 235 MYTVPTMLESLYK--ENRVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASELSFVTALVDEEsERRPNSVGR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 395 GMLPYDVQIIDENGNVLPPGKEGEIALRlkptRPFcFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDV 474
Cdd:PRK07638 312 PFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 475 IISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKsynpekltlELQDHVKKSTAPYKYPRKVE 554
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQ---------QLKSFCLQRLSSFKIPKEWH 457
|
490 500
....*....|....*....|.
gi 114643324 555 FVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK07638 458 FVDEIPYTNSGKIARMEAKSW 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
110-573 |
2.52e-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: 109.83 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCI-VASEEVAPAVESIvlecpDLKTK 188
Cdd:cd05915 45 GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLlFDPNLLPLVEAIR-----GELKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 189 LLVSPQSRNGWLSFQELFQFASEEHSCVETGSQ-EPMTIYFTSGTTGFPKMAQHSQSSLGIGFT---------------- 251
Cdd:cd05915 120 VQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLaaslvdgtalsekdvv 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 252 LCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTdtfldtlttypittlcSPPTVYRMLVQKD 331
Cdd:cd05915 200 LPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG----------------VPTVWLALADYLE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 332 LKRYKFKSLRHCLTGGEPlNPEVLEQWRAQTGLDLYEGYGQTEV---GMICANQKGQEIKPGSMGKGMLPYD-------- 400
Cdd:cd05915 264 STGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEEEKLTLKAKTglpiplvr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 401 VQIIDENGNVLPpgKEGEiALRLKPTRPFCFFSKYVDNPQKT-AATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSG 479
Cdd:cd05915 343 LRVADEEGRPVP--KDGK-ALGEVQLKGPWITGGYYGNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 480 YRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPEKLTLELQDHVKKSTAPYKY-PRKVEFVQE 558
Cdd:cd05915 420 EWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------GEKPTPEELNEHLLKAGFAKWQlPDAYVFAEE 493
|
490
....*....|....*
gi 114643324 559 LPKTITGKIKRNVLR 573
Cdd:cd05915 494 IPRTSAGKFLKRALR 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
66-572 |
5.04e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALwwvngKGDEVKWSFRELGSLSRKAANMLtkpcgLQRG----DRVAVILPPIPEWWLVNVACIRTGIIF 141
Cdd:PRK12316 4559 ERARMTPDAVAV-----VFDEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 142 MPGTIQLTAKDILYRLRASKAKCIVASEEVAPAvesivLECPDLKTKLLVSPQSRngWLSFqelfqfaSEEHSCVETGSQ 221
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR-----LPIPDGLASLALDRDED--WEGF-------PAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGsVFSSWLCGACVFVHRMAQFD 301
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSL-VNHLHATGERYELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 TDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQ-WRAQTGLDLYEGYGQTEVGMICA 380
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 381 NQK-------GQEIKPgsMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAAtir 447
Cdd:PRK12316 4853 LWKardgdacGAAYMP--IGTPLGNRSGYVLDGQLNPLPVGVAGELYLggegvaRGYLERPALTAERFVPDPFGAPG--- 4927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 448 GDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVkAFVVLAAPFKSY 527
Cdd:PRK12316 4928 GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALAD 5006
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 114643324 528 NPEK---LTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12316 5007 ADEAqaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
330-566 |
1.36e-24 |
|
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: 105.54 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 330 KDLKRYKFKSLRHCLTGGEPLNPEVLEQW-RAQTGLDLYEGYGQTEVGMI-------CANQKGQEIKPGSmgkgmlpyDV 401
Cdd:cd05924 126 RDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVDAFGSSETGFTgsghsagSGPETGPFTRANP--------DT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 402 QIIDENGNVLPPGKEGE--IALR-LKPTrpfcffsKYVDNPQKTAATIR---GDFY-VTGDRGVMDSDGYFWFVGRADDV 474
Cdd:cd05924 198 VVLDDDGRVVPPGSGGVgwIARRgHIPL-------GYYGDEAKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 475 IISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFksynpeKLTL-ELQDHVKKSTAPYKYPRKV 553
Cdd:cd05924 271 INTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGA------GVDLeELREHCRTRIARYKLPKQV 344
|
250
....*....|...
gi 114643324 554 EFVQELPKTITGK 566
Cdd:cd05924 345 VFVDEIERSPAGK 357
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
203-572 |
1.53e-24 |
|
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: 106.63 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 203 QELFQFASEEHSC--VETGSQEPMTIYFTSGTTGFPK--MAQHSQSSLGIGFTL--CGRYWLD--LKSSDIIWNMSdtgw 274
Cdd:cd12115 85 PERLRFILEDAQArlVLTDPDDLAYVIYTSGSTGRPKgvAIEHRNAAAFLQWAAaaFSAEELAgvLASTSICFDLS---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 275 vkaaIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLttypITTLCSPPTVYRMLVQKDlkryKF-KSLRHCLTGGEPLNPE 353
Cdd:cd12115 161 ----VFELFGPLATGGKVVLADNVLALPDLPAAAE----VTLINTVPSAAAELLRHD----ALpASVRVVNLAGEPLPRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 354 VLEQWRAQTGLD-LYEGYGQTE------VGMICANQKGQEikpgSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL----- 421
Cdd:cd12115 229 LVQRLYARLQVErVVNLYGPSEdttystVAPVPPGASGEV----SIGRPLANTQAYVLDRALQPVPLGVPGELYIggagv 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 422 -RlkptrpfcffsKYVDNPQKTAATIRGD-------FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIE 493
Cdd:cd12115 305 aR-----------GYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRS 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114643324 494 HPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSynpekLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd12115 374 IPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-574 |
1.69e-24 |
|
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: 107.17 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 81 NGKGDEVKWSfrELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRAS 160
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 161 KAK-CIVASEEVAPAVESIVLEcpDLKTKLLVSPQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMA 239
Cdd:cd05932 78 ESKaLFVGKLDDWKAMAPGVPE--GLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 240 QHSQSSLG---------IGFTLCGRYWLDLKSSDIIWNMS-DTGW-------------------VKAAIGSVFSS----W 286
Cdd:cd05932 156 MLTFGSFAwaaqagiehIGTEENDRMLSYLPLAHVTERVFvEGGSlyggvlvafaesldtfvedVQRARPTLFFSvprlW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 287 LcgacVFVHRMAQFDTDTFldtlttypITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEqWRAQTGLDL 366
Cdd:cd05932 236 T----KFQQGVQDKIPQQK--------LNLLLKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 367 YEGYGQTE-VGMICANQKGQEiKPGSMGKGMLPYDVQIidengnvlppGKEGEIALRLKPTrpfcfFSKYVDNPQKTAAT 445
Cdd:cd05932 303 LEAYGMTEnFAYSHLNYPGRD-KIGTVGNAGPGVEVRI----------SEDGEILVRSPAL-----MMGYYKDPEATAEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 446 IRGD-FYVTGDRGVMDSDGYFWFVGRADDVI-ISSGYRIGPFEVESALIEHPAVVESAVVSS--PDQIRGEVVKAFVVLA 521
Cdd:cd05932 367 FTADgFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLR 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 522 A-PFKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQElPKTI-------TGKIKRNVLRD 574
Cdd:cd05932 447 AdAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKD-PWSIdngiltpTLKIKRNVLEK 506
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
72-569 |
3.05e-24 |
|
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: 106.20 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALwwvngKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWwLVNV-ACIRTGIIFMPGTIQLTA 150
Cdd:cd12114 1 PDATAV-----ICGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQ-VVAVlGILAAGAAYVPVDIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KDILYRLRASKAKCIVASEEVAPAVEsivlECPDLKTKLLVspqsrngwlsfqelFQFASEEHSCVETGSQEPMTIYFTS 230
Cdd:cd12114 74 ARREAILADAGARLVLTDGPDAQLDV----AVFDVLILDLD--------------ALAAPAPPPPVDVAPDDLAYVIFTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 231 GTTGFPK--MAQHSQSSLGIGfTLCGRYWLDlkSSDIIWNMS----DTgwvkaaigSVFSSW--LC--GACVFV------ 294
Cdd:cd12114 136 GSTGTPKgvMISHRAALNTIL-DINRRFAVG--PDDRVLALSslsfDL--------SVYDIFgaLSagATLVLPdearrr 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 295 --HRMAQFDTDtfldtlttYPITTLCSPPTVYRMLV------QKDLKrykfkSLRHCLTGGEPLNPEVLEQWRAQT-GLD 365
Cdd:cd12114 205 dpAHWAELIER--------HGVTLWNSVPALLEMLLdvleaaQALLP-----SLRLVLLSGDWIPLDLPARLRALApDAR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 366 LYEGYGQTEVGmICANQkgQEIKPGSMGKGMLPYDV-------QIIDENGNVLPPGKEGEI-------ALrlkptrpfcf 431
Cdd:cd12114 272 LISLGGATEAS-IWSIY--HPIDEVPPDWRSIPYGRplanqryRVLDPRGRDCPDWVPGELwiggrgvAL---------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 432 fsKYVDNPQKTAA-----TIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAvVESAVVSSP 506
Cdd:cd12114 339 --GYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPG-VARAVVVVL 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 507 DQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHVkkstAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:cd12114 416 GDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTL----PAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-573 |
3.98e-24 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 106.41 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEWW--LVNVACIrtGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 SEEVAPAVESIVLECPDLKTKLLVSP--------QSRNGW--LSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPK 237
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPsdadsaaaHMPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 238 MAQHSQSSLgigftlcgryWL---DLKSSDIIWNMSDT------------GWvkaaiGSVFSSWLCGA-CVFVHRMAQFD 301
Cdd:PRK05620 198 GVVYSHRSL----------YLqslSLRTTDSLAVTHGEsflccvpiyhvlSW-----GVPLAAFMSGTpLVFPGPDLSAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 TDTFldtlttypITTLCSP------PTVYRMLVQKDLKRY-KFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTE 374
Cdd:PRK05620 263 TLAK--------IIATAMPrvahgvPTLWIQLMVHYLKNPpERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMIcanqkGQEIKP--GSMGKGMLPYDV-----------QIIDEnGNVLPPG--KEGEIALRlKPTRPFCFFSKYVDNP 439
Cdd:PRK05620 335 TSPV-----GTVARPpsGVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYHSPTEEG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 440 QKTAATIRGD-------------FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSP 506
Cdd:PRK05620 408 GGAASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYP 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114643324 507 DQIRGEVVKAFVVLAApfkSYNPEKLTLE-LQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK05620 488 DDKWGERPLAVTVLAP---GIEPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
344-574 |
1.59e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 103.54 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 344 LTGGEPLNPEVLEQWRaQTGLDLYEGYGQTEV-GMICAnQKGQEIKPGSMGKG-MLPYdVQIIdengnvLPPGKEGEIAL 421
Cdd:PRK07445 236 LLGGAPAWPSLLEQAR-QLQLRLAPTYGMTETaSQIAT-LKPDDFLAGNNSSGqVLPH-AQIT------IPANQTGNITI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 422 RLKPTrpfcFFSKYvdnPQKTAATIrgdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESA 501
Cdd:PRK07445 307 QAQSL----ALGYY---PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVC 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 502 VVSSPDQIRGEVVKAFVVLAAPfkSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRD 574
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYVPKDP--SISLE----ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
226-580 |
2.75e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.24 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWlDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRMAQFDTDTF 305
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSF-DGAQERFLWTLICGGCLVVRDNDLWDPEEL 3319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 306 LDTLTTYPITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRA---QTGLdlYEGYGQTEVGMI---- 378
Cdd:PRK12467 3320 WQAIHAHRISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAAFEQVKRklkPRGL--TNGYGPTEAVVTvtlw 3396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 379 -CANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAAtirGDFY 451
Cdd:PRK12467 3397 kCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIggvglaRGYHQRPSLTAERFVADPFSGSG---GRLY 3473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 452 VTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQiRGEVVKAFVVLAAPfksynPEK 531
Cdd:PRK12467 3474 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADP-----QGD 3547
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 114643324 532 LTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK12467 3548 WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS 3596
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
69-572 |
3.22e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.24 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 69 GERPANPALWWvngkgDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQL 148
Cdd:PRK12467 523 RQHPERPALVF-----GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 149 TAKDILYRLRASKAKCIVASEE------VAPAVESIVLECPDlktkllvspqsrngwlsfqELFQFASEEHSCVETGSQE 222
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLLTQSHllaqlpVPAGLRSLCLDEPA-------------------DLLCGYSGHNPEVALDPDN 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 223 PMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRyWLDLKSSDIiWNMSDTGWVKAAIGSVFSSWLCGACV-FVHRMAQFD 301
Cdd:PRK12467 658 LAYVIYTSGSTGQPKGVAISHGALANYVCVIAE-RLQLAADDS-MLMVSTFAFDLGVTELFGALASGATLhLLPPDCARD 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 TDTFLDTLTTYPITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRA-QTGLDLYEGYGQTE--VGMI 378
Cdd:PRK12467 736 AEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTEttVGVS 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 379 CANQKGQEIKPGS--MGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAAtirGDF 450
Cdd:PRK12467 815 TYELSDEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIggaglaRGYHRRPALTAERFVPDPFGADG---GRL 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVkAFVVLAAPFKSYNPE 530
Cdd:PRK12467 892 YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQ 970
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 114643324 531 KLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12467 971 ATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
88-575 |
1.81e-22 |
|
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: 101.35 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:cd17641 11 EFTWADYADRVRAFALGL-LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 S-EEVAPAVESIVLECPDLKTKLLVSPQS----RNGWL-SFQELFQFASE---------EHSCVETGSQEPMTIYFTSGT 232
Cdd:cd17641 90 EdEEQVDKLLEIADRIPSVRYVIYCDPRGmrkyDDPRLiSFEDVVALGRAldrrdpglyEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 233 TGFPKMAQ--------HSQSSLGIGFTLCGRYWL------------------------------------DLK------- 261
Cdd:cd17641 170 TGKPKLAMlshgnflgHCAAYLAADPLGPGDEYVsvlplpwigeqmysvgqalvcgfivnfpeepetmmeDLReigptfv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 262 ----------SSDIIWNMSDTGWVKAAIgsvfsswlcgacvFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKD 331
Cdd:cd17641 250 llpprvwegiAADVRARMMDATPFKRFM-------------FELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 332 LK-RYKFKSLRHCLTGGEPLNPEVLEQWRAqTGLDLYEGYGQTEV-GMICANQKGQeIKPGSMGkgmLPY-DVQI-IDEN 407
Cdd:cd17641 317 LRdRLGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELaGAYTVHRDGD-VDPDTVG---VPFpGTEVrIDEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 408 gnvlppgkeGEIALRLKPTrpfcfFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDV-IISSGYRIGPF 485
Cdd:cd17641 392 ---------GEILVRSPGV-----FVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 486 EVESALIEHPAVVEsAVVSSPDQirgEVVKAFVVL------------AAPFKSY-----NPEKLTLeLQDHVKKSTAPYK 548
Cdd:cd17641 458 FIENKLKFSPYIAE-AVVLGAGR---PYLTAFICIdyaivgkwaeqrGIAFTTYtdlasRPEVYEL-IRKEVEKVNASLP 532
|
570 580 590
....*....|....*....|....*....|....*.
gi 114643324 549 YPRKVEFVQELPK---------TITGKIKRNVLRDQ 575
Cdd:cd17641 533 EAQRIRRFLLLYKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
312-567 |
2.39e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 101.92 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 312 YPITTLCSPPTVYRM-LVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEV-GMICAN-------- 381
Cdd:PRK08633 871 HRATILLGTPTFLRLyLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETsPVASVNlpdvlaad 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 382 ---QKGQeiKPGSMGKGMLPYDVQIID-ENGNVLPPGKEGEIALR----LKptrpfcffsKYVDNPQKTAATIR----GD 449
Cdd:PRK08633 951 fkrQTGS--KEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGgpqvMK---------GYLGDPEKTAEVIKdidgIG 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 450 FYVTGDRGVMDSDGYFWFVGRaddviISSGYRIG----PF-EVESALIE--HPAVVESAVVSSPDQIRGEVVkafVVLAA 522
Cdd:PRK08633 1020 WYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVLHT 1091
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 114643324 523 PfksynPEKLTLELQDHVKKSTAP--YKyPRKVEFVQELPKTITGKI 567
Cdd:PRK08633 1092 C-----GAEDVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKL 1132
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
64-572 |
2.68e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 64 QKEKTGERPAnpalwWVNGkgdEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMP 143
Cdd:PRK12316 520 QVERTPEAPA-----LAFG---EETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 144 GTIQLTAKDILYRLRASKAKCIVASEEVAP------AVESIVLECPDLktkllvspqsrngWLSFQelfqfaSEEHSCVE 217
Cdd:PRK12316 591 LDPEYPAERLAYMLEDSGVQLLLSQSHLGRklplaaGVQVLDLDRPAA-------------WLEGY------SEENPGTE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 218 TGSQEPMTIYFTSGTTGFPKMAQHSQS-------------SLGIGFTLCGR--YWLDLKSSDIIWN-MSDTGWVKAAIGS 281
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRalsnrlcwmqqayGLGVGDTVLQKtpFSFDVSVWEFFWPlMSGARLVVAAPGD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 282 VFSswlcgACVFVHRMAQFDtdtfldtlttypITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRA- 360
Cdd:PRK12316 732 HRD-----PAKLVELINREG------------VDTLHFVPSMLQAFLQ-DEDVASCTSLRRIVCSGEALPADAQEQVFAk 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 361 --QTGLdlYEGYGQTEVGM-----ICANQKGQEIKPGSMGKGMLPYdvqIIDENGNVLPPGKEGEIAL------RLKPTR 427
Cdd:PRK12316 794 lpQAGL--YNLYGPTEAAIdvthwTCVEEGGDSVPIGRPIANLACY---ILDANLEPVPVGVLGELYLagrglaRGYHGR 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 428 PFCFFSKYVDNPQKTAATIrgdfYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSspd 507
Cdd:PRK12316 869 PGLTAERFVPSPFVAGERM----YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA--- 941
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 508 qIRGEVVKAFVVLAAPFKSynpekLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12316 942 -VDGKQLVGYVVLESEGGD-----WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
209-572 |
3.11e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.96 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 209 ASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGiGFTLCGRYWLDLKSSDIIWNMSdTGWVKAAIGSVFSSWLC 288
Cdd:PRK12316 3184 YAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALS-NHLCWMQQAYGLGVGDRVLQFT-TFSFDVFVEELFWPLMS 3261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 GACVFVHRMAQ-FDTDTFLDTLTTYPITTLCSPPTVYRMLVQkDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAqtGLDLY 367
Cdd:PRK12316 3262 GARVVLAGPEDwRDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLY 3338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 368 EGYGQTEVGMICANQKGQEIKPGS--MGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNP 439
Cdd:PRK12316 3339 NLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGELYLggeglaRGYHNRPGLTAERFVPDP 3418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 440 QKTAATIrgdfYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSspdqIRGEVVKAFVV 519
Cdd:PRK12316 3419 FVPGERL----YRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVV 3490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 520 LAAPfksynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12316 3491 PEDE-----AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
207-572 |
4.88e-22 |
|
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: 99.01 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 207 QFASEEHSC--VETGSQEPMTIYFTSGTTGFPK--MAQHsQSSLGIGFTLCGRYWLDLKSSDIIWNMSdtgwvkAAIGSV 282
Cdd:cd17648 78 QFILEDTGArvVITNSTDLAYAIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS------NYVFDF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 283 FSSWLCGACVFVHRMAQFDTDTFLDTLTTYPI------TTLCSPPTVyrmLVQKDLKRykFKSLRHCLTGGEPLNPEVLE 356
Cdd:cd17648 151 FVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYinrekvTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 357 QWRAQTGLDLYEGYGQTEVGMICANQ--KGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRP 428
Cdd:cd17648 226 KLRSRFAGLIINAYGPTETTVTNHKRffPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLggdgvaRGYLNRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 429 FCFFSKYVDNPQKTAATI-RGDF---YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVS 504
Cdd:cd17648 306 ELTAERFLPNPFQTEQERaRGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVA 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 505 S--PDQIRGEVVKAFVVLAAPfksyNPEKLT-LELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17648 386 KedASQAQSRIQKYLVGYYLP----EPGHVPeSDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
66-572 |
6.31e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.19 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALWWvngkGDEVkWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGT 145
Cdd:PRK12316 2011 EQAARAPEAIAVVF----GDQH-LSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLD 2084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIVASEEVAPAvesivLECPdlkTKLLVSPQSRNGWLsfqelfQFASEEHSCVETGSQEPMT 225
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRHLLER-----LPLP---AGVARLPLDRDAEW------ADYPDTAPAVQLAGENLAY 2150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWlDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRMAQFDTDTF 305
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFSF-DGAHEQWFHPLLNGARVLIRDDELWDPEQL 2228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 306 LDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQ-WRAQTGLDLYEGYGQTEVGMICANQKG 384
Cdd:PRK12316 2229 YDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEIKPGS-----MGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKptrpfCFFSKYVDNPQKTAATIRGD--------FY 451
Cdd:PRK12316 2309 RPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAERFVPDpfsasgerLY 2383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 452 VTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSpDQIRGEVVKAFVVLAAPfksynPEK 531
Cdd:PRK12316 2384 RTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDA-----AED 2457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 114643324 532 LTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12316 2458 LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
66-572 |
2.52e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALwwVNGkgdEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGT 145
Cdd:PRK12467 1582 DQAAATPEAVAL--VFG---EQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 146 IQLTAKDILYRLRASKAKCIVASEEVAP------AVESIVLECPDlktkllvspqsrnGWLSFQelfqfaSEEHSCVETG 219
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQSHLQArlplpdGLRSLVLDQED-------------DWLEGY------SDSNPAVNLA 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 220 SQEPMTIYFTSGTTGFPKMAQHSQSSLgIGFTLCGRYWLDLKSSDIiWNMSDTGWVKAAIGSVFSSWLCGACVFV----- 294
Cdd:PRK12467 1717 PQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADV-VLQFTSFAFDVSVWELFWPLINGARLVIappga 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 295 HRMAQFDTDTFLDTLttypITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTG-LDLYEGYGQT 373
Cdd:PRK12467 1795 HRDPEQLIQLIERQQ----VTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPT 1870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 374 EVGM-----ICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPqkt 442
Cdd:PRK12467 1871 ETAVdvthwTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLggvglaRGYLNRPALTAERFVADP--- 1947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 443 AATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSpDQIRGEVVKAFVVLAA 522
Cdd:PRK12467 1948 FGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTD 2026
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 523 P---FKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK12467 2027 PglvDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
66-572 |
3.69e-21 |
|
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: 96.47 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGER-PANPALWWvNGKgdevKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPG 144
Cdd:cd17645 5 EEQVERtPDHVAVVD-RGQ----SLTYKQLNEKANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 145 TIQLTAKDILYRLRASKAKCIVASEEvapavesivlecpDLKTKLLVSP---QSRNGWLSFQELFQFASEEHSCVETGSQ 221
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLTNPD-------------DLAYVIYTSGstgLPKGVMIEHHNLVNLCEWHRPYFGVTPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFpkmaqhsqsslgigftlcgrywldlkssdiIWNMsdtgwvkaaigsvFSSWLCGACVFVHRMA-QF 300
Cdd:cd17645 146 DKSLVYASFSFDAS------------------------------AWEI-------------FPHLTAGAALHVVPSErRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 301 DTDTFLDTLTTYPITTLCSPPTVYRMLVQKDlkrykFKSLRHCLTGGEPLNPEVleqwraQTGLDLYEGYGQTEVGMICA 380
Cdd:cd17645 183 DLDALNDYFNQEGITISFLPTGAAEQFMQLD-----NQSLRVLLTGGDKLKKIE------RKGYKLVNNYGPTENTVVAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 381 NQkgqEIKPG----SMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAATIrgdf 450
Cdd:cd17645 252 SF---EIDKPyaniPIGKPIDNTRVYILDEALQLQPIGVAGELCIageglaRGYLNRPELTAEKFIVHPFVPGERM---- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlaaPFKSYNPE 530
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT---APEEIPHE 401
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 114643324 531 kltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17645 402 ----ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
84-575 |
1.01e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 95.93 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVIlppipEWWLVNVACIRTGIIFMpGTIQLTakdILYRLRASKAK 163
Cdd:PRK07008 35 GDIHRYTYRDCERRAKQLAQALAA-LGVEPGDRVGTL-----AWNGYRHLEAYYGVSGS-GAVCHT---INPRLFPEQIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIV--ASEEV-------APAVESIVLECPDLKTKLLVS-----PQSRNGWLSFQELFQFASEEHSCVETGSQEPMTIYFT 229
Cdd:PRK07008 105 YIVnhAEDRYvlfdltfLPLVDALAPQCPNVKGWVAMTdaahlPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLCYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 230 SGTTGFPKMAQHSQSSlgigfTLCGRYW------LDLKSSDIIWNMSDTGWVKAAiGSVFSSWLCGA-CVF--------- 293
Cdd:PRK07008 185 SGTTGNPKGALYSHRS-----TVLHAYGaalpdaMGLSARDAVLPVVPMFHVNAW-GLPYSAPLTGAkLVLpgpdldgks 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 VHRMAQFDTdtfldtlttypITTLCSPPTVYRMLVQKdLKR--YKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYG 371
Cdd:PRK07008 259 LYELIEAER-----------VTFSAGVPTVWLGLLNH-MREagLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 372 QTEV---GMICA-NQKGQEIKPGS-------MGKGMLPYDVQIIDENGNVLP-PGKE-GEIALRlkptRPFCFFSKYvdn 438
Cdd:PRK07008 327 MTEMsplGTLCKlKWKHSQLPLDEqrkllekQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWVIDRYF--- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 439 pQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEvVKAFV 518
Cdd:PRK07008 400 -RGDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE-RPLLV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 114643324 519 VLAAPFKSYNPEkltlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK07008 478 VVKRPGAEVTRE----ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
205-567 |
1.20e-20 |
|
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: 94.85 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 205 LFQFASEEHSCVETGSQEPMT-------------IYFTSGTTGFPK---MAQHSQSSLGIGFTLCgrywLDLKSSDIIWN 268
Cdd:cd17654 89 VSYLLQNKELDNAPLSFTPEHrhfnirtdeclayVIHTSGTTGTPKivaVPHKCILPNIQHFRSL----FNITSEDILFL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 269 MS----DTGWVKaaigsVFSSWLCGACVFV--HRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRY---KFKS 339
Cdd:cd17654 165 TSpltfDPSVVE-----IFLSLSSGATLLIvpTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTvlsATSS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLnPE--VLEQWRAQ-TGLDLYEGYGQTEVGmiC---ANQKGQEIKPGSMGKGMLPYDVQIIDENGNvlpp 413
Cdd:cd17654 240 LRVLALGGEPF-PSlvILSSWRGKgNRTRIFNIYGITEVS--CwalAYKVPEEDSPVQLGSPLLGTVIEVRDQNGS---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 414 GKEGEIALRLKPTRpfCFFSKYVDNPQktaatirGDFYVTGDRgVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIE 493
Cdd:cd17654 313 EGTGQVFLGGLNRV--CILDDEVTVPK-------GTMRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114643324 494 HPAVVESAVVSSPDQirgeVVKAFVVLaapfksynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKI 567
Cdd:cd17654 383 CLGVESCAVTLSDQQ----RLIAFIVG--------ESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-575 |
1.98e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 95.00 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 69 GERPANPALWWVN-GKGDEVKWSFRELGSLSRKAANMLTKpcGLQRGDRVAVILPPIPEWWLVNVACIRTGII---FMPG 144
Cdd:cd05931 4 AARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQA--VGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 145 TIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLEcpdlktkllvSPQSRNGWLSFQELFQFASEEHSCV-ETGSQEP 223
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAAS----------RPAAGTPRLLVVDLLPDTSAADWPPpSPDPDDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 MTIYFTSGTTGFPK---------MAQHSQSSLGIGF----TLCGryWLDLkssdiiwnMSDTGwvkaAIGSVFSSWLCGA 290
Cdd:cd05931 152 AYLQYTSGSTGTPKgvvvthrnlLANVRQIRRAYGLdpgdVVVS--WLPL--------YHDMG----LIGGLLTPLYSGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 291 CV-------FVHR-------MAQfdtdtfldtlttYPITTLCSPPTVYRMLVQK----DLKRYKFKSLRHCLTGGEPLNP 352
Cdd:cd05931 218 PSvlmspaaFLRRplrwlrlISR------------YRATISAAPNFAYDLCVRRvrdeDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 353 EVLEQWR---AQTGLD---LYEGYGQTE------------------VGMICANQKGQEIKPG--------SMGKGMLPYD 400
Cdd:cd05931 286 ATLRRFAeafAPFGFRpeaFRPSYGLAEatlfvsggppgtgpvvlrVDRDALAGRAVAVAADdpaarelvSCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 401 VQIIDENGN-VLPPGKEGEIALRLKPTRpfcffSKYVDNPQKTAATIR-------GDFYVTGDRGVMdSDGYFWFVGRAD 472
Cdd:cd05931 366 VRIVDPETGrELPDGEVGEIWVRGPSVA-----SGYWGRPEATAETFGalaatdeGGWLRTGDLGFL-HDGELYITGRLK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 473 DVIISSGYRIgpfevesalieHPAVVESAVVSSPDQIRGEVVKAFVVLAAPfksynPEKLTLELqdHVKKSTAPYKY--- 549
Cdd:cd05931 440 DLIIVRGRNH-----------YPQDIEATAEEAHPALRPGCVAAFSVPDDG-----EERLVVVA--EVERGADPADLaai 501
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 114643324 550 ---------------PRKVEFV--QELPKTITGKIKRNVLRDQ 575
Cdd:cd05931 502 aaairaavarehgvaPADVVLVrpGSIPRTSSGKIQRRACRAA 544
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-572 |
5.45e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 93.31 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVA 167
Cdd:cd17656 13 KLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 168 SEEVAPAVE----SIVLECPDLktkllvspqsrngwlsFQElfqfaSEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQ 243
Cdd:cd17656 92 QRHLKSKLSfnksTILLEDPSI----------------SQE-----DTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVkaAIGSVFSSWLCGACVFVHRM-AQFDTDTFLDTLTTYPITTLCSPPT 322
Cdd:cd17656 151 KNMVNLLHFEREKTNINFSDKVLQFATCSFDV--CYQEIFSTLLSGGTLYIIREeTKRDVEQLFDLVKRHNIEVVFLPVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 323 VYRMLV-QKDLKRYKFKSLRHCLTGGEPL--NPEVLEQWRAQtGLDLYEGYGQTEVGMICA-----NQKGQEIKPgsMGK 394
Cdd:cd17656 229 FLKFIFsEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVTTytinpEAEIPELPP--IGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 395 GMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAATIrgdfYVTGDRGVMDSDGYFWFV 468
Cdd:cd17656 306 PISNTWIYILDQEQQLQPQGIVGELYIsgasvaRGYLNRQELTAEKFFPDPFDPNERM----YRTGDLARYLPDGNIEFL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 469 GRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVlaaPFKSYNpeklTLELQDHVKKSTAPYK 548
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---MEQELN----ISQLREYLAKQLPEYM 454
|
490 500
....*....|....*....|....
gi 114643324 549 YPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
84-571 |
5.73e-20 |
|
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: 92.81 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAK 163
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVaseevapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscVETGSQEPMTIYFTSGTTGFPK--MAQH 241
Cdd:cd17640 80 ALV-------------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 242 SQSSLGIgftlcgrywldlkssDIIWNMSDTGWVKAAIgSVFSSW-----LCGACVFVHRMAQFDTDTFLDTL--TTYPI 314
Cdd:cd17640 111 ANLLHQI---------------RSLSDIVPPQPGDRFL-SILPIWhsyerSAEYFIFACGCSQAYTSIRTLKDdlKRVKP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 315 TTLCSPPTVYRML---VQKDL------KRYKFKSL------RHCLTGGEPLNPEVLEQWRAqTGLDLYEGYGQTEVGMIC 379
Cdd:cd17640 175 HYIVSVPRLWESLysgIQKQVsksspiKQFLFLFFlsggifKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 380 ANQKGQEIKPGSMGKGMLPYDVQIIDENGN-VLPPGKEGEIALRLKPTrpfcfFSKYVDNPQKTAATIRGD-FYVTGDRG 457
Cdd:cd17640 254 SARRLKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDgWFNTGDLG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 458 VMDSDGYFWFVGRADDVII-SSGYRIGPFEVESALIEHPaVVESAVVSSPDQIR--GEVVKAFVVLAAPFKSYNP----- 529
Cdd:cd17640 329 WLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMVVGQDQKRlgALIVPNFEELEKWAKESGVkland 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 530 -------EKLTLELQDHVKK--STAP-YKYPRKVEFVQELPK--------TITGKIKRNV 571
Cdd:cd17640 408 rsqllasKKVLKLYKNEIKDeiSNRPgFKSFEQIAPFALLEEpfiengemTQTMKIKRNV 467
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
53-567 |
1.03e-18 |
|
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: 90.02 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 53 NFAADVLdqwsqkekTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEwwlVNV 132
Cdd:cd05943 71 NYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPE---AVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 133 ACIRT---GIIFMPGTIQLTAKDILYRLRASKAKCIVASEEV---------APAVESIVLECPDLKTKLLVS---PQSRN 197
Cdd:cd05943 139 AMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYtyngkrhdvREKVAELVKGLPSLLAVVVVPytvAAGQP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 198 GWLSFQE---LFQFASEEHSC----VETGSQEPMTIYFTSGTTGFPKMAQHSQssLGI------GFTLCGrywlDLKSSD 264
Cdd:cd05943 219 DLSKIAKaltLEDFLATGAAGelefEPLPFDHPLYILYSSGTTGLPKCIVHGA--GGTllqhlkEHILHC----DLRPGD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 265 IIWNMSDTGW-----------VKAAI----GSVF---SSWLCGacvFVHRMAqfdtdtfldtlttypITTLCSPPTVYRM 326
Cdd:cd05943 293 RLFYYTTCGWmmwnwlvsglaVGATIvlydGSPFypdTNALWD---LADEEG---------------ITVFGTSAKYLDA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 327 LVQKDLK---RYKFKSLRHCLTGGEPLNPE----VLEQWRAqtGLDLYEGYGQTEV-GMICANQKGQEIKPGSMGKGMLP 398
Cdd:cd05943 355 LEKAGLKpaeTHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTDIiSCFVGGNPLLPVYRGEIQCRGLG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 399 YDVQIIDENGNVLPpGKEGE-IALRLKPTRPFCFF-----SKYVD-----NPQKTAatiRGDFYVTGDRG--VMdsdgyf 465
Cdd:cd05943 433 MAVEAFDEEGKPVW-GEKGElVCTKPFPSMPVGFWndpdgSRYRAayfakYPGVWA---HGDWIEITPRGgvVI------ 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 466 wfVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPEKLTLELQDHVKK--- 542
Cdd:cd05943 503 --LGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLR------EGVELDDELRKRIRStir 574
|
570 580
....*....|....*....|....*.
gi 114643324 543 -STAPYKYPRKVEFVQELPKTITGKI 567
Cdd:cd05943 575 sALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-572 |
1.18e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYfTSGTTGFPK--------MAQHSQSSLGigftlcgRYwlDLKSSDIIWNMSDTGWvKAAIGSVFSSWLCGACVFVHRM 297
Cdd:PRK05691 2339 IY-TSGSTGKPKgvvvshgeIAMHCQAVIE-------RF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQ 2407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 298 AQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRA--QTGLdLYEGYGQTE- 374
Cdd:PRK05691 2408 GQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQafAPQL-FFNAYGPTEt 2486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 VGMICANQKGQEIKPGS----MGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAA 444
Cdd:PRK05691 2487 VVMPLACLAPEQLEEGAasvpIGRVVGARVAYILDADLALVPQGATGELYVggaglaQGYHDRPGLTAERFVADPFAADG 2566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 445 tirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVEsAVVSSPDQIRGEVVKAFVVLA-AP 523
Cdd:PRK05691 2567 ---GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAvAG 2642
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 114643324 524 FKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK05691 2643 QDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
321-575 |
1.67e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 89.04 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 321 PTVYRMLVQK-DLKRYKFKSLRHCLTGGEPLnPEVLEQWRAQTGLDLYEGYGQTE---VGMICANQKGQEIKPGS----- 391
Cdd:PRK06018 276 PTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEmspLGTLAALKPPFSKLPGDarldv 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 392 -MGKGMLPYDVQ--IIDENGNVLPpgKEGEIALRLKptrpfcffskyVDNPQKTAATIRGD--------FYVTGDRGVMD 460
Cdd:PRK06018 355 lQKQGYPPFGVEmkITDDAGKELP--WDGKTFGRLK-----------VRGPAVAAAYYRVDgeildddgFFDTGDVATID 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 461 SDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEvVKAFVVLAAPFKSYNPEkltlELQDHV 540
Cdd:PRK06018 422 AYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE-RPLLIVQLKPGETATRE----EILKYM 496
|
250 260 270
....*....|....*....|....*....|....*
gi 114643324 541 KKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK06018 497 DGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
56-575 |
2.37e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.78 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 56 ADVLDQWSQKektgeRPANPALwwvngKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACI 135
Cdd:PRK08279 40 GDVFEEAAAR-----HPDRPAL-----LFEDQSISYAELNARANRYAHWA-AARGVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 136 RTGIIF-MPGTiQLTAKDILYRLRASKAKCIVASEEVAPAVESiVLECPDLKTKLLVSPQSRNGWLS-FQELFQFASEEH 213
Cdd:PRK08279 109 KLGAVVaLLNT-QQRGAVLAHSLNLVDAKHLIVGEELVEAFEE-ARADLARPPRLWVAGGDTLDDPEgYEDLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 214 SCVETgSQEPMTI-----Y-FTSGTTGFPKMAQHSQS---SLGIGFTLCgrywLDLKSSDIIWN----------MSDTGW 274
Cdd:PRK08279 187 TTNPA-SRSGVTAkdtafYiYTSGTTGLPKAAVMSHMrwlKAMGGFGGL----LRLTPDDVLYCclplyhntggTVAWSS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 275 VKAAIGSV-----FSS---W----LCGACVFVHrmaqfdtdtfldtlttypITTLCspptvyRMLVQKDLKRY-KFKSLR 341
Cdd:PRK08279 262 VLAAGATLalrrkFSAsrfWddvrRYRATAFQY------------------IGELC------RYLLNQPPKPTdRDHRLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 342 HCLTGGepLNPEVLEQWRAQTGLD-LYEGYGQTE--VGMIcaNQKGqeiKPGSMG----KGMLP-----YDVQ----IID 405
Cdd:PRK08279 318 LMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGrvplWLAHPyaivkYDVDtgepVRD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 406 ENGNVLPPGKeGEIALRLKPTRPFCFFSKYVDnPQKTAATI------RGDFYV-TGDrgVM--DSDGYFWFVGRADDVii 476
Cdd:PRK08279 391 ADGRCIKVKP-GEVGLLIGRITDRGPFDGYTD-PEASEKKIlrdvfkKGDAWFnTGD--LMrdDGFGHAQFVDRLGDT-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 477 ssgYR-----IGPFEVESALIEHPAVVESAV--VSSPDQiRGEVVKAFVVLaAPFKSYNPEkltlELQDHVKKSTAPYKY 549
Cdd:PRK08279 465 ---FRwkgenVATTEVENALSGFPGVEEAVVygVEVPGT-DGRAGMAAIVL-ADGAEFDLA----ALAAHLYERLPAYAV 535
|
570 580
....*....|....*....|....*.
gi 114643324 550 PRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PRK08279 536 PLFVRLVPELETTGTFKYRKVDLRKE 561
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
26-572 |
6.00e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 88.18 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 26 DHQLWTPLTLADFEAINRCNRPLPKNFnfAADVLDQwsQKEKTgerPANPALwwvngKGDEVKWSFRELGSLSRKAANML 105
Cdd:PRK10252 433 DVDILLPGEYAQLAQVNATAVEIPETT--LSALVAQ--QAAKT---PDAPAL-----ADARYQFSYREMREQVVALANLL 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 106 TKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPgtIQLTAKD--ILYRLRASKAKCIVASEEVA---PAVESIVL 180
Cdd:PRK10252 501 RER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP--LDTGYPDdrLKMMLEDARPSLLITTADQLprfADVPDLTS 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 181 ECPDlktKLLVSPQSRNGWLSfqelfqfaseehscvetGSQEPMTIYFTSGTTGFPK--MAQHS---------QSSLGIG 249
Cdd:PRK10252 578 LCYN---APLAPQGAAPLQLS-----------------QPHHTAYIIFTSGSTGRPKgvMVGQTaivnrllwmQNHYPLT 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 250 F-------TLCgrywldlkSSDI-IWNMsdtgwvkaaigsvFSSWLCGACVFV-----HR----MAQfdtdtfldTLTTY 312
Cdd:PRK10252 638 AddvvlqkTPC--------SFDVsVWEF-------------FWPFIAGAKLVMaepeaHRdplaMQQ--------FFAEY 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 313 PITTLCSPPTVYRMLVQK---DLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEV----------GMIC 379
Cdd:PRK10252 689 GVTTTHFVPSMLAAFVASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAavdvswypafGEEL 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 380 ANQKGQEIKPGsmgkgmlpYDV-----QIIDENGNVLPPGKEGEIAL------RLKPTRPFCFFSKYVDNPQKTAATIrg 448
Cdd:PRK10252 769 AAVRGSSVPIG--------YPVwntglRILDARMRPVPPGVAGDLYLtgiqlaQGYLGRPDLTASRFIADPFAPGERM-- 838
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 449 dfYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHP----AVVESAVVSSPDQIRGEVVK--AFVVlaa 522
Cdd:PRK10252 839 --YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV--- 913
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 523 pfkSYNPEKLTLE-LQDHVKKSTAPYKYPrkVEFVQ--ELPKTITGKIKRNVL 572
Cdd:PRK10252 914 ---SQSGLPLDTSaLQAQLRERLPPHMVP--VVLLQldQLPLSANGKLDRKAL 961
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
400-569 |
1.27e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 86.10 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 400 DVQIIDENGNVLPPGKEGEIALrLKPTrpfcfFSK-YVDNPQKTAA---TIRGD-FYVTGDRGVMDsDGYFWFVGRADDV 474
Cdd:PRK04813 328 PLLIIDEEGTKLPDGEQGEIVI-SGPS-----VSKgYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 475 IISSGYRIGPFEVESALIEHPaVVESAVVSsPDQIRGEVVK--AFVVLAApfKSYNPE-KLTLELQDHVKKSTAPYKYPR 551
Cdd:PRK04813 401 IKLNGYRIELEEIEQNLRQSS-YVESAVVV-PYNKDHKVQYliAYVVPKE--EDFEREfELTKAIKKELKERLMEYMIPR 476
|
170
....*....|....*...
gi 114643324 552 KVEFVQELPKTITGKIKR 569
Cdd:PRK04813 477 KFIYRDSLPLTPNGKIDR 494
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-575 |
1.68e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 85.64 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 121 LPPIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPA-----VESIVLECPDLKTKLL----- 190
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralpLYSKVVEAAPAKAIVLpaage 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 191 -VSPQSRNGWLSFQELFQFASEEHSC-------VETGSQEPMTIYFTSGTTGFPKMAQHSQSSlGIGFTLCGRYWLDLKS 262
Cdd:PLN03051 81 pVAVPLREQDLSWCDFLGVAAAQGSVggneyspVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 263 SDIIWNMSDTGWVKAAIgSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTyPITTLCSPPTV---YRMLVQKDLKRYKFKS 339
Cdd:PLN03051 160 GDVVCWPTNLGWMMGPW-LLYSAFLNGATLALYGGAPLGRGFGKFVQDA-GVTVLGLVPSIvkaWRHTGAFAMEGLDWSK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLNPE---VLEQWRAQT--------GLDLYEGYGQTEVGMICAnqkgqeikPGSMGKGMLPYDVQIIDENG 408
Cdd:PLN03051 238 LRVFASTGEASAVDdvlWLSSVRGYYkpvieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLLNDNG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 409 NVLPPGKE--GEIALRLkptrPFCFFSKYVDNPQKTAATIRG-DFYVT--------GDRGVMDSDGYFWFVGRADDVIIS 477
Cdd:PLN03051 310 VPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmPMYGSkgmplrrhGDIMKRTPGGYFCVQGRADDTMNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 478 SGYRIGPFEVESALIE-HPAVVESAVVSSPDQIRGE----VVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYKYPRK 552
Cdd:PLN03051 386 GGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPLFKVSR 465
|
490 500
....*....|....*....|...
gi 114643324 553 VEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PLN03051 466 VKIVPELPRNASNKLLRRVLRDQ 488
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
70-539 |
2.19e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 70 ERPANPAL-----WWVNGKGDEVKWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFM-- 142
Cdd:PRK09274 18 ERPDQLAVavpggRGADGKLAYDELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 143 -PGtiqLTAKDILYRLRASKAKCIVASEEvAPAVESIVL-ECPDLKTKLLVSPqsRNGWLSFQeLFQF----ASEEHSCV 216
Cdd:PRK09274 97 dPG---MGIKNLKQCLAEAQPDAFIGIPK-AHLARRLFGwGKPSVRRLVTVGG--RLLWGGTT-LATLlrdgAAAPFPMA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 217 ETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWldlkssdiiwnmsdtGWVKAAIGS----VFS--SWLCGA 290
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDY---------------GIEPGEIDLptfpLFAlfGPALGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 291 CVFVHRM-----AQFDTDTFLDTLTTYPITTL-CSPP---TVYRMLVQKDLKrykFKSLRHCLTGGEPLNPEVLEQWRA- 360
Cdd:PRK09274 235 TSVIPDMdptrpATVDPAKLFAAIERYGVTNLfGSPAlleRLGRYGEANGIK---LPSLRRVISAGAPVPIAVIERFRAm 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 361 -QTGLDLYEGYGQTE---VGMICANQKGQEIKPGS-MGKGML------PYDVQIID---------ENGNVLPPGKEGEIA 420
Cdd:PRK09274 312 lPPDAEILTPYGATEalpISSIESREILFATRAATdNGAGICvgrpvdGVEVRIIAisdapipewDDALRLATGEIGEIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 421 LRlKP--TRpfcffsKYVDNPQKTA-ATIR---GDFY-VTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIE 493
Cdd:PRK09274 392 VA-GPmvTR------SYYNRPEATRlAKIPdgqGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNT 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 114643324 494 HPAVVESAVVSSPdqIRGEVVKAFVVLAAPFKSYNPEKLTLELQDH 539
Cdd:PRK09274 465 HPGVKRSALVGVG--VPGAQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
437-569 |
6.50e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 83.16 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 437 DNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKA 516
Cdd:PRK08308 279 NAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 517 FVVLAAPFKsynpeklTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKR 569
Cdd:PRK08308 359 KVISHEEID-------PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
66-572 |
9.41e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 83.52 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALWWVNGKGDevkWSFREL-GSLSRKAANMLTKpcGLQRGDRVAVILPPIPEWWLVNVACIRTGiifmpg 144
Cdd:PRK05857 22 EQARQQPEAIALRRCDGTSA---LRYRELvAEVGGLAADLRAQ--SVSRGSRVLVISDNGPETYLSVLACAKLG------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 145 TIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVlECPDLKTKLLVSPQSRNGWLSFQELFQFASEEH---SCVETGSQ 221
Cdd:PRK05857 91 AIAVMADGNLPIAAIERFCQITDPAAALVAPGSKM-ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslaGNADQGSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPK---MAQHSQSSLGIGFTLCGRYWLDlkssdiiWNMSDTGWV---KAAIGSVFSSWLC----GAC 291
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKavlLANRTFFAVPDILQKEGLNWVT-------WVVGETTYSplpATHIGGLWWILTClmhgGLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 292 VfvhrMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGG-EPLNPEVleQWRAQTGLDLYEG 369
Cdd:PRK05857 243 V----TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 370 YGQTEVG--MICA---NQKGQEIKPGSMGKgmlPY---DVQIIDENGN--VLPPGKEGEIALRLKPTRPFCFFSkYVDNP 439
Cdd:PRK05857 317 YGLSETGctALCLptdDGSIVKIEAGAVGR---PYpgvDVYLAATDGIgpTAPGAGPSASFGTLWIKSPANMLG-YWNNP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 440 QKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVV 519
Cdd:PRK05857 393 ERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 520 LAAPFKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK05857 473 ASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
84-575 |
1.53e-16 |
|
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: 82.72 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 84 GDEVKWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPP----IPEWWlvnvACIRTGII------FMPGTIQLTAKDI 153
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVpapltvPPTYDEPNARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 154 LYRLRASKAKCIV-ASEEVAPAVESIvlecpdlkTKLLVSPQSRngwLSFQELFQFASEEHSCVETGSQEPMTIYFTSGT 232
Cdd:cd05906 110 LRHIWQLLGSPVVlTDAELVAEFAGL--------ETLSGLPGIR---VLSIEELLDTAADHDLPQSRPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 233 TGFPKMAQHSQSSL-----GIGfTLCGrywldLKSSDIIWNmsdtgWV--KAAIGSVFSSW--LCGACVFVH-------- 295
Cdd:cd05906 179 TGFPKAVPLTHRNIlarsaGKI-QHNG-----LTPQDVFLN-----WVplDHVGGLVELHLraVYLGCQQVHvpteeila 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 ------RMAQFdtdtfldtlttYPITTLCSPPTVYRMLVQ-----KDlKRYKFKSLRHCLTGGEPLNPEV-------LEQ 357
Cdd:cd05906 248 dplrwlDLIDR-----------YRVTITWAPNFAFALLNDlleeiED-GTWDLSSLRYLVNAGEAVVAKTirrllrlLEP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 358 WRAQTGLdLYEGYGQTEV--GMICANQKGQEIKPG-----SMGKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTRpfc 430
Cdd:cd05906 316 YGLPPDA-IRPAFGMTETcsGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR-GPVV--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 431 fFSKYVDNPQKTAATIRGD-FYVTGDRGVMDsDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVES--AVVSSPD 507
Cdd:cd05906 391 -TKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRD 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 508 QirGEVVKAFVVLAAPfkSYNPEKLTLEL----QDHVKKS---TAPYKYPRKVEfvqELPKTITGKIKRNVLRDQ 575
Cdd:cd05906 469 P--GAETEELAIFFVP--EYDLQDALSETlraiRSVVSREvgvSPAYLIPLPKE---EIPKTSLGKIQRSKLKAA 536
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-575 |
5.33e-16 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 80.55 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEW---WL------VNVACIRTgiifmpgtiQLTAKDILYRLR 158
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFvalWLglakigVETALINS---------NLRLESLLHCIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 159 ASKAKCIVAseevapavesivlecpDLKTKLLVspqsrngwlsfqelfQFASEEHSCVETGSQEPMTIYFTSGTTGFPKM 238
Cdd:cd05939 73 VSKAKALIF----------------NLLDPLLT---------------QSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 239 A--QHSQS---SLGIGftlcgrYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRmaQFDTDTFLDTLTTYP 313
Cdd:cd05939 122 AviVHSRYyriAAGAY------YAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRK--KFSASNFWDDCVKYN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 314 ITTLCSPPTVYRMLVQKDLKRYKFKslrHC--LTGGEPLNPEVLEQWRAQTGL-DLYEGYGQTEVGMICANQKGQEIKPG 390
Cdd:cd05939 194 CTIVQYIGEICRYLLAQPPSEEEQK---HNvrLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNHVGACG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 391 SMGKgMLP--YDVQII-----------DENGNVLP--PGKEGEIALRLKPTRPFCFFSKYVD---NPQKTAATI--RGD- 449
Cdd:cd05939 271 FNSR-ILPsvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIARDVfkKGDs 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 450 FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVEsALIEHPAVVESAVVSSPD--QIRGEVVKAFVVlaAPFKSY 527
Cdd:cd05939 350 AFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVE-GILSNVLGLEDVVVYGVEvpGVEGRAGMAAIV--DPERKV 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 114643324 528 NPEKLTLELQdhvkKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:cd05939 427 DLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
90-551 |
1.09e-15 |
|
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: 80.03 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEW---WL------VNVACIRTGIIFMPgtiqltakdILYRLRAS 160
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLNTNIRSKS---------LLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 161 KAKCIVASEEVAPAVESIvleCPDLKTK----LLVSPQSR-NGWLSFQELFQFASEE-----HSCVETGSQEPMTIYfTS 230
Cdd:cd05938 78 GAKVLVVAPELQEAVEEV---LPALRADgvsvWYLSHTSNtEGVISLLDKVDAASDEpvpasLRAHVTIKSPALYIY-TS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 231 GTTGFPKMAQHSQSSL--GIGFT-LCGrywldLKSSDII------WNMSdtGWVKAAIGSV-----------FSS---WL 287
Cdd:cd05938 154 GTTGLPKAARISHLRVlqCSGFLsLCG-----VTADDVIyitlplYHSS--GFLLGIGGCIelgatcvlkpkFSAsqfWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 288 -C---GACVFVHrmaqfdtdtfldtlttypITTLCspptvyRMLV----QKDLKRYKFKslrhcLTGGEPLNPEVLEQWR 359
Cdd:cd05938 227 dCrkhNVTVIQY------------------IGELL------RYLCnqpqSPNDRDHKVR-----LAIGNGLRADVWREFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 360 AQTG-LDLYEGYGQTEVGMICANQKGqeiKPGSMGKG-----------MLPYDVQ----IIDENGNVLPPGKeGEIALRL 423
Cdd:cd05938 278 RRFGpIRIREFYGSTEGNIGFFNYTG---KIGAVGRVsylykllfpfeLIKFDVEkeepVRDAQGFCIPVAK-GEPGLLV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 424 KPTRPFCFFSKYVDNPQKTAATI------RGDFYV-TGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPA 496
Cdd:cd05938 354 AKITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDF 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 114643324 497 VVESAV--VSSPDQiRGEVVKAFVVLaAPFKSYNPEKLTlelqDHVKKSTAPYKYPR 551
Cdd:cd05938 434 LQEVNVygVTVPGH-EGRIGMAAVKL-KPGHEFDGKKLY----QHVREYLPAYARPR 484
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
453-573 |
8.59e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 76.24 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 453 TGDRGVMDsDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAApfksyNPEKL 532
Cdd:PRK07824 238 TDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDG-----GPAPT 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 114643324 533 TLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLR 573
Cdd:PRK07824 312 LEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
66-575 |
8.99e-15 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 77.43 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 66 EKTGERPANPALWWVNGKGDEV---KWSFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFM 142
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANALDA-LGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 143 PGTIQLTAKDILYRLRASKAKCIVASEEV---------------APAVESIVLecPDLKTKLLVspQSRNGWLSFQELFQ 207
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveAKAPKAIVL--PADGKSVRV--KLREGDMSWDDFLA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 208 FAS-----EEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSlgiGFTLCGRYW--LDLKSSDIIWNMSDTGWVKAAIg 280
Cdd:PLN03052 338 RANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT---PLRAAADAWahLDIRKGDIVCWPTNLGWMMGPW- 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 281 SVFSSWLCGACV--------------FVHRMAqfdtdtfldtlttypITTLCSPPTVYRMLVQKD-LKRYKFKSLRHCLT 345
Cdd:PLN03052 414 LVYASLLNGATLalyngsplgrgfakFVQDAK---------------VTMLGTVPSIVKTWKNTNcMAGLDWSSIRCFGS 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 346 GGEPLN-PEVLeqW---RAQtgldlY----EGYGQTEVGmiCANQKGQEIKPGSMGKGMLP---YDVQIIDENGNVLP-- 412
Cdd:PLN03052 479 TGEASSvDDYL--WlmsRAG-----YkpiiEYCGGTELG--GGFVTGSLLQPQAFAAFSTPamgCKLFILDDSGNPYPdd 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 413 -PGKeGEIALRlkptrPFCF-----------FSKYVDN-PQKTAATIR--GD-FYVTgdrgvmdSDGYFWFVGRADDVIi 476
Cdd:PLN03052 550 aPCT-GELALF-----PLMFgasstllnadhYKVYFKGmPVFNGKILRrhGDiFERT-------SGGYYRAHGRADDTM- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 477 ssgyRIGPFEVESALIE------HPAVVESAVVSSPDQIRG--EVVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYK 548
Cdd:PLN03052 616 ----NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLF 691
|
570 580
....*....|....*....|....*..
gi 114643324 549 YPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:PLN03052 692 KVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-580 |
1.09e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 226 IYfTSGTTGFPKmaqhsqsslGIGFT---LCGR-YWLD----LKSSDIIWNmsdtgwvKAAIGSVFSSWLC-----GACV 292
Cdd:PRK05691 1279 IY-TSGSTGQPK---------GVGNThaaLAERlQWMQatyaLDDSDVLMQ-------KAPISFDVSVWECfwpliTGCR 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 293 FV----------HRMAQFDTDtfldtlttYPITTLCSPPTVYRMLVQKDLKRyKFKSLRHCLTGGEPLNPEVLEQWRAQ- 361
Cdd:PRK05691 1342 LVlagpgehrdpQRIAELVQQ--------YGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRl 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 362 TGLDLYEGYGQTEVGM-----ICANQKGqEIKPgsMGKGMLPYDVQIIDENGNVLPPGKEGEIAL------RLKPTRPFC 430
Cdd:PRK05691 1413 PQVQLHNRYGPTETAInvthwQCQAEDG-ERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIggaglaRGYLGRPAL 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 431 FFSKYVDNPQKTAATirgDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIR 510
Cdd:PRK05691 1490 TAERFVPDPLGEDGA---RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG 1566
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 511 GEVVKAFVVLAApfksynPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR 580
Cdd:PRK05691 1567 AQLVGYYTGEAG------QEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR 1630
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
222-572 |
3.17e-14 |
|
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: 75.20 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPK--MAQHsQSSLGIGFTLCGRYWLDLKSSDIIwNMSDTGWvkaaigSVFSSWLC------GACVF 293
Cdd:cd17650 94 DLAYVIYTSGTTGKPKgvMVEH-RNVAHAAHAWRREYELDSFPVRLL-QMASFSF------DVFAGDFArsllngGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 294 VHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQK-DLKRYKFKSLRHCLTGGEplnpEVLEQWRAqtglDLYEGYGQ 372
Cdd:cd17650 166 CPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSD----GCKAQDFK----TLAARFGQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 373 tevGMICANQKG-----------QEIKPGSMGKGMLPYD-------VQIIDENGNVLPPGKEGEIAL------RLKPTRP 428
Cdd:cd17650 238 ---GMRIINSYGvteatidstyyEEGRDPLGDSANVPIGrplpntaMYVLDERLQPQPVGVAGELYIggagvaRGYLNRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 429 FCFFSKYVDNPqkTAATIRgdFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQ 508
Cdd:cd17650 315 ELTAERFVENP--FAPGER--MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 509 iRGEV-VKAFVVLAAPFKsynpeklTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17650 391 -GGEArLCAYVVAAATLN-------TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
312-575 |
1.83e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 72.91 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 312 YPITTLCSPPTVYRMLvqkdLKRYK--------FKSLRHCLTGGEPLNPEVLEQWRAQT---GLD---LYEGYGQTE--V 375
Cdd:cd05908 198 HKATIVSSPNFGYKYF----LKTLKpekandwdLSSIRMILNGAEPIDYELCHEFLDHMskyGLKrnaILPVYGLAEasV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 376 GMICANQ-----------KGQEIKPG---------------SMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPf 429
Cdd:cd05908 274 GASLPKAqspfktitlgrRHVTHGEPepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 430 cffsKYVDNPQKTAATIRGDFYV-TGDRGVMdSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVS---S 505
Cdd:cd05908 353 ----GYYNNPEATAKVFTDDGWLkTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvN 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 506 PDQIRGEVVKAFVVLAAPFKSYNPekLTLELQDHVKKSTApyKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:cd05908 428 NSNTRNEEIFCFIEHRKSEDDFYP--LGKKIKKHLNKRGG--WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-575 |
2.06e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 72.39 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 88 KWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIfmPGTI--QLTAKDILYRLRASKAKCI 165
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 166 VaseeVAPAvesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqepMTIYfTSGTTGFPKMA--QHSQ 243
Cdd:cd05940 80 V----VDAA-------------------------------------------------LYIY-TSGTTGLPKAAiiSHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGFtlcGRYWLDLKSSDIIW--------NMSDTGWVKA-------AIGSVFSS---W----LCGACVFVHrmaqfd 301
Cdd:cd05940 106 AWRGGAF---FAGSGGALPSDVLYtclplyhsTALIVGWSAClasgatlVIRKKFSAsnfWddirKYQATIFQY------ 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 302 tdtfldtlttypITTLCspptvyRMLV---QKDLKRykfkslRHCLTG--GEPLNPEVLEQWRAQTGL-DLYEGYGQTE- 374
Cdd:cd05940 177 ------------IGELC------RYLLnqpPKPTER------KHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEg 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 -VGMI-CANQKG-----QEIKPGSMGKGMLPYDVQ----IIDENGNV--LPPGKEGEIALRLKPTRPFcffSKYVDnPQK 441
Cdd:cd05940 233 nSGFInFFGKPGaigrnPSLLRKVAPLALVKYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEPF---DGYTD-PAA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 442 TAATI------RGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAV--VSSPDQiRGE 512
Cdd:cd05940 309 TEKKIlrdvfkKGDaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGT-DGR 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114643324 513 VVKAFVVLAAPfksyNPEKLTlELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQ 575
Cdd:cd05940 388 AGMAAIVLQPN----EEFDLS-ALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
90-503 |
1.14e-12 |
|
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: 70.18 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 90 SFRELGSLSRKAANMLTKpCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFM---PGTIqltakdilyrlRASKAKCIv 166
Cdd:cd05910 4 SFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVlidPGMG-----------RKNLKQCL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 167 asEEVAPAVesivlecpdlktkllvspqsrngwlsfqelfqFASEehscveTGSQEPMTIYFTSGTTGFPKMAQHS---- 242
Cdd:cd05910 71 --QEAEPDA--------------------------------FIGI------PKADEPAAILFTSGSTGTPKGVVYRhgtf 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 243 -------QSSLGI--------GFTLCGRYWLDLKSSDIIWNMSDTgwvkaaigsvfsswlcgacvfvhRMAQFDTDTFLD 307
Cdd:cd05910 111 aaqidalRQLYGIrpgevdlaTFPLFALFGPALGLTSVIPDMDPT-----------------------RPARADPQKLVG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 308 TLTTYPITTLCSPPTVYRMLVQKDLKR-YKFKSLRHCLTGGEPLNPEVLEQWRA--QTGLDLYEGYGQTEVGMICANQkG 384
Cdd:cd05910 168 AIRQYGVSIVFGSPALLERVARYCAQHgITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSIG-S 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 385 QEI-----KPGSMGKG-------------MLPYDVQIIDENGNV--LPPGKEGEIALRLKPTRPfcffsKYVDNPQKTAA 444
Cdd:cd05910 247 RELlatttAATSGGAGtcvgrpipgvrvrIIEIDDEPIAEWDDTleLPRGEIGEITVTGPTVTP-----TYVNRPVATAL 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114643324 445 TIRGD-----FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVV 503
Cdd:cd05910 322 AKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
314-572 |
2.11e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 314 ITTLCSPPT-VYRMLVQKdlkRYKFKSLRHCLTGGEPLNPEVLEQWRAQ-TGLDLYEGYGQTE---------VGMicANQ 382
Cdd:PRK05691 3961 ITVLESVPSlIQGMLAED---RQALDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPAEcsddvaffrVDL--AST 4035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 383 KGQEIKPGSmgkgmlPYD---VQIIDENGNVLPPGKEGEIalrlkptrpfCFFSK-----YVDNPQKTA-ATIRGDF--- 450
Cdd:PRK05691 4036 RGSYLPIGS------PTDnnrLYLLDEALELVPLGAVGEL----------CVAGTgvgrgYVGDPLRTAlAFVPHPFgap 4099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 ----YVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSpDQIRGEVVKAFVVLAAPFks 526
Cdd:PRK05691 4100 gerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTV-- 4176
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 114643324 527 YNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:PRK05691 4177 LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
335-567 |
2.44e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.91 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 335 YKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKgMLP------YDVQIIDENG 408
Cdd:PRK06814 904 YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGR-LLPgieyrlEPVPGIDEGG 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 409 NVLPPGKegEIAL-RLKPTRPfcffskYVDNPQKtaatirGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEV 487
Cdd:PRK06814 983 RLFVRGP--NVMLgYLRAENP------GVLEPPA------DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAV 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 488 ESALIEHPAVVESAVVSSPDQIRGEVvkafVVLAAPFKSYNPEkltlELQDHVKKSTAPYKY-PRKVEFVQELPKTITGK 566
Cdd:PRK06814 1049 EELAAELWPDALHAAVSIPDARKGER----IILLTTASDATRA----AFLAHAKAAGASELMvPAEIITIDEIPLLGTGK 1120
|
.
gi 114643324 567 I 567
Cdd:PRK06814 1121 I 1121
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-567 |
3.54e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.97 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 53 NFAADVLdqwsqkekTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 133 ACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASE---------EVAPAVESIVLECPDLKtKLLVSPQSRN------ 197
Cdd:PRK03584 158 ATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLE-HVVVVPYLGPaaaaaa 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 198 --GWLSFQELFQ-FASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQ--------------SSLGIG-----FTLCGr 255
Cdd:PRK03584 237 lpGALLWEDFLApAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHggillehlkelglhCDLGPGdrffwYTTCG- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 256 yWldlkssdIIWNMsdtgwvkaaigsVFSSWLCGACVFVH-------------RMAQFDTdtfldtlttypITTLCSPPT 322
Cdd:PRK03584 316 -W-------MMWNW------------LVSGLLVGATLVLYdgspfypdpnvlwDLAAEEG-----------VTVFGTSAK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 323 VYRMLVQKDL---KRYKFKSLRHCLTGGEPLNPE----VLEQWRAqtGLDLYEGYGQTEV--GMICANQkgqeIKP---G 390
Cdd:PRK03584 365 YLDACEKAGLvpgETHDLSALRTIGSTGSPLPPEgfdwVYEHVKA--DVWLASISGGTDIcsCFVGGNP----LLPvyrG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 391 SMGKGMLPYDVQIIDENGN-VLppGKEGEialrLKPTRPF-----CF-------------FSKYvDNpqktaaTIR-GDF 450
Cdd:PRK03584 439 EIQCRGLGMAVEAWDEDGRpVV--GEVGE----LVCTKPFpsmplGFwndpdgsryrdayFDTF-PG------VWRhGDW 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 451 YVTGDRGvmdsdGYFwFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAapfksyNPE 530
Cdd:PRK03584 506 IEITEHG-----GVV-IYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA------EGV 573
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 114643324 531 KLTLELQDHVK----KSTAPYKYPRKVEFVQELPKTITGKI 567
Cdd:PRK03584 574 TLDDALRARIRttirTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
315-569 |
6.49e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.02 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 315 TTLCSPPTVY-----RMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQT---GLD---LYEGYGQTE--------- 374
Cdd:PRK07768 248 TMTAAPNFAYallarRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGarfGLRpeaILPAYGMAEatlavsfsp 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 ------VGMICAN-----------QKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPfcffsKYVD 437
Cdd:PRK07768 328 cgaglvVDEVDADllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTP-----GYLT 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 438 NPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPdQIRGEVVKAF 517
Cdd:PRK07768 403 MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVR-LDAGHSREGF 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114643324 518 VVLAAPFKSYNPEKLT-LELQ------DHVKKStapykyPRKVEFVQ--ELPKTITGKIKR 569
Cdd:PRK07768 482 AVAVESNAFEDPAEVRrIRHQvahevvAEVGVR------PRNVVVLGpgSIPKTPSGKLRR 536
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
320-491 |
1.31e-10 |
|
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: 63.92 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 320 PPTVYRMLVQKDLKRYK----FKSLRHCLTGGEPLNPEVLEQWraqTGLD--LYEGYGQTEV-GMICANQKgQEIKPGSM 392
Cdd:cd05933 298 SPLFYRLAKKLVFKKVRkalgLDRCQKFFTGAAPISRETLEFF---LSLNipIMELYGMSETsGPHTISNP-QAYRLLSC 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 393 GKGMLPYDVQIIDENGNvlppgKEGEIALRLKPTrpfcfFSKYVDNPQKTAATIRGDFYV-TGDRGVMDSDGYFWFVGRA 471
Cdd:cd05933 374 GKALPGCKTKIHNPDAD-----GIGEICFWGRHV-----FMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRI 443
|
170 180
....*....|....*....|.
gi 114643324 472 DDVII-SSGYRIGPFEVESAL 491
Cdd:cd05933 444 KELIItAGGENVPPVPIEDAV 464
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-497 |
2.78e-10 |
|
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: 63.00 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 125 PEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASeevapavesivlecPDLKTkllvspqsrngwLSFQE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD--------------AGVKV------------YSLEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 205 LFQFASEEHSCVETGSQEP-MTIYFTSGTTGFPKMAQHSQSSLgigFTLCGRYWLDLKSSDIIwNMSDtgwvkaaigsVF 283
Cdd:cd05927 97 FEKLGKKNKVPPPPPKPEDlATICYTSGTTGNPKGVMLTHGNI---VSNVAGVFKILEILNKI-NPTD----------VY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 284 SSWLCGACVFvHRMAQFDTDTFLDTLTTY--PITTL------CSP---PTVYRML----------VQKD--LKR------ 334
Cdd:cd05927 163 ISYLPLAHIF-ERVVEALFLYHGAKIGFYsgDIRLLlddikaLKPtvfPGVPRVLnriydkifnkVQAKgpLKRklfnfa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 335 --YKFKSLRH---------------------------CLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQ 385
Cdd:cd05927 242 lnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 386 EIKPGSMGkGMLPY-DVQIID--E-NGNVLPPGKEGEIALrlkptRPFCFFSKYVDNPQKTAATIRGD-FYVTGDRGVMD 460
Cdd:cd05927 322 DTSVGHVG-GPLPCaEVKLVDvpEmNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALDEDgWLHTGDIGEWL 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 114643324 461 SDGYFWFVGRADDVI-ISSGYRIGPFEVESALIEHPAV 497
Cdd:cd05927 396 PNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFV 433
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
89-577 |
2.59e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 59.75 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 89 WSFRELGSLSRKAANMLTKPCGLQRGDRVAVILPPIPEW---W--LVNVACIRTGIIFmpgtiQLTAKDILYRLRASKAK 163
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFvflWlgLWSIGAAPAFINY-----NLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 164 CIVASEEVapavesivlecpdlktkllvspqsrngwlsfqelfqfaseehscvetgsqEPMTIYfTSGTTGFPKMAQHSQ 243
Cdd:cd05937 81 FVIVDPDD--------------------------------------------------PAILIY-TSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 244 SSLGIGFTLCGRyWLDLKSSDIIWN----MSDTGWVKAAIGSVFS-SWLCGACVFVHRMAQFDTDTFLDTLTTYpITTLC 318
Cdd:cd05937 110 RRTLVTSNLLSH-DLNLKNGDRTYTcmplYHGTAAFLGACNCLMSgGTLALSRKFSASQFWKDVRDSGATIIQY-VGELC 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 319 -----SPPTVYRmlvqkdlKRYKFKslrhcLTGGEPLNPEVLEQWRAQTGL-DLYEGYGQTE---------VGMICANQK 383
Cdd:cd05937 188 ryllsTPPSPYD-------RDHKVR-----VAWGNGLRPDIWERFRERFNVpEIGEFYAATEgvfaltnhnVGDFGAGAI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 384 GQEikpGSMGKGMLPYD---VQIIDENGNVL-----------PPGKEGEIALRLkPTRPFCFFSKYVDNPQKTAATI--- 446
Cdd:cd05937 256 GHH---GLIRRWKFENQvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrd 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 447 ---RGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAV--VSSPDQiRGEVVKAFVVL 520
Cdd:cd05937 332 vfrKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGH-DGRAGCAAITL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 114643324 521 AApfKSYNPEKLTLELQDHVKKSTAP-YKYPRKVEFVQELPKTITGKIKRNVLRDQEW 577
Cdd:cd05937 411 EE--SSAVPTEFTKSLLASLARKNLPsYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
222-569 |
1.90e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 56.70 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGR--YWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVH---- 295
Cdd:COG1541 84 EIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARslRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAgggn 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 296 -----RMAQFdtdtfldtlttYPITTLCSPPTVYRMLVQK------DLKRYKFKSLrhcLTGGEPLnpevLEQWRAQ--- 361
Cdd:COG1541 164 terqlRLMQD-----------FGPTVLVGTPSYLLYLAEVaeeegiDPRDLSLKKG---IFGGEPW----SEEMRKEiee 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 362 -TGLDLYEGYGQTEVGMI----CANQKGQEIKPGSMgkgmlpYdVQIID-ENGNVLPPGKEGEI---ALrlkptrpfcff 432
Cdd:COG1541 226 rWGIKAYDIYGLTEVGPGvayeCEAQDGLHIWEDHF------L-VEIIDpETGEPVPEGEEGELvvtTL----------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 433 skyvdnpQKTAA-TIRgdfYVTGDRGVMDSD----G------YFWFvGRADDVIISSGYRIGPFEVESALIEHPAVVES- 500
Cdd:COG1541 288 -------TKEAMpLIR---YRTGDLTRLLPEpcpcGrthpriGRIL-GRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEy 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114643324 501 -AVVSSP---DQIRgevVKafVVLAAPFksyNPEKLTLELQDHVKKSTapyKYPRKVEFVQ--ELPKTiTGKIKR 569
Cdd:COG1541 357 qIVVDREgglDELT---VR--VELAPGA---SLEALAEAIAAALKAVL---GLRAEVELVEpgSLPRS-EGKAKR 419
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-577 |
4.47e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 55.65 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 62 WSQkektgERPANPALwwvnGKGDEVkWSFRELGSLSRKAANMLTKPcGLQRGDRVAVILPPIPEWWLVNVACIRTGIIF 141
Cdd:PRK09029 12 WAQ-----VRPQAIAL----RLNDEV-LTWQQLCARIDQLAAGFAQQ-GVVEGSGVALRGKNSPETLLAYLALLQCGARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 142 MPGTIQLTAKDILYRLRASKAKCIVASEEVAPavesivlecPDLKTKLLVSPQSRNGWLSFQelfqfaseehscvetgSQ 221
Cdd:PRK09029 81 LPLNPQLPQPLLEELLPSLTLDFALVLEGENT---------FSALTSLHLQLVEGAHAVAWQ----------------PQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 222 EPMTIYFTSGTTGFPKMAQHS-----QSSLG----IGFTLCGRYWLDL-----KSSDIIWNmsdtgwvkaaigsvfssWL 287
Cdd:PRK09029 136 RLATMTLTSGSTGLPKAAVHTaqahlASAEGvlslMPFTAQDSWLLSLplfhvSGQGIVWR-----------------WL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 288 -CGACV-------FVHRMAQfdtdtfldtlttypiTTLCSpptvyrmLVQKDLKR---YKFK--SLRHCLTGGEPLNPEV 354
Cdd:PRK09029 199 yAGATLvvrdkqpLEQALAG---------------CTHAS-------LVPTQLWRlldNRSEplSLKAVLLGGAAIPVEL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 355 LEQWRAQtGLDLYEGYGQTEVG-MICAnqKGQEIKPGsmgkgmlpydvqiideNGNVLPpGKE-----GEIALRLKptrp 428
Cdd:PRK09029 257 TEQAEQQ-GIRCWCGYGLTEMAsTVCA--KRADGLAG----------------VGSPLP-GREvklvdGEIWLRGA---- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 429 fCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDsDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQ 508
Cdd:PRK09029 313 -SLALGYWRQGQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114643324 509 IRGEVVKAFVVLAAPFksyNPEKLTLELQDHVKKSTAPYKYPRkvefvqeLPKTI-TGKIK--RNVLrdQEW 577
Cdd:PRK09029 391 EFGQRPVAVVESDSEA---AVVNLAEWLQDKLARFQQPVAYYL-------LPPELkNGGIKisRQAL--KEW 450
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
229-497 |
3.79e-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: 52.63 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 229 TSGTTGFPKMAQHSQSSLgigftlcgRYWLDL----------KSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFvhRMA 298
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL--------DVWAELvarcldaagvTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVI--PAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 299 QFDTDTFLDTLTTYPITTLCSPPTVYRML---VQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTE- 374
Cdd:cd05913 156 GGNTERQLQLIKDFGPTVLCCTPSYALYLaeeAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEi 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 375 ----VGMICANQKGQEI-KPGsmgkgmlpYDVQIID-ENGNVLPPGKEGEIALRL--KPTRPFCFFS--KYVDNPQKTAA 444
Cdd:cd05913 236 igpgVAFECEEKDGLHIwEDH--------FIPEIIDpETGEPVPPGEVGELVFTTltKEAMPLIRYRtrDITRLLPGPCP 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 114643324 445 TIRgdFYVTGDRgvmdsdgyfwFVGRADDVIISSGYRIGPFEVESALIEHPAV 497
Cdd:cd05913 308 CGR--THRRIDR----------ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
335-566 |
4.00e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.18 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 335 YKFKSLRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTEVGMICANQKGQEIKPGSMGKgMLPydvqiiDENGNVLP-P 413
Cdd:PRK08043 476 YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGR-ILP------GMDARLLSvP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 414 GKEGEIALRLK-PTrpfcFFSKY--VDNP----QKTAATIRGD----FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRI 482
Cdd:PRK08043 549 GIEQGGRLQLKgPN----IMNGYlrVEKPgvleVPTAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMV 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 483 GPFEVES-ALIEHPAVVESAVVSSpDQIRGEVVKAFVVLAapfksynpeKLTLE-LQDHVKKSTAP-YKYPRKVEFVQEL 559
Cdd:PRK08043 625 SLEMVEQlALGVSPDKQHATAIKS-DASKGEALVLFTTDS---------ELTREkLQQYAREHGVPeLAVPRDIRYLKQL 694
|
....*..
gi 114643324 560 PKTITGK 566
Cdd:PRK08043 695 PLLGSGK 701
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
393-497 |
5.54e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 52.31 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 393 GKGMLPYDVQIIDENGNVLPPGKEGEIALRlKPTrpfcFFSKYVDNpQKTAATIRGDFYV-TGDRGVMdSDGYFWFVGRA 471
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRD-EESQDVLAADGWLdTGDLGYL-LDGYLYITGRA 460
|
90 100
....*....|....*....|....*.
gi 114643324 472 DDVIISSGYRIGPFEVESALIEHPAV 497
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEWIAEQEPEL 486
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
339-494 |
3.15e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.81 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 339 SLRHCLTGGEPLNPEVLEQ-WRAQTGLDLYEGYGQTEVG-MICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVlpPGKE 416
Cdd:PRK06334 300 SLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEETKV--PVSS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 417 GEIALRLkpTRPFCFFSKYVDN-PQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEH 494
Cdd:PRK06334 378 GETGLVL--TRGTSLFSGYLGEdFGQGFVELGGEtWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
32-553 |
4.10e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 49.76 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 32 PLTlADFEAINRCNRPLPKnfnFAADVLDQWSQKEKTGERPANPALWWVNGKGD-EVKWSF-----RELGSLSRKAANML 105
Cdd:cd17632 9 PLE-AVTEAIRRPGLRLAQ---IIATVMTGYADRPALGQRATELVTDPATGRTTlRLLPRFetityAELWERVGAVAAAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 106 TKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPgtiqLTAKDILYRLRA----SKAKCIVASEEVAPAVESIVLE 181
Cdd:cd17632 85 DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVP----LQAGASAAQLAPilaeTEPRLLAVSAEHLDLAVEAVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 182 C------------PDLKTKLLVSPQSRNGWLSFQELFQFASE-----------EHSCVETGSQEPMTIYFTSGTTGFPKM 238
Cdd:cd17632 161 GgtpprlvvfdhrPEVDAHRAALESARERLAAVGIPVTTLTLiavrgrdlppaPLFRPEPDDDPLALLIYTSGSTGTPKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 239 AQHSQSslgigftLCGRYWLDLKS-------SDIIWN---MSDTGWVKAAIGSVFSSwlcGACVFVhrMAQFDTDTFLDT 308
Cdd:cd17632 241 AMYTER-------LVATFWLKVSSiqdirppASITLNfmpMSHIAGRISLYGTLARG---GTAYFA--AASDMSTLFDDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 309 LTTYPiTTLCSPPTVYRMLVQK----------------DLKRYKFKSLRHCLTGGE---------PLNPEvLEQWRAQT- 362
Cdd:cd17632 309 ALVRP-TELFLVPRVCDMLFQRyqaeldrrsvagadaeTLAERVKAELRERVLGGRllaavcgsaPLSAE-MKAFMESLl 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 363 GLDLYEGYGQTEVGMICANqkGQEIKPGSMgkgmlpyDVQIID--ENGNVLP--PGKEGEiaLRLKPTRpfcFFSKYVDN 438
Cdd:cd17632 387 DLDLHDGYGSTEAGAVILD--GVIVRPPVL-------DYKLVDvpELGYFRTdrPHPRGE--LLVKTDT---LFPGYYKR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 439 PQKTAATIRGD-FYVTGDrgVMDSDG--YFWFVGRADDVIISSGyriGPFEVESALiehpavvESAVVSSPD--QI--RG 511
Cdd:cd17632 453 PEVTAEVFDEDgFYRTGD--VMAELGpdRLVYVDRRNNVLKLSQ---GEFVTVARL-------EAVFAASPLvrQIfvYG 520
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 114643324 512 EVVKAF---VVLAAP--FKSYNPEKLTLELQDHVKK-----STAPYKYPRKV 553
Cdd:cd17632 521 NSERAYllaVVVPTQdaLAGEDTARLRAALAESLQRiareaGLQSYEIPRDF 572
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
340-497 |
4.22e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.81 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLNPEVLEQWRAQTGLDLYEGYGQTE-VGMICANQKGQEIKPGSMGKGMLPYDVQI--IDENG-NVLPPGK 415
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTEtLGPTTLGFPDEMCMLGTVGAPAVYNELRLeeVPEMGyDPLGEPP 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 416 EGEIALRLKptrpfCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVI-ISSGYRIGPFEVESALIEH 494
Cdd:PLN02430 465 RGEICVRGK-----CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQN 539
|
...
gi 114643324 495 PAV 497
Cdd:PLN02430 540 PIV 542
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
339-569 |
1.08e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.22 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 339 SLRHCLTGGEPLNPEVLEQWRAQT---GLD---LYEGYGQTEVgmICAnqkgqeIKPGSMGKGMLPYDVQIIDENGN--- 409
Cdd:PRK05851 273 ALRVALNGGEPVDCDGFERFATAMapfGFDagaAAPSYGLAES--TCA------VTVPVPGIGLRVDEVTTDDGSGArrh 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 410 -VLP---PGKEGEIALRLKPT------------RPFCFFSKYVDnpqktAATIR-GDFYVTGDRGVMdSDGYFWFVGRAD 472
Cdd:PRK05851 345 aVLGnpiPGMEVRISPGDGAAgvagreigeieiRGASMMSGYLG-----QAPIDpDDWFPTGDLGYL-VDGGLVVCGRAK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 473 DVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGevVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTApyKYPRK 552
Cdd:PRK05851 419 ELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSD 494
|
250
....*....|....*....
gi 114643324 553 VEFVQ--ELPKTITGKIKR 569
Cdd:PRK05851 495 VVFVApgSLPRTSSGKLRR 513
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-573 |
2.16e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALWWVNGKGDE-VKWSFRELGSLSRKAANMLTKPCGLqrGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQLTA 150
Cdd:PRK05691 23 PDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 151 KdilyRLRASKAKCIVASEEvapavesivlecPDLktkLLVSPQSRNGWLSFQELFQFASEEHSCVET-------GSQEP 223
Cdd:PRK05691 101 R----RHHQERLLSIIADAE------------PRL---LLTVADLRDSLLQMEELAAANAPELLCVDTldpalaeAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 224 MT-------IYFTSGTTGFPKMAQHSQSSLGIGFTLCGR-YWLDLKSSDII--W--NMSDTGWVKAAIGSVFSSWLC--- 288
Cdd:PRK05691 162 ALqpddiafLQYTSGSTALPKGVQVSHGNLVANEQLIRHgFGIDLNPDDVIvsWlpLYHDMGLIGGLLQPIFSGVPCvlm 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 289 GACVFVHRMAQfdtdtFLDTLTTYPITTLCSPPTVYRMLVQK----DLKRYKFKSLRHCLTGGEPLNPEVLEQWR---AQ 361
Cdd:PRK05691 242 SPAYFLERPLR-----WLEAISEYGGTISGGPDFAYRLCSERvsesALERLDLSRWRVAYSGSEPIRQDSLERFAekfAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 362 TGLD---LYEGYGQTEVGMICA-NQKGQEI---------------KPG------SMGKGMLPYDVQIID-ENGNVLPPGK 415
Cdd:PRK05691 317 CGFDpdsFFASYGLAEATLFVSgGRRGQGIpaleldaealarnraEPGtgsvlmSCGRSQPGHAVLIVDpQSLEVLGDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 416 EGEIaLRLKPTrpfcFFSKYVDNPQKTAATI---RGDFYV-TGDRGVMdSDGYFWFVGRADDVIISSGYRIGPFEVESal 491
Cdd:PRK05691 397 VGEI-WASGPS----IAHGYWRNPEASAKTFvehDGRTWLrTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 492 iehpaVVESAVvsspDQIRGEVVKAFVVlaapfkSYNPEK---LTLELQDHVKKSTAP---YKYPRKV--EFVQE----- 558
Cdd:PRK05691 469 -----TVEREV----EVVRKGRVAAFAV------NHQGEEgigIAAEISRSVQKILPPqalIKSIRQAvaEACQEapsvv 533
|
570 580
....*....|....*....|..
gi 114643324 559 -------LPKTITGKIKRNVLR 573
Cdd:PRK05691 534 lllnpgaLPKTSSGKLQRSACR 555
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
446-572 |
1.48e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 446 IRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVV------ 519
Cdd:cd17647 369 PRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVprfdkp 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114643324 520 --------LAAPFKSYNP--------EKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVL 572
Cdd:cd17647 449 ddesfaqeDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
72-246 |
1.09e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 41.93 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 72 PANPALW---WVNGKGDEVKW-SFRELGSLSRKAANMLtKPCGLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPGTIQ 147
Cdd:PLN02614 59 PNNPMLGrreIVDGKPGKYVWqTYQEVYDIVIKLGNSL-RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 148 LTAKDILYRLRASKAKCIVASEEVAPaveSIVLECPD----LKTKLL---VSPQSRNGWLSFQeLFQFASEEHSCVETGS 220
Cdd:PLN02614 138 LGAGAVEFIISHSEVSIVFVEEKKIS---ELFKTCPNsteyMKTVVSfggVSREQKEEAETFG-LVIYAWDEFLKLGEGK 213
|
170 180 190
....*....|....*....|....*....|....*
gi 114643324 221 QEPM---------TIYFTSGTTGFPKMAQHSQSSL 246
Cdd:PLN02614 214 QYDLpikkksdicTIMYTSGTTGDPKGVMISNESI 248
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
110-246 |
2.08e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 40.85 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 110 GLQRGDRVAVILPPIPEWWLVNVACIRTGIIFMPgtiqltakdiLY-RLRASKAKCIVASEEVA-----PAVESIVL--- 180
Cdd:PLN02736 99 GIPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVAaifcvPQTLNTLLscl 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114643324 181 -ECPDLK--------TKLLVSPQSRNG--WLSFQELF-QFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSL 246
Cdd:PLN02736 169 sEIPSVRlivvvggaDEPLPSLPSGTGveIVTYSKLLaQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNL 246
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
340-470 |
5.65e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.57 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114643324 340 LRHCLTGGEPLNPEVLEQWRAQTGLdLYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQI--IDENGNVLPPGKEG 417
Cdd:PTZ00216 430 VRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLldTEEYKHTDTPEPRG 508
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 114643324 418 EIALRlkptRPFcFFSKYVDNPQKTAATIRGD-FYVTGDRGVMDSDGYFWFVGR 470
Cdd:PTZ00216 509 EILLR----GPF-LFKGYYKQEELTREVLDEDgWFHTGDVGSIAANGTLRIIGR 557
|
|
| |
