|
Name |
Accession |
Description |
Interval |
E-value |
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1-628 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 1319.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 1 MSFSEFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEE 80
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTETDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIV 160
Cdd:PRK10524 82 ERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVPVAWLESNETSCILYT 240
Cdd:PRK10524 162 SADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARVPVEWLESNEPSYILYT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWT 320
Cdd:PRK10524 242 SGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 321 IVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIAR 400
Cdd:PRK10524 322 IVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPILAIAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 401 GLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWG 480
Cdd:PRK10524 402 GVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFGRQVYSTFDWG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 481 IRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEK 560
Cdd:PRK10524 482 IRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 561 AIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLDQIRQAMEE 628
Cdd:PRK10524 562 EIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALEE 629
|
|
| propion_prpE |
TIGR02316 |
propionate--CoA ligase; This family contains one of three readily separable clades of proteins ... |
1-628 |
0e+00 |
|
propionate--CoA ligase; This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate.
Pssm-ID: 131369 [Multi-domain] Cd Length: 628 Bit Score: 1257.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 1 MSFSEFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEE 80
Cdd:TIGR02316 1 MRYEEFYQRSIEQPEAFWAEQARRIDWQTPPQRILDYSNPPFARWFAGGRTNLCHNALDRHLDERGEQLALVTVSSETGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIV 160
Cdd:TIGR02316 81 ERTLTYRQLHREVNVFASALRALGVGRGDRVLIYMPMIAEAVFAMLACARIGAIHSVVFGGFASHSLALRIDDATPKLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVPVAWLESNETSCILYT 240
Cdd:TIGR02316 161 SADAGMRGGKVIPYKPLLDAAIAEAQHPPPHVLLVDRGLAPMRLIPGRDVDYAALRTQHEDAQVPVEWLESNEPSYILYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWT 320
Cdd:TIGR02316 241 SGTTGKPKGVQRDVGGYAVALALSMWAIFGIRAGQVMFSASDVGWVVGHSYIVYAPLLAGAATVLYEGLPTNPDPGVWWS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 321 IVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIAR 400
Cdd:TIGR02316 321 IVERYGVRTMFSAPTAIRVLKKQDAAWLRKHDLSSLHWLFLAGEPLDEPTAHWITDGLGKPVIDNYWQTETGWPVLAIMP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 401 GLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWG 480
Cdd:TIGR02316 401 GLDLKPVKLGSPGLPMYGYHLRVLDEATGRPCGPNEKGVLTVVPPLPPGCLSTVWGDDARFLKTYWSHFKRPLYSSFDWG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 481 IRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEK 560
Cdd:TIGR02316 481 IRDEDGYTFILGRTDDVINVAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKESDSAGDAHDPHAVET 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 561 AIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLDQIRQAMEE 628
Cdd:TIGR02316 561 GMMDCVVRQLGAVARPARVYFVAALPKTRSGKLLRRSIQALAEGRDPGDLTTIDDPGALEQVRRAMER 628
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
3-622 |
0e+00 |
|
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: 1024.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 3 FSEFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEK-QPEALALIAVSSETEEE 81
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAgRGDQIALIYDSPVTGTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVS 161
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARV-SGRDVDFASLRHQHIgaRVPVAWLESNETSCILYT 240
Cdd:cd05967 161 ASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTkPGRDLDWSELLAKAE--PVDCVPVAATDPLYILYT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPT-WPDCGVWW 319
Cdd:cd05967 239 SGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 320 TIVEKYQVSRMFSAPTAIRVLKKFPTAE--IRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMA 397
Cdd:cd05967 319 RVIEKYQVNALFTAPTAIRAIRKEDPDGkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 398 IARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKTYWSLFsRPVYATF 477
Cdd:cd05967 399 NPVGLEPLPIKAGSPGKPVPGYQVQVLDE-DGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKF-PGYYDTG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 478 DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSledrDVAHS 557
Cdd:cd05967 477 DAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVK----ITAEE 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 558 QEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLDQI 622
Cdd:cd05967 553 LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
44-624 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 695.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 44 RWFCEGRTNLCHNAIDRWLEKQPEALALIAVSsETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHI 123
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 124 TLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIPYKKLLDDAISQAQHqPRHVLLVDRGLAKmA 203
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS-LEHVIVVGRTGAD-V 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 204 RVSGrDVDFASLRHQHiGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDI 283
Cdd:COG0365 158 PMEG-DLDWDELLAAA-SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 284 GWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAG 363
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 364 EPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIARGLddrPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVE 443
Cdd:COG0365 316 EPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGL---PVKPGSMGKPVPGYDVAVVDE-DGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 GPLpPGCIQTIWGDDGRFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEV 523
Cdd:COG0365 392 GPW-PGMFRGYWNDPERYRETYFGRFPG-WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 524 AVVGVKDALKGQVAVAFVIPKESDSLEDRDVahsqeKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICE 603
Cdd:COG0365 470 AVVGVPDEIRGQVVKAFVVLKPGVEPSDELA-----KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
570 580
....*....|....*....|.
gi 16128320 604 GRDPGDLTTIDDPASLDQIRQ 624
Cdd:COG0365 545 GRPLGDTSTLEDPEALDEIKE 565
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
5-615 |
0e+00 |
|
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: 672.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 5 EFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHS-NPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEEERT 83
Cdd:cd05966 5 ELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSkGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPDQSRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSAD 163
Cdd:cd05966 85 ITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 AGARGGKIIPYKKLLDDAISQAqHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIgARVPVAWLESNETSCILYTSGT 243
Cdd:cd05966 165 GGYRGGKVIPLKEIVDEALEKC-PSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQS-PECEPEWMDSEDPLFILYTSGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 244 TGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIVE 323
Cdd:cd05966 243 TGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 324 KYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL---DVPVIDNYWQTESGWPIMAIAR 400
Cdd:cd05966 323 KHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIgkeRCPIVDTWWQTETGGIMITPLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 401 GLddRPTRLGSPGVPMYGYNVQLLNEVtGEPCGVNEKGMLVVEGPLpPGCIQTIWGDDGRFVKTYWSLFSrPVYATFDWG 480
Cdd:cd05966 403 GA--TPLKPGSATRPFFGIEPAILDEE-GNEVEGEVEGYLVIKRPW-PGMARTIYGDHERYEDTYFSKFP-GYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 481 IRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDvahsqEK 560
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDEL-----RK 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 561 AIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDP-GDLTTIDD 615
Cdd:cd05966 553 ELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEElGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
5-625 |
0e+00 |
|
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: 660.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 5 EFYQRSINEPEQFWAEQARR-IDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEEERT 83
Cdd:TIGR02188 9 ELYEESIEDPDKFWAKLARElLDWFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEGDEPGEVRK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSAD 163
Cdd:TIGR02188 89 ITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 AGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDR-GLAKMARVSGRDVDFASLRhQHIGARVPVAWLESNETSCILYTSG 242
Cdd:TIGR02188 169 EGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRtGNPVVPWVEGRDVWWHDLM-AKASAYCEPEPMDSEDPLFILYTSG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 243 TTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIV 322
Cdd:TIGR02188 248 STGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEII 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 323 EKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDePTAsW------VSNTlDVPVIDNYWQTESGWPIM 396
Cdd:TIGR02188 328 EKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPIN-PEA-WmwyykvVGKE-RCPIVDTWWQTETGGIMI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 AIARGLddRPTRLGSPGVPMYGYNVQLLNEvTGEPC-GVNEKGMLVVEGPLpPGCIQTIWGDDGRFVKTYWSLFsRPVYA 475
Cdd:TIGR02188 405 TPLPGA--TPTKPGSATLPFFGIEPAVVDE-EGNPVeGPGEGGYLVIKQPW-PGMLRTIYGDHERFVDTYFSPF-PGYYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 476 TFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRdva 555
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE--- 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 556 hsQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDP--GDLTTIDDPASLDQIRQA 625
Cdd:TIGR02188 557 --LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEilGDTSTLEDPSVVEELIEA 626
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
5-628 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 657.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 5 EFYQRSINEPEQFWAEQARRIDWQTPFTQTLDhSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEEERTF 84
Cdd:PRK00174 21 ALYQESVEDPEGFWAEQAKRLDWFKPFDTVLD-WNAPFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGDSRKI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADA 164
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 165 GARGGKIIPYKKLLDDAISQAQHQpRHVLLVDRGLAKMARVSGRDVDFASLRhQHIGARVPVAWLESNETSCILYTSGTT 244
Cdd:PRK00174 180 GVRGGKPIPLKANVDEALANCPSV-EKVIVVRRTGGDVDWVEGRDLWWHELV-AGASDECEPEPMDAEDPLFILYTSGST 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 245 GKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIVEK 324
Cdd:PRK00174 258 GKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 325 YQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDePTA-SWVSNTL---DVPVIDNYWQTESGwPIM---- 396
Cdd:PRK00174 338 HKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPIN-PEAwEWYYKVVggeRCPIVDTWWQTETG-GIMitpl 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 --AIarglddrPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLpPGCIQTIWGDDGRFVKTYWSLFsRPVY 474
Cdd:PRK00174 416 pgAT-------PLKPGSATRPLPGIQPAVVDE-EGNPLEGGEGGNLVIKDPW-PGMMRTIYGDHERFVKTYFSTF-KGMY 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 475 ATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDV 554
Cdd:PRK00174 486 FTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELR 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 555 ahsqeKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDP-GDLTTIDDPASLDQIRQAMEE 628
Cdd:PRK00174 566 -----KELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEIlGDTSTLADPSVVEKLIEARQN 635
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3-594 |
0e+00 |
|
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: 557.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 3 FSEFYQRSINEPEQFWAEQARRIDWQTPFTQ---TLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETE 79
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKvknTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 80 EERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLI 159
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 VSADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVPVAwLESNETSCILY 239
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEA-MNAEDPLFILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWW 319
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 320 TIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLD---VPVIDNYWQTESGWPIM 396
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 AIARGLDdrPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCiQTIWGDDGRFVKTYWSLFsRPVYAT 476
Cdd:cd17634 400 TPLPGAI--ELKAGSATRPVFGVQPAVVDN-EGHPQPGGTEGNLVITDPWPGQT-RTLFGDHERFEQTYFSTF-KGMYFS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 477 FDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVI--PKESDSLEDRDv 554
Cdd:cd17634 475 GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVlnHGVEPSPELYA- 553
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 16128320 555 ahsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKML 594
Cdd:cd17634 554 ------ELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
3-622 |
1.01e-140 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 424.70 E-value: 1.01e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 3 FSEFYQRSINEPEQFWAEQARRIDW------QTPFTQTLDHSNPPFA-RWFCEGRTNLCHNAIDRWLEK-QPEALALIAV 74
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDIASQFYWkqkwegDEVCSENLDVRKGPISiEWFKGGKTNICYNCLDRNVEAgNGDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 75 SSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDA 154
Cdd:PLN02654 112 GNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 155 KPVLIVSADAGARGGKIIPYKKLLDDAISQAQHQPRHV---LLVDRGLAkMARVS-----GRDV---DFASlrhqHIGAR 223
Cdd:PLN02654 192 KPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVgicLTYENQLA-MKREDtkwqeGRDVwwqDVVP----NYPTK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 VPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMAT 303
Cdd:PLN02654 267 CEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 304 IVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLD---V 380
Cdd:PLN02654 347 LVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrC 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 381 PVIDNYWQTESGWPIMAIARGLddRPTRLGSPGVPMYGYNVQLL----NEVTGEpCgvneKGMLVVEGPLpPGCIQTIWG 456
Cdd:PLN02654 427 PISDTWWQTETGGFMITPLPGA--WPQKPGSATFPFFGVQPVIVdekgKEIEGE-C----SGYLCVKKSW-PGAFRTLYG 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 457 DDGRFVKTYWSLFSrPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQV 536
Cdd:PLN02654 499 DHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQG 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 537 AVAFVIPKESdsledrdVAHSQE--KAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGR--DPGDLTT 612
Cdd:PLN02654 578 IYAFVTLVEG-------VPYSEElrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQldELGDTST 650
|
650
....*....|
gi 16128320 613 IDDPASLDQI 622
Cdd:PLN02654 651 LADPGVVDQL 660
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2-616 |
1.71e-129 |
|
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: 393.78 E-value: 1.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 2 SFSEFYQRSINEPEQFWAEQARRID--WQTPFTQTLDHSN-PPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAvSSET 78
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLSGgKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRW-EGED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVL 158
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 159 IVSADAGARGGKIIPYKKLLDDAISQAQhQPRHVLLVDRGLAKMARVSGRDVDFASlrhQHIGARVPVAWLESNETSCIL 238
Cdd:cd05968 167 LITADGFTRRGREVNLKEEADKACAQCP-TVEKVVVVRHLGNDFTPAKGRDLSYDE---EKETAGDGAERTESEDPLMII 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGhSYIVYAPLLAGMATIVYEGLPTWPDCGVW 318
Cdd:cd05968 243 YTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 WTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL---DVPVIDNYWQTE-SGwp 394
Cdd:cd05968 322 WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgRNPIINYSGGTEiSG-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 395 imAIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCgVNEKGMLVVEGPLpPGCIQTIWGDDGRFVKTYWSLFSRpVY 474
Cdd:cd05968 400 --GILGNVLIKPIKPSSFNGPVPGMKADVLDE-SGKPA-RPEVGELVLLAPW-PGMTRGFWRDEDRYLETYWSRFDN-VW 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 475 ATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKesdslEDRDV 554
Cdd:cd05968 474 VHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLK-----PGVTP 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 555 AHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDP 616
Cdd:cd05968 549 TEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
45-615 |
6.65e-87 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 281.78 E-value: 6.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 45 WFCEGRTNLCHNAIDRWLEK-QPEALALIAVSSETEEerTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHI 123
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGgRKDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 124 TLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAgarggkiipykkLLDDAISQAQHQPRHVLLVDRGlakmA 203
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPA------------LLERKPADDLPSLKHVLLVGED----V 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 204 RVSGRDVDFASLRHQHiGARVPVAWLESNETSCILYTSGTTGKPKGV---------QRDVGGYAVALatsmdtifggKAG 274
Cdd:PRK04319 178 EEGPGTLDFNALMEQA-SDEFDIEWTDREDGAILHYTSGSTGKPKGVlhvhnamlqHYQTGKYVLDL----------HED 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 275 SVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPtwpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLS 354
Cdd:PRK04319 247 DVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 355 SLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIARGLDDRPtrlGSPGVPMYGYNVQLLNEVTGEPcGV 434
Cdd:PRK04319 324 SLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPAMDIKP---GSMGKPLPGIEAAIVDDQGNEL-PP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 435 NEKGMLVVEGPLPpGCIQTIWGDDGRfvktYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESI 514
Cdd:PRK04319 400 NRMGNLAIKKGWP-SMMRGIWNNPEK----YESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 515 SSHPGVAEVAVVGVKDALKGQVAVAFVIPKE----SDSLedrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRS 590
Cdd:PRK04319 475 MEHPAVAEAGVIGKPDPVRGEIIKAFVALRPgyepSEEL---------KEEIRGFVKKGLGAHAAPREIEFKDKLPKTRS 545
|
570 580
....*....|....*....|....*
gi 16128320 591 GKMLRRTIQAICEGRDPGDLTTIDD 615
Cdd:PRK04319 546 GKIMRRVLKAWELGLPEGDLSTMED 570
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
58-501 |
1.05e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 273.80 E-value: 1.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQPEALALiavssETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSV 137
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 138 VFGGFASHSVAARIDDAKPVLIVSADAgarggkiipYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRH 217
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA---------LKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 218 qhigarVPVAWLESNETSCILYTSGTTGKPKGVQRDVgGYAVALATSM----DTIFGGKAGSVFFCASDIGWVVGHSYIV 293
Cdd:pfam00501 147 ------PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 294 YAPLLAGMATIVYEGLPTWPDCGvWWTIVEKYQVSRMFSAPTAIRVLkkFPTAEIRKHDLSSLEVLYLAGEPLDEPTASW 373
Cdd:pfam00501 220 LGPLLAGATVVLPPGFPALDPAA-LLELIERYKVTVLYGVPTLLNML--LEAGAPKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 374 VSNTLDVPVIDNYWQTESGwPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGplpPGCIQT 453
Cdd:pfam00501 297 FRELFGGALVNGYGLTETT-GVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG---PGVMKG 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128320 454 IWGDDGRFVKTYWslfSRPVYATFDWGIRDADGYHFILGRTDDVINVA 501
Cdd:pfam00501 373 YLNDPELTAEAFD---EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
84-601 |
8.89e-84 |
|
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: 269.76 E-value: 8.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARID--DAKpVLIVS 161
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLEnsEAK-VLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADagarggkiipykkllddaisqaqhqprhvlLVDRglakmarvsgrdvdfaslrhqhigarvpvawLESNETSCILYTS 241
Cdd:cd05969 80 EE------------------------------LYER-------------------------------TDPEDPTLLHYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 242 GTTGKPKGV---QRDVGGYAVALATSMDTifggKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPtwpDCGVW 318
Cdd:cd05969 99 GTTGTPKGVlhvHDAMIFYYFTGKYVLDL----HPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAESW 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 WTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAI 398
Cdd:cd05969 172 YGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIAN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 399 ARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEgPLPPGCIQTIWGDDGRFVKTywslFSRPVYATFD 478
Cdd:cd05969 252 YPCMPIKP---GSMGKPLPGVKAAVVDE-NGNELPPGTKGILALK-PGWPSMFRGIWNDEERYKNS----FIDGWYLTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 479 WGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKE----SDSLEDRDV 554
Cdd:cd05969 323 LAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEgfepSDELKEEII 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16128320 555 AHSQEKAIMALVdsqignfgrPAHVWFVSQLPKTRSGKMLRRTIQAI 601
Cdd:cd05969 403 NFVRQKLGAHVA---------PREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
55-600 |
1.56e-83 |
|
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: 269.37 E-value: 1.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:COG0318 2 ADLLRRAAARHPDRPALV------FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HSVVFGGFASHSVAARIDDAKPVLIVSAdagarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfas 214
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVTA---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 lrhqhigarvpvawlesnetsCILYTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVY 294
Cdd:COG0318 104 ---------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 APLLAGmATIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLYLAGEPLDEPTASWV 374
Cdd:COG0318 162 APLLAG-ATLV---LLPRFDPERVLELIERERVTVLFGVPTMLARLLRHP--EFARYDLSSLRLVVSGGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTLDVPVIDNYWQTESGWPIMAiaRGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGciqt 453
Cdd:COG0318 236 EERFGVRIVEGYGLTETSPVVTV--NPEDPGERRPGSVGRPLPGVEVRIVDE-DGRELPPGEVGEIVVRGPnVMKG---- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 454 IWGDDGRFVKTywslFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALK 533
Cdd:COG0318 309 YWNDPEATAEA----FRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 534 GQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:COG0318 385 GERVVAFVVLRPGAELD--------AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
84-600 |
7.04e-79 |
|
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: 256.50 E-value: 7.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSad 163
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 agarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfaslrhqhigarvpvawlESNETSCILYTSGT 243
Cdd:cd05972 79 ------------------------------------------------------------------DAEDPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 244 TGKPKGVQRDVGgYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDcgVWWTIVE 323
Cdd:cd05972 93 TGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAE--RILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 324 KYQVSRMFSAPTAIRVLKKfptAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPImAIARGLD 403
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIK---QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTV-GNFPDMP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 404 DRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlPPGCIQTIWGDDGRFVKTywslFSRPVYATFDWGIRD 483
Cdd:cd05972 246 VKP---GSMGRPTPGYDVAIIDD-DGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEAS----IRGDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 484 ADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVahsqeKAIM 563
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELA-----EELQ 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 16128320 564 ALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:cd05972 392 GHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
7-598 |
8.26e-73 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 246.58 E-value: 8.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 7 YQRSINEPEQFWAEQARR-IDWQTPFTQTLDhSNPPFARWFCEGRTNLCHNAIDRWLeKQP---EALALIAVSSETEEER 82
Cdd:PTZ00237 14 SNYANSNPESFWDEVAKKyVHWDKMYDKVYS-GDEIYPDWFKGGELNTCYNVLDIHV-KNPlkrDQDALIYECPYLKKTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSA 162
Cdd:PTZ00237 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 DAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLakmarvsgrDVDFASLRHQHIGARVP--VAW------------ 228
Cdd:PTZ00237 172 NYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRND---------ITSESDLKKIETIPTIPntLSWydeikkikennq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 229 --------LESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIvYAPLLAG 300
Cdd:PTZ00237 243 spfyeyvpVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 MATIVYEGLPTWPDC--GVWWTIVEKYQVSRMFSAPTAIRVLKKF-PTAEI--RKHDLSSLEVLYLAGEPLDEPTASWVS 375
Cdd:PTZ00237 322 NTFVMFEGGIIKNKHieDDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATIirSKYDLSNLKEIWCGGEVIEESIPEYIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 376 NTLDVPVIDNYWQTESGwpiMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCIQTIW 455
Cdd:PTZ00237 402 NKLKIKSSRGYGQTEIG---ITYLYCYGHINIPYNATGVPSIFIKPSILSE-DGKELNVNEIGEVAFKLPMPPSFATTFY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 GDDGRFVKtywsLFSR--PVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALK 533
Cdd:PTZ00237 478 KNDEKFKQ----LFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDC 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 534 GQVAVAFVIPKESDSLEDRDVAHSQEKaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:PTZ00237 554 YNVPIGLLVLKQDQSNQSIDLNKLKNE-INNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
237-592 |
1.34e-63 |
|
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: 213.30 E-value: 1.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGVQRDVGGYaVALATSMDTIFGGKAGSVFFCASDIGWVvGHSYIVYAPLLAGMATIVYEGlptwPDCG 316
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK----FDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 317 VWWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIM 396
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAP--ESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 AIARGLDDRptRLGSPGVPMYGYNVQLLNEVTGEpCGVNEKGMLVVEGPLPpgcIQTIWGDDGRfvktyWSLFSRP-VYA 475
Cdd:cd04433 157 TGPPDDDAR--KPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSV---MKGYWNNPEA-----TAAVDEDgWYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 476 TFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdva 555
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLD----- 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 16128320 556 hsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:cd04433 301 ---AEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
2-628 |
1.95e-61 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 215.81 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 2 SFSEFYQRSINEPEQFWAEQAR--RIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIdRWleKQPEALALIAVSsETE 79
Cdd:PRK03584 35 DYAALWRWSVEDLEAFWQSVWDffGVIGSTPYTVVLAGRRMPGARWFPGARLNYAENLL-RH--RRDDRPAIIFRG-EDG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 80 EERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLI 159
Cdd:PRK03584 111 PRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 VSADAGARGGKIIPykklLDDAISQ-AQHQP--RHVLLVDR-GLAKMARVSGRDVDFASLRHQHIGARVPVAWLESNETS 235
Cdd:PRK03584 191 IAVDGYRYGGKAFD----RRAKVAElRAALPslEHVVVVPYlGPAAAAAALPGALLWEDFLAPAEAAELEFEPVPFDHPL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 236 CILYTSGTTGKPKGVQRDVGG----YAVALATSMDTifggKAGSVFFCASDIGW------VVGhsyivyapLLAGmATIV 305
Cdd:PRK03584 267 WILYSSGTTGLPKCIVHGHGGilleHLKELGLHCDL----GPGDRFFWYTTCGWmmwnwlVSG--------LLVG-ATLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 306 -YEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL--DVPv 382
Cdd:PRK03584 334 lYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVkaDVW- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 383 idnyWQTESGW-----------PIMAIARGlddrptRLGSPGVpmyGYNVQLLNEvTGEPCgVNEKGMLVVEGPLP--PG 449
Cdd:PRK03584 413 ----LASISGGtdicscfvggnPLLPVYRG------EIQCRGL---GMAVEAWDE-DGRPV-VGEVGELVCTKPFPsmPL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 450 CiqtIWGDDG--RFVKTYWSLFSrPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREI----------EESISSH 517
Cdd:PRK03584 478 G---FWNDPDgsRYRDAYFDTFP-GVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIyrqvealpevLDSLVIG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 518 pgvaevavvgvKDALKGQVAVA-FVIPKESDSLEDrdvahsqekAIMALVDSQIgnfgR--------PAHVWFVSQLPKT 588
Cdd:PRK03584 554 -----------QEWPDGDVRMPlFVVLAEGVTLDD---------ALRARIRTTI----RtnlsprhvPDKIIAVPDIPRT 609
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 16128320 589 RSGKMLRRTIQAICEGRDPGD---LTTIDDPASLDQIRQAMEE 628
Cdd:PRK03584 610 LSGKKVELPVKKLLHGRPVKKavnRDALANPEALDWFADLAEL 652
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-620 |
3.90e-60 |
|
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: 211.75 E-value: 3.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 2 SFSEFYQRSINEPEQFWAEQAR--RIDWQTPFTQTLDHSNP-PFARWFCEGRTNLCHNAIDRwlEKQPEALALIAvsSET 78
Cdd:cd05943 18 DYAALHRWSVDDPGAFWAAVWDfsGVRGSKPYDVVVVSGRImPGARWFPGARLNYAENLLRH--ADADDPAAIYA--AED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVL 158
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 159 IVSADAGARGGKIIPykklLDDAISQAQHQ---PRHVLLVDRGLAKM---ARVSGRDVDFASLRHQHIGARVPVAWLESN 232
Cdd:cd05943 174 LFAVDAYTYNGKRHD----VREKVAELVKGlpsLLAVVVVPYTVAAGqpdLSKIAKALTLEDFLATGAAGELEFEPLPFD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 233 ETSCILYTSGTTGKPKGVQRDVGGY------AVALATSMdtifggKAGSVFFCASDIGWVVGHSYIvyAPLLAGmATIV- 305
Cdd:cd05943 250 HPLYILYSSGTTGLPKCIVHGAGGTllqhlkEHILHCDL------RPGDRLFYYTTCGWMMWNWLV--SGLAVG-ATIVl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 306 YEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL--DVPvi 383
Cdd:cd05943 321 YDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIkpDVL-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 384 dnyWQTESGWP--IMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCgVNEKGMLVVEGPLPPGCIQtIWGD-DG- 459
Cdd:cd05943 399 ---LASISGGTdiISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDE-EGKPV-WGEKGELVCTKPFPSMPVG-FWNDpDGs 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RFVKTYWSLFSrPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPgvaevavvgvkdalkgQVAVA 539
Cdd:cd05943 473 RYRAAYFAKYP-GVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIP----------------EVEDS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 540 FVIPKESDSLEDRDV-------AHSQEKAIMALVDSQIGNFGRPAHV----WFVSQLPKTRSGKMLRRTIQAICEGRDPG 608
Cdd:cd05943 536 LVVGQEWKDGDERVIlfvklreGVELDDELRKRIRSTIRSALSPRHVpakiIAVPDIPRTLSGKKVEVAVKKIIAGRPVK 615
|
650
....*....|..
gi 16128320 609 DLTTIDDPASLD 620
Cdd:cd05943 616 NAGALANPESLD 627
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-595 |
2.86e-59 |
|
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: 204.67 E-value: 2.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARID--DAKpVLIVS 161
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRtsGAR-LVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADAgarggkiipykkllddaisqaqhqpRHVLlvDRGLAKMarvsgrdvdfaslrhqhigarvpvawlesnetsciLYTS 241
Cdd:cd05973 80 AAN-------------------------RHKL--DSDPFVM-----------------------------------MFTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 242 GTTGKPKGVQRDVGgYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCgvwWTI 321
Cdd:cd05973 98 GTTGLPKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVEST---WRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 322 VEKYQVSRMFSAPTAIRVLKKFPtAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPImAIARG 401
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL-ANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 402 LDdRPTRLGSPGVPMYGYNVQLLNEVTGEPcGVNEKGMLVVEGPLPPgciqTIWgddgrfVKTYWSL----FSRPVYATF 477
Cdd:cd05973 252 LE-HPVHAGSAGRAMPGWRVAVLDDDGDEL-GPGEPGRLAIDIANSP----LMW------FRGYQLPdtpaIDGGYYLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 478 DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESdsledRDVAHS 557
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG-----HEGTPA 394
|
490 500 510
....*....|....*....|....*....|....*...
gi 16128320 558 QEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-600 |
2.08e-57 |
|
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: 199.97 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYM---PMIAEAHITLLacaRIGAIHSVVFGGFASHSVAARIddakpvliv 160
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLsqgPECAIAHIAIL---RSGAIAVPLFALFGPEALEYRL--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 sADAGARggkiipykkllddaisqaqhqprhVLLVDrglakmarvsgrdvdfaslrhqhigarvpvawlESNETSCILYT 240
Cdd:cd05971 75 -SNSGAS------------------------ALVTD---------------------------------GSDDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGV---QRDVGGYAVALATSMDtiFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEglPTWPDCGV 317
Cdd:cd05971 97 SGTTGPPKGAlhaHRVLLGHLPGVQFPFN--LFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHR--MTKFDPKA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 318 WWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGwpiMA 397
Cdd:cd05971 173 ALDLMSRYGVTTAFLPPTALKMMRQQG--EQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECN---LV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 398 IARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCIqTIWGDDGRFVKTYWSLFSRpvyaTF 477
Cdd:cd05971 248 IGNCSALFPIKPGSMGKPIPGHRVAIVDD-NGTPLPPGEVGEIAVELPDPVAFL-GYWNNPSATEKKMAGDWLL----TG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 478 DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDrdvahS 557
Cdd:cd05971 322 DLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD-----A 396
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 16128320 558 QEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:cd05971 397 LAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
52-599 |
4.40e-51 |
|
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: 185.01 E-value: 4.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 52 NLCHNAIDRWLEKQPEALALIAVSSETEEeRTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARI 131
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKLALVWCDDAGEE-RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 132 GAIHSVVFGGFASHSVAARIDDAKPVLIVSADagargGKIIPykKLLDDAISQAQHQPRHVLL----------VDRGLAK 201
Cdd:cd05970 96 GAIAIPATHQLTAKDIVYRIESADIKMIVAIA-----EDNIP--EEIEKAAPECPSKPKLVWVgdpvpegwidFRKLIKN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 202 MARVSGRDVDFASlrhqhigarvpvawlESNETSCILY-TSGTTGKPKGVQRDVGGYAVALATSM---DTifggKAGSVF 277
Cdd:cd05970 169 ASPDFERPTANSY---------------PCGEDILLVYfSSGTTGMPKMVEHDFTYPLGHIVTAKywqNV----REGGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 278 FCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVwwTIVEKYQVSRMFSAPTAIRVLKKfptAEIRKHDLSSLE 357
Cdd:cd05970 230 LTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALL--EKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 358 VLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPImAIARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEK 437
Cdd:cd05970 305 YCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTI-ATFPWMEPKP---GSMGKPAPGYEIDLIDR-EGRSCEAGEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVV---EGpLPPGCIQTIWGDDGRFVKTywslFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESI 514
Cdd:cd05970 380 GEIVIrtsKG-KPVGLFGGYYKDAEKTAEV----WHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 515 SSHPGVAEVAVVGVKDALKGQVAVAFVIP----KESDSLedrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRS 590
Cdd:cd05970 455 IQHPAVLECAVTGVPDPIRGQVVKATIVLakgyEPSEEL---------KKELQDHVKKVTAPYKYPRIVEFVDELPKTIS 525
|
....*....
gi 16128320 591 GKMLRRTIQ 599
Cdd:cd05970 526 GKIRRVEIR 534
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
53-598 |
2.72e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 182.31 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 53 LCHNAidrwlEKQPEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIG 132
Cdd:PRK06187 12 LRHGA-----RKHPDKEAV------YFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 AI-HSV-VFggFASHSVAARIDDAKP-VLIVSADagarggkiipYKKLLDDAISQAQHQpRHVLLVDRGlaKMARVSGRD 209
Cdd:PRK06187 81 AVlHPInIR--LKPEEIAYILNDAEDrVVLVDSE----------FVPLLAAILPQLPTV-RTVIVEGDG--PAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 210 VDFASLRHQHIGARVPVAwLESNETSCILYTSGTTGKPKGVQ---RDVGGYAVALATSMDtifggkagsvfFCASDIGWV 286
Cdd:PRK06187 146 GEYEELLAAASDTFDFPD-IDENDAAAMLYTSGTTGHPKGVVlshRNLFLHSLAVCAWLK-----------LSRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 287 V---GHSY---IVYAPLLAGmATIVYeglptwPDC---GVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAeiRKHDLSSLE 357
Cdd:PRK06187 214 IvpmFHVHawgLPYLALMAG-AKQVI------PRRfdpENLLDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDFSSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 358 VLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGwPIMAIAR---GLDDRPTRLGSPGVPMYGYNVQLLNEVTGE-PCG 433
Cdd:PRK06187 285 LVIYGGAALPPALLREFKEKFGIDLVQGYGMTETS-PVVSVLPpedQLPGQWTKRRSAGRPLPGVEARIVDDDGDElPPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 434 VNEKGMLVVEGPlppgCI-QTIWGDDGRFVKTY---WslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTRE 509
Cdd:PRK06187 364 GGEVGEIIVRGP----WLmQGYWNRPEATAETIdggW-------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 510 IEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTR 589
Cdd:PRK06187 433 LEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLD--------AKELRAFLRGRLAKFKLPKRIAFVDELPRTS 504
|
....*....
gi 16128320 590 SGKMLRRTI 598
Cdd:PRK06187 505 VGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
58-595 |
3.30e-49 |
|
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: 177.42 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHsv 137
Cdd:cd17631 1 LRRRARRHPDRTALV------FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 138 vfggfasHSVAARIDDAKPVLIVsADAGArggkiipyKKLLDDaisqaqhqprhvllvdrglakmarvsgrdvdfaslrh 217
Cdd:cd17631 73 -------VPLNFRLTPPEVAYIL-ADSGA--------KVLFDD------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 218 qhigarvpVAWlesnetscILYTSGTTGKPKGV---QRDVGGYAVALATSMDTIFGgkagSVFFCASDIGWVVGHSYIVY 294
Cdd:cd17631 100 --------LAL--------LMYTSGTTGRPKGAmltHRNLLWNAVNALAALDLGPD----DVLLVVAPLFHIGGLGVFTL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 APLLAGMATIVYEGlptwPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAeiRKHDLSSLEVLYLAGEPLDEPTASWV 374
Cdd:cd17631 160 PTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAPMPERLLRAL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTlDVPVIDNYWQTESGWPIMAIARglDDRPTRLGSPGVPMYGYNVQLLNEVtGEPCGVNEKGMLVVEGP-LPPGciqt 453
Cdd:cd17631 234 QAR-GVKFVQGYGMTETSPGVTFLSP--EDHRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPhVMAG---- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 454 IWGDDGRFVKTY---WslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKD 530
Cdd:cd17631 306 YWNRPEATAAAFrdgW-------FHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPD 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 531 ALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd17631 379 EKWGEAVVAVVVPRPGAELD--------EDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
79-594 |
1.76e-48 |
|
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: 176.63 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKP-V 157
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPkV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 158 LIVSADAgarggkiipYKKLLDDAiSQAQHQPRHVLLVDRGLAKmarVSGRDVDFASLRHQHIgARVPVAWLESNETSCI 237
Cdd:cd05911 86 IFTDPDG---------LEKVKEAA-KELGPKDKIIVLDDKPDGV---LSIEDLLSPTLGEEDE-DLPPPLKDGKDDTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 238 LYTSGTTGKPKGVQ---RDVggyaVALATSMDTIFGGKAGS--VFFCASDIGWVVGHSYIVYAPLLagmativyeGLPTW 312
Cdd:cd05911 152 LYSSGTTGLPKGVClshRNL----IANLSQVQTFLYGNDGSndVILGFLPLYHIYGLFTTLASLLN---------GATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 313 ----PDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAeiRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYW- 387
Cdd:cd05911 219 impkFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLL--DKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 388 QTESGwPIMAIARGLDDRPtrlGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppgciqTIWG--------DDG 459
Cdd:cd05911 297 MTETG-GILTVNPDGDDKP---GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGP-------QVMKgyynnpeaTKE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RFVKTYWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVA 539
Cdd:cd05911 366 TFDEDGW-------LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 540 FVIPKESDSLEdrdvahsqEKAIMALVDSQIGNF----GRpahVWFVSQLPKTRSGKML 594
Cdd:cd05911 439 YVVRKPGEKLT--------EKEVKDYVAKKVASYkqlrGG---VVFVDEIPKSASGKIL 486
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
52-595 |
2.93e-48 |
|
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: 176.89 E-value: 2.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 52 NLCHNAIDRWLEKQ-----PEALALIAVSSETEEERtFTFRQLHDEVNAVASMLR-SLGVQRGDRVLVYMPMIAEAHITL 125
Cdd:cd05928 6 NFASDVLDQWADKEkagkrPPNPALWWVNGKGDEVK-WSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 126 LACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIPYK------KLLddaisqAQHQPRHVLLVDRGL 199
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASEcpslktKLL------VSEKSRDGWLNFKEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 200 AKmarvsgrdvdFASLRHQHIGARvpvawleSNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFC 279
Cdd:cd05928 159 LN----------EASTEHHCVETG-------SQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 280 ASDIGWVVGHSYIVYAPLLAGMATIVYEgLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKfptAEIRKHDLSSLEVL 359
Cdd:cd05928 222 TSDTGWIKSAWSSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQ---QDLSSYKFPSLQHC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 360 YLAGEPLD-EPTASWVSNT-LDVpvIDNYWQTESGWpIMAIARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEK 437
Cdd:cd05928 297 VTGGEPLNpEVLEKWKAQTgLDI--YEGYGQTETGL-ICANFKGMKIKP---GSMGKASPPYDVQIIDD-NGNVLPPGTE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVVE-GPLPPGCIQTIWGDDGrfVKTYwSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISS 516
Cdd:cd05928 370 GDIGIRvKPIRPFGLFSGYVDNP--EKTA-ATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 517 HPGVAEVAVVGVKDALKGQVAVAFVIpkesdsLEDRDVAHSQEKAIMAL---VDSQIGNFGRPAHVWFVSQLPKTRSGKM 593
Cdd:cd05928 447 HPAVVESAVVSSPDPIRGEVVKAFVV------LAPQFLSHDPEQLTKELqqhVKSVTAPYKYPRKVEFVQELPKTVTGKI 520
|
..
gi 16128320 594 LR 595
Cdd:cd05928 521 QR 522
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
81-596 |
5.17e-46 |
|
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: 169.28 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsVVfggfashsvaariddakpvliv 160
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV--VV---------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 sadagarggkiipykkllddaisqaqhqPRHVLLVDRGLAKMARVSG-----RDVDFASLRHQHIGARVPVAwLESNETS 235
Cdd:cd05936 78 ----------------------------PLNPLYTPRELEHILNDSGakaliVAVSFTDLLAAGAPLGERVA-LTPEDVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 236 CILYTSGTTGKPKGV---QRDVggYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYegLPTW 312
Cdd:cd05936 129 VLQYTSGTTGVPKGAmltHRNL--VANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALG-ATIVL--IPRF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 313 PDCGVWWTIvEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESG 392
Cdd:cd05936 204 RPIGVLKEI-RKHRVTIFPGVPTMYIALLNAP--EFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 393 wPImaIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGE-PCGvnEKGMLVVEGP--------LPPGCIQTIwgDDGRFvk 463
Cdd:cd05936 281 -PV--VAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEElPPG--EVGELWVRGPqvmkgywnRPEETAEAF--VDGWL-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 464 tywslfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIP 543
Cdd:cd05936 352 -----------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 16128320 544 KESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05936 421 KEGASLT--------EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRR 465
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
55-596 |
1.89e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 168.21 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAV--SSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIG 132
Cdd:PRK07529 28 YELLSRAAARHPDAPALSFLldADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 aIHSVVFGGFASHSVAA--RIDDAKPVLIVSADAGARggkiIPYKklLDDAISQAqHQPRHVLLVD---------RGLAK 201
Cdd:PRK07529 108 -IANPINPLLEPEQIAEllRAAGAKVLVTLGPFPGTD----IWQK--VAEVLAAL-PELRTVVEVDlarylpgpkRLAVP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 202 MARVSG--RDVDF-ASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGSVFF 278
Cdd:PRK07529 180 LIRRKAhaRILDFdAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 279 CASDIGWVVGHSYIVYAPLLAGmATIVYEGLPTWPDCGV---WWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkHDLSS 355
Cdd:PRK07529 259 CGLPLFHVNALLVTGLAPLARG-AHVVLATPQGYRGPGVianFWKIVERYRINFLSGVPTVYAALLQVPVDG---HDISS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 356 LEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESgwpIMAIARGLDDRPTRLGSPGVPMYGYNVQLLnEVTGE----- 430
Cdd:PRK07529 335 LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEA---TCVSSVNPPDGERRIGSVGLRLPYQRVRVV-ILDDAgrylr 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 431 PCGVNEKGMLVVEGP------LPPGCIQTIWGDDGRFvktywslfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHR 504
Cdd:PRK07529 411 DCAVDEVGVLCIAGPnvfsgyLEAAHNKGLWLEDGWL-------------NTGDLGRIDADGYFWLTGRAKDLIIRGGHN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 505 LGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPK-----ESDSLEDRDVAHSQEKAimALvdsqignfgrPAHV 579
Cdd:PRK07529 478 IDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKpgasaTEAELLAFARDHIAERA--AV----------PKHV 545
|
570 580
....*....|....*....|.
gi 16128320 580 WFVSQLPKTRSGKM----LRR 596
Cdd:PRK07529 546 RILDALPKTAVGKIfkpaLRR 566
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-620 |
1.05e-43 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 166.21 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 3 FSEFYQRSINEPEQFWAE--QARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAidrwLEKQPEALALIAVSsETEE 80
Cdd:TIGR01217 37 YDALHRWSVDELDTFWKAvwEWFDVRFSTPCARVVDDRTMPGAQWFPGARLNYAENL----LRAAGTEPALLYVD-ETHE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIV 160
Cdd:TIGR01217 112 PAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SADAGARGGKIIPYKKLLdDAISQAQHQPRHVLLVDRGL--AKMARVSGRDVDFASLRHQHIGARVPVAWLESNETSCIL 238
Cdd:TIGR01217 192 TVDGYRYNGKEHDRRDKV-AEVRKELPTLRAVVHIPYLGprETEAPKIDGALDLEDFTAAAQAAELVFEQLPFDHPLWIL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVgHSYIVYApLLAGMATIVYEGLPTWPDCGVW 318
Cdd:TIGR01217 271 FSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMM-WNWLVSG-LATGATLVLYDGSPGFPATNVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 WTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVidnYWQTESGWP--IM 396
Cdd:TIGR01217 349 WDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVYDEIKADV---WLASISGGTdiCS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 AIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCgVNEKGMLVVEGPLPPGCIQtIWGD-DG-RFVKTYWSLFSRpVY 474
Cdd:TIGR01217 426 CFAGANPTLPVHIGEIQAPGLGTAVQSWDP-EGKPV-TGEVGELVCTNPMPSMPIR-FWNDpDGsKYRDAYFDTYPG-VW 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 475 ATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPgvaevavvgvkdalkgQVAVAFVIPKESDSLEDRDV 554
Cdd:TIGR01217 502 RHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLD----------------EVRESLCIGQEQPDGGYRVV 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 555 -------AHSQEKAIMALVDSQIGNFGRPAHV----WFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLD 620
Cdd:TIGR01217 566 lfvhlapGATLDDALLDRIKRTIRAGLSPRHVpdeiIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGAIDNPELLD 642
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
66-598 |
5.64e-42 |
|
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: 158.63 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAVSSETEeertFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:cd05926 1 PDAPALVVPGSTPA----LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPVLIvsadagarggkIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVP 225
Cdd:cd05926 77 EFEFYLADLGSKLV-----------LTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VawlESNETSCILYTSGTTGKPKGV---QRDvggyavaLATSMDTIfggkAGSVFFCASDIGWVV-----GHSYI--VYA 295
Cdd:cd05926 146 P---LPDDLALILHTSGTTGRPKGVpltHRN-------LAASATNI----TNTYKLTPDDRTLVVmplfhVHGLVasLLS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 296 PLLAGMATIVYEGLptwpDCGVWWTIVEKYQVSrMFSA-PTAIRVLKKFPTAEIRkHDLSSLEVLYLAGEPLDEPTASWV 374
Cdd:cd05926 212 TLAAGGSVVLPPRF----SASTFWPDVRDYNAT-WYTAvPTIHQILLNRPEPNPE-SPPPKLRFIRSCSASLPPAVLEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTLDVPVIDNYWQTESGWPIMAiaRGLDDRPTRLGSPGVPmYGYNVQLLNEvTGEPCGVNEKGMLVVEGPL-------P 447
Cdd:cd05926 286 EATFGAPVLEAYGMTEAAHQMTS--NPLPPGPRKPGSVGKP-VGVEVRILDE-DGEILPPGVVGEICLRGPNvtrgylnN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 448 PGCIQTIWGDDGRFvktywslfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVG 527
Cdd:cd05926 362 PEANAEAAFKDGWF-------------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFG 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 528 VKDALKGQVAVAFVIPKESdsledrdvAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd05926 429 VPDEKYGEEVAAAVVLREG--------ASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
81-595 |
4.31e-41 |
|
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: 154.93 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakPVLIv 160
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI---------------------AVVI- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 sadagarggkiipykkllddaisqaqhqprHVLLVDRGLAKMARvsgrdvdfaslrhqHIGARVPVAwlESNETSCILYT 240
Cdd:cd05919 66 ------------------------------NPLLHPDDYAYIAR--------------DCEARLVVT--SADDIAYLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGV---QRDVGGYAVALATSmdtIFGGKAGSVFFCASDI--GWVVGHSyiVYAPLLAGMATIVYeglPTWPDC 315
Cdd:cd05919 100 SGTTGPPKGVmhaHRDPLLFADAMARE---ALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 316 -GVWWTIVEkYQVSRMFSAPTAIRVLkkFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWP 394
Cdd:cd05919 172 eRVLATLAR-FRPTVLYGVPTFYANL--LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 395 IMAiargldDRP--TRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGciqtiwgddgrfvktYWSLFSR 471
Cdd:cd05919 249 FLS------NRPgaWRLGSTGRPVPGYEIRLVDE-EGHTIPPGEEGDLLVRGPsAAVG---------------YWNNPEK 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 472 PV-------YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPK 544
Cdd:cd05919 307 SRatfnggwYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLK 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16128320 545 -ESDSLEdrdvahSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd05919 387 sPAAPQE------SLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
66-596 |
1.59e-40 |
|
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: 153.45 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVfggfASH 145
Cdd:cd05930 1 PDAVAVVD------GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDakpvlivsadagarggkiipykkLLDDAisqaqhQPRHVLLVDRGLAkmarvsgrdvdfaslrhqhigarvp 225
Cdd:cd05930 71 YPAERLAY-----------------------ILEDS------GAKLVLTDPDDLA------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 vawlesnetsCILYTSGTTGKPKGV---QRDVggyaVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIvYAPLLAGmA 302
Cdd:cd05930 97 ----------YVIYTSGSTGKPKGVmveHRGL----VNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAG-A 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 303 TIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLkkfpTAEIRKHDLSSLEVLYLAGEPLDEPTA-SWVSNTLDVP 381
Cdd:cd05930 161 TLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL----LQELELAALPSLRLVLVGGEALPPDLVrRWRELLPGAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 382 VIDNYWQTESGwpIMAIARGLDDRPTRLGSP--GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGCiqtiWGDD 458
Cdd:cd05930 237 LVNLYGPTEAT--VDATYYRVPPDDEEDGRVpiGRPIPNTRVYVLDE-NLRPVPPGVPGELYIGGAgLARGY----LNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 459 G----RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:cd05930 310 EltaeRFVPNPFGPGER-MYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGE 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 535 QVAVAFVIPKESDSLEDRDV-AHSQEK--AIMalvdsqignfgRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05930 389 KRLVAYVVPDEGGELDEEELrAHLAERlpDYM-----------VPSAFVVLDALPLTPNGKVDRK 442
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
82-595 |
4.19e-40 |
|
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: 153.68 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVV--------FGGFASHSvAARidd 153
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlltpddYAYYLEDS-RAR--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 154 akpVLIVSadagargGKIIPykkLLDDAISQAQHQPRHVLLVDRglakmARVSGRDVDFASLRHQHIGARVPVAwLESNE 233
Cdd:cd05959 104 ---VVVVS-------GELAP---VLAAALTKSEHTLVVLIVSGG-----AGPEAGALLLAELVAAEAEQLKPAA-THADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 234 TSCILYTSGTTGKPKGV---QRDVggyAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLP 310
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVvhlHADI---YWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 311 TwPDCgVWWTIVEkYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPtaswvsntldvpvIDNYWQTE 390
Cdd:cd05959 242 T-PAA-VFKRIRR-YRPTVFFGVPTLYAAMLAAPNLP--SRDLSSLRLCVSAGEALPAE-------------VGERWKAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 391 SGWPIM-------AIARGLDDRP--TRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGCIQTIWG--DDG 459
Cdd:cd05959 304 FGLDILdgigsteMLHIFLSNRPgrVRYGTTGKPVPGYEVELRDE-DGGDVADGEPGELYVRGP---SSATMYWNnrDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RFV-KTYWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAV 538
Cdd:cd05959 380 RDTfQGEW-------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPK 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 539 AFVIPK----ESDSLEDRDVAHSQEKaimalvdsqIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd05959 453 AFVVLRpgyeDSEALEEELKEFVKDR---------LAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
85-520 |
3.65e-39 |
|
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: 148.95 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSL-GVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVfggfASHSVAARIDDakpvliVSAD 163
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL----DPAYPAERLAF------ILED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 AGARggkiipykkllddaisqaqhqprhVLLVDRGLAK-MARVSGRDVDFASLRHQHIGARVPVAWLES----NETSCIL 238
Cdd:TIGR01733 71 AGAR------------------------LLLTDSALASrLAGLVLPVILLDPLELAALDDAPAPPPPDApsgpDDLAYVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIvYAPLLAGMATIVYEGLPTWPDCGVW 318
Cdd:TIGR01733 127 YTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 WTIVEKYQVSRMFSAPTAIRVLkkfptAEIRKHDLSSLEVLYLAGEPLDEPTA-SWVSNTLDVPVIDNYWQTESgwPIMA 397
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALL-----AAALPPALASLRLVILGGEALTPALVdRWRARGPGARLINLYGPTET--TVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 398 IARGLDDRPTRLGSP---GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGciqtIWGDDG----RFVK-TYWSL 468
Cdd:TIGR01733 278 TATLVDPDDAPRESPvpiGRPLANTRLYVLDD-DLRPVPVGVVGELYIGGPgVARG----YLNRPEltaeRFVPdPFAGG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16128320 469 FSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHR--LGtrEIEESISSHPGV 520
Cdd:TIGR01733 353 DGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRieLG--EIEAALLRHPGV 404
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
55-598 |
1.74e-37 |
|
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: 145.73 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAVSSETEeertFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:cd05923 4 FEMLRRAASRAPDACAIADPARGLR----LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HSVVFGGFASHSVAARIDDAKPVLIVSADAgarggkiipykKLLDDAISQAqhqprhvllVDRGLAKMARVSGRDVDFAS 214
Cdd:cd05923 80 PALINPRLKAAELAELIERGEMTAAVIAVD-----------AQVMDAIFQS---------GVRVLALSDLVGLGEPESAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 lrhQHIGARVPvawlESNETSCILYTSGTTGKPKGV---QRDVGGYAVALATSMDTIFGgkAGSVFFCASDIGWVVGHsY 291
Cdd:cd05923 140 ---PLIEDPPR----EPEQPAFVFYTSGTTGLPKGAvipQRAAESRVLFMSTQAGLRHG--RHNVVLGLMPLYHVIGF-F 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 292 IVYAPLLAGMATIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLkkFPTAEIRKHDLSSLEVLYLAGEPLDEPTA 371
Cdd:cd05923 210 AVLVAALALDGTYV---VVEEFDPADALKLIEQERVTSLFATPTHLDAL--AAAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 372 SWVSNTLDVPVIDNYWQTEsgwpimaIARGLDDRPTRLGSPGVPMYGYNVQL--LNEVTGEPCGVNEKGMLVVEGplppg 449
Cdd:cd05923 285 ERVNQHLPGEKVNIYGTTE-------AMNSLYMRDARTGTEMRPGFFSEVRIvrIGGSPDEALANGEEGELIVAA----- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 450 ciqtiwGDDGRFVKtYWSLFSRPV-------YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAE 522
Cdd:cd05923 353 ------AADAAFTG-YLNQPEATAkklqdgwYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTE 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 523 VAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQekaimalvDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd05923 426 VVVIGVADERWGQSVTACVVPREGTLSADELDQFCR--------ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
59-600 |
1.76e-37 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 146.44 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 59 DRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsVV 138
Cdd:COG1021 32 RRRAERHPDRIAVVD------GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 139 F----------GGFASHSvaaridDAKPVLIVSADAGARggkiipYKKLLDDAISQAQHqPRHVLLVDRglakmarvSGR 208
Cdd:COG1021 104 FalpahrraeiSHFAEQS------EAVAYIIPDRHRGFD------YRALARELQAEVPS-LRHVLVVGD--------AGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 209 DVDFASLRHQHIGARVP------VAWLesnetsciLYTSGTTGKPKGVQRDVGGYAVALATSMDtIFGGKAGSVFFCASD 282
Cdd:COG1021 163 FTSLDALLAAPADLSEPrpdpddVAFF--------QLSGGTTGLPKLIPRTHDDYLYSVRASAE-ICGLDADTVYLAALP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 283 IGwvvgHSYIVYAP-----LLAGmATIVyegLPTWPDCGVWWTIVEKYQVSrmFSA---PTAIRVLKkfpTAEIRKHDLS 354
Cdd:COG1021 234 AA----HNFPLSSPgvlgvLYAG-GTVV---LAPDPSPDTAFPLIERERVT--VTAlvpPLALLWLD---AAERSRYDLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 355 SLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYwqtesGwpiMAiaRGL-------DDRPTRLGSPGVPMYGYN-VQLLNE 426
Cdd:COG1021 301 SLRVLQVGGAKLSPELARRVRPALGCTLQQVF-----G---MA--EGLvnytrldDPEEVILTTQGRPISPDDeVRIVDE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 427 vTGEPCGVNEKGMLVVEGPLppgciqTIWG-------------DDGrfvktywslFsrpvYATFDWGIRDADGYHFILGR 493
Cdd:COG1021 371 -DGNPVPPGEVGELLTRGPY------TIRGyyrapehnaraftPDG---------F----YRTGDLVRRTPDGYLVVEGR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 494 TDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKES--------DSLEDRDVAHsqekaimal 565
Cdd:COG1021 431 AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEpltlaelrRFLRERGLAA--------- 501
|
570 580 590
....*....|....*....|....*....|....*....
gi 16128320 566 vdsqignFGRPAHVWFVSQLPKTRSGK----MLRRTIQA 600
Cdd:COG1021 502 -------FKLPDRLEFVDALPLTAVGKidkkALRAALAA 533
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
81-596 |
1.25e-36 |
|
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: 142.23 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQR-GDRVLVYMPMIAEAHITLLACARIGAIHSVVFggfashsvaariddakPVLi 159
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATM----------------PLL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 vsadagaRGGKiipYKKLLDDAisqaqhQPRHVLLVDRglakmarvsgrdvdfaslrhqhigarvpvawLESNETSCIL- 238
Cdd:cd05958 71 -------RPKE---LAYILDKA------RITVALCAHA-------------------------------LTASDDICILa 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGV---QRDV----GGYAValatsmdTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGlpT 311
Cdd:cd05958 104 FTSGTTGAPKATmhfHRDPlasaDRYAV-------NVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE--A 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 312 WPDcgVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTES 391
Cdd:cd05958 175 TPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDAA--GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 392 gWPIMAIARGLDDRPTRLGSPgVPmyGYNVQLLNEvTGEPCGVNEKGMLVVEGPlpPGCiqtiWGDDGRFVKTYwslFSR 471
Cdd:cd05958 251 -FHIFISARPGDARPGATGKP-VP--GYEAKVVDD-EGNPVPDGTIGRLAVRGP--TGC----RYLADKRQRTY---VQG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 472 PVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKeSDSLED 551
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLR-PGVIPG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16128320 552 RDVAHsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05958 396 PVLAR----ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRF 436
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
63-596 |
2.10e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 143.12 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 63 EKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsVV---- 138
Cdd:PRK07656 16 RRFGDKEAYV------FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV--VVplnt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 139 -FGGFASHSVAARiDDAKPVLIVsadagargGKIIPYKKLLDDAISQAQHQprhVLLVDRGLAKMARVSGRDVDFasLRH 217
Cdd:PRK07656 88 rYTADEAAYILAR-GDAKALFVL--------GLFLGVDYSATTRLPALEHV---VICETEEDDPHTEKMKTFTDF--LAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 218 QHIGARVPVawLESNETSCILYTSGTTGKPKGVQ----------RDVGGYA-------VALATSMDTIFGGKAGsvffca 280
Cdd:PRK07656 154 GDPAERAPE--VDPDDVADILFTSGTTGRPKGAMlthrqllsnaADWAEYLgltegdrYLAANPFFHVFGYKAG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 281 sdigwvvghsyiVYAPLLAGmATIVYegLPTW-PDCGVwwTIVEKYQVSRMFSAPTAIRVLKKFPTAeiRKHDLSSLEVL 359
Cdd:PRK07656 226 ------------VNAPLMRG-ATILP--LPVFdPDEVF--RLIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 360 YLAGEPLDEPTASWVSNTLDVP-VIDNYWQTESGwPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVtGEPCGVNEKG 438
Cdd:PRK07656 287 VTGAASMPVALLERFESELGVDiVLTGYGLSEAS-GVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNEL-GEEVPVGEVG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 439 MLVVEGP--------LPPGCIQTIWGDDgrfvktyWsLFsrpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGTREI 510
Cdd:PRK07656 365 ELLVRGPnvmkgyydDPEATAAAIDADG-------W-LH------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEV 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 511 EESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDV-AHSQEKaiMAlvdsqigNFGRPAHVWFVSQLPKTR 589
Cdd:PRK07656 431 EEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELiAYCREH--LA-------KYKVPRSIEFLDELPKNA 501
|
....*..
gi 16128320 590 SGKMLRR 596
Cdd:PRK07656 502 TGKVLKR 508
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
62-598 |
1.22e-35 |
|
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: 139.69 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 62 LEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGG 141
Cdd:cd05945 1 AAANPDRPAVV------EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 142 FASHSVAARIDDAKPVLIVSADagarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfaslrhqhig 221
Cdd:cd05945 75 SPAERIREILDAAKPALLIADG---------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 arvpvawlesNETSCILYTSGTTGKPKGVQrdVGGYAVALATS-MDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAG 300
Cdd:cd05945 97 ----------DDNAYIIFTSGSTGRPKGVQ--ISHDNLVSFTNwMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGA 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 MATIVYEGLPTWPdcGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTaeIRKHDLSSLEVLYLAGEPLDEPTAS-WVSNTLD 379
Cdd:cd05945 165 TLVPVPRDATADP--KQLFRFLAEHGITVWVSTPSFAAMCLLSPT--FTPESLPSLRHFLFCGEVLPHKTARaLQQRFPD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 380 VPVIDNYWQTESGWPIMAIA--RGLDDRPTRLgsP-GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGciqtIW 455
Cdd:cd05945 241 ARIYNTYGPTEATVAVTYIEvtPEVLDGYDRL--PiGYAKPGAKLVILDE-DGRPVPPGEKGELVISGPsVSKG----YL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 GDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ 535
Cdd:cd05945 314 NNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVT 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 536 VAVAFVIPKESDSLEDrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd05945 394 ELIAFVVPKPGAEAGL-------TKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
82-596 |
7.45e-35 |
|
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: 138.52 E-value: 7.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVS 161
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADAGarggkiipYKKLLDDAISqaqhqprhVLLVDRGLAKMARVSGRDVDFASlrhqhigARVPVAWLESNETSCILYTS 241
Cdd:cd05904 111 TAEL--------AEKLASLALP--------VVLLDSAEFDSLSFSDLLFEADE-------AEPPVVVIKQDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 242 GTTGKPKGVQRDVGGYaVALATSMDTIFG--GKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLptwpDCGVWW 319
Cdd:cd05904 168 GTTGRSKGVMLTHRNL-IAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRF----DLEELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 320 TIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSNTL-DVPVIDNYWQTESGwPIMAI 398
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLALVKSPIVD--KYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTEST-GVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 399 ARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppgCIqtiwgddgrfVKTYwslFSRP--VYAT 476
Cdd:cd05904 320 CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGP----SI----------MKGY---LNNPeaTAAT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 477 FD---W------GIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESD 547
Cdd:cd05904 383 IDkegWlhtgdlCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGS 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16128320 548 SLedrdvahsQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05904 463 SL--------TEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRK 503
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
85-596 |
8.39e-35 |
|
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: 136.84 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsVVfggfashsvaariddakpvlivsada 164
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV--VV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 165 garggkiipykkllddaisqaqhqPRHVLLVDRGLAKMARVSGrdvdfaslrhqhigARVPVAWLESNETSCILYTSGTT 244
Cdd:cd05935 55 ------------------------PINPMLKERELEYILNDSG--------------AKVAVVGSELDDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 245 GKPKGVQRdVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYEGLptWpDCGVWWTIVEK 324
Cdd:cd05935 97 GLPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVG-GTYVLMAR--W-DRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 325 YQVSRMFSAPTAIRVLkkFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTEsgwpimAIARGLDD 404
Cdd:cd05935 172 YKVTFWTNIPTMLVDL--LATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE------TMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 405 RPTRLGSP--GVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIR 482
Cdd:cd05935 244 PPLRPKLQclGIP*FGVDARVIDIETGRELPPNEVGEIVVRGP---QIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYM 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 483 DADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKEsdslEDRdvAHSQEKAI 562
Cdd:cd05935 321 DEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP----EYR--GKVTEEDI 394
|
490 500 510
....*....|....*....|....*....|....
gi 16128320 563 MALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05935 395 IEWAREQMAAYKYPREVEFVDELPRSASGKILWR 428
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
81-606 |
2.36e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 137.04 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSvvfggfASHSVAARIDDAkpvlIV 160
Cdd:PRK06188 35 DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT------ALHPLGSLDDHA----YV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SADAGARggkiipykKLLDDAisqaqhqprhVLLVDRGLAKMARVSGRD-----------VDFASLRHQhIGARVPVAWL 229
Cdd:PRK06188 105 LEDAGIS--------TLIVDP----------APFVERALALLARVPSLKhvltlgpvpdgVDLLAAAAK-FGPAPLVAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 230 ESNETSCILYTSGTTGKPKGV---QRDVGGYAVALATSmdtiFGGKAGSVFFCASDIGWVVGhsYIVYAPLLAGMATIVY 306
Cdd:PRK06188 166 LPPDIAGLAYTGGTTGKPKGVmgtHRSIATMAQIQLAE----WEWPADPRFLMCTPLSHAGG--AFFLPTLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 307 EGLptwpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLYLAGEPLDePTAswVSNTLDV--PVID 384
Cdd:PRK06188 240 AKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHP--DLRTRDLSSLETVYYGASPMS-PVR--LAEAIERfgPIFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 385 NYW-QTESGWPIMAIARG--LDDRPTRLGSPGVPMYGYNVQLLNEVtGEPCGVNEKGMLVVEGPLppgciqtiwgddgrF 461
Cdd:PRK06188 311 QYYgQTEAPMVITYLRKRdhDPDDPKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPL--------------V 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 462 VKTYWSL-------FSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:PRK06188 376 MDGYWNRpeetaeaFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWG 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 535 QVAVAFVIPKESdslEDRDVAhsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA-ICEGRD 606
Cdd:PRK06188 456 EAVTAVVVLRPG---AAVDAA-----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRArYWEGRG 520
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
61-596 |
2.94e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 136.25 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 61 WLEKQ----PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhs 136
Cdd:PRK03640 7 WLKQRafltPDRTAIEF------EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 137 VVF--GGFASHSVAARIDDAKPVLIVSADagarggkiiPYKKLLddaisqaqhqprhvllvdrglakmarVSGRDVDFAS 214
Cdd:PRK03640 79 AVLlnTRLSREELLWQLDDAEVKCLITDD---------DFEAKL--------------------------IPGISVKFAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 LRhqhIGARVPVAWLES---NETSCILYTSGTTGKPKGVQRDVGG-YAVALATSMDtiFGGKAGSVFFCASDIGWVVGHS 290
Cdd:PRK03640 124 LM---NGPKEEAEIQEEfdlDEVATIMYTSGTTGKPKGVIQTYGNhWWSAVGSALN--LGLTEDDCWLAAVPIFHISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 291 YIvyapllagMATIVYeGLPTwpdcgvwwTIVEKYQVSR-----------MFSAPTAI--RVLKKFPtaEIRKHdlSSLE 357
Cdd:PRK03640 199 IL--------MRSVIY-GMRV--------VLVEKFDAEKinkllqtggvtIISVVSTMlqRLLERLG--EGTYP--SSFR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 358 VLYLAGEPLDEPTASwVSNTLDVPVIDNYWQTESGWPIMAIArgLDDRPTRLGSPGVPMYGynVQLLNEVTGEPCGVNEK 437
Cdd:PRK03640 258 CMLLGGGPAPKPLLE-QCKEKGIPVYQSYGMTETASQIVTLS--PEDALTKLGSAGKPLFP--CELKIEKDGVVVPPFEE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVVEGP-LPPGCIQtiwgddgRFVKTYWSlFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISS 516
Cdd:PRK03640 333 GEIVVKGPnVTKGYLN-------REDATRET-FQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 517 HPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDrdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK03640 405 HPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEE----------LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
59-600 |
1.64e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 135.18 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 59 DRWLEKQPEALALIAVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVV 138
Cdd:PRK13295 31 DACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 139 FGGFASHSVAARIDDAKP-VLIVSADAgaRGgkiipykklLDDAISQAQHQP-----RHVLLVD--------RGLAKMAR 204
Cdd:PRK13295 111 MPIFRERELSFMLKHAESkVLVVPKTF--RG---------FDHAAMARRLRPelpalRHVVVVGgdgadsfeALLITPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 205 VSGRDVD--FASLRhqhigarvpvawLESNETSCILYTSGTTGKPKGVQRD----VGGYaVALATSMDTifggKAGSVFF 278
Cdd:PRK13295 180 EQEPDAPaiLARLR------------PGPDDVTQLIYTSGTTGEPKGVMHTantlMANI-VPYAERLGL----GADDVIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 279 CASDIGWVVGHSYIVYAPLLAGmATIVYegLPTW-PDCGVwwTIVEKYQVSRMFSAPTAIRVLKKfpTAEIRKHDLSSLE 357
Cdd:PRK13295 243 MASPMAHQTGFMYGLMMPVMLG-ATAVL--QDIWdPARAA--ELIRTEGVTFTMASTPFLTDLTR--AVKESGRPVSSLR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 358 VLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGwpiMAIARGLDDRPTRLG-SPGVPMYGYNVQLLNEvTGEPCGVNE 436
Cdd:PRK13295 316 TFLCAGAPIPGALVERARAALGAKIVSAWGMTENG---AVTLTKLDDPDERAStTDGCPLPGVEVRVVDA-DGAPLPAGQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 437 KGMLVVEGPlppgciqtiwgddGRFVktywSLFSRPV---------YATFDWGIRDADGYHFILGRTDDVINVAGHRLGT 507
Cdd:PRK13295 392 IGRLQVRGC-------------SNFG----GYLKRPQlngtdadgwFDTGDLARIDADGYIRISGRSKDVIIRGGENIPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 508 REIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEKAIMALvdsQIgnfgRPAHVWFVSQLPK 587
Cdd:PRK13295 455 VEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAK---QY----IPERLVVRDALPR 527
|
570
....*....|....*..
gi 16128320 588 TRSGKM----LRRTIQA 600
Cdd:PRK13295 528 TPSGKIqkfrLREMLRG 544
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
50-596 |
1.65e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 134.68 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 50 RTNLCHNAIDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYmpmiaeAH------I 123
Cdd:PRK08316 9 RRQTIGDILRRSARRYPDKTALV------FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAAL------GHnsdayaL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 124 TLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAgarggkiipykkLLDDAISQAQHQPRHVLLVDRGLAKMA 203
Cdd:PRK08316 77 LWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA------------LAPTAEAALALLPVDTLILSLVLGGRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 204 rVSGRDVDFASLRHQHiGARVPVAWLESNETSCILYTSGTTGKPKGVQ---RDVggyavaLATSMDTIFGGKagsvfFCA 280
Cdd:PRK08316 145 -APGGWLDFADWAEAG-SVAEPDVELADDDLAQILYTSGTESLPKGAMlthRAL------IAEYVSCIVAGD-----MSA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 281 SDIGWvvgHSYIVY--APLLAGMATIVYEG----LPTWPDCGVWWTIVEKYQVSRMFSAPTA-IRVLKKfptAEIRKHDL 353
Cdd:PRK08316 212 DDIPL---HALPLYhcAQLDVFLGPYLYVGatnvILDAPDPELILRTIEAERITSFFAPPTVwISLLRH---PDFDTRDL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 354 SSLEVLY-----LAGEPLDEPTASWVsntlDVPVIDNYWQTESGwPiMAIARGLDDRPTRLGSPGVPmyGYNVQ--LLNE 426
Cdd:PRK08316 286 SSLRKGYygasiMPVEVLKELRERLP----GLRFYNCYGQTEIA-P-LATVLGPEEHLRRPGSAGRP--VLNVEtrVVDD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 427 vTGEPCGVNEKGMLVVEGPlppgciQTIWGddgrfvktYWSlfsRPVY--ATF--------DWGIRDADGYHFILGRTDD 496
Cdd:PRK08316 358 -DGNDVAPGEVGEIVHRSP------QLMLG--------YWD---DPEKtaEAFrggwfhsgDLGVMDEEGYITVVDRKKD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 497 VINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRP 576
Cdd:PRK08316 420 MIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVT--------EDELIAHCRARLAGFKVP 491
|
570 580
....*....|....*....|
gi 16128320 577 AHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK08316 492 KRVIFVDELPRNPSGKILKR 511
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-599 |
3.56e-33 |
|
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: 132.03 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakpvlIV 160
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SADAGARGgkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfASLRHQ--HIGARVPVAwlesnETSCIL 238
Cdd:cd05934 57 PINTALRG--------------------------------------------DELAYIidHSGAQLVVV-----DPASIL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGV---QRdvggYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYegLPTWPDC 315
Cdd:cd05934 88 YTSGTTGPPKGVvitHA----NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVG-ATLVL--LPRFSAS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 316 GvWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLssLEVLYLAGEPLDEPTAswVSNTLDVPVIDNYWQTESGWPI 395
Cdd:cd05934 161 R-FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHR--LRAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 396 MAiARgldDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKtywsLFSRPVYA 475
Cdd:cd05934 236 IG-PR---DEPRRPGSIGRPAPGYEVRIVDD-DGQELPAGEPGELVIRGLRGWGFFKGYYNMPEATAE----AMRNGWFH 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 476 TFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG-QVAVAFVIPKESDSLEDrdv 554
Cdd:cd05934 307 TGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEdEVKAVVVLRPGETLDPE--- 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16128320 555 ahsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:cd05934 384 ------ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-610 |
8.25e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 132.86 E-value: 8.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI----------H 135
Cdd:PRK07470 21 PDRIALV------WGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVwvptnfrqtpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 136 SVVFGGFAShsvAARiddakpVLIVSADAGARGgkiipykklldDAISQAQHQPRHVLLVDRGLAkmarvsGRDVDfaSL 215
Cdd:PRK07470 95 EVAYLAEAS---GAR------AMICHADFPEHA-----------AAVRAASPDLTHVVAIGGARA------GLDYE--AL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 216 RHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSvffcasDIGWVVghsyivyA 295
Cdd:PRK07470 147 VARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQ------DASLVV-------A 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 296 PL------------LAGMATIVyegLPTWP-DCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLE-VLYl 361
Cdd:PRK07470 214 PLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVD--RYDHSSLRyVIY- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 362 AGEPL---DEPTAswvsntLDV--PVIDNYWQ----TESGWPIMAIARGLDDRP-TRLGSPGVPMYGYNVQLLNEVtGEP 431
Cdd:PRK07470 288 AGAPMyraDQKRA------LAKlgKVLVQYFGlgevTGNITVLPPALHDAEDGPdARIGTCGFERTGMEVQIQDDE-GRE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 432 CGVNEKGMLVVEGPlppGCIQTIWGDDGRFVKTY---WslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTR 508
Cdd:PRK07470 361 LPPGETGEICVIGP---AVFAGYYNNPEANAKAFrdgW-------FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 509 EIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKT 588
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD--------EAELLAWLDGKVARYKLPKRFFFWDALPKS 502
|
570 580
....*....|....*....|..
gi 16128320 589 RSGKMLRRTIQAICEGRdpGDL 610
Cdd:PRK07470 503 GYGKITKKMVREELEER--GLL 522
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
82-595 |
2.54e-32 |
|
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: 131.11 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKP-VLIV 160
Cdd:TIGR02262 29 SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRArVVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 161 SadagargGKIIPykkLLDDAISQAQHQpRHVLLVDRGLAKmarvsgrDVDFASLRHQHIGARVPVAwLESNETSCILYT 240
Cdd:TIGR02262 109 S-------GALLP---VIKAALGKSPHL-EHRVVVGRPEAG-------EVQLAELLATESEQFKPAA-TQADDPAFWLYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTwPDcgVWWT 320
Cdd:TIGR02262 170 SGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 321 IVEKYQVSRMFSAPTAIRVLKKFPTaeIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPImaiar 400
Cdd:TIGR02262 247 RLRRHQPTIFYGVPTLYAAMLADPN--LPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIF----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 401 gLDDRPTRL--GSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGCIQTIWGDDGRFVKTYWSLFSRpvyaTFD 478
Cdd:TIGR02262 320 -LSNLPGDVryGTSGKPVPGYRLRLVGD-GGQDVADGEPGELLISGP---SSATMYWNNRAKSRDTFQGEWTR----SGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 479 WGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKE-SDSLEDRDVAHs 557
Cdd:TIGR02262 391 KYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPgQTALETELKEH- 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 16128320 558 qekaimalVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:TIGR02262 470 --------VKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-595 |
1.03e-31 |
|
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: 128.27 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddAKPVLIvsa 162
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV-------------------TNPILP--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 dagarggkiipykkllddaiSQAQHQPRHVLlvDRGLAKMARVSGRdvdFASLRHQHIGArvpvawlesnETSCILYTSG 242
Cdd:cd05903 59 --------------------FFREHELAFIL--RRAKAKVFVVPER---FRQFDPAAMPD----------AVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 243 TTGKPKGV---QRDVGGYAVALATSMdtifGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEglpTW-PDCGVw 318
Cdd:cd05903 104 TTGEPKGVmhsHNTLSASIRQYAERL----GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWdPDKAL- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 wTIVEKYQVSRMFSAPTAIRVLKKfpTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAI 398
Cdd:cd05903 176 -ALMREHGVTFMMGATPFLTDLLN--AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 399 ARGLDDRptRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppgciQTIWG--DD----GRFVKTYWslfsrp 472
Cdd:cd05903 253 TPAPEDR--RLYTDGRPLPGVEIKVVDD-TGATLAPGVEGELLSRGP------SVFLGylDRpdltADAAPEGW------ 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 473 vYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDR 552
Cdd:cd05903 318 -FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD 396
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 16128320 553 DVAHSQEKAimalvdsQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd05903 397 ELVAYLDRQ-------GVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
239-592 |
1.56e-31 |
|
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: 126.06 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYEGLPTWPDCGVW 318
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASG-AHVVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 ---WTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkhDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESgwpI 395
Cdd:cd05944 87 dnfWKLVERYRITSLSTVPTVYAALLQVPVNA----DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEA---T 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 396 MAIARGLDDRPTRLGSPGVPMYGYNVQL--LNEVTGE--PCGVNEKGMLVVEGP-LPPGCIQTIwGDDGRFVKTYWslfs 470
Cdd:cd05944 160 CLVAVNPPDGPKRPGSVGLRLPYARVRIkvLDGVGRLlrDCAPDEVGEICVAGPgVFGGYLYTE-GNKNAFVADGW---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 471 rpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPK-----E 545
Cdd:cd05944 235 ---LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKpgavvE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16128320 546 SDSLEDRDVAHSQEKAIMalvdsqignfgrPAHVWFVSQLPKTRSGK 592
Cdd:cd05944 312 EEELLAWARDHVPERAAV------------PKHIEVLEELPVTAVGK 346
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
60-604 |
8.99e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 127.08 E-value: 8.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 60 RWLEKQPEALALIAVSSETeeertfTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVF 139
Cdd:PRK06178 41 AWARERPQRPAIIFYGHVI------TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 140 GGFASHSVAARIDDAKPVLIVSADAgarggkIIPY-KKLLDD-------AISQAQHQPRHVLLVDRGLAKMARVSGRDVD 211
Cdd:PRK06178 115 PLFREHELSYELNDAGAEVLLALDQ------LAPVvEQVRAEtslrhviVTSLADVLPAEPTLPLPDSLRAPRLAAAGAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 212 --FASLRHQHIGARVPVAWLESneTSCILYTSGTTGKPKGV---QRD-VGGYAVALATSMdtifGGKAGSVFFCASDIGW 285
Cdd:PRK06178 189 dlLPALRACTAPVPLPPPALDA--LAALNYTGGTTGMPKGCehtQRDmVYTAAAAYAVAV----VGGEDSVFLSFLPEFW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 VVGHSYIVYAPLLAGmATIVYegLPTWpDCGVWWTIVEKYQVSRMF-SAPTAIRVLKkfpTAEIRKHDLSSLEVLylage 364
Cdd:PRK06178 263 IAGENFGLLFPLFSG-ATLVL--LARW-DAVAFMAAVERYRVTRTVmLVDNAVELMD---HPRFAEYDLSSLRQV----- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 365 pldePTASWVSNtLDvPVIDNYWQTESGWPIMAIARGL---------------DD-----RPTRLGSPgVPmyGYNVQLL 424
Cdd:PRK06178 331 ----RVVSFVKK-LN-PDYRQRWRALTGSVLAEAAWGMtethtcdtftagfqdDDfdllsQPVFVGLP-VP--GTEFKIC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 425 NEVTGEPCGVNEKGMLVVEGPlppgciqtiwgddgRFVKTYWS-------LFSRPVYATFDWGIRDADGY-HFiLGRTDD 496
Cdd:PRK06178 402 DFETGELLPLGAEGEIVVRTP--------------SLLKGYWNkpeataeALRDGWLHTGDIGKIDEQGFlHY-LGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 497 VINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKesdslEDRDVAhsqEKAIMALVDSQIGNFGRP 576
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLK-----PGADLT---AAALQAWCRENMAVYKVP 538
|
570 580
....*....|....*....|....*...
gi 16128320 577 aHVWFVSQLPKTRSGKMLRRTIQAICEG 604
Cdd:PRK06178 539 -EIRIVDALPMTATGKVRKQDLQALAEE 565
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
53-600 |
2.02e-30 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 125.66 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 53 LCHNAIDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIG 132
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALV------HHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 AIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARggkiipykkLLDDAISQAqHQPRHVLLVDrglakmarvsgrdvDF 212
Cdd:TIGR03098 75 GVFVPINPLLKAEQVAHILADCNVRLLVTSSERLD---------LLHPALPGC-HDLRTLIIVG--------------DP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 213 ASLRHQHIGARvPVAWLE--------------SNETSCILYTSGTTGKPKGV---QRDVGGYAVALATSMDTIFGGKAGS 275
Cdd:TIGR03098 131 AHASEGHPGEE-PASWPKllalgdadpphpviDSDMAAILYTSGSTGRPKGVvlsHRNLVAGAQSVATYLENRPDDRLLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 276 VFFCASDIG-------WVVGHSYIVYAPLLAG--MATIVYEGLPTWPDCGVWWTivekyQVSRMFSAPTAIRVLKKFPTA 346
Cdd:TIGR03098 210 VLPLSFDYGfnqlttaFYVGATVVLHDYLLPRdvLKALEKHGITGLAAVPPLWA-----QLAQLDWPESAAPSLRYLTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 347 --EIRKHDLSSLEVLYlagePLDEP------TASWVSNTLDvpvidnywqtesgwpimaiARGLDDRPTRLGSpGVPmyG 418
Cdd:TIGR03098 285 ggAMPRATLSRLRSFL----PNARLflmyglTEAFRSTYLP-------------------PEEVDRRPDSIGK-AIP--N 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 419 YNVQLLNEvTGEPCGVNEKGMLVVEGPLppgCIQTIWGD----DGRFVKT--YWSLFSRPVYATF--DWGIRDADGYHFI 490
Cdd:TIGR03098 339 AEVLVLRE-DGSECAPGEEGELVHRGAL---VAMGYWNDpektAERFRPLppFPGELHLPELAVWsgDTVRRDEEGFLYF 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 491 LGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLeDRDvahsqekAIMALVDSQI 570
Cdd:TIGR03098 415 VGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEEL-DRA-------ALLAECRARL 486
|
570 580 590
....*....|....*....|....*....|
gi 16128320 571 GNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:TIGR03098 487 PNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
63-599 |
4.03e-30 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 124.41 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 63 EKQPEALALIaVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGF 142
Cdd:PRK08008 18 DVYGHKTALI-FESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 143 ASHSVAARIDDAKPVLIVSADAgarggkIIP-YKKLLDDAisqaQHQPRHVLLVDRGLAKMARVSgrdvDFASLRHQHIG 221
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQ------FYPmYRQIQQED----ATPLRHICLTRVALPADDGVS----SFTQLKAQQPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 ARVPVAWLESNETSCILYTSGTTGKPKGVqrdvggyavaLATSMDTIFGG--KAGSVFFCASDIGWVVGHSYIVYAPLLA 299
Cdd:PRK08008 163 TLCYAPPLSTDDTAEILFTSGTTSRPKGV----------VITHYNLRFAGyySAWQCALRDDDVYLTVMPAFHIDCQCTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 300 GMATIVyeglptwpdCGVWWTIVEKYQVSRMF------------SAPTAIRVLKKFPTAEI-RKHDLSslEVLYLAgePL 366
Cdd:PRK08008 233 AMAAFS---------AGATFVLLEKYSARAFWgqvckyratiteCIPMMIRTLMVQPPSANdRQHCLR--EVMFYL--NL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 367 DEPTASWVSNTLDVPVIDNYWQTESgwpIMAIargLDDRPT---RLGSPGVPMYGYNVQLlnevtgepcgVNEKGMlvve 443
Cdd:PRK08008 300 SDQEKDAFEERFGVRLLTSYGMTET---IVGI---IGDRPGdkrRWPSIGRPGFCYEAEI----------RDDHNR---- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 gPLPPGCIQTIW--GDDGR-FVKTYwslFSRPVYA-----------TFDWGIRDADGYHFILGRTDDVINVAGHRLGTRE 509
Cdd:PRK08008 360 -PLPAGEIGEICikGVPGKtIFKEY---YLDPKATakvleadgwlhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 510 IEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLedrdvahsQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTR 589
Cdd:PRK08008 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETL--------SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNC 507
|
570
....*....|
gi 16128320 590 SGKMLRRTIQ 599
Cdd:PRK08008 508 SGKIIKKNLK 517
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
82-599 |
5.22e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 124.69 E-value: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASML-RSLGVQRGDRVLVYM---PMIAEAHITLLacaRIGAIhsVVfggfashsvaaridDAKPV 157
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMqnsPQFVIAYYAIL---RANAV--VV--------------PVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 158 LI------VSADAGARGGkiIPYKKLLDDAIS-QAQHQPRHVLLVDrgLAKMARVSGRDVDFASLRHQHIGARVP----V 226
Cdd:PRK08314 95 NReeelahYVTDSGARVA--IVGSELAPKVAPaVGNLRLRHVIVAQ--YSDYLPAEPEIAVPAWLRAEPPLQALApggvV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 227 AWLE-------------SNETSCIL-YTSGTTGKPKG---VQRDVGGYAVALATsmdtIFGGKAGSVFFCASDIGWVVGH 289
Cdd:PRK08314 171 AWKEalaaglappphtaGPDDLAVLpYTSGTTGVPKGcmhTHRTVMANAVGSVL----WSNSTPESVVLAVLPLFHVTGM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 290 SYIVYAPLLAGmATIVYegLPTWpDCGVWWTIVEKYQVSRMFSAPTAirVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEP 369
Cdd:PRK08314 247 VHSMNAPIYAG-ATVVL--MPRW-DREAAARLIERYRVTHWTNIPTM--VVDFLASPGLAERDLSSLRYIGGGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 370 TASWVSNTLDVPVIDNYWQTESGWPIMAIARgldDRPtRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppG 449
Cdd:PRK08314 321 VAERLKELTGLDYVEGYGLTETMAQTHSNPP---DRP-KLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGP---Q 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 450 CIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVK 529
Cdd:PRK08314 394 VFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 530 DALKGQVAVAFVIPKEsdslEDRDVAHSQEkaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:PRK08314 474 DPRRGETVKAVVVLRP----EARGKTTEEE--IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQ 537
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
83-596 |
7.55e-30 |
|
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: 122.07 E-value: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLivsa 162
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 dagarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfaslrhqhigarvpvawlesNETSCILYTSG 242
Cdd:cd05912 77 ---------------------------------------------------------------------DDIATIMYTSG 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 243 TTGKPKGVQRDVGG-YAVALATSMDtiFGGKAGSVFFCASDIGWVVGHSYIVYApllagmatiVYEGLPTwpdcgvwwTI 321
Cdd:cd05912 88 TTGKPKGVQQTFGNhWWSAIGSALN--LGLTEDDNWLCALPLFHISGLSILMRS---------VIYGMTV--------YL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 322 VEKYQVSR-----------MFSAPTAI--RVLKKFPtaeirKHDLSSLEVLYLAGEPLDEPTASwVSNTLDVPVIDNYWQ 388
Cdd:cd05912 149 VDKFDAEQvlhlinsgkvtIISVVPTMlqRLLEILG-----EGYPNNLRCILLGGGPAPKPLLE-QCKEKGIPVYQSYGM 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 389 TESGWPIMAIArgLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEkgmLVVEGP-LPPGCIqtiwgddGRFVKTYWS 467
Cdd:cd05912 223 TETCSQIVTLS--PEDALNKIGSAGKPLFPVELKIEDD-GQPPYEVGE---ILLKGPnVTKGYL-------NRPDATEES 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 468 lFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESD 547
Cdd:cd05912 290 -FENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI 368
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16128320 548 SLEDrdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05912 369 SEEE----------LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-595 |
9.51e-30 |
|
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: 122.29 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakpvlivsad 163
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 agarggkIIPYKKLLddaiSQAQHQPRhvllVDRGLAKMARVsgrdvdfaslrhqhigarvpVAWLESNETSCILYTSGT 243
Cdd:cd05974 52 -------VIPATTLL----TPDDLRDR----VDRGGAVYAAV--------------------DENTHADDPMLLYFTSGT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 244 TGKPKGVQRDVGGYAVALATSMDTIfGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEglPTWPDCGVWWTIVE 323
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFN--YARFDAKRVLAALV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 324 KYQVSRMFSAPTAIRVLKKFPTAEIRkhdlSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESgwpiMAIARGLD 403
Cdd:cd05974 174 RYGVTTLCAPPTVWRMLIQQDLASFD----VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET----TALVGNSP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 404 DRPTRLGSPGVPMYGYNVQLLNEVTGEpcgVNEKGM-LVVEGPLPPGCIQTIWGDDGRFVKTYWSLFsrpvYATFDWGIR 482
Cdd:cd05974 246 GQPVKAGSMGRPLPGYRVALLDPDGAP---ATEGEVaLDLGDTRPVGLMKGYAGDPDKTAHAMRGGY----YRTGDIAMR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 483 DADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKeSDSLEDRDVAhsqeKAI 562
Cdd:cd05974 319 DEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLR-AGYEPSPETA----LEI 393
|
490 500 510
....*....|....*....|....*....|...
gi 16128320 563 MALVDSQIGNFGRPAHVWFVsQLPKTRSGKMLR 595
Cdd:cd05974 394 FRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
58-591 |
1.17e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 123.31 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSV 137
Cdd:PRK06164 16 LDAHARARPDAVALI------DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 138 VFGGFASHSVAARIDDAKPVLIVSADaGARGgkiIPYKKLLDDAISQAQHQPRHVLLVDRGLAKM-ARVSGRDVDFASLr 216
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWP-GFKG---IDFAAILAAVPPDALPPLRAIAVVDDAADATpAPAPGARVQLFAL- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 217 hqHIGARVPVAWLESNETS--CILY-TSGTTGKPKGVQRDVG-----GYAVALATSMDtifggkAGSVFFCASDIGWVVG 288
Cdd:PRK06164 165 --PDPAPPAAAGERAADPDagALLFtTSGTTSGPKLVLHRQAtllrhARAIARAYGYD------PGAVLLAALPFCGVFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 289 HSYIVYAplLAGMATIVYEglPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLkkFPTAEIRKhDLSSLEVLYLAG-EPLD 367
Cdd:PRK06164 237 FSTLLGA--LAGGAPLVCE--PVF-DAARTARALRRHRVTHTFGNDEMLRRI--LDTAGERA-DFPSARLFGFASfAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 368 EPTASWVSnTLDVPVIDNYWQTESgWPIMAIARGLDDRPTRLGSPGVPMYG-YNVQLLNEVTGEPCGVNEKGMLVVEGPL 446
Cdd:PRK06164 309 GELAALAR-ARGVPLTGLYGSSEV-QALVALQPATDPVSVRIEGGGRPASPeARVRARDPQDGALLPDGESGEIEIRAPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 -------PPGCIQTIWGDDGRFvktywslfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPG 519
Cdd:PRK06164 387 lmrgyldNPDATARALTDDGYF-------------RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 520 VAEVAVVGVKdaLKGQ-VAVAFVIPKESDSLedrdvahsQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSG 591
Cdd:PRK06164 454 VAAAQVVGAT--RDGKtVPVAFVIPTDGASP--------DEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
66-602 |
2.47e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 122.73 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVympmIAEAH----ITLLACARIGAIHSVVFGG 141
Cdd:PRK07788 63 PDRAALI------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAV----LARNHrgfvLALYAAGKVGARIILLNTG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 142 FAS---HSVAARiDDAKPVLIVSAdagarggkiipYKKLLDDAisqaqHQPRHVLLVDRGLAKMARVSGRDVD-FASLRH 217
Cdd:PRK07788 133 FSGpqlAEVAAR-EGVKALVYDDE-----------FTDLLSAL-----PPDLGRLRAWGGNPDDDEPSGSTDEtLDDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 218 QHIGARVPVAwleSNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTI-FggKAGSVFFCASDI--GWVVGHsyivy 294
Cdd:PRK07788 196 GSSTAPLPKP---PKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVpF--RAGETTLLPAPMfhATGWAH----- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 apLLAGMA---TIV----YEGLPTWPDcgvwwtiVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLD 367
Cdd:PRK07788 266 --LTLAMAlgsTVVlrrrFDPEATLED-------IAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 368 EPTASWVSNTLDvPVIDN-YWQTESGWPIMAIARGLDDRPTRLGSPGVpmyGYNVQLLNEvTGEPCGVNEKGMLVVEGPL 446
Cdd:PRK07788 337 PELATRALEAFG-PVLYNlYGSTEVAFATIATPEDLAEAPGTVGRPPK---GVTVKILDE-NGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 P------PGCIQTIwgdDGrfvktywsLFSrpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGV 520
Cdd:PRK07788 412 PfegytdGRDKQII---DG--------LLS-----SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 521 AEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK07788 476 VEAAVIGVDDEEFGQRLRAFVVKAPGAALD--------EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
..
gi 16128320 601 IC 602
Cdd:PRK07788 548 MD 549
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
66-596 |
4.47e-29 |
|
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: 121.23 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAihsvVFGGFASH 145
Cdd:cd17646 12 PDAPAVVD------EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGA----AYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDdakpvlIVSADAGARggkiipykkllddaisqaqhqprhVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVP 225
Cdd:cd17646 82 YPADRLA------YMLADAGPA------------------------VVLTTADLAARLPAGGDVALLGDEALAAPPATPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATsMDTIFGGKAGSVFFCASDIGWVVGhSYIVYAPLLAGmATIV 305
Cdd:cd17646 132 LVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAG-ARLV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 306 YEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkhDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDN 385
Cdd:cd17646 209 VARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG----SCASLRRVFCSGEALPPELAARFLALPGAELHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 386 YWQTE-----SGWPimaiARGLDDRPTRlgSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGplppgcIQTIWGDDGR 460
Cdd:cd17646 285 YGPTEaaidvTHWP----VRGPAETPSV--PIGRPVPNTRLYVLDD-ALRPVPVGVPGELYLGG------VQLARGYLGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 461 -------FVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALK 533
Cdd:cd17646 352 paltaerFVPDPFGPGSR-MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAG 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 534 GQVAVAFVIPkeSDSLEDRDVAHSQEKAIMALVDSQIgnfgrPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd17646 431 AARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMV-----PAAFVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
63-596 |
4.73e-29 |
|
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: 120.91 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 63 EKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGF 142
Cdd:cd17651 6 ARTPDAPALVA------EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 143 ASHSVAARIDDAKPVLIVSADAgarggkiipykkllddaisqaqhqprhvllvDRGLAKMARVSGRDVDFASLRHQHIGA 222
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPA-------------------------------LAGELAVELVAVTLLDQPGAAAGADAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 223 RVPVawLESNETSCILYTSGTTGKPKGVqRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIvYAPLLAGmA 302
Cdd:cd17651 129 PDPA--LDADDLAYVIYTSGSTGRPKGV-VMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAG-A 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 303 TIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKhdLSSLEVLYLAGEPL--DEPTASWVSNTLDV 380
Cdd:cd17651 204 TLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVR--LAALRYLLTGGEQLvlTEDLREFCAGLPGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 381 PVIDNYWQTESGWPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGCIqtiwGDDG 459
Cdd:cd17651 282 RLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDA-ALRPVPPGVPGELYIGGAgLARGYL----NRPE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 ----RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ 535
Cdd:cd17651 357 ltaeRFVPDPFVPGAR-MYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 536 VAVAFVIPkesDSLEDRDVAhsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd17651 436 RLVAYVVG---DPEAPVDAA-----ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
65-593 |
4.82e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.07 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 65 QPEALALIAVSSEteeeRTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFAS 144
Cdd:PRK09088 8 QPQRLAAVDLALG----RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 145 HSVAARIDDAKPVLIVSADAGARGGKIipykkllddaisqaqhqprhvllvdrglakmarvsgrDVDFASLRHQHIGAR- 223
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVAAGRTD-------------------------------------VEDLAAFIASADALEp 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 VPVAWLESNETSCILYTSGTTGKPKGV---QRDVGGYAV--ALATSMDtifggkAGSVFFCASDIGWVVGHSYIVYAPLL 298
Cdd:PRK09088 127 ADTPSIPPERVSLILFTSGTSGQPKGVmlsERNLQQTAHnfGVLGRVD------AHSSFLCDAPMFHIIGLITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 299 AGMATIVYEGLPtwPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKhdLSSLEVLYLAGEP-LDEPTASWVSNt 377
Cdd:PRK09088 201 VGGSILVSNGFE--PKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAA--LRHLTALFTGGAPhAAEDILGWLDD- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 378 lDVPVIDNYWQTESGWPI-MAIARGLDDrpTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGciqtiw 455
Cdd:PRK09088 276 -GIPMVDGFGMSEAGTVFgMSVDCDVIR--AKAGAAGIPTPTVQTRVVDD-QGNDCPAGVPGELLLRGPnLSPG------ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 gddgrfvktYWSlfsRPV-----------YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVA 524
Cdd:PRK09088 346 ---------YWR---RPQataraftgdgwFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECA 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 525 VVGVKDALKGQVAVAFVIPKESDSLEDRDVAhsqekaimALVDSQIGNFGRPAHVWFVSQLPKTRSGKM 593
Cdd:PRK09088 414 VVGMADAQWGEVGYLAIVPADGAPLDLERIR--------SHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
60-598 |
2.17e-28 |
|
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: 118.97 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 60 RWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVF 139
Cdd:cd05920 23 RSAARHPDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 140 GGFASHSVAARIDDAKPVLIVsadagarggkiipykklLDDAISQAQHQPrhvllvdrglakMARvsgrdvdfaSLRHQH 219
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYI-----------------VPDRHAGFDHRA------------LAR---------ELAESI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 220 igarvpvawlesNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDtIFGGKAGSVFFCASDigwvVGHSYIVYAP--- 296
Cdd:cd05920 139 ------------PEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAE-VCGLDQDTVYLAVLP----AAHNFPLACPgvl 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 297 --LLAGmATIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKfpTAEIRKHDLSSLEVLYLAGEPLDEPTASWV 374
Cdd:cd05920 202 gtLLAG-GRVV---LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLD--AAASRRADLSSLRLLQVGGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTLDVPVIDNYwqtesgwpimAIARGLDDRpTRLGSP--------GVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPL 446
Cdd:cd05920 276 PPVLGCTLQQVF----------GMAEGLLNY-TRLDDPdeviihtqGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 ppgciqTIWG-------------DDGrfvktywslfsrpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEES 513
Cdd:cd05920 345 ------TIRGyyrapehnaraftPDG-------------FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENL 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 514 ISSHPGVAEVAVVGVKDALKGQVAVAFVIPkesdsledRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKM 593
Cdd:cd05920 406 LLRHPAVHDAAVVAMPDELLGERSCAFVVL--------RDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
....*
gi 16128320 594 LRRTI 598
Cdd:cd05920 478 DKKAL 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
79-600 |
4.35e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 115.63 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVympmIAEAH----ITLLACARIGAiHSVVFG-GFASHSVAARIDD 153
Cdd:PRK13382 64 DELGTLTWRELDERSDALAAALQALPIGEPRVVGI----MCRNHrgfvEALLAANRIGA-DILLLNtSFAGPALAEVVTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 154 AKpVLIVSADAgarggkiiPYKKLLDDAISQAQHQPRHVLLVDrglakmarvSGRDVDFASLRHQHIGARVPVAwleSNE 233
Cdd:PRK13382 139 EG-VDTVIYDE--------EFSATVDRALADCPQATRIVAWTD---------EDHDLTVEVLIAAHAGQRPEPT---GRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 234 TSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIfGGKAGSVFFCASDIGWVVGHSYIVYAPLLAgmATIVYEGLPTwP 313
Cdd:PRK13382 198 GRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRT-PWRAEEPTVIVAPMFHAWGFSQLVLAASLA--CTIVTRRRFD-P 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 314 DCGVwwTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLdEPTAswVSNTLDV--PVI-DNYWQTE 390
Cdd:PRK13382 274 EATL--DLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRM-RPDV--VIAFMDQfgDVIyNNYNATE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 391 SGWPIMAIARGLDDRPTRLGSPgvPMyGYNVQLLNEVTGEpcgvnekgmlvvegpLPPGCIQTIWGDDGRFVKTYWSLFS 470
Cdd:PRK13382 349 AGMIATATPADLRAAPDTAGRP--AE-GTEIRILDQDFRE---------------VPTGEVGTIFVRNDTQFDGYTSGST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 471 RPVYATF----DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKEs 546
Cdd:PRK13382 411 KDFHDGFmasgDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP- 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16128320 547 dsledrDVAHSQEKaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK13382 490 ------GASATPET-LKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-596 |
7.39e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 114.07 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 93 VNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVF-------GGFASHSVAAridDAKPVlIVSADAG 165
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnptlKESVLRYLVA---DAGGR-IVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 166 ARggkiipykKLLDDAISQAqHQPRHVLLVDRglakmARVSGRDVDfaslrhqhigaRVPVawlESNETSCILYTSGTTG 245
Cdd:cd05922 79 AA--------DRLRDALPAS-PDPGTVLDADG-----IRAARASAP-----------AHEV---SHEDLALLLYTSGSTG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 246 KPKGV---QRDVggyaVALATSMDTIFGGKAGSVFFCASDIGWVVGHSyIVYAPLLAGmATIVYEGLPTWPDcGVWwTIV 322
Cdd:cd05922 131 SPKLVrlsHQNL----LANARSIAEYLGITADDRALTVLPLSYDYGLS-VLNTHLLRG-ATLVLTNDGVLDD-AFW-EDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 323 EKYQVSRMFSAPTAIRVLK--KFPTAEirkhdLSSLEVLYLAGEPLDEPTASWVSNTL---DVPVIdnYWQTESgWPIMA 397
Cdd:cd05922 203 REHGATGLAGVPSTYAMLTrlGFDPAK-----LPSLRYLTQAGGRLPQETIARLRELLpgaQVYVM--YGQTEA-TRRMT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 398 I--ARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLppgciqtiwgddgrFVKTYWSLFSRP--- 472
Cdd:cd05922 275 YlpPERILEKP---GSIGLAIPGGEFEILDD-DGTPTPPGEPGEIVHRGPN--------------VMKGYWNDPPYRrke 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 473 -----VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESD 547
Cdd:cd05922 337 grgggVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKID 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16128320 548 SledrdvahsqeKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd05922 417 P-----------KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
59-596 |
1.78e-26 |
|
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: 113.06 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 59 DRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHsvv 138
Cdd:cd12117 4 EEQAARTPDAVAVVY------GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 139 fggfashsvaARIDDAKPVLIVS---ADAGARggkiipykkllddaisqaqhqprhVLLVDRGLAKMARVSGRDVDFASL 215
Cdd:cd12117 75 ----------VPLDPELPAERLAfmlADAGAK------------------------VLLTDRSLAGRAGGLEVAVVIDEA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 216 RHQHiGARVPVAWLESNETSCILYTSGTTGKPKGV---QRDVggyaVALATSMDTIfGGKAGSVFFCASDIGWVVGhSYI 292
Cdd:cd12117 121 LDAG-PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVavtHRGV----VRLVKNTNYV-TLGPDDRVLQTSPLAFDAS-TFE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 293 VYAPLLAGMATIVYEGlPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLkkfptAEIRKHDLSSLEVLYLAGEPLDeptAS 372
Cdd:cd12117 194 IWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVLWLTAALFNQL-----ADEDPECFAGLRELLTGGEVVS---PP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 373 WVSNTL----DVPVIDNYWQTES-----GWPIMAIARGLDDRPTrlgspGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVE 443
Cdd:cd12117 265 HVRRVLaacpGLRLVNGYGPTENttfttSHVVTELDEVAGSIPI-----GRPIANTRVYVLDE-DGRPVPPGVPGELYVG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 GplpPGCIQTIWGDDG----RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPg 519
Cdd:cd12117 339 G---DGLALGYLNRPAltaeRFVADPFGPGER-LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHP- 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 520 vaevavvgvkdalkgQVAVAFVIPKESDSLEDRDVAH------SQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKM 593
Cdd:cd12117 414 ---------------GVREAVVVVREDAGGDKRLVAYvvaegaLDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
...
gi 16128320 594 LRR 596
Cdd:cd12117 479 DRR 481
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
55-596 |
1.99e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 115.34 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMP----MIaeahITLLACAR 130
Cdd:COG1020 479 HELFEAQAARTPDAVAVVF------GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErsleMV----VALLAVLK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 131 IGAIHsvvfggfashsV-------AARIDDakpVLivsADAGARggkiipykkllddaisqaqhqprhVLLVDRGLAkmA 203
Cdd:COG1020 549 AGAAY-----------VpldpaypAERLAY---ML---EDAGAR------------------------LVLTQSALA--A 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 204 RVSGRDVDFASLRHQHIG---ARVPVAWLESNETSCILYTSGTTGKPKGV---QRDVggyaVALATSMDTIFGGKAGSVF 277
Cdd:COG1020 586 RLPELGVPVLALDALALAaepATNPPVPVTPDDLAYVIYTSGSTGRPKGVmveHRAL----VNLLAWMQRRYGLGPGDRV 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 278 FCASDIGWVVGHsYIVYAPLLAGmATIV---YEGLPtwpDCGVWWTIVEKYQVSRMFSAPTAIRVLkkfptAEIRKHDLS 354
Cdd:COG1020 662 LQFASLSFDASV-WEIFGALLSG-ATLVlapPEARR---DPAALAELLARHRVTVLNLTPSLLRAL-----LDAAPEALP 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 355 SLEVLYLAGEPLDEPTAS-WVSNTLDVPVIDNYWQTESGwpIMAIARGLDDRPTRLGSP--GVPMYGYNVQLLNEvTGEP 431
Cdd:COG1020 732 SLRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETT--VDSTYYEVTPPDADGGSVpiGRPIANTRVYVLDA-HLQP 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 432 CGVNEKGMLVVEGPlppGCIQTIWGDDG----RFVKTYWSLFSRPVYATFDWGIRDADG---YhfiLGRTDDVINVAGHR 504
Cdd:COG1020 809 VPVGVPGELYIGGA---GLARGYLNRPEltaeRFVADPFGFPGARLYRTGDLARWLPDGnleF---LGRADDQVKIRGFR 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 505 --LGtrEIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEKAIMALVDsqignfgrPAHVWFV 582
Cdd:COG1020 883 ieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMV--------PAAVVLL 952
|
570
....*....|....
gi 16128320 583 SQLPKTRSGKMLRR 596
Cdd:COG1020 953 LPLPLTGNGKLDRL 966
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
224-601 |
5.12e-26 |
|
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: 112.24 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 VPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMAT 303
Cdd:cd17642 176 KPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 304 IVYegLPTWPDcGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVI 383
Cdd:cd17642 256 VVL--MYKFEE-ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVD--KYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 384 -DNYWQTESGWPIMAIARGlDDRPtrlGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPL-------PPGCIQTIW 455
Cdd:cd17642 331 rQGYGLTETTSAILITPEG-DDKP---GAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMimkgyvnNPEATKALI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 GDDGrfvktyWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ 535
Cdd:cd17642 407 DKDG------W-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 536 VAVAFVIPKESDSLedrdvahsQEKAIMALVDSQIGNFGR-PAHVWFVSQLPKTRSGKMLRRTIQAI 601
Cdd:cd17642 474 LPAAVVVLEAGKTM--------TEKEVMDYVASQVSTAKRlRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
5-57 |
8.68e-26 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 100.24 E-value: 8.68e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16128320 5 EFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNA 57
Cdd:pfam16177 3 ALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPFAKWFVGGKLNVCYNC 55
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
66-596 |
6.35e-25 |
|
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: 108.16 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHsvvfggfash 145
Cdd:cd17643 1 PEAVAVVD------EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAY---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 svaARIDDAKPVLIVSAdagarggkiipykkLLDDAisqaqhQPRhvLLVDRGlakmarvsgrdvdfaslrhqhigarvp 225
Cdd:cd17643 65 ---VPIDPAYPVERIAF--------------ILADS------GPS--LLLTDP--------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 vawlesNETSCILYTSGTTGKPKGVQ---RDVggyaVALATSMDTIFGgkagsvfFCASDIgWVVGHSYI-------VYA 295
Cdd:cd17643 93 ------DDLAYVIYTSGSTGRPKGVVvshANV----LALFAATQRWFG-------FNEDDV-WTLFHSYAfdfsvweIWG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 296 PLLAGMATIVyegLPTW----PDcgVWWTIVEKYQVSRMFSAPTAIRVLkkFPTAEIRKHDLSSLEVLYLAGEPLDEPT- 370
Cdd:cd17643 155 ALLHGGRLVV---VPYEvarsPE--DFARLLRDEGVTVLNQTPSAFYQL--VEAADRDGRDPLALRYVIFGGEALEAAMl 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 371 ASWVSN-TLDVP-VIDNYWQTESgwPIMAIARGLD--DRPTRLGSP-GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP 445
Cdd:cd17643 228 RPWAGRfGLDRPqLVNMYGITET--TVHVTFRPLDaaDLPAAAASPiGRPLPGLRVYVLDA-DGRPVPPGVVGELYVSGA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 446 lppGCIQTIWGDDG----RFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVA 521
Cdd:cd17643 305 ---GVARGYLGRPEltaeRFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVR 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 522 EVAVVGVKDALKGQVAVAFVIPKESDSLEDRDV-AHSQEKaimaLVDsqignFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd17643 382 DAAVIVREDEPGDTRLVAYVVADDGAAADIAELrALLKEL----LPD-----YMVPARYVPLDALPLTVNGKLDRA 448
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
58-595 |
7.76e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.41 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQ----PEALALIAvsseteEERTFTFRQLHDEVNAVASMLR-SLGVQRGDRVLVYMPMIAEAHITLLACARIG 132
Cdd:PRK06839 4 IAYWIEKRaylhPDRIAIIT------EEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 AIhsvvfggfashSVAARIDDAKPVLIVS-ADAGARggkiipykKLLddaiSQAQHQPRHVLLVDR-GLAKMARVSGRDv 210
Cdd:PRK06839 78 CI-----------AVPLNIRLTENELIFQlKDSGTT--------VLF----VEKTFQNMALSMQKVsYVQRVISITSLK- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 211 dfASLRHQHIGARVPvawlESNETSCILYTSGTTGKPKGvqrdvggyavALATSMDTIFGG--KAGSVFFCASDIGWVV- 287
Cdd:PRK06839 134 --EIEDRKIDNFVEK----NESASFIICYTSGTTGKPKG----------AVLTQENMFWNAlnNTFAIDLTMHDRSIVLl 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 288 ------GHSYIVYAPLLAGMATIVYEGLPtwPDCGVwwTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYL 361
Cdd:PRK06839 198 plfhigGIGLFAFPTLFAGGVIIVPRKFE--PTKAL--SMIEKHKVTVVMGVPTIHQALINCSKFE--TTNLQSVRWFYN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 362 AGEPLDEPTASWVSNTlDVPVIDNYWQTESGWPIMAIARglDDRPTRLGSPGVPMYGYNVQLLNEVTGEpCGVNEKGMLV 441
Cdd:PRK06839 272 GGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSE--EDARRKVGSIGKPVLFCDYELIDENKNK-VEVGEVGELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 442 VEGPlppgciqtiwgddgRFVKTYWSlfsRPV----------YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIE 511
Cdd:PRK06839 348 IRGP--------------NVMKEYWN---RPDateetiqdgwLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 512 ESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLedrdvahsQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSG 591
Cdd:PRK06839 411 QVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL--------IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATG 482
|
....
gi 16128320 592 KMLR 595
Cdd:PRK06839 483 KIQK 486
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
79-607 |
1.77e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 107.30 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDD--AKp 156
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDsgAK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 157 VLIVSADagarggkiipykkLLDDAISQAQHQPRHV--LLVDRGlakmaRVSGRDvDFASLRHQHIGARVPVAWLESNet 234
Cdd:PRK08276 86 VLIVSAA-------------LADTAAELAAELPAGVplLLVVAG-----PVPGFR-SYEEALAAQPDTPIADETAGAD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 235 scILYTSGTTGKPKGVQR-----DVGGYAVALATSMDTIFGGKAGSVFFCASDIgwvvGHSyivyAPLLAGMA------T 303
Cdd:PRK08276 145 --MLYSSGTTGRPKGIKRplpglDPDEAPGMMLALLGFGMYGGPDSVYLSPAPL----YHT----APLRFGMSalalggT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 304 IVYegLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTA----SWVSntld 379
Cdd:PRK08276 215 VVV--MEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKramiDWWG---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 380 vPVIDNYWQ-TESGWPIMAIARGLDDRPtrlGSPGVPMYGyNVQLLNEvTGEPCGVNEKGMLVVEGPLPPgciQTIWGDD 458
Cdd:PRK08276 288 -PIIHEYYAsSEGGGVTVITSEDWLAHP---GSVGKAVLG-EVRILDE-DGNELPPGEIGTVYFEMDGYP---FEYHNDP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 459 GRFVKTY----WSlfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:PRK08276 359 EKTAAARnphgWV-------TVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMG 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 535 QVAVAFVIPKESdslEDRDVAHSQEkaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIqaicegRDP 607
Cdd:PRK08276 432 ERVKAVVQPADG---ADAGDALAAE--LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL------RDR 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
81-598 |
6.23e-24 |
|
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: 105.06 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASML-RSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLI 159
Cdd:cd05941 9 GDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 VsadagarggkiipykkllddaisqaqhqprhvllvDRGLakmarvsgrdvdfaslrhqhigarvpvawlesnetscILY 239
Cdd:cd05941 89 L-----------------------------------DPAL-------------------------------------ILY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGV---QRDVGGYAVALA-----TSMDTI------------FGGKAGSVFFCASDIgWVVGHSYIVYAPLLA 299
Cdd:cd05941 97 TSGTTGRPKGVvltHANLAANVRALVdawrwTEDDVLlhvlplhhvhglVNALLCPLFAGASVE-FLPKFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 300 GMATIVYEGLPTwpdcgVWWTIVEKYQvsRMFSAPTAIRvlkKFPTAEIRkhdlsslevLYLAGE-PLDEPT-ASWVSNT 377
Cdd:cd05941 176 MPSITVFMGVPT-----IYTRLLQYYE--AHFTDPQFAR---AAAAERLR---------LMVSGSaALPVPTlEEWEAIT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 378 LDVpVIDNYWQTESGwpiMAIARGLD-DRptRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppGCIQTIWG 456
Cdd:cd05941 237 GHT-LLERYGMTEIG---MALSNPLDgER--RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGP---SVFKEYWN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 457 ----------DDGRFVktywslfsrpvyaTFDWGIRDADGYHFILGRT-DDVINVAGHRLGTREIEESISSHPGVAEVAV 525
Cdd:cd05941 308 kpeatkeeftDDGWFK-------------TGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 526 VGVKDALKGQVAVAFVIPKESD---SLED-RDVAhsqeKAIMAlvdsqigNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd05941 375 IGVPDPDWGERVVAVVVLRAGAaalSLEElKEWA----KQRLA-------PYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
57-593 |
1.08e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 105.24 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 57 AIDRWLEKQPEALALIAvsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI-- 134
Cdd:PRK12583 23 AFDATVARFPDREALVV----RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 ----------------HSVVFG-----GFASHSVAARIDDAKPVLiVSADAGARGGKIIPYkklLDDAISQAQHQPRHVL 193
Cdd:PRK12583 99 ninpayraseleyalgQSGVRWvicadAFKTSDYHAMLQELLPGL-AEGQPGALACERLPE---LRGVVSLAPAPPPGFL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 194 LVDRGLAKMARVSGRDVDFASlrhqhigarvpvAWLESNETSCILYTSGTTGKPKGVqrdvggyavalATSMDTIFGgka 273
Cdd:PRK12583 175 AWHELQARGETVSREALAERQ------------ASLDRDDPINIQYTSGTTGFPKGA-----------TLSHHNILN--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 274 gSVFFCASDIGWVVGHSYIVYAPL----------LAGM---ATIVYEGLPTWPDCGVwwTIVEKYQVSRMFSAPTAIrvL 340
Cdd:PRK12583 229 -NGYFVAESLGLTEHDRLCVPVPLyhcfgmvlanLGCMtvgACLVYPNEAFDPLATL--QAVEEERCTALYGVPTMF--I 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 341 KKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVP-VIDNYWQTESGwPIMAIARGLDDRPTRLGSPGVPMYGY 419
Cdd:PRK12583 304 AELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETS-PVSLQTTAADDLERRVETVGRTQPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 420 NVQLLnEVTGEPCGVNEKGMLVVEGPLppgCIQTIWGDDGRfvkTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVIN 499
Cdd:PRK12583 383 EVKVV-DPDGATVPRGEIGELCTRGYS---VMKGYWNNPEA---TAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMII 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 500 VAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVI--PKESDSLED-RDVAHsqekaimalvdSQIGNFGRP 576
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRlhPGHAASEEElREFCK-----------ARIAHFKVP 524
|
570
....*....|....*..
gi 16128320 577 AHVWFVSQLPKTRSGKM 593
Cdd:PRK12583 525 RYFRFVDEFPMTVTGKV 541
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
77-600 |
2.35e-23 |
|
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: 103.95 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 77 ETEEERTFTFRQLHDEVNAVASMLRSlGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakP 156
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKV---------------------P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 157 VLIvSADAGARGgkiipykklLDDAISQAQhqPRHVLLVDRGLAKMARVSGRDVDFA-------SLRHQ---------HI 220
Cdd:cd05909 59 VML-NYTAGLRE---------LRACIKLAG--IKTVLTSKQFIEKLKLHHLFDVEYDarivyleDLRAKiskadkckaFL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 221 GARVPVAWL---------ESNETSCILYTSGTTGKPKGV---QRDVggyaVALATSMDTIFGGKAGSVFFCASDIGWVVG 288
Cdd:cd05909 127 AGKFPPKWLlrifgvapvQPDDPAVILFTSGSEGLPKGVvlsHKNL----LANVEQITAIFDPNPEDVVFGALPFFHSFG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 289 HSYIVYAPLLAGMAtIVYEGLPTWPDCGVwwTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkhDLSSLEVLYLAGEPLDE 368
Cdd:cd05909 203 LTGCLWLPLLSGIK-VVFHPNPLDYKKIP--ELIYDKKATILLGTPTFLRGYARAAHPE----DFSSLRLVVAGAEKLKD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 369 PTASWVSNTLDVPVIDNYWQTESGwPIMAIARGLDDRptRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGP-LP 447
Cdd:cd05909 276 TLRQEFQEKFGIRILEGYGTTECS-PVISVNTPQSPN--KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPnVM 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 448 PGCIQTIWGDDGRFVKTYwslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSH-PGVAEVAVV 526
Cdd:cd05909 353 LGYLNEPELTSFAFGDGW--------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVV 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128320 527 GVKDALKGQVAVAFVIPKESDSLEDRDVAHSqekaimalvdSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:cd05909 425 SVPDGRKGEKIVLLTTTTDTDPSSLNDILKN----------AGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
79-518 |
7.30e-23 |
|
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: 101.90 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAihsVVFGGFASHSVAAriddakpVL 158
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA---VPVPIYPTSSAEQ-------IA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 159 IVSADAGARggkiipykkllddaisqaqhqprhVLLVDrglakmarvsgrdvdfaslrhqhigarvpvawlESNETSCIL 238
Cdd:cd05907 71 YILNDSEAK------------------------ALFVE---------------------------------DPDDLATII 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGYaVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYEGLPTwpdcgvw 318
Cdd:cd05907 94 YTSGTTGRPKGVMLSHRNI-LSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAG-ARIYFASSAE------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 wTIVEKYQVSR---MFSAPtaiRVLKKFpTAEIRKHD-------------LSSLEVLYLAGEPLDEPTASWvSNTLDVPV 382
Cdd:cd05907 165 -TLLDDLSEVRptvFLAVP---RVWEKV-YAAIKVKAvpglkrklfdlavGGRLRFAASGGAPLPAELLHF-FRALGIPV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 383 IDNYWQTESGwPIMAIARGLDdrpTRLGSPGVPMYGYNVQllnevtgepcgVNEKGMLVVEGplpPGCIQTIWGDDGrfv 462
Cdd:cd05907 239 YEGYGLTETS-AVVTLNPPGD---NRIGTVGKPLPGVEVR-----------IADDGEILVRG---PNVMLGYYKNPE--- 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 463 KTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVI-NVAGHRLGTREIEESISSHP 518
Cdd:cd05907 298 ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASP 354
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
66-592 |
9.12e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 102.27 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:PRK07798 17 PDRVALVC------GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPV-LIVSADAGARGGKIIPYKKLLddaisqaqhqpRHVLLVDRGLAKMARVSGrdVDFASLRHQHIGARV 224
Cdd:PRK07798 91 ELRYLLDDSDAVaLVYEREFAPRVAEVLPRLPKL-----------RTLVVVEDGSGNDLLPGA--VDYEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 225 PVAwlESNETSCILYTSGTTGKPKGV---QRDV-----GGYAVALATSMDTIFG------GKAGSVFFCASDI--G---W 285
Cdd:PRK07798 158 FGE--RSPDDLYLLYTGGTTGMPKGVmwrQEDIfrvllGGRDFATGEPIEDEEElakraaAGPGMRRFPAPPLmhGagqW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 VvghsyiVYAPLLAGMATIVYEGLPTWPDcGVWWTIvEKYQVSRMFSAPTA-----IRVLkkfptAEIRKHDLSSLEVLY 360
Cdd:PRK07798 236 A------AFAALFSGQTVVLLPDVRFDAD-EVWRTI-EREKVNVITIVGDAmarplLDAL-----EARGPYDLSSLFAIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 361 LAGEPLDEPT-ASWVSNTLDVPVIDNYWQTESGWPIMAIArglDDRPTRLGSPGVPMyGYNVQLLNEVTGE-PCGVNEKG 438
Cdd:PRK07798 303 SGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTV---AKGAVHTGGPRFTI-GPRTVVLDEDGNPvEPGSGEIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 439 MLVVEGPLPPGciqtIWGDDGRFVKTY-------WSLfsrpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIE 511
Cdd:PRK07798 379 WIARRGHIPLG----YYKDPEKTAETFptidgvrYAI-------PGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 512 ESISSHPGVAevavvgvkDALK--------GQVAVAFVIPKESDSLEDRDVAhsqekaimALVDSQIGNFGRPAHVWFVS 583
Cdd:PRK07798 448 EALKAHPDVA--------DALVvgvpderwGQEVVAVVQLREGARPDLAELR--------AHCRSSLAGYKVPRAIWFVD 511
|
....*....
gi 16128320 584 QLPKTRSGK 592
Cdd:PRK07798 512 EVQRSPAGK 520
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
59-592 |
1.72e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 101.81 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 59 DRWLEKQPEALALIAVssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI---- 134
Cdd:PRK08315 23 DRTAARYPDREALVYR----DQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIlvti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 --------------HS-----VVFGGFASHSVAARIDDAKPVLiVSADAGARGGKIIPYkklLDDAISQAQHQPRHVLLV 195
Cdd:PRK08315 99 npayrlseleyalnQSgckalIAADGFKDSDYVAMLYELAPEL-ATCEPGQLQSARLPE---LRRVIFLGDEKHPGMLNF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 196 DRGLAkmarvSGRDVDFASLRHqhIGARvpvawLESNETSCILYTSGTTGKPKGV---QRDVG--GYAVALA---TSMDT 267
Cdd:PRK08315 175 DELLA-----LGRAVDDAELAA--RQAT-----LDPDDPINIQYTSGTTGFPKGAtltHRNILnnGYFIGEAmklTEEDR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 268 I-----FggkagsvFFCasdIGWVVGhsyiVYAPLLAGmATIVY--EGLptwpDCGVWWTIVEK------YQVSRMFsap 334
Cdd:PRK08315 243 LcipvpL-------YHC---FGMVLG----NLACVTHG-ATMVYpgEGF----DPLATLAAVEEerctalYGVPTMF--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 335 taIRVL--KKFPtaeirKHDLSSLEVLYLAGEPLDEPTASwvsntldvPVIDN---------YWQTESGwPIMAIARGLD 403
Cdd:PRK08315 301 --IAELdhPDFA-----RFDLSSLRTGIMAGSPCPIEVMK--------RVIDKmhmsevtiaYGMTETS-PVSTQTRTDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 404 DRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPL--------PPGCIQTIwgDDGRFVKTYwslfsrpvya 475
Cdd:PRK08315 365 PLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSvmkgywndPEKTAEAI--DADGWMHTG---------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 476 tfDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdva 555
Cdd:PRK08315 433 --DLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLT----- 505
|
570 580 590
....*....|....*....|....*....|....*..
gi 16128320 556 hsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:PRK08315 506 ---EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
66-596 |
1.93e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 101.31 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAVSSETeeerTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:PRK13391 11 PDKPAVIMASTGE----VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKP-VLIVSADAgarggkiipykklLDDAISQAQHQP--RHVLLVDrGLAKMARVsgrdVDFASLRHQHIGA 222
Cdd:PRK13391 87 EAAYIVDDSGArALITSAAK-------------LDVARALLKQCPgvRHRLVLD-GDGELEGF----VGYAEAVAGLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 223 RVPVAWLESNetscILYTSGTTGKPKGVQRDVGGYAVALATSM----DTIFGGKAGSVFFCASDigwvVGHSyivyAPLL 298
Cdd:PRK13391 149 PIADESLGTD----MLYSSGTTGRPKGIKRPLPEQPPDTPLPLtaflQRLWGFRSDMVYLSPAP----LYHS----APQR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 299 AGMAT-------IVYEGLptwpDCGVWWTIVEKYQVSRMFSAPTA-IRVLKkFPTAEIRKHDLSSLEVLYLAGEP----L 366
Cdd:PRK13391 217 AVMLVirlggtvIVMEHF----DAEQYLALIEEYGVTHTQLVPTMfSRMLK-LPEEVRDKYDLSSLEVAIHAAAPcppqV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 367 DEPTASWVSntldvPVIDNYWQTESGWPIMAI--ARGLDDRptrlGSPGVPMYGyNVQLLNEvTGEPCgvnekgmlvveg 444
Cdd:PRK13391 292 KEQMIDWWG-----PIIHEYYAATEGLGFTACdsEEWLAHP----GTVGRAMFG-DLHILDD-DGAEL------------ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 445 plPPGCIQTIWGDDGR-FV------KTYWSLFSRPVYATF-DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISS 516
Cdd:PRK13391 349 --PPGEPGTIWFEGGRpFEylndpaKTAEARHPDGTWSTVgDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLIT 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 517 HPGVAEVAVVGVKDALKGQVAVAFVIPKESdslEDRDVAHSQEkaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK13391 427 HPKVADAAVFGVPNEDLGEEVKAVVQPVDG---VDPGPALAAE--LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKR 501
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-598 |
2.04e-22 |
|
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: 101.17 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 74 VSSETEEERT-FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI-HSVVFGGFASHsVAARI 151
Cdd:cd12119 15 VSRTHEGEVHrYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINPRLFPEQ-IAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 152 DDAKP-VLIVSADAGARGGKIIPYKKLLddaisqaqhqpRHVLLVDRGLAKMARVSGRDVDFASLrhqhIGARVPVA-WL 229
Cdd:cd12119 94 NHAEDrVVFVDRDFLPLLEAIAPRLPTV-----------EHVVVMTDDAAMPEPAGVGVLAYEEL----LAAESPEYdWP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 230 ESNET--SCILYTSGTTGKPKGV---QRDVggYAVALATSMdtifggkAGSVFFCASDIGWVV-----GHSY-IVYAPLL 298
Cdd:cd12119 159 DFDENtaAAICYTSGTTGNPKGVvysHRSL--VLHAMAALL-------TDGLGLSESDVVLPVvpmfhVNAWgLPYAAAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 299 AGmATIVYEGLPTWPDcgVWWTIVEKYQVSrmFSA--PTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSN 376
Cdd:cd12119 230 VG-AKLVLPGPYLDPA--SLAELIEREGVT--FAAgvPTVWQGLLDHLEAN--GRDLSSLRRVVIGGSAVPRSLIEAFEE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 377 tLDVPVIDNYWQTESGwPIMAIAR--------GLDDRPTRLGSPGVPMYGYNVQLLNEVTGE-PCGVNEKGMLVVEGPL- 446
Cdd:cd12119 303 -RGVRVIHAWGMTETS-PLGTVARppsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGRElPWDGKAVGELQVRGPWv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 ------PPGCIQTIWgDDGRFvktywslfsrpvyATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGV 520
Cdd:cd12119 381 tksyykNDEESEALT-EDGWL-------------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 521 AEVAVVGVKDALKGQVAVAFVIPKesdslEDRDVAHsqeKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd12119 447 AEAAVIGVPHPKWGERPLAVVVLK-----EGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
82-600 |
2.82e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.83 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARiddakpvlivs 161
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQ----------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 adAGARGGKIIpykkllddaISQAQHQPR-HVLLVDRGLAKMARVSGRD--VDFASLRhQHIGARVPVAWLESNETSCIL 238
Cdd:PLN02246 118 --AKASGAKLI---------ITQSCYVDKlKGLAEDDGVTVVTIDDPPEgcLHFSELT-QADENELPEVEISPDDVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGYAVALATSMDtifgGKAGSVFFCASDIGWVV---GHSYIVYAPLLAGM---ATIVYegLPTW 312
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLVTSVAQQVD----GENPNLYFHSDDVILCVlpmFHIYSLNSVLLCGLrvgAAILI--MPKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 313 pDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVI-DNYWQTES 391
Cdd:PLN02246 260 -EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVE--KYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 392 GwPI--MAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPL--------PPGCIQTIwGDDGrf 461
Cdd:PLN02246 337 G-PVlaMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQimkgylndPEATANTI-DKDG-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 462 vktyWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFV 541
Cdd:PLN02246 413 ----W-------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 542 I-PKESDSLEDrdvahsqekAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PLN02246 482 VrSNGSEITED---------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
66-602 |
4.13e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALiavssETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:PRK07514 16 RDAPFI-----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPVLIVSADAGArggkiipykklldDAISQ--AQHQPRHV--LLVDRGLAKMARVSGRDVDFASlrhqhig 221
Cdd:PRK07514 91 ELDYFIGDAEPALVVCDPANF-------------AWLSKiaAAAGAPHVetLDADGTGSLLEAAAAAPDDFET------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 arVPVAwleSNETSCILYTSGTTGKPKGV---QRDVGGYAVALA-----TSMDTIFggKAGSVF-----FCASDIGWVVG 288
Cdd:PRK07514 151 --VPRG---ADDLAAILYTSGTTGRSKGAmlsHGNLLSNALTLVdywrfTPDDVLI--HALPIFhthglFVATNVALLAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 289 HSYIvYAP------LLAGM--ATiVYEGLPTWpdcgvwwtivekYqvSRMFSAPTairvLKKFPTAEIRkhdlsslevLY 360
Cdd:PRK07514 224 ASMI-FLPkfdpdaVLALMprAT-VMMGVPTF------------Y--TRLLQEPR----LTREAAAHMR---------LF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 361 LAGE-PLDEPT-ASWVSNTlDVPVIDNYWQTESGwpiMAIARGLD-DRptRLGSPGVPMYGYNVQLLNEVTGEPCGVNEK 437
Cdd:PRK07514 275 ISGSaPLLAEThREFQERT-GHAILERYGMTETN---MNTSNPYDgER--RAGTVGFPLPGVSLRVTDPETGAELPPGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVVEGplpPGCIQTIW----------GDDGRFVktywslfsrpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGT 507
Cdd:PRK07514 349 GMIEVKG---PNVFKGYWrmpektaeefRADGFFI-------------TGDLGKIDERGYVHIVGRGKDLIISGGYNVYP 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 508 REIEESISS-------------HPGVaevavvgvkdalkGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFG 574
Cdd:PRK07514 413 KEVEGEIDElpgvvesavigvpHPDF-------------GEGVTAVVVPKPGAALD--------EAAILAALKGRLARFK 471
|
570 580 590
....*....|....*....|....*....|..
gi 16128320 575 RPAHVWFVSQLPKTRSGK----MLRRTIQAIC 602
Cdd:PRK07514 472 QPKRVFFVDELPRNTMGKvqknLLREQYADLF 503
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
237-592 |
4.63e-22 |
|
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: 98.12 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGV---QRDV--GGYAVALA---TSMDTI-----FggkagsvFFCasdIGWVVGhsyiVYAPLLAGmAT 303
Cdd:cd05917 7 IQFTSGTTGSPKGAtltHHNIvnNGYFIGERlglTEQDRLcipvpL-------FHC---FGSVLG----VLACLTHG-AT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 304 IVYEGlPTWPDCGVWWTIVEK-----YQVSRMFsaptaIRVLKkfpTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL 378
Cdd:cd05917 72 MVFPS-PSFDPLAVLEAIEKEkctalHGVPTMF-----IAELE---HPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 379 ---DVPVIdnYWQTESGwPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppGCIQTIW 455
Cdd:cd05917 143 nmkDVTIA--YGMTETS-PVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGY---SVMKGYW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 GDDGRFVKTY----WslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDA 531
Cdd:cd05917 217 NDPEKTAEAIdgdgW-------LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 532 LKGQVAVAFVIPKESDSLEDRDvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:cd05917 290 RYGEEVCAWIRLKEGAELTEED--------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
83-595 |
5.88e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 99.82 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfaSHSVAARIDDAKPVLIVSA 162
Cdd:PRK06087 49 SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV---------SVPLLPSWREAELVWVLNK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 dAGARGgKIIP--YKKL-LDDAISQAQHQP---RHVLLVDRGLAKMARVSGRDV--DFASLRHQhigarVPVAwleSNET 234
Cdd:PRK06087 120 -CQAKM-FFAPtlFKQTrPVDLILPLQNQLpqlQQIVGVDKLAPATSSLSLSQIiaDYEPLTTA-----ITTH---GDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 235 SCILYTSGTTGKPKGVqrdvggyavaLATSMDTIFGGKA---------GSVFFCASDIGWVVGHSYIVYAPLLAGMATIV 305
Cdd:PRK06087 190 AAVLFTSGTEGLPKGV----------MLTHNNILASERAycarlnltwQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 306 YEGLPtwPDCGVwwTIVEKYQVSRMFSA-PTAIRVLKkfptaEIRKH--DLSSLEVLYLAGEPLDEPTA--SWVSNTLDV 380
Cdd:PRK06087 260 LDIFT--PDACL--ALLEQQRCTCMLGAtPFIYDLLN-----LLEKQpaDLSALRFFLCGGTTIPKKVAreCQQRGIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 381 PVidnYWQTESGWPIMAiarGLDDRPTRLGS-PGVPMYGYNVQLLNEVTGE-PCGvnEKGMLVVEGPL-------PPGCI 451
Cdd:PRK06087 331 SV---YGSTESSPHAVV---NLDDPLSRFMHtDGYAAAGVEIKVVDEARKTlPPG--CEGEEASRGPNvfmgyldEPELT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 452 QTIWGDDGrfvktyWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDA 531
Cdd:PRK06087 403 ARALDEEG------W-------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 532 LKGQVAVAFVIPKE---SDSLEDRdVAHSQEKaimalvdsQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:PRK06087 470 RLGERSCAYVVLKAphhSLTLEEV-VAFFSRK--------RVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
81-592 |
6.29e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 99.83 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGA----IHSVVFGGFASHSVAaridDAKP 156
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAiavpINTALRGPQLEHILR----NSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 157 VLIVsADAGarggkiipykkLLD--DAISQAQHQPRHVLLVDRGLAKMArvsgrDVDFASLRHQHIGARVPVAWLESNET 234
Cdd:PRK06155 120 RLLV-VEAA-----------LLAalEAADPGDLPLPAVWLLDAPASVSV-----PAGWSTAPLPPLDAPAPAAAVQPGDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 235 SCILYTSGTTGKPKGV-----QRDVGGYAVA----------LATSMdTIFGGKAGSVFFCAsdigwvvghsyivyapLLA 299
Cdd:PRK06155 183 AAILYTSGTTGPSKGVccphaQFYWWGRNSAedleigaddvLYTTL-PLFHTNALNAFFQA----------------LLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 300 GmATIVYEglPTWPDCGVWWTIVEK-----YQVSRMFSAptairVLKKFPTAEIRKHdlsSLEVLYLAGEPLDEPTAswV 374
Cdd:PRK06155 246 G-ATYVLE--PRFSASGFWPAVRRHgatvtYLLGAMVSI-----LLSQPARESDRAH---RVRVALGPGVPAALHAA--F 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTLDVPVIDNYWQTESGWPIMAIARglDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCIQTI 454
Cdd:PRK06155 313 RERFGVDLLDGYGSTETNFVIAVTHG--SQRP---GSMGRLAPGFEARVVDE-HDQELPDGEPGELLLRADEPFAFATGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 455 WGDDGRFVKTYWSLFsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:PRK06155 387 FGMPEKTVEAWRNLW----FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGE 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 535 QVAVAFVIPKESDSLEDRDVAHSQEkaimalvdSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:PRK06155 463 DEVMAAVVLRDGTALEPVALVRHCE--------PRLAYFAVPRYVEFVAALPKTENGK 512
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
2-602 |
6.70e-22 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 100.54 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 2 SFSEFYQRSINEPEQFWA----EQArrIDWQTPFTQTLDHSNP--PFARWFCEGRTNLCHNAIdrwLEKQPEALALIAVS 75
Cdd:PLN03052 121 SFSEFQRFSVENPEVYWSivldELS--LVFSVPPRCILDTSDEsnPGGQWLPGAVLNVAECCL---TPKPSKTDDSIAII 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 76 SETEEE-----RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAAR 150
Cdd:PLN03052 196 WRDEGSddlpvNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 151 IDDAKPVLIVSADAGARGGKIIP-YKKLLDdaiSQAqhqPRHVLLVDRGLAKMARVSGRDV---DFASL-RHQHIGARVP 225
Cdd:PLN03052 276 LKISKAKAIFTQDVIVRGGKSIPlYSRVVE---AKA---PKAIVLPADGKSVRVKLREGDMswdDFLARaNGLRRPDEYK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATS---MDTifggKAGSVFFCASDIGWVVGHsYIVYAPLLAGMA 302
Cdd:PLN03052 350 AVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAwahLDI----RKGDIVCWPTNLGWMMGP-WLVYASLLNGAT 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 303 TIVYEGLPTWPDCGvwwTIVEKYQVSRMFSAPTAIRVLKKfpTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDV-P 381
Cdd:PLN03052 425 LALYNGSPLGRGFA---KFVQDAKVTMLGTVPSIVKTWKN--TNCMAGLDWSSIRCFGSTGEASSVDDYLWLMSRAGYkP 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 382 VIDNYWQTESGwpiMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGM-LVVEGPLPPGCIQTIWGDD-- 458
Cdd:PLN03052 500 IIEYCGGTELG---GGFVTGSLLQPQAFAAFSTPAMGCKLFILDD-SGNPYPDDAPCTgELALFPLMFGASSTLLNADhy 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 459 -----------GRFVKTYWSLFSRPVyatfdwgirdaDGYHFILGRTDDVINVAGHRLGTREIEESI-SSHPGVAEVAVV 526
Cdd:PLN03052 576 kvyfkgmpvfnGKILRRHGDIFERTS-----------GGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAI 644
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 527 GVKDALKG--QVAVAFVIPKESDSLEDRDvahSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAIC 602
Cdd:PLN03052 645 GVPPPGGGpeQLVIAAVLKDPPGSNPDLN---ELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQL 719
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
55-598 |
1.88e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 98.57 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAVSSEteeertFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHI----TLLAC-- 128
Cdd:PRK06710 27 HKYVEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIgyygTLLAGgi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 129 ---------------------ARIGAIHSVVFGGFASHSVAARIDDakpvLIVSadagaRGGKIIPYKKLLDDAISQAQH 187
Cdd:PRK06710 101 vvqtnplytereleyqlhdsgAKVILCLDLVFPRVTNVQSATKIEH----VIVT-----RIADFLPFPKNLLYPFVQKKQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 188 QPRHVLLVDRGLAKMARVSGRDVDFAslrhqhigarVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDT 267
Cdd:PRK06710 172 SNLVVKVSESETIHLWNSVEKEVNTG----------VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 268 IFGGKAGS-VFFCASDIGWVVGHSYIVYAPLLAGMATIVyegLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTa 346
Cdd:PRK06710 242 LYNCKEGEeVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPL- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 347 eIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGwPIMAIARGLDDRPTrlGSPGVPMYGYNVQLLNE 426
Cdd:PRK06710 317 -LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVP--GSIGVPWPDTEAMIMSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 427 VTGEPCGVNEKGMLVVEGPlppgciqtiwgddgRFVKTYW-------SLFSRPVYATFDWGIRDADGYHFILGRTDDVIN 499
Cdd:PRK06710 393 ETGEALPPGEIGEIVVKGP--------------QIMKGYWnkpeetaAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 500 VAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEKAIMAlvdsqignFGRPAHV 579
Cdd:PRK06710 459 ASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAA--------YKVPKVY 530
|
570
....*....|....*....
gi 16128320 580 WFVSQLPKTRSGKMLRRTI 598
Cdd:PRK06710 531 EFRDELPKTTVGKILRRVL 549
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
81-607 |
3.03e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 97.46 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYM----PMIAEAhitlLACARIGAIHSVVFGGFASHSVAARIDDAKP 156
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMrndfAFFEAA----YAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 157 -VLIVSADagarggkiipykkLLDdaiSQAQHQPRHV-LLVDRGLAKMARVSGRDVDFASLRHQHIGARvpvAWLESNE- 233
Cdd:PRK12406 85 rVLIAHAD-------------LLH---GLASALPAGVtVLSVPTPPEIAAAYRISPALLTPPAGAIDWE---GWLAQQEp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 234 --------TSCILYTSGTTGKPKGVQRDVG--GYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmaT 303
Cdd:PRK12406 146 ydgppvpqPQSMIYTSGTTGHPKGVRRAAPtpEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGG--V 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 304 IVYEglPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEP----LDEPTASWVSntld 379
Cdd:PRK12406 224 LVLQ--PRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPcpadVKRAMIEWWG---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 380 vPVIDNYW-QTESGWPIMAIARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPGCiqTIWGDD 458
Cdd:PRK12406 297 -PVIYEYYgSTESGAVTFATSEDALSHP---GTVGKAAPGAELRFVDE-DGRPLPQGEIGEIYSRIAGNPDF--TYHNKP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 459 GRFVKTywslfSRPVYATF-DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVA 537
Cdd:PRK12406 370 EKRAEI-----DRGGFITSgDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 538 VAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIqaicegRDP 607
Cdd:PRK12406 445 MAVVEPQPGATLD--------EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL------RDP 500
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
115-600 |
1.08e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 95.65 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 115 MPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIP-YKKLLDDAISQAQHQPrhvl 193
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPlYSKVVEAAPAKAIVLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 194 lvdrglakmarVSGRDV------------DF---ASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRD----- 253
Cdd:PLN03051 77 -----------AAGEPVavplreqdlswcDFlgvAAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWThlspl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 254 ---VGGYAvalatSMDTifggKAGSVFFCASDIGWVVGhSYIVYAPLLAGMATIVYEGLPTWPDCGvwwTIVEKYQVSRM 330
Cdd:PLN03051 146 rcaSDGWA-----HMDI----QPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFG---KFVQDAGVTVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 331 FSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNT--LDVPVIDNYWQTE--SGWPIMAIArglddRP 406
Cdd:PLN03051 213 GLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVrgYYKPVIEYCGGTElaSGYISSTLL-----QP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 407 TRLGSPGVPMYGYNVQLLNEV-TGEPCGVNEKGMLVVEGPLpPGCIQTIWGDDGRfvKTYWSlfSRPVYATF-------- 477
Cdd:PLN03051 288 QAPGAFSTASLGTRFVLLNDNgVPYPDDQPCVGEVALAPPM-LGASDRLLNADHD--KVYYK--GMPMYGSKgmplrrhg 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 478 DWGIRDADGYHFILGRTDDVINVAGHRLGTREIE-------ESISSHPGVAEVAVVGVKDALKgQVAVAFVIPKESDSLE 550
Cdd:PLN03051 363 DIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIEracdravAGIAETAAVGVAPPDGGPELLV-IFLVLGEEKKGFDQAR 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 16128320 551 DRDVAHSQEKAImalvDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PLN03051 442 PEALQKKFQEAI----QTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
66-596 |
1.16e-20 |
|
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: 95.44 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:cd12116 1 PDATAV------RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPVLIVSADAGARGGkiipykkllddaisqaqhqPRHVLLVDRGLAKMARvsgrdvdfaslrhQHIGARVP 225
Cdd:cd12116 75 RLRYILEDAEPALVLTDDALPDRL-------------------PAGLPVLLLALAAAAA-------------APAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VAwleSNETSCILYTSGTTGKPKGV---QRDVggyaVALATSMDTIFGGKAG----SVFFCASDIgwvvghSYI-VYAPL 297
Cdd:cd12116 123 VS---PDDLAYVIYTSGSTGRPKGVvvsHRNL----VNFLHSMRERLGLGPGdrllAVTTYAFDI------SLLeLLLPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 298 LAGmATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKkfpTAEIRkhDLSSLEVLyLAGEPLDEPTASWVSNT 377
Cdd:cd12116 190 LAG-ARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLL---DAGWQ--GRAGLTAL-CGGEALPPDLAARLLSR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 378 LDVpVIDNYWQTESG-WPIMAIARGLDDRPTRlgspGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGCIQTIWG 456
Cdd:cd12116 263 VGS-LWNLYGPTETTiWSTAARVTAAAGPIPI----GRPLANTQVYVLDA-ALRPVPPGVPGELYIGGD---GVAQGYLG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 457 D----DGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDAL 532
Cdd:cd12116 334 RpaltAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 533 KGQVaVAFVIPKESDSLEDRDV-AHSQEkaimALVDSQIgnfgrPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd12116 414 DRRL-VAYVVLKAGAAPDAAALrAHLRA----TLPAYMV-----PSAFVRLDALPLTANGKLDRK 468
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
57-599 |
1.26e-20 |
|
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: 94.68 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 57 AIDRWLEKQPEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHS 136
Cdd:cd17653 2 AFERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 137 VVFGGFASHSVAARIDDAKPVLIVSADAGarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdfaslr 216
Cdd:cd17653 76 PLDAKLPSARIQAILRTSGATLLLTTDSP--------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 217 hqhigarvpvawlesNETSCILYTSGTTGKPKGV---QRDVGGYAVALATSMDTIFGGKAGSVFFCASDIgwvvghSYIV 293
Cdd:cd17653 105 ---------------DDLAYIIFTSGSTGIPKGVmvpHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDA------CIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 294 YAPLLAGMATIVYEGlPTWPdcgvwWTIVEKyQVSRMFSAPTAIRVLKkfPTaeirkhDLSSLEVLYLAGEPldePTASW 373
Cdd:cd17653 164 IFSTLCNGGTLVLAD-PSDP-----FAHVAR-TVDALMSTPSILSTLS--PQ------DFPNLKTIFLGGEA---VPPSL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 374 VSNTLDVPVIDN-YWQTESGWPImAIARGLDDRPTRLGSP--GVPMYgynvqLLNEvTGEPCGVNEKGMLVVEGP-LPPG 449
Cdd:cd17653 226 LDRWSPGRRLYNaYGPTECTISS-TMTELLPGQPVTIGKPipNSTCY-----ILDA-DLQPVPEGVVGEICISGVqVARG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 450 CIQTIWGDDGRFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESI-SSHPGVAEVAVVGV 528
Cdd:cd17653 299 YLGNPALTASKFVPDPFWPGSR-MYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVV 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 529 KDALkgqvaVAFVIPkesdslEDRDVAHSQEKAimalvDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:cd17653 378 NGRL-----VAFVTP------ETVDVDGLRSEL-----AKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
65-600 |
1.45e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 95.44 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 65 QPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAihsVVFGGFAS 144
Cdd:PRK10946 36 ASDAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV---APVNALFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 145 H------SVAARIDDAkpVLIVSADAGARGGkiipykkllDDAISQAQHQ---PRHVLLvdrglakmarvsgrdvdfasl 215
Cdd:PRK10946 107 HqrselnAYASQIEPA--LLIADRQHALFSD---------DDFLNTLVAEhssLRVVLL--------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 216 rHQHIGARVPVAWLESNETSCILYTS------------GTTGKPKGVQRDVGGYAVALATSMDtIFGGKAGSVFFCASDi 283
Cdd:PRK10946 155 -LNDDGEHSLDDAINHPAEDFTATPSpadevaffqlsgGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 284 gwvVGHSYIVYAP-----LLAGmATIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEV 358
Cdd:PRK10946 232 ---AAHNYPMSSPgalgvFLAG-GTVV---LAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 359 LYLAGEPLDEPTASWVSntldvPVIDNYWQTESGwpimaIARGL------DDRPTR-LGSPGVPMYGYN-VQLLNEvTGE 430
Cdd:PRK10946 305 LQVGGARLSETLARRIP-----AELGCQLQQVFG-----MAEGLvnytrlDDSDERiFTTQGRPMSPDDeVWVADA-DGN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 431 PCGVNEKGMLVVEGP-------LPPGCIQTIWGDDGrfvktywslfsrpVYATFDWGIRDADGYHFILGRTDDVINVAGH 503
Cdd:PRK10946 374 PLPQGEVGRLMTRGPytfrgyyKSPQHNASAFDANG-------------FYCSGDLVSIDPDGYITVVGREKDQINRGGE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 504 RLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESdsledrdvahsqEKAIMA---LVDSQIGNFGRPAHVW 580
Cdd:PRK10946 441 KIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP------------LKAVQLrrfLREQGIAEFKLPDRVE 508
|
570 580
....*....|....*....|....
gi 16128320 581 FVSQLPKTRSGKM----LRRTIQA 600
Cdd:PRK10946 509 CVDSLPLTAVGKVdkkqLRQWLAS 532
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
55-596 |
2.09e-20 |
|
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: 94.31 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:cd12115 2 HDLVEAQAARTPDAIALVC------GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HsvvfggfashsvaARIDDAKPVlivsadagARGGKIipykklLDDAisqaqhQPRHVLLvdrglakmarvsgrdvdfas 214
Cdd:cd12115 76 Y-------------VPLDPAYPP--------ERLRFI------LEDA------QARLVLT-------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 lrhqhigarvpvawlESNETSCILYTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGSVFFCASDIGWVVGhSYIVY 294
Cdd:cd12115 103 ---------------DPDDLAYVIYTSGSTGRPKGVAIEHRN-AAAFLQWAAAAFSAEELAGVLASTSICFDLS-VFELF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 APLLAGMATIVYEGLPTWPDCGVwwtiveKYQVSRMFSAPTAIRVL---KKFPTaeirkhdlsSLEVLYLAGEPL----- 366
Cdd:cd12115 166 GPLATGGKVVLADNVLALPDLPA------AAEVTLINTVPSAAAELlrhDALPA---------SVRVVNLAGEPLprdlv 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 367 ----DEPTASWVSNtLDVPVIDNYWQTESgwpimAIARGLDDRPtrlgSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVV 442
Cdd:cd12115 231 qrlyARLQVERVVN-LYGPSEDTTYSTVA-----PVPPGASGEV----SIGRPLANTQAYVLDR-ALQPVPLGVPGELYI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 443 EGPlppGCIQTIWGDDG----RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHP 518
Cdd:cd12115 300 GGA---GVARGYLGRPGltaeRFLPDPFGPGAR-LYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIP 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 519 GVAEVAVVGVKDALKGQVAVAFVIPKESdsledrdvAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd12115 376 GVREAVVVAIGDAAGERRLVAYIVAEPG--------AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-596 |
1.16e-19 |
|
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: 92.69 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 60 RWLEKQPEALALIAVSSETEEERTFTFRQLHDEVNAVASMLRSLGvQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVF 139
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 140 ---GGFASHSVAARIDDAKPVLIVSADAGARGgkiipykkLLDDAISQAQHQPRHVLLVDRglakmarvsgrdVDFASlr 216
Cdd:cd05931 80 pptPGRHAERLAAILADAGPRVVLTTAAALAA--------VRAFAASRPAAGTPRLLVVDL------------LPDTS-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 217 hqhiGARVPVAWLESNETSCILYTSGTTGKPKGVQ---RDVggyaVALATSMDTIFGGKAGSVffCAS------DIGWVV 287
Cdd:cd05931 138 ----AADWPPPSPDPDDIAYLQYTSGSTGTPKGVVvthRNL----LANVRQIRRAYGLDPGDV--VVSwlplyhDMGLIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 288 GhsyiVYAPLLAG-----MATIVYEGLPtwpdcGVWWTIVEKYQVSRMFsAPT-AIR-VLKKFPTAEIRKHDLSSLEVLY 360
Cdd:cd05931 208 G----LLTPLYSGgpsvlMSPAAFLRRP-----LRWLRLISRYRATISA-APNfAYDlCVRRVRDEDLEGLDLSSWRVAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 361 LAGEPLDEPT--------------ASWVS-------NTLDV--------PVIDNYWQTESGWPIMAIARGlDDRPTRLGS 411
Cdd:cd05931 278 NGAEPVRPATlrrfaeafapfgfrPEAFRpsyglaeATLFVsggppgtgPVVLRVDRDALAGRAVAVAAD-DPAARELVS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 412 PGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGP-LPPGciqtIWGDDGRFVKTYWSLF---SRPVYATFDWGIRdADGY 487
Cdd:cd05931 357 CGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPsVASG----YWGRPEATAETFGALAatdEGGWLRTGDLGFL-HDGE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 488 HFILGRTDDVINVAGHRLGTREIEESISSHPgvaevavvgvkDALKGQVAVAFVIPKESD----------SLEDRDVAHS 557
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAH-----------PALRPGCVAAFSVPDDGEerlvvvaeveRGADPADLAA 500
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 16128320 558 QEKAIMALVDSQIGNfgRPAHVWFVSQ--LPKTRSGKmLRR 596
Cdd:cd05931 501 IAAAIRAAVAREHGV--APADVVLVRPgsIPRTSSGK-IQR 538
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
66-595 |
1.28e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 92.38 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsSETEEerTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVfggfASH 145
Cdd:PRK13390 11 PDRPAVIV--AETGE--QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAI----NHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDdakpvlIVSADAGARggkIIPYKKLLDDAISQAqhqprhvllvdrGLAKMARVS-GRDVD-FASLRHQHIGAR 223
Cdd:PRK13390 83 LTAPEAD------YIVGDSGAR---VLVASAALDGLAAKV------------GADLPLRLSfGGEIDgFGSFEAALAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 VPVAwlesnETSC---ILYTSGTTGKPKGVQ-----RDV---GGYAVALATSMdtiFGGKAGSVFFCASDIGWVVGHSYI 292
Cdd:PRK13390 142 PRLT-----EQPCgavMLYSSGTTGFPKGIQpdlpgRDVdapGDPIVAIARAF---YDISESDIYYSSAPIYHAAPLRWC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 293 VYAPLLAGmaTIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTA-IRVLKKfpTAEIR-KHDLSSLEVLYLAGEP----L 366
Cdd:PRK13390 214 SMVHALGG--TVV---LAKRFDAQATLGHVERYRITVTQMVPTMfVRLLKL--DADVRtRYDVSSLRAVIHAAAPcpvdV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 367 DEPTASWVSntldvPVIDNYWQTESGWPIMAIargldDRPTRLGSPGvpmygynvQLLNEVTGEPCGVNEKGmlvveGPL 446
Cdd:PRK13390 287 KHAMIDWLG-----PIVYEYYSSTEAHGMTFI-----DSPDWLAHPG--------SVGRSVLGDLHICDDDG-----NEL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 PPGCIQTIWGDDGRFVKTYWSLFSR---------PVYATF-DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISS 516
Cdd:PRK13390 344 PAGRIGTVYFERDRLPFRYLNDPEKtaaaqhpahPFWTTVgDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTM 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 517 HPGVAEVAVVGVKDALKGQVAVAFVIPKESdsledrdVAHSQEKAiMALVD---SQIGNFGRPAHVWFVSQLPKTRSGKM 593
Cdd:PRK13390 424 HPAVHDVAVIGVPDPEMGEQVKAVIQLVEG-------IRGSDELA-RELIDytrSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
..
gi 16128320 594 LR 595
Cdd:PRK13390 496 VK 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-600 |
1.30e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.25 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:PRK12316 514 HRLFEEQVERTPEAPAL------AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGA 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HSVVFGGFASHSVAARIDDAKPVLIVSadagarggkiipykkllddaisqaQHQPRHVLLVDRGLAKMarvsgrDVDFAS 214
Cdd:PRK12316 588 YVPLDPEYPAERLAYMLEDSGVQLLLS------------------------QSHLGRKLPLAAGVQVL------DLDRPA 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 LRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVqrdvGGYAVALATSMD---TIFGGKAGSVFFCASDIGWVVGHsY 291
Cdd:PRK12316 638 AWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGA----GNRHRALSNRLCwmqQAYGLGVGDTVLQKTPFSFDVSV-W 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 292 IVYAPLLAGMATIV-YEGLPTWPDcgVWWTIVEKYQVSRMFSAPTAIRVLKKFPtaeiRKHDLSSLEVLYLAGEPLDEPT 370
Cdd:PRK12316 713 EFFWPLMSGARLVVaAPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDE----DVASCTSLRRIVCSGEALPADA 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 371 ASWVSNTLDVP-VIDNYWQTESGWPIM---AIARGLDDRPTrlgspGVPMYGYNVQLLnEVTGEPCGVNEKGMLVVEGPl 446
Cdd:PRK12316 787 QEQVFAKLPQAgLYNLYGPTEAAIDVThwtCVEEGGDSVPI-----GRPIANLACYIL-DANLEPVPVGVLGELYLAGR- 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 ppGCIQTIWGDDG----RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAE 522
Cdd:PRK12316 860 --GLARGYHGRPGltaeRFVPSPFVAGER-MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 523 VAVVgvkdALKGQVAVAFVIPKesdsledrDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK12316 937 AAVL----AVDGKQLVGYVVLE--------SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
56-595 |
1.94e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 92.15 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 56 NAIDRWLEKQPEALALIAVSseteeeRTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIh 135
Cdd:PRK07786 21 NQLARHALMQPDAPALRFLG------NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 136 svvfggfaSHSVAARIDDAKPVLIVSaDAGARGgkIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASl 215
Cdd:PRK07786 94 --------AVPVNFRLTPPEIAFLVS-DCGAHV--VVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 216 rhqhIGARVPVAWLESNETSCILYTSGTTGKPKGVqrdVGGYAVALATSMDTIFGGKA---GSVFFCASDIGWVVGHSYI 292
Cdd:PRK07786 162 ----AGPAHAPVDIPNDSPALIMYTSGTTGRPKGA---VLTHANLTGQAMTCLRTNGAdinSDVGFVGVPLFHIAGIGSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 293 VyAPLLAGMATIVYeglPTWP-DCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRkhDLsSLEVLYLAGEPLDEPTA 371
Cdd:PRK07786 235 L-PGLLLGAPTVIY---PLGAfDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPR--DL-ALRVLSWGAAPASDTLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 372 SWVSNTL-DVPVIDNYWQTESGwPIMAIARGlDDRPTRLGSPGVPMYGYNVQLLNEVTGEpCGVNEKGMLVVEGplpPGC 450
Cdd:PRK07786 308 RQMAATFpEAQILAAFGQTEMS-PVTCMLLG-EDAIRKLGSVGKVIPTVAARVVDENMND-VPVGEVGEIVYRA---PTL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 451 IQTIWGDDgrfvKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKD 530
Cdd:PRK07786 382 MSGYWNNP----EATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAD 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 531 ALKGQVAVAFVIPK-ESDSLEDRDVAhsqekaimALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:PRK07786 458 EKWGEVPVAVAAVRnDDAALTLEDLA--------EFLTDRLARYKHPKALEIVDALPRNPAGKVLK 515
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
85-596 |
4.53e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 90.85 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIG-------------------------AIhsVVF 139
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyvvvnvnplytprelehqlkdsgaeAI--VVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 140 GGFAsHSVAARID--DAKPVLIVS-ADAGARGGKIIPY-----KKLLddaisQAQHQPRHVLLVDrGLAKMARVSgrdvd 211
Cdd:PRK07059 128 ENFA-TTVQQVLAktAVKHVVVASmGDLLGFKGHIVNFvvrrvKKMV-----PAWSLPGHVRFND-ALAEGARQT----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 212 fasLRHQHIGARvPVAWLEsnetscilYTSGTTGKPKG---VQRDVGGYAVALATSMDTIFGGKAGS---VFFCASDIgw 285
Cdd:PRK07059 196 ---FKPVKLGPD-DVAFLQ--------YTGGTTGVSKGatlLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPL-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 vvghsYIVYAPLLAGMATIVYEGL----PTWPDCGVWWTIVEKYQVSrMFSA-PTAIRVLKKFPtaEIRKHDLSSLEVLY 360
Cdd:PRK07059 262 -----YHIFALTVCGLLGMRTGGRniliPNPRDIPGFIKELKKYQVH-IFPAvNTLYNALLNNP--DFDKLDFSKLIVAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 361 LAGEPLDEPTAS-WVSNTlDVPVIDNYWQTESGwPIMAIARGLDDRPTrlGSPGVPMYGYNVQLLNEvTGEPCGVNEKGM 439
Cdd:PRK07059 334 GGGMAVQRPVAErWLEMT-GCPITEGYGLSETS-PVATCNPVDATEFS--GTIGLPLPSTEVSIRDD-DGNDLPLGEPGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 440 LVVEGPlppgciQTIWGddgrfvktYWSlfsRP-----------VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTR 508
Cdd:PRK07059 409 ICIRGP------QVMAG--------YWN---RPdetakvmtadgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 509 EIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEkaimalvdsQIGNFGRPAHVWFVSQLPKT 588
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKE---------RLTNYKRPKFVEFRTELPKT 542
|
....*...
gi 16128320 589 RSGKMLRR 596
Cdd:PRK07059 543 NVGKILRR 550
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
85-620 |
1.31e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 90.09 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfgGFASHSVAARIDDAKPvlivsaDA 164
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM------AFLANPELHRDDHALA------AR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 165 GARGGKIIPYKKLLDdaisqaQHQPRHVLLVDRGLAKMARVSGRDVDFASlrhqhigarvpvawleSNETSCILYTSGTT 244
Cdd:PRK06060 100 NTEPALVVTSDALRD------RFQPSRVAEAAELMSEAARVAPGGYEPMG----------------GDALAYATYTSGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 245 GKPKG-VQRDVGGYAVALATSMDTIFGGKAgSVFFCASDIGWVVGHSYIVYAPLLAGMATIVyEGLPTWPDCGVwwTIVE 323
Cdd:PRK06060 158 GPPKAaIHRHADPLTFVDAMCRKALRLTPE-DTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAA--ILSA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 324 KYQVSRMFSAPTAI-RVLKKFPTAEIRkhdlsSLEVLYLAGEPLDEPTASWVSNTLD-VPVIDNYWQTESGWPImaIARG 401
Cdd:PRK06060 234 RFGPSVLYGVPNFFaRVIDSCSPDSFR-----SLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTF--VSNR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 402 LDD-RPTRLGSPgVPMYGYNVQLLNEVTGEPCGvneKGMLVVEGPlppgciqtiwgddgRFVKTYWSlFSRPVYATFDW- 479
Cdd:PRK06060 307 VDEwRLGTLGRV-LPPYEIRVVAPDGTTAGPGV---EGDLWVRGP--------------AIAKGYWN-RPDSPVANEGWl 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 480 GIRD-----ADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDV 554
Cdd:PRK06060 368 DTRDrvcidSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVM 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 555 AHSQEKAImalvdSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTI----DDPASLD 620
Cdd:PRK06060 448 RDLHRGLL-----NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTepgsGVRAQRD 512
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
66-597 |
2.05e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 88.48 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVfggfASH 145
Cdd:cd12114 1 PDATAVIC------GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV----DID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDakpvliVSADAGARggkiipykkllddaisqaqhqprhVLLVDRGLAKmARVSGRDVDFASLRHQHIGARVP 225
Cdd:cd12114 71 QPAARREA------ILADAGAR------------------------LVLTDGPDAQ-LDVAVFDVLILDLDALAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VAWLESNETSCILYTSGTTGKPKGVQRDvggYAVALATSMDTI--FGGKAGSVFFCASDIGW---VvghsYIVYAPLLAG 300
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMIS---HRAALNTILDINrrFAVGPDDRVLALSSLSFdlsV----YDIFGALSAG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 mATIVYeglptwPDCG------VWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRkhDLSSLEVLYLAGE--PLDEPTAS 372
Cdd:cd12114 193 -ATLVL------PDEArrrdpaHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA--LLPSLRLVLLSGDwiPLDLPARL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 373 WVSnTLDVPVIDNYWQTESGwpIMAIARGLDDRPTRLGS-P-GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGC 450
Cdd:cd12114 264 RAL-APDARLISLGGATEAS--IWSIYHPIDEVPPDWRSiPyGRPLANQRYRVLDP-RGRDCPDWVPGELWIGGR---GV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 451 IQTIWGDDGRfvkTYWSLFSRP----VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVV 526
Cdd:cd12114 337 ALGYLGDPEL---TAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 527 GVKDALKGQVAvAFVIPKESDSLEDRDVAHSQEKAimalvdsQIGNFGRPAHVWFVSQLPKTRSGKMLRRT 597
Cdd:cd12114 414 VLGDPGGKRLA-AFVVPDNDGTPIAPDALRAFLAQ-------TLPAYMIPSRVIALEALPLTANGKVDRAA 476
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
55-603 |
2.73e-18 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 87.98 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGai 134
Cdd:cd05918 2 HDLIEERARSQPDAPAVCA------WDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 hsvvfGGF----ASHSVAaRIDDakpvliVSADAGARggkiipykkllddaisqaqhqprhVLLVDRglakmarvsgrdv 210
Cdd:cd05918 74 -----GAFvpldPSHPLQ-RLQE------ILQDTGAK------------------------VVLTSS------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 211 dfaslrhqhigarvpvawleSNETSCILYTSGTTGKPKGVQRDVGgyavALATSMDT---IFGGKAGSVFFC----ASDI 283
Cdd:cd05918 105 --------------------PSDAAYVIFTSGSTGKPKGVVIEHR----ALSTSALAhgrALGLTSESRVLQfasyTFDV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 284 gwvvgHSYIVYAPLLAGmATIV-------YEGLPTWpdcgvwwtiVEKYQVSRMFSAPTAIRVLkkfptaeiRKHDLSSL 356
Cdd:cd05918 161 -----SILEIFTTLAAG-GCLCipseedrLNDLAGF---------INRLRVTWAFLTPSVARLL--------DPEDVPSL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 357 EVLYLAGEPLDEPTAS-WVSNtldVPVIDNYWQTEsgWPIMAIAR--GLDDRPTRLGSPgvpmYGYNVQLLN-EVTGEPC 432
Cdd:cd05918 218 RTLVLGGEALTQSDVDtWADR---VRLINAYGPAE--CTIAATVSpvVPSTDPRNIGRP----LGATCWVVDpDNHDRLV 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 433 GVNEKGMLVVEGPL-------PPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHR- 504
Cdd:cd05918 289 PIGAVGELLIEGPIlargylnDPEKTAAAFIEDPAWLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRv 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 505 -LGtrEIEESISSHPGVAEVAV---VGVKDALKGQVAVAFVIPKESDS---------LEDRDVAHSQEKAIMALVDSQIG 571
Cdd:cd05918 369 eLG--EIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslfLEPSDEFRALVAELRSKLRQRLP 446
|
570 580 590
....*....|....*....|....*....|..
gi 16128320 572 NFGRPAHVWFVSQLPKTRSGKMLRRTIQAICE 603
Cdd:cd05918 447 SYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-600 |
4.06e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:PRK12316 3060 HRLFEEQVERTPDAVALAF------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGA 3133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HSVVFGGFASHSVAARIDDAKPVLIVSadagarggkiipykkllDDAISQAQHQPRHVLLVDRGlakmarvsgrdvdfas 214
Cdd:PRK12316 3134 YVPLDPEYPEERLAYMLEDSGAQLLLS-----------------QSHLRLPLAQGVQVLDLDRG---------------- 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 lrHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIgwVVGHSYIVY 294
Cdd:PRK12316 3181 --DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS--FDVFVEELF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 APLLAGmATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLkkfpTAEIRKHDLSSLEVLYLAGEPLdePTASWV 374
Cdd:PRK12316 3257 WPLMSG-ARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF----LEEEDAHRCTSLKRIVCGGEAL--PADLQQ 3329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 375 SNTLDVPVIDNYWQTESgwPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNE-VTGEPCGVNEKGMLVVEGpLPPGCIQT 453
Cdd:PRK12316 3330 QVFAGLPLYNLYGPTEA--TITVTHWQCVEEGKDAVPIGRPIANRACYILDGsLEPVPVGALGELYLGGEG-LARGYHNR 3406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 454 IWGDDGRFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVgvkdALK 533
Cdd:PRK12316 3407 PGLTAERFVPDPFVPGER-LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVD 3481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 534 GQVAVAFVIPKESDSlEDRDVAHSQEKAimALVDSQIgnfgrPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK12316 3482 GRQLVAYVVPEDEAG-DLREALKAHLKA--SLPEYMV-----PAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
51-399 |
5.89e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 87.26 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 51 TNLChnaidRWLE----KQPEALALIA----VSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAH 122
Cdd:PRK09274 6 ANIA-----RHLPraaqERPDQLAVAVpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 123 ITLLACARIGAIHSVVFGGFASHSVAARIDDAKP-VLIVSADAG-ARggKIIPYKKLLddaisqaqhqPRHVLLVDRGLA 200
Cdd:PRK09274 81 ALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPdAFIGIPKAHlAR--RLFGWGKPS----------VRRLVTVGGRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 201 KMARVSgrdvdfASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAvALATSMDTIFGGKAGSVffca 280
Cdd:PRK09274 149 WGGTTL------ATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFE-AQIEALREDYGIEPGEI---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 281 sDIgwvvgHSYIVYA--PLLAGMATIVYEGLPTWP---DCGVWWTIVEKYQVSRMFSAPTAIRVLKKFptAEIRKHDLSS 355
Cdd:PRK09274 218 -DL-----PTFPLFAlfGPALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRY--GEANGIKLPS 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16128320 356 LEVLYLAGEPLdePTASW--VSNTL--DVPVIDNYWQTESgWPIMAIA 399
Cdd:PRK09274 290 LRRVISAGAPV--PIAVIerFRAMLppDAEILTPYGATEA-LPISSIE 334
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
64-598 |
8.31e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.86 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 64 KQPEALALIAvsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAihsvvfggfa 143
Cdd:PRK05852 28 RLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 144 shsVAARIDDAKPVLIVSADAGARGGKIIpykklLDDAISQAQHQPRHVllvdRGLAKMARVSGRDVDFASLRHQHIGAR 223
Cdd:PRK05852 94 ---VVVPLDPALPIAEQRVRSQAAGARVV-----LIDADGPHDRAEPTT----RWWPLTVNVGGDSGPSGGTLSVHLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 VPVAWLES------NETSCILYTSGTTGKPKGVQRDVGGyavaLATSMDTIFGGKAGSvffcASDIGWVV-----GHSYI 292
Cdd:PRK05852 162 TEPTPATStpeglrPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIITGYRLS----PRDATVAVmplyhGHGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 293 vyAPLLAGMATIVYEGLPT---------WPDCGV----WWTIVekyqvsrmfsaPTAIRVLKKFPTAEIRKHDLSSLEVL 359
Cdd:PRK05852 234 --AALLATLASGGAVLLPArgrfsahtfWDDIKAvgatWYTAV-----------PTIHQILLERAATEPSGRKPAALRFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 360 YLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAiarglddrpTRLGSPGvpmYGYNVQLLNEVTGEPCGVNEKGM 439
Cdd:PRK05852 301 RSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTT---------TQIEGIG---QTENPVVSTGLVGRSTGAQIRIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 440 LVVEGPLPPGCIQTIWGDDGRFVKTYW-------SLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEE 512
Cdd:PRK05852 369 GSDGLPLPAGAVGEVWLRGTTVVRGYLgdptitaANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 513 SISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESdsledrdvAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES--------APPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520
|
....*.
gi 16128320 593 MLRRTI 598
Cdd:PRK05852 521 LDRRAV 526
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
239-595 |
9.75e-18 |
|
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: 84.76 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVQRDVGGYAVALaTSMDTIFGGKAGSVFFCAsdiGWVVgHSYIVYAPLLA---GMATIVYEGLptwpDC 315
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF-VCNEDLFNISGEDAILAP---GPLS-HSLFLYGAISAlylGGTFIGQRKF----NP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 316 GVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkhdlSSLEVLYLAGEPLDEPTASWVSNTL-DVPVIDNYWQTESGWp 394
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTLEPE------SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSF- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 395 imaIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPLPPGCIQtiwgddgrfvKTYWslfsrpvY 474
Cdd:cd17633 151 ---ITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSN----------PDGW-------M 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 475 ATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVipkESDSLEDRDv 554
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQ- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 16128320 555 ahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd17633 287 -------LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
66-596 |
2.91e-17 |
|
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: 84.73 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAihsvVFGGFASH 145
Cdd:cd17649 1 PDAVALVF------GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGG----AYVPLDPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDdakpvLIVSaDAGARggkiipykkLLDdaisqaQHQPRHVllvdrglakmarvsgrdvdfaslrhqhigarvp 225
Cdd:cd17649 71 YPAERLR-----YMLE-DSGAG---------LLL------THHPRQL--------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 vAWlesnetscILYTSGTTGKPKGVQRDVGGYAVALATSMDTiFGGKAGSVFFCASDIGWVVGHSYiVYAPLLAGmATIV 305
Cdd:cd17649 97 -AY--------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQ-LLPPLICG-ACVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 306 YEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLkkfptAEIRKHDLS----SLEVLYLAGEPLDePTASWVSNTLDVP 381
Cdd:cd17649 165 LRPDELWASADELAEMVRELGVTVLDLPPAYLQQL-----AEEADRTGDgrppSLRLYIFGGEALS-PELLRRWLKAPVR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 382 VIDNYWQTESGWPIMA--IARGLDDRPTRLgsP-GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGP-LPPGCIQTIWGD 457
Cdd:cd17649 239 LFNAYGPTEATVTPLVwkCEAGAARAGASM--PiGRPLGGRSAYILDA-DLNPVPVGVTGELYIGGEgLARGYLGRPELT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 458 DGRFVKtywSLFSRP---VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:cd17649 316 AERFVP---DPFGAPgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGK 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 535 QVaVAFVIPKESDSLEDrDVAHsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd17649 393 QL-VAYVVLRAAAAQPE-LRAQ-----LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
48-608 |
3.25e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.06 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 48 EGRTNLCHNAIDRWLE---KQPEALALIAVSSETEeertFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHIT 124
Cdd:PRK05857 7 QAMPQLPSTVLDRVFEqarQQPEAIALRRCDGTSA----LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 125 LLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIPYKKLLDDAISqaqhqprhvllVDRGLAKMAR 204
Cdd:PRK05857 83 VLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIA-----------VDIAAVTRES 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 205 VSGRDVDFASlRHQHIGARVPVAwlesnetscILYTSGTTGKPKgvqrdvggyAVALATsmdtifggkagSVFFCASDIG 284
Cdd:PRK05857 152 EHSLDAASLA-GNADQGSEDPLA---------MIFTSGTTGEPK---------AVLLAN-----------RTFFAVPDIL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 285 WVVGHSYIVYaplLAGMATivYEGLPTWPDCGVWWT----------------------IVEKYQVSRMFSAPTAI-RVLK 341
Cdd:PRK05857 202 QKEGLNWVTW---VVGETT--YSPLPATHIGGLWWIltclmhgglcvtggenttslleILTTNAVATTCLVPTLLsKLVS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 342 KFPTAEIrkhDLSSLEVLYLAGEPLDEPTASWVSNTlDVPVIDNYWQTESGwpIMAIARGLDDRP---TRLGSPGVPMYG 418
Cdd:PRK05857 277 ELKSANA---TVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLSETG--CTALCLPTDDGSivkIEAGAVGRPYPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 419 YNVQLLNEVTGEPcgvnekgmlVVEGPLPPGCIQTIWGDDGRFVKTYWS--LFSRPVYA-----TFDWGIRDADGYHFIL 491
Cdd:PRK05857 351 VDVYLAATDGIGP---------TAPGAGPSASFGTLWIKSPANMLGYWNnpERTAEVLIdgwvnTGDLLERREDGFFYIK 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 492 GRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ-VAVAFVIPKESDSLEDRDVAHSqekaIMALVDSQI 570
Cdd:PRK05857 422 GRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAlVGLAVVASAELDESAARALKHT----IAARFRRES 497
|
570 580 590
....*....|....*....|....*....|....*...
gi 16128320 571 GNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPG 608
Cdd:PRK05857 498 EPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
164-598 |
1.25e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.12 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 164 AGARGGKIIPYK-KLLDDAISQA--QHQPRhVLLVDRGLAKmaRVSGRD-----VDFASLRHQHIGARVPVAwlesNETS 235
Cdd:PRK13383 105 VGLLGADVVPIStEFRSDALAAAlrAHHIS-TVVADNEFAE--RIAGADdavavIDPATAGAEESGGRPAVA----APGR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 236 CILYTSGTTGKPKGVQRD------VG-------------GYAVALATSMdtIFGGKAGSVFFCASDIGWVVGHSYIVYAP 296
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRApqlrsaVGvwvtildrtrlrtGSRISVAMPM--FHGLGLGMLMLTIALGGTVLTHRHFDAEA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 297 LLAGMATIVYEGLPTWPdcgvwwtivekYQVSRMFSAPTAIRVlkkfptaeirKHDLSSLEVLYLAGEPLDEPTASWVSN 376
Cdd:PRK13383 256 ALAQASLHRADAFTAVP-----------VVLARILELPPRVRA----------RNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 377 TLDVPVIDNYWQTESGWPIMAIARGLDDRPTRLGSPgvpMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPLPPgciQTIWG 456
Cdd:PRK13383 315 TYGDILYNGYGSTEVGIGALATPADLRDAPETVGKP---VAGCPVRILDR-NNRPVGPRVTGRIFVGGELAG---TRYTD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 457 DDGRFVKTywslfsrPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQV 536
Cdd:PRK13383 388 GGGKAVVD-------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHR 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 537 AVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:PRK13383 461 LAAFVVLHPGSGVD--------AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
51-250 |
1.96e-16 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 82.84 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 51 TNLCHnAIDRWLEKQPEALALIAVssETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACAR 130
Cdd:COG1022 11 DTLPD-LLRRRAARFPDRVALREK--EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 131 IGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAgarggkiipykKLLDDAISQAQHQP--RHVLLVD-RGLAKMARV-- 205
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQ-----------EQLDKLLEVRDELPslRHIVVLDpRGLRDDPRLls 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128320 206 ------SGRDVDFASLRHQHIGARVPvawlesNETSCILYTSGTTGKPKGV 250
Cdd:COG1022 157 ldellaLGREVADPAELEARRAAVKP------DDLATIIYTSGTTGRPKGV 201
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
233-598 |
4.42e-16 |
|
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: 81.27 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 233 ETSCILYTSGTTGKPKGVQRDVGGYAVALATSMD--TIFGGKAGSVFFCASDIGWVVGHSYIVYApLLAGMATIVYEGLp 310
Cdd:cd05929 126 AGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAaaLGFGPGADSVYLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKF- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 311 twpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPT-ASWVSntLDVPVIDNYWQ- 388
Cdd:cd05929 204 ---DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVkEQWID--WGGPIIWEYYGg 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 389 TE-SGwpiMAIARGlDDRPTRLGSPGVPmygynvqllneVTGEPCGVNEKGmlvveGPLPPGCIQTIWGDDG-RFVKTYW 466
Cdd:cd05929 279 TEgQG---LTIING-EEWLTHPGSVGRA-----------VLGKVHILDEDG-----NEVPPGEIGEVYFANGpGFEYTND 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 467 SLFSRPVYATFDW------GIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAF 540
Cdd:cd05929 339 PEKTAAARNEGGWstlgdvGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 541 VIPKESdslEDRDVAHSQEkaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd05929 419 VQPAPG---ADAGTALAEE--LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
84-604 |
1.30e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKP-VLIVSA 162
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPkILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 DAGARGGKIIpykKLLddAISQAQHQPRHVLLVDRGLAKmaRVSGRDVDFASL--RHQHIGARVPVAWLESNETSCIL-- 238
Cdd:PLN03102 120 SFEPLAREVL---HLL--SSEDSNLNLPVIFIHEIDFPK--RPSSEELDYECLiqRGEPTPSLVARMFRIQDEHDPISln 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 239 YTSGTTGKPKGVqrdVGGYAVALATSMDTIFGGKAGS---------VFFCAsdiGWVvgHSYIVYApllAGMATIVYEGL 309
Cdd:PLN03102 193 YTSGTTADPKGV---VISHRGAYLSTLSAIIGWEMGTcpvylwtlpMFHCN---GWT--FTWGTAA---RGGTSVCMRHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 310 pTWPDCgvwWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIrKHDLSSLEVLyLAGEPldePTASWVSNT--LDVPVIDNYW 387
Cdd:PLN03102 262 -TAPEI---YKNIEMHNVTHMCCVPTVFNILLKGNSLDL-SPRSGPVHVL-TGGSP---PPAALVKKVqrLGFQVMHAYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 388 QTESGWPIMAIArgLDDRPTRL---------GSPGVPMYGY-NVQLLNEVTGEPCGVNEKGM--LVVEGP-LPPGCIQTi 454
Cdd:PLN03102 333 LTEATGPVLFCE--WQDEWNRLpenqqmelkARQGVSILGLaDVDVKNKETQESVPRDGKTMgeIVIKGSsIMKGYLKN- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 455 wgddgrfVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKG 534
Cdd:PLN03102 410 -------PKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 535 QVAVAFVIPK--ESDSLEDRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEG 604
Cdd:PLN03102 483 ETPCAFVVLEkgETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
82-600 |
1.75e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 79.66 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI---HSVVF------GGFASHsvAARI- 151
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPLYtaheleHPFEDH--GARVa 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 152 ---DDAKPVL-----------IVSAD----------------------------AGARGgkIIPYKKLLDDAIsqaqhqp 189
Cdd:PRK05605 134 ivwDKVAPTVerlrrttpletIVSVNmiaampllqrlalrlpipalrkaraaltGPAPG--TVPWETLVDAAI------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 190 rhvlLVDRGLAKMARVSGRDVDFaslrhqhigarvpvawlesnetscILYTSGTTGKPKGVQRDVGGYAVALATsmdtif 269
Cdd:PRK05605 205 ----GGDGSDVSHPRPTPDDVAL------------------------ILYTSGTTGKPKGAQLTHRNLFANAAQ------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 270 gGKAgsvffcasdigWVvghsyivyaPLLAGMATIVYEGLPTWPDCGVwwTIVEKYQVS---RM-----FSAPTAIRVLK 341
Cdd:PRK05605 251 -GKA-----------WV---------PGLGDGPERVLAALPMFHAYGL--TLCLTLAVSiggELvllpaPDIDLILDAMK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 342 K-FPT---------------AEIRKHDLSSLEVLYLAGEPLDEPT-ASWVSNTLDVpVIDNYWQTESGwPIMAIARGLDD 404
Cdd:PRK05605 308 KhPPTwlpgvpplyekiaeaAEERGVDLSGVRNAFSGAMALPVSTvELWEKLTGGL-LVEGYGLTETS-PIIVGNPMSDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 405 RptRLGSPGVPMYGYNVQLLN-EVTGEPCGVNEKGMLVVEGPlppgciQTIWGddgrfvktYW-------SLFSRPVYAT 476
Cdd:PRK05605 386 R--RPGYVGVPFPDTEVRIVDpEDPDETMPDGEEGELLVRGP------QVFKG--------YWnrpeetaKSFLDGWFRT 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 477 FDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvah 556
Cdd:PRK05605 450 GDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALD------ 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 16128320 557 sqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK05605 524 --PEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-600 |
2.59e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.21 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 53 LCHNAIDRWLEKQPEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLAcarig 132
Cdd:PRK12467 1575 LVHQLIEDQAAATPEAVAL------VFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLA----- 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 aihsvvfggfashsvaariddakpvlIVSAdagarGGKIIPykklLDdaisqaQHQPRhvllvDRgLAKMARVSGRDVdf 212
Cdd:PRK12467 1644 --------------------------ILKA-----GGAYVP----LD------PEYPR-----ER-LAYMIEDSGIEL-- 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 213 aSLRHQHIGARVPV-------------AWLESNETSC------------ILYTSGTTGKPKGVQrDVGGYAVALATSMDT 267
Cdd:PRK12467 1675 -LLTQSHLQARLPLpdglrslvldqedDWLEGYSDSNpavnlapqnlayVIYTSGSTGRPKGAG-NRHGALVNRLCATQE 1752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 268 IFGgkagsvfFCASDIgWVVGHSYI-------VYAPLLAGmATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVL 340
Cdd:PRK12467 1753 AYQ-------LSAADV-VLQFTSFAfdvsvweLFWPLING-ARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQL 1823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 341 KKFPTAEIRKhdlSSLEVLYLAGEPLD-EPTASWVSNTLDVPVIDNYWQTESG-----WPIMaiargLDDRPTRLGSP-G 413
Cdd:PRK12467 1824 LQMDEQVEHP---LSLRRVVCGGEALEvEALRPWLERLPDTGLFNLYGPTETAvdvthWTCR-----RKDLEGRDSVPiG 1895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 414 VPMYGYNVQLLNEvtgepcGVNekgmlvvegPLPPGCIQTIW-GDDG--------------RFVKTYWSLFSRPVYATFD 478
Cdd:PRK12467 1896 QPIANLSTYILDA------SLN---------PVPIGVAGELYlGGVGlargylnrpaltaeRFVADPFGTVGSRLYRTGD 1960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 479 WGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAeVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQ 558
Cdd:PRK12467 1961 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVR-EAVVIAQDGANGKQLVAYVVPTDPGLVDDDEAQVAL 2039
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 16128320 559 EKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK12467 2040 RAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
509-592 |
4.01e-15 |
|
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: 70.27 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 509 EIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKT 588
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELL--------EEELVAHVREELGPYAVPKEVVFVDELPKT 72
|
....
gi 16128320 589 RSGK 592
Cdd:pfam13193 73 RSGK 76
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
80-595 |
4.17e-15 |
|
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: 78.25 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 80 EERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLI 159
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 vsadagarggkiipykkllddaisqaqhqprhvllvdrglakmarvsgrdvdFASlrhqhigarvpvawlESNETSCILY 239
Cdd:cd05914 84 ----------------------------------------------------FVS---------------DEDDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGVQ---RDVggyaVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGmATIVYEGLPTWPDCg 316
Cdd:cd05914 97 TSGTTGNSKGVMltyRNI----VSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNG-AHVVFLDKIPSAKI- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 317 vwwTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLS-----------SLEVLYLAGEPLDE----------------- 368
Cdd:cd05914 171 ---IALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKkfkfklakkinNRKIRKLAFKKVHEafggnikefviggakin 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 369 PTASWVSNTLDVPVIDNYWQTESGwPIMAIARgldDRPTRLGSPGVPMYGYNVQllnevTGEPCGVNEKGMLVVEGP--- 445
Cdd:cd05914 248 PDVEEFLRTIGFPYTIGYGMTETA-PIISYSP---PNRIRLGSAGKVIDGVEVR-----IDSPDPATGEGEIIVRGPnvm 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 446 ----LPPGCIQTIWGDDGrfvktyWslfsrpvYATFDWGIRDADGYHFILGRTDDVI-NVAGHRLGTREIEESISSHPGV 520
Cdd:cd05914 319 kgyyKNPEATAEAFDKDG------W-------FHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFV 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 521 AEVAVVGVKDALkgqVAVAFVIPKESDSLEDRDVAhsQEKAIM-ALVD---SQIGNFGRPAHVWFV-SQLPKTRSGKMLR 595
Cdd:cd05914 386 LESLVVVQEKKL---VALAYIDPDFLDVKALKQRN--IIDAIKwEVRDkvnQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-596 |
8.49e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.46 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 50 RTNLCHNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACA 129
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVVF------DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVL 4622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 130 RIGAIHSVVFGGFASHSVAARIDDAKPVLIvsadagarggkiipykkllddaISQAQHQPRhvLLVDRGLAKMArvSGRD 209
Cdd:PRK12316 4623 KAGGAYVPLDPEYPRERLAYMMEDSGAALL----------------------LTQSHLLQR--LPIPDGLASLA--LDRD 4676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 210 VDFASLrhqhiGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYaVALATSMDTIFGGKAG-------SVFFCASD 282
Cdd:PRK12316 4677 EDWEGF-----PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSL-VNHLHATGERYELTPDdrvlqfmSFSFDGSH 4750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 283 IGWvvghsyivYAPLLAGMATIVyeglptwPDCGVW-----WTIVEKYQVSRMFSAPTAIRVLKKFPTaeiRKHDLSSLE 357
Cdd:PRK12316 4751 EGL--------YHPLINGASVVI-------RDDSLWdperlYAEIHEHRVTVLVFPPVYLQQLAEHAE---RDGEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 358 VLYLAGEPLDEPTASWVSNTLDVPVIDN-YWQTESG-WPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLnEVTGEPCGVN 435
Cdd:PRK12316 4813 VYCFGGEAVAQASYDLAWRALKPVYLFNgYGPTETTvTVLLWKARDGDACGAAYMPIGTPLGNRSGYVL-DGQLNPLPVG 4891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 436 EKGMLVVEGPlppGCIQTIWGDDG----RFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIE 511
Cdd:PRK12316 4892 VAGELYLGGE---GVARGYLERPAltaeRFVPDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIE 4968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 512 ESISSHPGVAEVAVVGVKDALkGQVAVAFVIPKESDSLEDRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSG 591
Cdd:PRK12316 4969 ARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNG 5047
|
....*
gi 16128320 592 KMLRR 596
Cdd:PRK12316 5048 KLDRK 5052
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
64-601 |
8.64e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.57 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 64 KQPEALALIAVSSETEEERTftfrQLHDEVNAVASML-RSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGF 142
Cdd:PLN02574 51 NHNGDTALIDSSTGFSISYS----ELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 143 ASHSVAARIDDAKPVLIVSA-----DAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDvdfaslrh 217
Cdd:PLN02574 127 SLGEIKKRVVDCSVGLAFTSpenveKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQD-------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 218 qhigarvpvawlesnETSCILYTSGTTGKPKGVQRDVGGyavaLATSMDTIFGGKAG--------SVFFCASDIGWVVGH 289
Cdd:PLN02574 199 ---------------DVAAIMYSSGTTGASKGVVLTHRN----LIAMVELFVRFEASqyeypgsdNVYLAALPMFHIYGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 290 SYIVYAPLLAGMATIVYEGLptwpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKfPTAEIRKHDLSSLEVLYLAGEPLDEP 369
Cdd:PLN02574 260 SLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 370 TASWVSNTL-DVPVIDNYWQTESgwpiMAIA-RGLD-DRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGP- 445
Cdd:PLN02574 335 FIQDFVQTLpHVDFIQGYGMTES----TAVGtRGFNtEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPg 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 446 LPPGCIQTIWGDDGRFVKTYWSLFSRPVYAtfdwgirDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAV 525
Cdd:PLN02574 411 VMKGYLNNPKATQSTIDKDGWLRTGDIAYF-------DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 526 VGVKDALKGQVAVAFVIPKESDSLedrdvahSQEkAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAI 601
Cdd:PLN02574 484 TAVPDKECGEIPVAFVVRRQGSTL-------SQE-AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
192-609 |
8.96e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.41 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 192 VLLVDRGLAKMAR-----VSGRDVD---FASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGV---QRDVGGYAVA 260
Cdd:PRK07867 104 LVLTESAHAELLDgldpgVRVINVDspaWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVrctHRKVASAGVM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 261 LATSmdtiFGGKAGSVFFCASDIGwvvgHSYIV---YAPLLAGMATIVyeglptwpdcgvwwtivekyqVSRMFSAPTAI 337
Cdd:PRK07867 184 LAQR----FGLGPDDVCYVSMPLF----HSNAVmagWAVALAAGASIA---------------------LRRKFSASGFL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 338 RVLKKF----------PTAEI-----RKHDLS-SLEVLYlaGEPLDEPTASWVSNTLDVPVIDNYWQTESGwpiMAIARG 401
Cdd:PRK07867 235 PDVRRYgatyanyvgkPLSYVlatpeRPDDADnPLRIVY--GNEGAPGDIARFARRFGCVVVDGFGSTEGG---VAITRT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 402 LDDRPTRLGsPGVPmygyNVQLLNEVTGEPCGVNEK------------GMLV-VEGplpPGCIQTIWGD---------DG 459
Cdd:PRK07867 310 PDTPPGALG-PLPP----GVAIVDPDTGTECPPAEDadgrllnadeaiGELVnTAG---PGGFEGYYNDpeadaermrGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RfvktYWSlfsrpvyatFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVA 539
Cdd:PRK07867 382 V----YWS---------GDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 540 FVIPKESDSLedrDVAhsqekAIMALVDSQ--IGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAicEGRDPGD 609
Cdd:PRK07867 449 ALVLAPGAKF---DPD-----AFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA--EGVDCAD 510
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
234-596 |
1.12e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 76.95 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 234 TSCILYTSGTTGKPKGVQ---RDVGGYAVALA-----TSMDT---------IFG---GKAGSVffcasDIGWVVGH---- 289
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVlsrRAIAADLDALAeawqwTADDVlvhglplfhVHGlvlGVLGPL-----RIGNRFVHtgrp 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 290 SYIVYAPLLAGMATIvYEGLPTwpdcgVWwtivekyqvSRMFSAPTAIRVLkkfptaeirkhdlSSLEVLYLAGEPLDEP 369
Cdd:PRK07787 205 TPEAYAQALSEGGTL-YFGVPT-----VW---------SRIAADPEAARAL-------------RGARLLVSGSAALPVP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 370 TASWVSNTLDVPVIDNYWQTESGWPIMAIARGlddrPTRLGSPGVPMYGYNVQLLNEvTGE--PCGVNEKGMLVVEGPL- 446
Cdd:PRK07787 257 VFDRLAALTGHRPVERYGMTETLITLSTRADG----ERRPGWVGLPLAGVETRLVDE-DGGpvPHDGETVGELQVRGPTl 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 447 ------PPGCIQTIWGDDGrfvktyWslfsrpvYATFDWGIRDADGYHFILGR-TDDVINVAGHRLGTREIEESISSHPG 519
Cdd:PRK07787 332 fdgylnRPDATAAAFTADG------W-------FRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPG 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 520 VAEVAVVGVKDALKGQVAVAFVIPKEsdsledrDVAhsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK07787 399 VREAAVVGVPDDDLGQRIVAYVVGAD-------DVA---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKK 465
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
237-600 |
1.55e-14 |
|
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: 75.06 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGVqrdVGGYAVALATSMDT--IFGGKAGSVFFCASDIGWVVGHsYIVYAPLLAGMATIVYEglPTWPd 314
Cdd:cd17630 5 VILTSGSTGTPKAV---VHTAANLLASAAGLhsRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLE--RNQA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 315 cgvwwtivekYQVSRMFSAPTAIRV----LKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSnTLDVPVIDNYWQTE 390
Cdd:cd17630 78 ----------LAEDLAPPGVTHVSLvptqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAA-DRGIPLYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 391 SGWPIMAIARGLDDRptrlGSPGVPMYGYNVQLLNEvtgepcgvnekGMLVVEGP-LPPGCIQTIWGDDGrfvktywslF 469
Cdd:cd17630 147 TASQVATKRPDGFGR----GGVGVLLPGRELRIVED-----------GEIWVGGAsLAMGYLRGQLVPEF---------N 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 470 SRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSL 549
Cdd:cd17630 203 EDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 16128320 550 EDrdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:cd17630 283 AE----------LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
237-592 |
3.97e-14 |
|
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: 74.34 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGV---QRDVGGyavALATSMDTIFG-------------GKAGSVFFCASDIgwVVGHSYIVYAPLLAG 300
Cdd:cd05924 8 ILYTGGTTGMPKGVmwrQEDIFR---MLMGGADFGTGeftpsedahkaaaAAAGTVMFPAPPL--MHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 MATIVYEGLPTWPDcGVWWTIvEKYQVSRMFSAPTAI-RVLKKfptaEIRK---HDLSSLEVLYLAGEPLD-EPTASWVS 375
Cdd:cd05924 83 GQTVVLPDDRFDPE-EVWRTI-EKHKVTSMTIVGDAMaRPLID----ALRDagpYDLSSLFAISSGGALLSpEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 376 NTLDVPVIDNYWQTESGWPIMAIARGLDD--RPTRLGSPGVpmygynvQLLNEVTGE-PCGVNEKGMLVVEGPLPPGciq 452
Cdd:cd05924 157 LVPNITLVDAFGSSETGFTGSGHSAGSGPetGPFTRANPDT-------VVLDDDGRVvPPGSGGVGWIARRGHIPLG--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 453 tIWGDDGRFVKTY-------WSLfsrpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAV 525
Cdd:cd05924 227 -YYGDEAKTAETFpevdgvrYAV-------PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 526 VGVKDALKGQVAVAFVipkesdslEDRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGK 592
Cdd:cd05924 299 VGRPDERWGQEVVAVV--------QLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
58-593 |
5.08e-14 |
|
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: 74.64 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIA---EAHITLLACariGAI 134
Cdd:cd12118 10 LERAAAVYPDRTSIV------YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPamyELHFGVPMA---GAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HSVVFGGFASHSVAARIddakpvlivsadagarggkiipykkllddaisqaQHQPRHVLLVDRGLAKMARVSGRDVDFAS 214
Cdd:cd12118 81 LNALNTRLDAEEIAFIL----------------------------------RHSEAKVLFVDREFEYEDLLAEGDPDFEW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 215 LRHQhigarvpvawlESNETSCILYTSGTTGKPKGV---QRdvGGYAVALATSMDtiFGGKAGSVFFCASDI----GWvv 287
Cdd:cd12118 127 IPPA-----------DEWDPIALNYTSGTTGRPKGVvyhHR--GAYLNALANILE--WEMKQHPVYLWTLPMfhcnGW-- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 288 GHSYIVYAplLAGmaTIVYegLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDlSSLEVLyLAGEPld 367
Cdd:cd12118 190 CFPWTVAA--VGG--TNVC--LRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLP-HRVHVM-TAGAP-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 368 ePTASWVS--NTLDVPVIDNYWQTESGWPIMAIA--RGLDDRPT----RLGS-PGVPMYGYN-VQLLNEVTGEPCGVNEK 437
Cdd:cd12118 259 -PPAAVLAkmEELGFDVTHVYGLTETYGPATVCAwkPEWDELPTeeraRLKArQGVRYVGLEeVDVLDPETMKPVPRDGK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 --GMLVVEGPLppgCIQTIWGDDgrfVKTYwSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESIS 515
Cdd:cd12118 338 tiGEIVFRGNI---VMKGYLKNP---EATA-EAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 516 SHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDvahsqekaIMALVDSQIGNFGRPAHVWFvSQLPKTRSGKM 593
Cdd:cd12118 411 KHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEE--------IIAFCREHLAGFMVPKTVVF-GELPKTSTGKI 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
61-604 |
6.55e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 74.54 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 61 WLEKQPEALALIAVSSEteeertFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFG 140
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 141 GFASHSVAARIDDA-KPVLIVSADAGARGGkiIPYKKLLDDAISQAqhqprhvllvdrglakmarvsgrDVDFASLRHQH 219
Cdd:PRK06145 85 RLAADEVAYILGDAgAKLLLVDEEFDAIVA--LETPKIVIDAAAQA-----------------------DSRRLAQGGLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 220 IGARVPVAwleSNETSCILYTSGTTGKPKGVQRDVGGYAvalATSMDTIFggkagSVFFCASDIGWVVGHSYIVYAPLLA 299
Cdd:PRK06145 140 IPPQAAVA---PTDLVRLMYTSGTTDRPKGVMHSYGNLH---WKSIDHVI-----ALGLTASERLLVVGPLYHVGAFDLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 300 GMATIVYEGLPTWP---DCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAGEPLDEPTASWVSN 376
Cdd:PRK06145 209 GIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEKTPESRIRDFTR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 377 TL-DVPVIDNYWQTE--SGWPIMAIARGLDdrptRLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGCIQT 453
Cdd:PRK06145 287 VFtRARYIDAYGLTEtcSGDTLMEAGREIE----KIGSTGRALAHVEIRIADG-AGRWLPPNMKGEICMRGP---KVTKG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 454 IWGDDGRFVKTYWSLFSRpvyaTFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALK 533
Cdd:PRK06145 359 YWKDPEKTAEAFYGDWFR----SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 534 GQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEG 604
Cdd:PRK06145 435 GERITAVVVLNPGATLT--------LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
349-596 |
9.53e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 74.03 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 349 RKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTE-----SGWPIMAIarglddrptRLGSPGVPMYGYNVQL 423
Cdd:PRK05677 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTEtspvvSVNPSQAI---------QVGTIGIPVPSTLCKV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 424 LNEVtGEPCGVNEKGMLVVEGPlppgciqtiwgddgRFVKTYW--------SLFSRPVYATFDWGIRDADGYHFILGRTD 495
Cdd:PRK05677 392 IDDD-GNELPLGEVGELCVKGP--------------QVMKGYWqrpeatdeILDSDGWLKTGDIALIQEDGYMRIVDRKK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 496 DVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGR 575
Cdd:PRK05677 457 DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT--------KEQVMEHMRANLTGYKV 528
|
250 260
....*....|....*....|.
gi 16128320 576 PAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILRR 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
210-601 |
1.02e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 74.09 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 210 VDFASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGyavaLATSMDTI------FGGKAGSVFFCASDI 283
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGN----LVANMLQVraclsqLGPDGQPLMKEGQEV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 284 GWV---VGHSYIVYAPLLAGMATIVYEGLPTWP-DCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVL 359
Cdd:PRK12492 261 MIAplpLYHIYAFTANCMCMMVSGNHNVLITNPrDIPGFIKELGKWRFSALLGLNTLFVALMDHP--GFKDLDFSALKLT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 360 YLAGEPLDEPTAS-WVSNTlDVPVIDNYWQTESGwPImAIARGLDDRpTRLGSPGVPMYGYNVQLLNEVTGE-PCGvnEK 437
Cdd:PRK12492 339 NSGGTALVKATAErWEQLT-GCTIVEGYGLTETS-PV-ASTNPYGEL-ARLGTVGIPVPGTALKVIDDDGNElPLG--ER 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVVEGPlppgciqtiwgddgRFVKTYW--------SLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTRE 509
Cdd:PRK12492 413 GELCIKGP--------------QVMKGYWqqpeataeALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 510 IEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPkesdsledRDVAHSQEKaIMALVDSQIGNFGRPAHVWFVSQLPKTR 589
Cdd:PRK12492 479 IEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVA--------RDPGLSVEE-LKAYCKENFTGYKVPKHIVLRDSLPMTP 549
|
410
....*....|..
gi 16128320 590 SGKMLRRTIQAI 601
Cdd:PRK12492 550 VGKILRRELRDI 561
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
233-595 |
1.73e-13 |
|
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: 71.76 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 233 ETSCILYTSGTTGKPKGV----QRDVGGYA----VALATSMDTI---------FGGKAGsvffcasdigWVVGhsyivya 295
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVmcahRQTLRAAAawadCADLTEDDRYliinpffhtFGYKAG----------IVAC------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 296 pLLAGmATIVYEGLPtwpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPtaEIRKHDLSSLEVLylagepldeptaswVS 375
Cdd:cd17638 64 -LLTG-ATVVPVAVF---DVDAILEAIERERITVLPGPPTLFQSLLDHP--GRKKFDLSSLRAA--------------VT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 376 NTLDVPV-----------IDN----YWQTESGWPIMAiaRGLDDRPTRLGSPGVPMYGYNVQLLNEvtGEpcgVNEKGML 440
Cdd:cd17638 123 GAATVPVelvrrmrselgFETvltaYGLTEAGVATMC--RPGDDAETVATTCGRACPGFEVRIADD--GE---VLVRGYN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 441 VVEGPL--PPGCIQTIwGDDGrfvktyWslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHP 518
Cdd:cd17638 196 VMQGYLddPEATAEAI-DADG------W-------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHP 261
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 519 GVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd17638 262 GVAQVAVIGVPDERMGEVGKAFVVARPGVTLT--------EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
83-596 |
1.79e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRS-LGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDD--AKPVLI 159
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDsgAKAIVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 VSADAGArggkiipYKKLLDdaisqaQHQPRHVLLVDRGlAKMARVSGRDVDFA-----------------SLRHQ-HIG 221
Cdd:PRK08974 128 VSNFAHT-------LEKVVF------KTPVKHVILTRMG-DQLSTAKGTLVNFVvkyikrlvpkyhlpdaiSFRSAlHKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 ARV----PVawLESNETSCILYTSGTTGKPKGvqrdvggyavALATSMDTIfggkaGSVFFCASdigwvvghsyiVYAPL 297
Cdd:PRK08974 194 RRMqyvkPE--LVPEDLAFLQYTGGTTGVAKG----------AMLTHRNML-----ANLEQAKA-----------AYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 298 LAGMATIVYEGLPTWP------DCGVWwtiVEKYQVSRMFSAPTAI----RVLKKFP-TA---------------EIRKH 351
Cdd:PRK08974 246 LHPGKELVVTALPLYHifaltvNCLLF---IELGGQNLLITNPRDIpgfvKELKKYPfTAitgvntlfnallnneEFQEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 352 DLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIARGLDDRPtrlGSPGVPMYGYNVQLLNEvTGEP 431
Cdd:PRK08974 323 DFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYS---GSIGLPVPSTEIKLVDD-DGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 432 CGVNEKGMLVVEGPlppgciQTIWGddgrfvktYWSlfsRPV----------YATFDWGIRDADGYHFILGRTDDVINVA 501
Cdd:PRK08974 399 VPPGEPGELWVKGP------QVMLG--------YWQ---RPEatdevikdgwLATGDIAVMDEEGFLRIVDRKKDMILVS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 502 GHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEkaimalvdsQIGNFGRPAHVWF 581
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRR---------HLTGYKVPKLVEF 532
|
570
....*....|....*
gi 16128320 582 VSQLPKTRSGKMLRR 596
Cdd:PRK08974 533 RDELPKSNVGKILRR 547
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-596 |
1.79e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.43 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 4 SEFYQRSINEPEQFWAEQAR-RIDWQTPFTQTLDHSnppfarwfcegrtnlCHNAIDRWLEKQPEALALiavsseTEEER 82
Cdd:PRK12467 478 AEPRRRLGELPLLDAEERAReLVRWNAPATEYAPDC---------------VHQLIEAQARQHPERPAL------VFGEQ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSA 162
Cdd:PRK12467 537 VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 DAGARggkiipykkLLD--DAISqaqhqprhVLLVDRGLAKMARVSGRDVDFAslrhqhigarvpvawLESNETSCILYT 240
Cdd:PRK12467 617 SHLLA---------QLPvpAGLR--------SLCLDEPADLLCGYSGHNPEVA---------------LDPDNLAYVIYT 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 241 SGTTGKPKGV---QRDVGGYAVALATSMDTIFGGKAGSVFFCASDIG-WVVghsyivYAPLLAGmATIVYEGLPTWPDCG 316
Cdd:PRK12467 665 SGSTGQPKGVaisHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGvTEL------FGALASG-ATLHLLPPDCARDAE 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 317 VWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIrkhdLSSLEVLYLAGE--PLDEPtASWVSNTLDVPVIDNYWQTESGWP 394
Cdd:PRK12467 738 AFAALMADQGVTVLKIVPSHLQALLQASRVAL----PRPQRALVCGGEalQVDLL-ARVRALGPGARLINHYGPTETTVG 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 395 IMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTgEPCGVNEKGMLVVEGP-LPPGCIQTIWGDDGRFVKTYWSLFSRPV 473
Cdd:PRK12467 813 VSTYELSDEERDFGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAgLARGYHRRPALTAERFVPDPFGADGGRL 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 474 YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVaVAFVIPKESdsledRD 553
Cdd:PRK12467 892 YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL-VAYLVPAAV-----AD 965
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 16128320 554 VAHSQEK--AIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK12467 966 GAEHQATrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
233-595 |
5.04e-13 |
|
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: 70.75 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 233 ETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYApLLAGMATIVYEGLPTW 312
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 313 PDcgvWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRkhDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESG 392
Cdd:cd17635 81 KS---LFKILTTNAVTTTCLVPTLLSKLVSELKSANA--TVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 393 wpiMAIARGLDDRPTRLGSPGVPMYGYNVQLlnevtgepcgVNEKGMLVVEGPLppgciQTIWGDDGRFVKTYW------ 466
Cdd:cd17635 156 ---TALCLPTDDDSIEINAVGRPYPGVDVYL----------AATDGIAGPSASF-----GTIWIKSPANMLGYWnnpert 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 467 -SLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKE 545
Cdd:cd17635 218 aEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16128320 546 SDsleDRDVAHSQEKAImalvDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd17635 298 EL---DENAIRALKHTI----RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
82-599 |
5.34e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 71.83 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVAS-MLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAAR-IDDAKPVLI 159
Cdd:PRK08751 49 KTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQlIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 160 VSADAGARGGKII---PYKKLLDDAISQAQHQPRHVLL--VDRGLAKMA---RVSG--RDVDFASLRHQHigaRVPVAWL 229
Cdd:PRK08751 129 VIDNFGTTVQQVIadtPVKQVITTGLGDMLGFPKAALVnfVVKYVKKLVpeyRINGaiRFREALALGRKH---SMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 230 ESNETSCILYTSGTTGKPKG---VQRDV-------------------GGYAVALATSMDTIFGGKAGSVFFCasDIGwvv 287
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGamlTHRNLvanmqqahqwlagtgkleeGCEVVITALPLYHIFALTANGLVFM--KIG--- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 288 GHSYIVYAPllagmativyEGLPTWpdcgvwwtiVEKYQVSRmFSAPTAIRVL--KKFPTAEIRKHDLSSLEVLYLAGEP 365
Cdd:PRK08751 281 GCNHLISNP----------RDMPGF---------VKELKKTR-FTAFTGVNTLfnGLLNTPGFDQIDFSSLKMTLGGGMA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 366 LDEPTASWVSNTLDVPVIDNYWQTESGwPIMAIarglddRPTRL----GSPGVPMYGYNVQLLNEvTGEPCGVNEKGMLV 441
Cdd:PRK08751 341 VQRSVAERWKQVTGLTLVEAYGLTETS-PAACI------NPLTLkeynGSIGLPIPSTDACIKDD-AGTVLAIGEIGELC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 442 VEGPlppgciQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVA 521
Cdd:PRK08751 413 IKGP------QVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 522 EVAVVGVKDALKGQVaVAFVIPKESDSLEDRDV-AHSQekaimalvdSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:PRK08751 487 EVAAVGVPDEKSGEI-VKVVIVKKDPALTAEDVkAHAR---------ANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
58-596 |
5.82e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 72.38 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 58 IDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSV 137
Cdd:PRK10252 464 VAQQAAKTPDAPALAD------ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 138 VFGGFASHSVAARIDDAKPVLIVSAD------AGARGGKIIPYKKLL--DDAISQAQHQPRHvllvdrglakmarvsgrd 209
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAdqlprfADVPDLTSLCYNAPLapQGAAPLQLSQPHH------------------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 210 vdfaslrhqhigarvpvawlesneTSCILYTSGTTGKPKGVQrdVGGYA-VALATSMDTIFGGKAGSVFF----CASDIG 284
Cdd:PRK10252 600 ------------------------TAYIIFTSGSTGRPKGVM--VGQTAiVNRLLWMQNHYPLTADDVVLqktpCSFDVS 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 285 -WVvghsyiVYAPLLAGmATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAG 363
Cdd:PRK10252 654 vWE------FFWPFIAG-AKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 364 EPLD-EPTASWVSNTlDVPVIDNYWQTE-----SGWPimaiARGLDDRPTRlGSPgVPMygynvqllnevtGEPcgVNEK 437
Cdd:PRK10252 727 EALPaDLCREWQQLT-GAPLHNLYGPTEaavdvSWYP----AFGEELAAVR-GSS-VPI------------GYP--VWNT 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 438 GMLVVEG---PLPPGC--------IQTIWGDDG-------RFVKTYWSLFSRpVYATFDWGIRDADGYHFILGRTDDVIN 499
Cdd:PRK10252 786 GLRILDArmrPVPPGVagdlyltgIQLAQGYLGrpdltasRFIADPFAPGER-MYRTGDVARWLDDGAVEYLGRSDDQLK 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 500 VAGHRLGTREIEESISSHPGVAEVAVVG---VKDALKGQVA---VAFVIPKESDSLeDRDV--AHSQEKAIMALVdsqig 571
Cdd:PRK10252 865 IRGQRIELGEIDRAMQALPDVEQAVTHAcviNQAAATGGDArqlVGYLVSQSGLPL-DTSAlqAQLRERLPPHMV----- 938
|
570 580
....*....|....*....|....*
gi 16128320 572 nfgrPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK10252 939 ----PVVLLQLDQLPLSANGKLDRK 959
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
63-596 |
6.57e-13 |
|
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: 71.20 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 63 EKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHsvvfggf 142
Cdd:cd17655 8 EKTPDHTAVVF------EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAY------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 143 ashsvaARIDDAKPVlivsadagarggKIIPYkkLLDDaiSQAQhqprhVLLVDRGLAKMARVSGR--DVDFASLRHQHi 220
Cdd:cd17655 75 ------LPIDPDYPE------------ERIQY--ILED--SGAD-----ILLTQSHLQPPIAFIGLidLLDEDTIYHEE- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 221 GARVPVAwLESNETSCILYTSGTTGKPKGV---QRDVGGYAVALATSM-----DTIfgGKAGSVFFCASdigwvvghSYI 292
Cdd:cd17655 127 SENLEPV-SKSDDLAYVIYTSGSTGKPKGVmieHRGVVNLVEWANKVIyqgehLRV--ALFASISFDAS--------VTE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 293 VYAPLLAGMATIVYEGLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKkfptaEIRKHDLSSLEVLYLAGEPLDEPTAS 372
Cdd:cd17655 196 IFASLLSGNTLYIVRKETVL-DGQALTQYIRQNRITIIDLTPAHLKLLD-----AADDSEGLSLKHLIVGGEALSTELAK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 373 -WVSNTLDVPVIDN-YWQTESgwPIMAIARGLDDRPTRLGSP--GVPMYGYNVQLLNE--------VTGEPC----GV-- 434
Cdd:cd17655 270 kIIELFGTNPTITNaYGPTET--TVDASIYQYEPETDQQVSVpiGKPLGNTRIYILDQygrpqpvgVAGELYiggeGVar 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 435 ---------NEKgmlVVEGPLPPGciqtiwgddGRfvktywslfsrpVYATFDWGIRDADGYHFILGRTDDVINVAGHRL 505
Cdd:cd17655 348 gylnrpeltAEK---FVDDPFVPG---------ER------------MYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 506 GTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKesdslEDRDVAHSQEKAIMALVDSQIgnfgrPAHVWFVSQL 585
Cdd:cd17655 404 ELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE-----KELPVAQLREFLARELPDYMI-----PSYFIKLDEI 473
|
570
....*....|.
gi 16128320 586 PKTRSGKMLRR 596
Cdd:cd17655 474 PLTPNGKVDRK 484
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-600 |
1.85e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 55 HNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:PRK12316 2006 HQRIAEQAARAPEAIAVVF------GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGA 2079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 135 HsvvfggfashsvaARIDDAKP---VLIVSADAGARggkiipykkLLddaISQAQHQPRhvLLVDRGLAKMArvSGRDVD 211
Cdd:PRK12316 2080 Y-------------VPLDPNYPaerLAYMLEDSGAA---------LL---LTQRHLLER--LPLPAGVARLP--LDRDAE 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 212 FASLRHQHigarvPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVF------FCASDIGW 285
Cdd:PRK12316 2131 WADYPDTA-----PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELqfmsfsFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 vvghsyivYAPLLAGMATIVYEGlPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKfpTAEIRKHDLSsLEVLYLAGEP 365
Cdd:PRK12316 2206 --------FHPLLNGARVLIRDD-ELW-DPEQLYDEMERHGVTILDFPPVYLQQLAE--HAERDGRPPA-VRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 366 LDEPTASWVSNTLD-VPVIDNYWQTESGW-PIMAIARGLDDRptrlGSPGVPMygynvqllnevtGEPCGvNEKGMLVVE 443
Cdd:PRK12316 2273 VPAASLRLAWEALRpVYLFNGYGPTEAVVtPLLWKCRPQDPC----GAAYVPI------------GRALG-NRRAYILDA 2335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 G--PLPPGCIQTIW-GDDG--------------RFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLG 506
Cdd:PRK12316 2336 DlnLLAPGMAGELYlGGEGlargylnrpgltaeRFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIE 2415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 507 TREIEESISSHPGVAeVAVVGVKDALKGQVAVAFVIPkesdsledRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLP 586
Cdd:PRK12316 2416 LGEIEARLQAHPAVR-EAVVVAQDGASGKQLVAYVVP--------DDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
570
....*....|....
gi 16128320 587 KTRSGKMLRRTIQA 600
Cdd:PRK12316 2487 LNPNGKLDRKALPK 2500
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
237-592 |
2.17e-12 |
|
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: 69.42 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGVqrdvggyAVALATSMDTIFGgkAGSVFFCASDIgWVVGHSYIVYAP--------LLAGmATIVYEG 308
Cdd:cd17654 123 VIHTSGTTGTPKIV-------AVPHKCILPNIQH--FRSLFNITSED-ILFLTSPLTFDPsvveiflsLSSG-ATLLIVP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 309 LPTWPDCGVWWTIV-EKYQVSRMFSAPTairVLKKFPTAEIRKHDLS---SLEVLYLAGEPLDEPT--ASWVSNTLDVPV 382
Cdd:cd17654 192 TSVKVLPSKLADILfKRHRITVLQATPT---LFRRFGSQSIKSTVLSatsSLRVLALGGEPFPSLVilSSWRGKGNRTRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 383 IDNYWQTE-SGWPIMAIARGLDDrPTRLGSPgvpmygynvqLLNEV--TGEPCGVNEKGMLVVEGpLPPGCIqtIWGDDG 459
Cdd:cd17654 269 FNIYGITEvSCWALAYKVPEEDS-PVQLGSP----------LLGTVieVRDQNGSEGTGQVFLGG-LNRVCI--LDDEVT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RfVKTYWslfsrpvYATFDWgIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHpgvaEVAVVGVKDALKGQVAVA 539
Cdd:cd17654 335 V-PKGTM-------RATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC----LGVESCAVTLSDQQRLIA 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16128320 540 FVIPKESDSLEDRDVaHSQEKAIMALvdsqignfgrPAHVWFVSQLPKTRSGK 592
Cdd:cd17654 402 FIVGESSSSRIHKEL-QLTLLSSHAI----------PDTFVQIDKLPLTSHGK 443
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
57-248 |
2.17e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 69.90 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 57 AIDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGA--- 133
Cdd:PRK08279 42 VFEEAAARHPDRPALL------FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvva 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 134 -IHSVVFGGFASHSVaaRIDDAKpVLIVSAD-----AGARGgkiipykkLLDDAISQAQHQPRHVLLVDRGLAKMARVSG 207
Cdd:PRK08279 116 lLNTQQRGAVLAHSL--NLVDAK-HLIVGEElveafEEARA--------DLARPPRLWVAGGDTLDDPEGYEDLAAAAAG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128320 208 RDVDFASLRhqhigARVPvawleSNETSCILYTSGTTGKPK 248
Cdd:PRK08279 185 APTTNPASR-----SGVT-----AKDTAFYIYTSGTTGLPK 215
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
70-599 |
7.88e-12 |
|
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: 67.84 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 70 ALIAVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAA 149
Cdd:cd05915 11 KEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 150 RIDDAKP-VLIVSADAGARGGKIIpykKLLDDAISQAQHQPRHVLLVDRglakmarVSGRDVDFASLRhqhigarvPVaw 228
Cdd:cd05915 91 ILNHAEDkVLLFDPNLLPLVEAIR---GELKTVQHFVVMDEKAPEGYLA-------YEEALGEEADPV--------RV-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 229 lESNETSCILYTSGTTGKPKGV-QRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYE 307
Cdd:cd05915 151 -PERAACGMAYTTGTTGLPKGVvYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 308 glpTWPDCGVWWTIVeKYQVSRMFSAPTAIRVL--------KKFP-TAEIRKHDLSSLEVLyLAGEPLDEPTASWVSNTL 378
Cdd:cd05915 230 ---RLDPASLVELFD-GEGVTFTAGVPTVWLALadylestgHRLKtLRRLVVGGSAAPRSL-IARFERMGVEVRQGYGLT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 379 DVPVIDN--YWQTEsgWPIMAiarglDDRPTRLGS-PGVPMYGYNVQLLNEVTgepCGVNEKGMLVVEGPLPPGCIQTIW 455
Cdd:cd05915 305 ETSPVVVqnFVKSH--LESLS-----EEEKLTLKAkTGLPIPLVRLRVADEEG---RPVPKDGKALGEVQLKGPWITGGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 456 GDDGRfvKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ 535
Cdd:cd05915 375 YGNEE--ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 536 VAVAFVIPKEsdsledrdvAHSQEKAIMALVDSQIGNFGR-PAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:cd05915 453 RPLAVVVPRG---------EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
66-596 |
1.01e-11 |
|
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: 67.28 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:cd17652 1 PDAPAVVF------GDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPVLIVSadagarggkiipykkllddaisqaqhQPRHvllvdrgLAKmarvsgrdvdfaslrhqhigarvp 225
Cdd:cd17652 75 RIAYMLADARPALLLT--------------------------TPDN-------LAY------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 vawlesnetscILYTSGTTGKPKGVQRDVGGYAvALATSMDTIFGGKAGS-VFFCASdIGWVVGHSYIVYApLLAGMATI 304
Cdd:cd17652 98 -----------VIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSrVLQFAS-PSFDASVWELLMA-LLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 305 VYEGLPTWPDCGVWWTIVEkYQVSRMFSAPTAIRVLkkfPTAeirkhDLSSLEVLYLAGEPLD-EPTASWVSNTLdvpVI 383
Cdd:cd17652 164 LAPAEELLPGEPLADLLRE-HRITHVTLPPAALAAL---PPD-----DLPDLRTLVVAGEACPaELVDRWAPGRR---MI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 384 DNYWQTESG-WPIMAIARGLDDRPTrlgsPGVPMYGYNVQLLNEvTGEPCGVNEKGMLVVEGPlppGCIQTIWGDDG--- 459
Cdd:cd17652 232 NAYGPTETTvCATMAGPLPGGGVPP----IGRPVPGTRVYVLDA-RLRPVPPGVPGELYIAGA---GLARGYLNRPGlta 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 -RFVKtywSLFSRP---VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ 535
Cdd:cd17652 304 eRFVA---DPFGAPgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDK 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 536 VAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:cd17652 381 RLVAYVVPAPGAAPT--------AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
82-599 |
1.37e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 67.31 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVS 161
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADA--GARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLrhqhigarvPvawlesnetscilY 239
Cdd:PLN02330 134 NDTnyGKVKGLGLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEILQTDLCAL---------P-------------F 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSV-------FFcasDIGWVVGhsyIVYAPLLAGMATIVYEGLptw 312
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVvtlglipFF---HIYGITG---ICCATLRNKGKVVVMSRF--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 313 pDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEV--LYLAGEPLDEPTASWVSNTL-DVPVIDNYWQT 389
Cdd:PLN02330 263 -ELRTFLNALITQEVSFAPIVPPIILNLVKNPIVE--EFDLSKLKLqaIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 390 ESGwpIMAIARGLDDRP---TRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppgCIQTIWGDDGRfvKTYW 466
Cdd:PLN02330 340 EHS--CITLTHGDPEKGhgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQ----CVMQGYYNNKE--ETDR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 467 SLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVI--PK 544
Cdd:PLN02330 412 TIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVinPK 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 545 ESDSLEDrdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:PLN02330 492 AKESEED----------ILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-596 |
2.49e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 53 LCHNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIG 132
Cdd:PRK12467 3096 LVHQLIEAQVARTPEAPALVF------GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 133 AIHSVVFGGFASHSVAARIDDAKpvlivsadagarggkiipyKKLLddaISQA---QHQPR----HVLLVDRGlakmarv 205
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSG-------------------VKLL---LTQAhllEQLPApagdTALTLDRL------- 3220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 206 sgrdvDFASLRHqhigaRVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALaTSMDTIFGGKAGSVFFCASDIGW 285
Cdd:PRK12467 3221 -----DLNGYSE-----NNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHL-CWIAEAYELDANDRVLLFMSFSF 3289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 VVGHSYiVYAPLLAGMATIVYEGLPTWPDcgVWWTIVEKYQVSRMFSAPTAIRVLKKFptAEIRkhDLSSLEVLYLAGEP 365
Cdd:PRK12467 3290 DGAQER-FLWTLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAED--AGGA--DCASLDIYVFGGEA 3362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 366 LDEPTASWVSNTL-DVPVIDNYWQTESGWPIMAIARGLDDRPTRLGSP-GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVE 443
Cdd:PRK12467 3363 VPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPiGRPVAGRSIYVLDG-QLNPVPVGVAGELYIG 3441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 GP-LPPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAe 522
Cdd:PRK12467 3442 GVgLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR- 3520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128320 523 VAVVGVKDALKGQVAVAFVIPK-ESDSLEDRDVAHSQekaimalvdSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK12467 3521 EAVVLARDGAGGKQLVAYVVPAdPQGDWRETLRDHLA---------ASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
66-598 |
2.53e-11 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 65.95 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGaihsvvfggfash 145
Cdd:cd17650 1 PDAIAVS------DATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAG------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 svaariddakpvlivsadagargGKIIPykklLDDAISQAQhqprhvllvdrgLAKMARVSGrdvdfaslrhqhigarVP 225
Cdd:cd17650 62 -----------------------GAYVP----IDPDYPAER------------LQYMLEDSG----------------AK 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 226 VAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALAT--------------------SMDTIFGGKAGSVFFCasdigw 285
Cdd:cd17650 87 LLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyeldsfpvrllqmasfSFDVFAGDFARSLLNG------ 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 286 vvGHSYIVYAPLLAGMATIvYEglptwpdcgvwwtIVEKYQVSRMFSAPTAIRVLKKFptAEIRKHDLSSLEVLYLAGep 365
Cdd:cd17650 161 --GTLVICPDEVKLDPAAL-YD-------------LILKSRITLMESTPALIRPVMAY--VYRNGLDLSAMRLLIVGS-- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 366 lDEPTASWVSNTLD-----VPVIDNYWQTE----SGWPIMAIARGLDDRPTRLGSP--GVPMYgynvqLLNE-------- 426
Cdd:cd17650 221 -DGCKAQDFKTLAArfgqgMRIINSYGVTEatidSTYYEEGRDPLGDSANVPIGRPlpNTAMY-----VLDErlqpqpvg 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 427 VTGEPC----GVnEKGML---------VVEGPLPPGciqtiwgddGRfvktywslfsrpVYATFDWGIRDADGYHFILGR 493
Cdd:cd17650 295 VAGELYiggaGV-ARGYLnrpeltaerFVENPFAPG---------ER------------MYRTGDLARWRADGNVELLGR 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 494 TDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDAlKGQVA-VAFVIPKESdsledRDVAHSQEKAIMALVDSQIgn 572
Cdd:cd17650 353 VDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARlCAYVVAAAT-----LNTAELRAFLAKELPSYMI-- 424
|
570 580
....*....|....*....|....*.
gi 16128320 573 fgrPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd17650 425 ---PSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
66-603 |
3.34e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 66.12 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIA---EAHitlLACARIGAIhsvvfggf 142
Cdd:PRK08162 32 PDRPAVI------HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPamvEAH---FGVPMAGAV-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 143 aSHSVAARID-----------DAKpVLIVSADagarggkiipYKKLLDDAISQAQHQprHVLLVDrglakmarvsgrDVD 211
Cdd:PRK08162 95 -LNTLNTRLDaasiafmlrhgEAK-VLIVDTE----------FAEVAREALALLPGP--KPLVID------------VDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 212 FASLRHQHIGARVPVAWLES-----------NETSCIL--YTSGTTGKPKGV---QRdvGGYAVALATSMDTIFGGKAG- 274
Cdd:PRK08162 149 PEYPGGRFIGALDYEAFLASgdpdfawtlpaDEWDAIAlnYTSGTTGNPKGVvyhHR--GAYLNALSNILAWGMPKHPVy 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 275 ----SVFFCAsdiGWvvGHSYIVYAplLAGmaTIVyegLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRK 350
Cdd:PRK08162 227 lwtlPMFHCN---GW--CFPWTVAA--RAG--TNV---CLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 351 --HDLSSLevlyLAGEPldePTASWVSNT----LDV-----------PVIDNYWQteSGWPimaiARGLDDRPTRLGSPG 413
Cdd:PRK08162 295 idHPVHAM----VAGAA---PPAAVIAKMeeigFDLthvygltetygPATVCAWQ--PEWD----ALPLDERAQLKARQG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 414 VPmygYNVQ----LLNEVTGEPCG--------VNEKGMLVVEGPLppgciqtiwgddgRFVKTYWSLFSRPVYATFDWGI 481
Cdd:PRK08162 362 VR---YPLQegvtVLDPDTMQPVPadgetigeIMFRGNIVMKGYL-------------KNPKATEEAFAGGWFHTGDLAV 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 482 RDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVipkesdslEDRDVAHSQEKA 561
Cdd:PRK08162 426 LHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV--------ELKDGASATEEE 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 16128320 562 IMALVDSQIGNFGRPAHVWFvSQLPKTRSGK----MLRRTIQAICE 603
Cdd:PRK08162 498 IIAHCREHLAGFKVPKAVVF-GELPKTSTGKiqkfVLREQAKSLKA 542
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
56-251 |
6.47e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.92 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 56 NAIDRWLEKQPEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGaiH 135
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYD------YLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 136 SVVfgGFASHSVAARIDD----AKPVLIVSA---DAGARGGKIIPYKKLLDdaisqaqhqprhvllvdrglakmARVSGR 208
Cdd:PRK04813 78 AYI--PVDVSSPAERIEMiievAKPSLIIATeelPLEILGIPVITLDELKD-----------------------IFATGN 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128320 209 DVDFASlrhqhigarvpvaWLESNETSCILYTSGTTGKPKGVQ 251
Cdd:PRK04813 133 PYDFDH-------------AVKGDDNYYIIFTSGTTGKPKGVQ 162
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
322-595 |
4.72e-10 |
|
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: 61.52 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 322 VEKYQVSRMFS-APTAIRVLkkfptAEIRKH--DLSSLEvlYLAGEPLDEPTASWVSNTlDVPVIDNYWQTE-SGWPIMA 397
Cdd:cd17637 84 IEEEKVTLMGSfPPILSNLL-----DAAEKSgvDLSSLR--HVLGLDAPETIQRFEETT-GATFWSLYGQTEtSGLVTLS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 398 IARgldDRPTRLGSPGvPMYgyNVQLLNEvTGEPCGVNEKGMLVVEGPLppgciqtiwgddgrFVKTYWSLFSRPVYA-- 475
Cdd:cd17637 156 PYR---ERPGSAGRPG-PLV--RVRIVDD-NDRPVPAGETGEIVVRGPL--------------VFQGYWNLPELTAYTfr 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 476 -----TFDWGIRDADGYHFILGRT--DDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDS 548
Cdd:cd17637 215 ngwhhTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16128320 549 LEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:cd17637 295 LT--------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
82-302 |
1.76e-09 |
|
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: 60.51 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVS 161
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 ADAgARGGKIIPykkllddaISQAQHQPRHVLLVD-RGLAKMARvsGRDVDFASL--RHQHIGARVP------VAWLESN 232
Cdd:cd17641 90 EDE-EQVDKLLE--------IADRIPSVRYVIYCDpRGMRKYDD--PRLISFEDVvaLGRALDRRDPglyereVAAGKGE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128320 233 ETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDtiFGGK-AGSVFFCASDIGWVVGHSYIVYAPLLAGMA 302
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPLgPGDEYVSVLPLPWIGEQMYSVGQALVCGFI 227
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
225-592 |
2.93e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.32 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 225 PVAWLES--------NETSCILYTSGTTGKPKGVQ---RDVGGYAVAL-----ATSMDTIfggkAGSV-FFcasdigwvv 287
Cdd:PRK08633 767 PARLLKRlygptfkpDDTATIIFSSGSEGEPKGVMlshHNILSNIEQIsdvfnLRNDDVI----LSSLpFF--------- 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 288 gHS--YIV--YAPLLAGMATiVYEGLPTwpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirKHDLSSLEVLYLAG 363
Cdd:PRK08633 834 -HSfgLTVtlWLPLLEGIKV-VYHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLH--PLMFASLRLVVAGA 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 364 EPLDEPTASWVSNTLDVPVIDNYWQTESGwPIMA-------IARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNE 436
Cdd:PRK08633 908 EKLKPEVADAFEEKFGIRILEGYGATETS-PVASvnlpdvlAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFEELPPGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 437 KGMLVVEGPlppgciQTIWGDDGRFVKTY----------WslfsrpvYATFDWGIRDADGYHFILGRTDDVINVAGHRLG 506
Cdd:PRK08633 987 DGLILIGGP------QVMKGYLGDPEKTAevikdidgigW-------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVP 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 507 TREIEESIS--SHPGVAEVAVVGVKDALKG-QVAVAFvipkesdSLEDRDVAHSQEKaimaLVDSQIGNFGRPAHVWFVS 583
Cdd:PRK08633 1054 LGAVEEELAkaLGGEEVVFAVTAVPDEKKGeKLVVLH-------TCGAEDVEELKRA----IKESGLPNLWKPSRYFKVE 1122
|
....*....
gi 16128320 584 QLPKTRSGK 592
Cdd:PRK08633 1123 ALPLLGSGK 1131
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
66-598 |
3.13e-09 |
|
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: 59.80 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALIavssetEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGaihsvvfGGFASh 145
Cdd:cd17656 2 PDAVAVV------FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAG-------GAFVP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 svaarIDDAKP---VLIVSADAGARggkIIPYKKLLDDAISQAQhqpRHVLLVDRGLAKmarVSGRDVDFASlrhqhiga 222
Cdd:cd17656 68 -----IDPEYPeerRIYIMLDSGVR---VVLTQRHLKSKLSFNK---STILLEDPSISQ---EDTSNIDYIN-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 223 rvpvawlESNETSCILYTSGTTGKPKGVQRDVGGYAVALA---TSMDTIFGGKAGSVFFCASDigwvVGHSYIVYAPLLA 299
Cdd:cd17656 126 -------NSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHferEKTNINFSDKVLQFATCSFD----VCYQEIFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 300 GMATIVYEglPTWPDCGVWWTIVEKYQVSRMFsAPTA----IRVLKKF--PTAEIRKHdlsslevLYLAGEPLDeptasw 373
Cdd:cd17656 195 GTLYIIRE--ETKRDVEQLFDLVKRHNIEVVF-LPVAflkfIFSEREFinRFPTCVKH-------IITAGEQLV------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 374 VSNTL-------DVPVIDNYWQTESGWPIMAIARGLDDRPtRLGSPGVPMYGYNVQLLNEV-TGEPCGVneKGMLVVEGp 445
Cdd:cd17656 259 ITNEFkemlhehNVHLHNHYGPSETHVVTTYTINPEAEIP-ELPPIGKPISNTWIYILDQEqQLQPQGI--VGELYISG- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 446 lppgcIQTIWGDDGRFVKTYWSLFSRP------VYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPG 519
Cdd:cd17656 335 -----ASVARGYLNRQELTAEKFFPDPfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPG 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 520 VAEVAVVGVKDALKGQVAVAFVIPKESdsledrdVAHSQEKAIMAlvdSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd17656 410 VSEAVVLDKADDKGEKYLCAYFVMEQE-------LNISQLREYLA---KQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
233-600 |
4.69e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 58.89 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 233 ETSCILYTSGTTGKPK-------GVQRDVGGYAVALATSMDTIfggkagSVFFCAsdigwvVGHSYIVYAPLLAGMA--- 302
Cdd:PRK08308 102 EPSLLQYSSGTTGEPKlirrswtEIDREIEAYNEALNCEQDET------PIVACP------VTHSYGLICGVLAALTrgs 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 303 --TIVYEGLPTWPdcgvwWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHdlssleVLYLAGEPLDEPT-ASWVSNTLD 379
Cdd:PRK08308 170 kpVIITNKNPKFA-----LNILRNTPQHILYAVPLMLHILGRLLPGTFQFH------AVMTSGTPLPEAWfYKLRERTTY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 380 VpvIDNYWQTESGwpIMAIARGLDDrPTRLGSPgvpmygynvqlLNEVTGEpCGVNEKGmlvvegplpPGCIQtIWGDDG 459
Cdd:PRK08308 239 M--MQQYGCSEAG--CVSICPDMKS-HLDLGNP-----------LPHVSVS-AGSDENA---------PEEIV-VKMGDK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 460 RFvktywslfsrpvyATFDWGIRDADGY-HFiLGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQ-VA 537
Cdd:PRK08308 292 EI-------------FTKDLGYKSERGTlHF-MGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVK 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 538 VAFVIPKESDSLEDRdvahsqEKAIMALVDSQIgnfgrPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK08308 358 AKVISHEEIDPVQLR------EWCIQHLAPYQV-----PHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
67-550 |
3.15e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 57.00 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 67 EALALIAVSSETeeeRTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHS 146
Cdd:TIGR03443 257 ETPSFLDPSSKT---RSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 147 VAARIDDAKP-VLIVSADAGARGGKIIPYkklLDDAISQAQHQPRHVLLVDRGLAKmARVSGRDVD----FASLRHQHIG 221
Cdd:TIGR03443 334 QTIYLSVAKPrALIVIEKAGTLDQLVRDY---IDKELELRTEIPALALQDDGSLVG-GSLEGGETDvlapYQALKDTPTG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 ARV-PvawlESNETscILYTSGTTGKPKGVQrdvgGYAVALA---TSMDTIFGGKAGSVFFCASDIgwvvGHSYI---VY 294
Cdd:TIGR03443 410 VVVgP----DSNPT--LSFTSGSEGIPKGVL----GRHFSLAyyfPWMAKRFGLSENDKFTMLSGI----AHDPIqrdMF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 295 APLLAGMATIVyeglPTWPDCGV------WwtiVEKYQVSRMFSAPTAIRVLKKFPTAEI-------------RKHDLSS 355
Cdd:TIGR03443 476 TPLFLGAQLLV----PTADDIGTpgrlaeW---MAKYGATVTHLTPAMGQLLSAQATTPIpslhhaffvgdilTKRDCLR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 356 LEVLylagepldeptaswvsnTLDVPVIDNYWQTE-----SGWPIMAIArgldDRPTRLGS------PGVPMygYNVQLL 424
Cdd:TIGR03443 549 LQTL-----------------AENVCIVNMYGTTEtqravSYFEIPSRS----SDSTFLKNlkdvmpAGKGM--KNVQLL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 425 ----NEVTgEPCGVNEKGMLVV------EGPL-PPGC-----IQTIWGDDGRFVKT----------YWSLFSRPVYATFD 478
Cdd:TIGR03443 606 vvnrNDRT-QTCGVGEVGEIYVragglaEGYLgLPELnaekfVNNWFVDPSHWIDLdkennkpereFWLGPRDRLYRTGD 684
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128320 479 WGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPK-ESDSLE 550
Cdd:TIGR03443 685 LGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdKSDELE 757
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
221-600 |
4.41e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.19 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 221 GARVPVAWLESNETSCILYTSGTTGKPKGVqRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGwvvgHSYIVYA---PL 297
Cdd:PRK13388 139 GALTPHREVDAMDPFMLIFTSGTTGAPKAV-RCSHGRLAFAGRALTERFGLTRDDVCYVSMPLF----HSNAVMAgwaPA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 298 LAGMATIVYEglPTW------PDcgvwwtiVEKYQVSRMFSAPTAIRVLkkFPTAEiRKHDLSSLEVLYLAGEPLDEPTA 371
Cdd:PRK13388 214 VASGAAVALP--AKFsasgflDD-------VRRYGATYFNYVGKPLAYI--LATPE-RPDDADNPLRVAFGNEASPRDIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 372 SWvSNTLDVPVIDNYWQTESGwpiMAIARGLDDRPTRLGSPGVpmygyNVQLLNEVTGEPCGV---NEKGMLVVegplPP 448
Cdd:PRK13388 282 EF-SRRFGCQVEDGYGSSEGA---VIVVREPGTPPGSIGRGAP-----GVAIYNPETLTECAVarfDAHGALLN----AD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 449 GCIQTIWGDDG-RFVKTYWS-------LFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGV 520
Cdd:PRK13388 349 EAIGELVNTAGaGFFEGYYNnpeataeRMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 521 AEVAVVGVKDALKG-QVAVAFVIPKESDSLEDrdvahsqekAIMALVDSQ--IGNFGRPAHVWFVSQLPKTRSGKMLRRT 597
Cdd:PRK13388 429 NRVAVYAVPDERVGdQVMAALVLRDGATFDPD---------AFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRE 499
|
...
gi 16128320 598 IQA 600
Cdd:PRK13388 500 LIA 502
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
84-518 |
9.90e-08 |
|
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: 54.78 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAK-PVLIVsa 162
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEsKALFV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 dagargGKiipykklLDDAISQAQHQPRHVLLVdrgLAKMARVSGRDVDFASLRHQH---IGARVPvawlESNETSCILY 239
Cdd:cd05932 85 ------GK-------LDDWKAMAPGVPEGLISI---SLPPPSAANCQYQWDDLIAQHpplEERPTR----FPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGVQRDVGGYAVALATSMDTIfGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWpdcgvww 319
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTF------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 320 tiVEKYQVSR---MFSAPT-----AIRVLKKFPTAEI--------------RK-HDLSSLEVLYLAG---EPLDEPTASW 373
Cdd:cd05932 217 --VEDVQRARptlFFSVPRlwtkfQQGVQDKIPQQKLnlllkipvvnslvkRKvLKGLGLDQCRLAGcgsAPVPPALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 374 VSNtLDVPVIDNYWQTES-GWPIMaiargldDRP--TRLGSPGVPMYGYNVQllnevtgepcgVNEKGMLVVEGplpPGC 450
Cdd:cd05932 295 YRS-LGLNILEAYGMTENfAYSHL-------NYPgrDKIGTVGNAGPGVEVR-----------ISEDGEILVRS---PAL 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 451 IQTIWGDDgrfVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVA-GHRLGTREIEESISSHP 518
Cdd:cd05932 353 MMGYYKDP---EATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHD 418
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-518 |
1.12e-07 |
|
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: 54.77 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 82 RTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakPVLIvs 161
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV---------------------PVLI-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 162 aDAGARGGKIipyKKLLDDAISQAqhqprhvllvdrglakmarvsgrdvdfaslrhqHIGarVPVAwlesNETSCILYTS 241
Cdd:cd05910 58 -DPGMGRKNL---KQCLQEAEPDA---------------------------------FIG--IPKA----DEPAAILFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 242 GTTGKPKGVQRDVGGYAVALATsMDTIFGGKAGSVFFCASDIgwvvghsYIVYAPLLaGMATIVYEGLPTWP---DCGVW 318
Cdd:cd05910 95 GSTGTPKGVVYRHGTFAAQIDA-LRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTRParaDPQKL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 319 WTIVEKYQVSRMFSAPTAIRVLKKFptAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTL--DVPVIDNYWQTESgWPIM 396
Cdd:cd05910 166 VGAIRQYGVSIVFGSPALLERVARY--CAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPVS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 397 AIA-RGLDDRPTRLGSP------GVPMYGYNVQLLnEVTGEPCG---------VNEKGMLVVEGPL---------PPGCI 451
Cdd:cd05910 243 SIGsRELLATTTAATSGgagtcvGRPIPGVRVRII-EIDDEPIAewddtlelpRGEIGEITVTGPTvtptyvnrpVATAL 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 452 QTIWGDDGRFvktywslfsrpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHP 518
Cdd:cd05910 322 AKIDDNSEGF-----------WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHP 377
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
465-609 |
1.33e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 54.23 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 465 YWSLF--SRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVI 542
Cdd:PRK07445 315 YYPQIldSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV 394
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 543 PKESDSLEDRdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGD 609
Cdd:PRK07445 395 PKDPSISLEE---------LKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLGLP 452
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
221-596 |
1.39e-07 |
|
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: 54.33 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 221 GARVPVAwlESNETSCILYTSGTTGKPKGVQRDVGGyAVALATSMDTIFGGKAGS---VFFCASdigWVVGHSY--IVYA 295
Cdd:cd17648 85 GARVVIT--NSTDLAYAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNGdeaVLFFSN---YVFDFFVeqMTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 296 pLLAGMATIVYEGlPTWPDCGVWWTIVEKYQVSRMFSAPTairVLKKFPTAEirkhdLSSLEVLYLAGEPLDEPTASWVS 375
Cdd:cd17648 159 -LLNGQKLVVPPD-EMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLAR-----LPHLKRVDAAGEEFTAPVFEKLR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 376 NTLDVPVIDNYWQTESGwpIMAIARGL--DDRPTRlgSPGVPMYGYNVQLLNEVTgEPCGVNEKGMLVVEGP-LPPGCIQ 452
Cdd:cd17648 229 SRFAGLIINAYGPTETT--VTNHKRFFpgDQRFDK--SLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDgVARGYLN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 453 TIWGDDGRFVKTYW--------SLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVA 524
Cdd:cd17648 304 RPELTAERFLPNPFqteqerarGRNAR-LYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECA 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 525 VVGVKDALKGQVA-----VAFVIPkESDSLEDRDVAHSQEKAIMALVdsqignfgRPAHVWFVSQLPKTRSGKM-LRR 596
Cdd:cd17648 383 VVAKEDASQAQSRiqkylVGYYLP-EPGHVPESDLLSFLRAKLPRYM--------VPARLVRLEGIPVTINGKLdVRA 451
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
83-445 |
2.77e-07 |
|
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: 53.52 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 83 TFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhSVVFGGFAShsvaarIDDAKPVLivsA 162
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-DVVRGSDSS------VEELLYIL---N 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 163 DAGARggkiipykkllddaisqaqhqprhVLLVDRGlakmarvsgrdvdfaslrhqhigarvpvawleSNETSCILYTSG 242
Cdd:cd17640 75 HSESV------------------------ALVVEND--------------------------------SDDLATIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 243 TTGKPKGVQRDVGGYAVALaTSMDTIFGGKAGSVFFCASDIgWvvgHSY---IVYAPLLAGMAtIVYEGLPTWPD----- 314
Cdd:cd17640 99 TTGNPKGVMLTHANLLHQI-RSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGCS-QAYTSIRTLKDdlkrv 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 315 --------CGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSslevlylAGEPLdEPTASWVSNTLDVPVIDNY 386
Cdd:cd17640 173 kphyivsvPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIFKFGIS-------GGGAL-PPHVDTFFEAIGIEVLNGY 244
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128320 387 WQTESGwPIMAIARglDDRPTRlGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGP 445
Cdd:cd17640 245 GLTETS-PVVSARR--LKCNVR-GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
66-566 |
2.39e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 50.59 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALI-AVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFAS 144
Cdd:cd17647 2 PERTCVVeTPSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 145 HSVAARIDDAKP-VLIVSADAGArggkiipykkllddaisqaqhqprhvllvdrglakmarVSGRDvdfaslrhqhigar 223
Cdd:cd17647 82 ARQNIYLGVAKPrGLIVIRAAGV--------------------------------------VVGPD-------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 224 vpvawleSNETscILYTSGTTGKPKGVQrdvgGYAVALA---TSMDTIFGGKAGSVFFCASDIgwvvGHSYI---VYAPL 297
Cdd:cd17647 110 -------SNPT--LSFTSGSEGIPKGVL----GRHFSLAyyfPWMAKRFNLSENDKFTMLSGI----AHDPIqrdMFTPL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 298 LAGMATIVyeglPTWPDCGV------WwtiVEKYQVSRMFSAPTAIRVLKKFPTAEIrkhdlSSLEVLYLAGEPLDEPTA 371
Cdd:cd17647 173 FLGAQLLV----PTQDDIGTpgrlaeW---MAKYGATVTHLTPAMGQLLTAQATTPF-----PKLHHAFFVGDILTKRDC 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 372 SWVSNTLDVPVIDNYW---QTESGWPIMAIARGLDDrPTRLGS-PGVPMYG---YNVQLL----NEVTgEPCGVNEKGML 440
Cdd:cd17647 241 LRLQTLAENVRIVNMYgttETQRAVSYFEVPSRSSD-PTFLKNlKDVMPAGrgmLNVQLLvvnrNDRT-QICGIGEVGEI 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 441 VVE-GPLPPG-----------CIQTIWGDDGRFV----------KTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVI 498
Cdd:cd17647 319 YVRaGGLAEGyrglpelnkekFVNNWFVEPDHWNyldkdnnepwRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQV 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128320 499 NVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPK------ESDSLEDRDVAHSQEKAIMALV 566
Cdd:cd17647 399 KIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddESFAQEDVPKEVSTDPIVKGLI 472
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
240-442 |
2.77e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 240 TSGTTGKPKGV---QRDVGGYAVALATSMdTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIvyeglPTWP-DC 315
Cdd:COG1541 91 SSGTTGKPTVVgytRKDLDRWAELFARSL-RAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVI-----PAGGgNT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 316 GVWWTIVEKYQVSRMFSAPT-AIRVLKKFPTAEIRKHDLSsLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGwP 394
Cdd:COG1541 165 ERQLRLMQDFGPTVLVGTPSyLLYLAEVAEEEGIDPRDLS-LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVG-P 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 395 IMAI---AR-GL----DDRptrlgspgvpmYgynVQLLNEVTGEPCGVNEKGMLVV 442
Cdd:COG1541 243 GVAYeceAQdGLhiweDHF-----------L---VEIIDPETGEPVPEGEEGELVV 284
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
79-250 |
2.87e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 50.17 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLR-SLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKP- 156
Cdd:PRK05620 34 AEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 157 VLIVSADAGARGGKIIPYKKLL--------DDAISQAQHQPRHVLLVDRglakMARVSGRDVDFAslrhqhigarvpvaW 228
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECPCVravvfigpSDADSAAAHMPEGIKVYSY----EALLDGRSTVYD--------------W 175
|
170 180
....*....|....*....|....
gi 16128320 229 LESNETS--CILYTSGTTGKPKGV 250
Cdd:PRK05620 176 PELDETTaaAICYSTGTTGAPKGV 199
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-603 |
3.37e-06 |
|
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: 49.97 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 76 SETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYmpmIAEAHITLLAcarigaIHSVVFGGFashsVAARIddak 155
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQ---FDDNEDFIPA------FWACVLAGF----VPAPL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 156 PVLIVSADAGARGGKIIPYKKLLDdaisqaqhQPrhVLLVD-------RGLAKMARVSGRDVDFASLRHQHIGarvPVAW 228
Cdd:cd05906 95 TVPPTYDEPNARLRKLRHIWQLLG--------SP--VVLTDaelvaefAGLETLSGLPGIRVLSIEELLDTAA---DHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 229 LESNETS--CILYTSGTTGKPKGV-QRDVGGYAVALATSmdTIFGGKAGSVFFcasdiGW-----VVGHSYIVYAPLLAG 300
Cdd:cd05906 162 PQSRPDDlaLLMLTSGSTGFPKAVpLTHRNILARSAGKI--QHNGLTPQDVFL-----NWvpldhVGGLVELHLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 MATI-VYEGL----PTwpdcgVWWTIVEKYQVSRMFSAPTAI----RVLKKFPTaeiRKHDLSSLEVLYLAGEPLDEPTA 371
Cdd:cd05906 235 CQQVhVPTEEiladPL-----RWLDLIDRYRVTITWAPNFAFallnDLLEEIED---GTWDLSSLRYLVNAGEAVVAKTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 372 SWVSNTLD---VP--VIDNYW---QTESGwpiMAIARGL--DDRPT--RLGSPGVPMYGYNVQLLNEvTGEPCGVNEKGM 439
Cdd:cd05906 307 RRLLRLLEpygLPpdAIRPAFgmtETCSG---VIYSRSFptYDHSQalEFVSLGRPIPGVSMRIVDD-EGQLLPEGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 440 LVVEGPL-------PPGCIQTIWGDDGrfvktyWslfsrpvYATFDWGIRDaDGYHFILGRTDDVINVAGHRLGTREIEE 512
Cdd:cd05906 383 LQVRGPVvtkgyynNPEANAEAFTEDG------W-------FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 513 SISSHPGVAE--VAVVGVKDALKG--QVAVAFViPkesdSLEDRDVAHSQEKAIMALVDSQIGnfGRPAHVWFV--SQLP 586
Cdd:cd05906 449 AVEEVPGVEPsfTAAFAVRDPGAEteELAIFFV-P----EYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLpkEEIP 521
|
570
....*....|....*..
gi 16128320 587 KTRSGKMLRRTIQAICE 603
Cdd:cd05906 522 KTSLGKIQRSKLKAAFE 538
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
222-598 |
5.11e-06 |
|
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: 49.36 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 222 ARVPVAWLESNETSCILYTSGTTGKPKGV---QRDVGGYAVAL-----ATSMDTIfgGKAGSVFFCASdigwvvghSYIV 293
Cdd:cd17644 96 AQISVLLTQPENLAYVIYTSGSTGKPKGVmieHQSLVNLSHGLikeygITSSDRV--LQFASIAFDVA--------AEEI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 294 YAPLLAGmATIVYEGLPTWPDCGVWWTIVEKYQVSrMFSAPTA-----IRVLKKfPTAEIrkhdLSSLEVLYLAGEPLDE 368
Cdd:cd17644 166 YVTLLSG-ATLVLRPEEMRSSLEDFVQYIQQWQLT-VLSLPPAywhllVLELLL-STIDL----PSSLRLVIVGGEAVQP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 369 PT-ASWVSNTLDVP-VIDNYWQTESgwPIMA-IARGLDDRPTRLGSP--GVPMYGYNVQLLNEvTGEPCGVNEKGMLVVE 443
Cdd:cd17644 239 ELvRQWQKNVGNFIqLINVYGPTEA--TIAAtVCRLTQLTERNITSVpiGRPIANTQVYILDE-NLQPVPVGVPGELHIG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 G-PLPPGCIQTIWGDDGRFVKT--YWSLFSRpVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGV 520
Cdd:cd17644 316 GvGLARGYLNRPELTAEKFISHpfNSSESER-LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128320 521 AEVAVVGVKDALKGQVAVAFVIPKESDSLedrDVAHSQEKAIMALVDSQIgnfgrPAHVWFVSQLPKTRSGKMLRRTI 598
Cdd:cd17644 395 KTAVVIVREDQPGNKRLVAYIVPHYEESP---STVELRQFLKAKLPDYMI-----PSAFVVLEELPLTPNGKIDRRAL 464
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
85-250 |
5.57e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.14 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 85 TFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIhsvvfggfashsvaariddakpvlIVSAda 164
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIP------------------------IVTV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 165 garggkiipYKKLLDDAISQAQHQPRHVLLVdrglakmarVSGRDVDFAslrhqhigarvpvawlesnetsCILYTSGTT 244
Cdd:cd17639 61 ---------YATLGEDALIHSLNETECSAIF---------TDGKPDDLA----------------------CIMYTSGST 100
|
....*.
gi 16128320 245 GKPKGV 250
Cdd:cd17639 101 GNPKGV 106
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
84-595 |
1.11e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 48.55 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 84 FTFRQLHDEVNAVASMLRSLGVQRGDRVlvympmiaeahITLlacARIGAIH-SVVFG----GFASHSVAARIDDAKPVL 158
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRV-----------GTL---AWNGYRHlEAYYGvsgsGAVCHTINPRLFPEQIAY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 159 IVSADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRglAKMARVSGRDVDFASLRHQHIGArvpVAW--LESNETSC 236
Cdd:PRK07008 106 IVNHAEDRYVLFDLTFLPLVDALAPQCPNVKGWVAMTDA--AHLPAGSTPLLCYETLVGAQDGD---YDWprFDENQASS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 237 ILYTSGTTGKPKGV---QRD--VGGYAVALATSM-----DTI------FGGKAGSVFFCASdigwVVGHSYIVYAPLLAG 300
Cdd:PRK07008 181 LCYTSGTTGNPKGAlysHRStvLHAYGAALPDAMglsarDAVlpvvpmFHVNAWGLPYSAP----LTGAKLVLPGPDLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 301 MAtiVYEglptwpdcgvwwtIVEKYQVSrmFSA--PTA-IRVLKKFPTAEIRkhdLSSLEVLYLAGEPLDEPTASWVSNT 377
Cdd:PRK07008 257 KS--LYE-------------LIEAERVT--FSAgvPTVwLGLLNHMREAGLR---FSTLRRTVIGGSACPPAMIRTFEDE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 378 LDVPVIDNYWQTESGwPIMAI--------ARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGE-PCGVNEKGMLVVEGPlpp 448
Cdd:PRK07008 317 YGVEVIHAWGMTEMS-PLGTLcklkwkhsQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRElPWDGKAFGDLQVRGP--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 449 gciqtiWGDDGRFvKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGV 528
Cdd:PRK07008 393 ------WVIDRYF-RGDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIAC 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 529 KDALKGQVAVAFVIPKESdsledrdvAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLR 595
Cdd:PRK07008 466 AHPKWDERPLLVVVKRPG--------AEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQK 524
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
478-605 |
1.56e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.85 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 478 DWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVipKESdsledrdvAHS 557
Cdd:PRK07638 367 DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGS--------ATK 436
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 16128320 558 QEkaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGR 605
Cdd:PRK07638 437 QQ--LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
474-600 |
1.76e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.92 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 474 YATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKE-SDSLEDR 552
Cdd:PLN02479 432 FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPgVDKSDEA 511
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 16128320 553 DVAHSqekaIMALVDSQIGNFGRPAHVWFvSQLPKTRSGKMLRRTIQA 600
Cdd:PLN02479 512 ALAED----IMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
53-599 |
4.99e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 46.28 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 53 LCHNAIDRWLEKQPEAlALIAVSSETEEERTfTFRQLHDEVNAVASMLRSLGVQRGDRVLVyMPMIAEAHI-TLLACARI 131
Cdd:PRK06018 11 LCHRIIDHAARIHGNR-EVVTRSVEGPIVRT-TYAQIHDRALKVSQALDRDGIKLGDRVAT-IAWNTWRHLeAWYGIMGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 132 GAIhsvvfggfaSHSVAARIDDAKPVLIVSAdagaRGGKII----PYKKLLDDAISQAQHQPRHVLLVDRglAKMARVSG 207
Cdd:PRK06018 88 GAI---------CHTVNPRLFPEQIAWIINH----AEDRVVitdlTFVPILEKIADKLPSVERYVVLTDA--AHMPQTTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 208 RD-VDFASLRHQHIGArvpVAWLESNE-TSCIL-YTSGTTGKPKGV---------------QRDVGGyavalATSMDTI- 268
Cdd:PRK06018 153 KNaVAYEEWIAEADGD---FAWKTFDEnTAAGMcYTSGTTGDPKGVlyshrsnvlhalmanNGDALG-----TSAADTMl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 269 -----FGGKAGSVFFCASdigwVVGHSYIVYAPLLAGMAtiVYEGLPTwpdcgvwwtivEKyqVSRMFSAPTAIRVLKKF 343
Cdd:PRK06018 225 pvvplFHANSWGIAFSAP----SMGTKLVMPGAKLDGAS--VYELLDT-----------EK--VTFTAGVPTVWLMLLQY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 344 PTAEIRKhdLSSLEVLYLAGEPLDEPTASWVSNtLDVPVIDNYWQTESGwPIMAIAR--------GLDDRPTRLGSPGVP 415
Cdd:PRK06018 286 MEKEGLK--LPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMS-PLGTLAAlkppfsklPGDARLDVLQKQGYP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 416 MYGYNVQLLNEVTGE-PCGVNEKGMLVVEGPLPPGCI----QTIWGDDGRFvktywslfsrpvyATFDWGIRDADGYHFI 490
Cdd:PRK06018 362 PFGVEMKITDDAGKElPWDGKTFGRLKVRGPAVAAAYyrvdGEILDDDGFF-------------DTGDVATIDAYGYMRI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 491 LGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDvahsqekaIMALVDSQI 570
Cdd:PRK06018 429 TDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREE--------ILKYMDGKI 500
|
570 580
....*....|....*....|....*....
gi 16128320 571 GNFGRPAHVWFVSQLPKTRSGKMLRRTIQ 599
Cdd:PRK06018 501 AKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-134 |
7.92e-05 |
|
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: 45.42 E-value: 7.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 16128320 81 ERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV 54
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
66-600 |
1.80e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 66 PEALALiavsseTEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASH 145
Cdd:PRK05691 2202 PQAPAL------TFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 146 SVAARIDDAKPVLIVSadagarggkiipYKKLLDDAISQAQHQPRHVLLVDrgLAKMARVSGRDVDFASL-RHQhigarv 224
Cdd:PRK05691 2276 RLHYMIEDSGIGLLLS------------DRALFEALGELPAGVARWCLEDD--AAALAAYSDAPLPFLSLpQHQ------ 2335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 225 pvAWLesnetsciLYTSGTTGKPKGVQRDVGGYAVALATSMDTiFGGKAG-------SVFFCASdigwvvghSYIVYAPL 297
Cdd:PRK05691 2336 --AYL--------IYTSGSTGKPKGVVVSHGEIAMHCQAVIER-FGMRADdcelhfySINFDAA--------SERLLVPL 2396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 298 LAGmATIVYEGLPTWpDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkHDLSSLEVLYLAGEPLDEPTASWVSNT 377
Cdd:PRK05691 2397 LCG-ARVVLRAQGQW-GAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQ---GEQLPVRMCITGGEALTGEHLQRIRQA 2471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 378 LDVPVIDN-YWQTESgwPIMAIARGLDDRpTRLGSPGVPM---YGYNVQLLNEVTGEPCGVNEKGMLVVEGPlppGCIQT 453
Cdd:PRK05691 2472 FAPQLFFNaYGPTET--VVMPLACLAPEQ-LEEGAASVPIgrvVGARVAYILDADLALVPQGATGELYVGGA---GLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 454 IWGDDG----RFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVk 529
Cdd:PRK05691 2546 YHDRPGltaeRFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL- 2624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128320 530 DALKGQVAVAFVIpkeSDSLEDRDVAHSQ-EKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQA 600
Cdd:PRK05691 2625 DTPSGKQLAGYLV---SAVAGQDDEAQAAlREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
79-250 |
2.52e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.20 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 79 EEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFG---------GFASHSVAA 149
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYAnlgedalayALRETECKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 150 RIDDAK--PVLIVSADAGARGGKIIPYKKLLDDAISQAQHQprhvllvdrglakmaRVSGRDV-DFASLRHQHIGARVPv 226
Cdd:PTZ00216 197 IVCNGKnvPNLLRLMKSGGMPNTTIIYLDSLPASVDTEGCR---------------LVAWTDVvAKGHSAGSHHPLNIP- 260
|
170 180
....*....|....*....|....
gi 16128320 227 awLESNETSCILYTSGTTGKPKGV 250
Cdd:PTZ00216 261 --ENNDDLALIMYTSGTTGDPKGV 282
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
59-250 |
3.34e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 43.71 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 59 DRWLEKQPEALALiAVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYM-PMIAEAhitLLACArigAIH-- 135
Cdd:PRK08180 46 VHWAQEAPDRVFL-AERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSgNSIEHA---LLALA---AMYag 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 136 ----------SVVFGGFAS-HSVAARIddaKPVLIVSADAGarggkiiPYKKLLDDAIsqaqhqPRHVLLVdrgLAKMAR 204
Cdd:PRK08180 119 vpyapvspaySLVSQDFGKlRHVLELL---TPGLVFADDGA-------AFARALAAVV------PADVEVV---AVRGAV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128320 205 VSGRDVDFASLRHQHIGARVPVAWLESNETSC--ILYTSGTTGKPKGV 250
Cdd:PRK08180 180 PGRAATPFAALLATPPTAAVDAAHAAVGPDTIakFLFTSGSTGLPKAV 227
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
61-133 |
3.35e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 43.32 E-value: 3.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 61 WLEKQPEALALIAVsseteeERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVympmIAEAHITL----LACARIGA 133
Cdd:PRK09029 12 WAQVRPQAIALRLN------DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVAL----RGKNSPETllayLALLQCGA 78
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
484-595 |
8.69e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 42.30 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 484 ADGYHFILGRTDDVINVAGHRLGTREIEESISSHPgvaevavvgvkdALKGQVAVAFVIPKESD------------SLED 551
Cdd:PRK09192 450 LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEP------------ELRSGDAAAFSIAQENGekivllvqcrisDEER 517
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 16128320 552 RDVAHSQekaIMALVDSQignFGRPAHVWFVS--QLPKTRSGKMLR 595
Cdd:PRK09192 518 RGQLIHA---LAALVRSE---FGVEAAVELVPphSLPRTSSGKLSR 557
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
80-248 |
3.12e-03 |
|
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: 40.35 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 80 EERTFTFRQLHDEVNAVASMLRS-LGVQRGDRVLVYMPMIAEAHITLLACARIGAihSVVFGGFAS------HSVaaRID 152
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGC--PVAFLNTNIrsksllHCF--RCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 153 DAKpVLIVSADAGARGGKIIPykKLLDDAIsqaqhqprHVLLVDRG---------LAKMARVSGRDVDfASLRhqhigar 223
Cdd:cd05938 78 GAK-VLVVAPELQEAVEEVLP--ALRADGV--------SVWYLSHTsntegvislLDKVDAASDEPVP-ASLR------- 138
|
170 180
....*....|....*....|....*
gi 16128320 224 VPVAWlesNETSCILYTSGTTGKPK 248
Cdd:cd05938 139 AHVTI---KSPALYIYTSGTTGLPK 160
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
80-134 |
4.11e-03 |
|
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: 40.11 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128320 80 EERTFTFRQLHDEVNAVASMLRS-LGVQRGDRVLVYMPMIAEAHITLLACARIGAI 134
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA 57
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-596 |
6.91e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.77 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 47 CEGRTNLCHNAIDRWLEKQPEALALIAvsseteEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLL 126
Cdd:PRK05691 1126 CAPAQAWLPELLNEQARQTPERIALVW------DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLL 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 127 ACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAgarggkiipykkLLDDaisqaqhqprhvllvdrgLAKMARVS 206
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSH------------LLER------------------LPQAEGVS 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 207 GrdVDFASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTiFGGKAGSVFFCASDIGWV 286
Cdd:PRK05691 1250 A--IALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQAT-YALDDSDVLMQKAPISFD 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 287 VGhSYIVYAPLLAGmATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEirkhDLSSLEVLYLAGEPL 366
Cdd:PRK05691 1327 VS-VWECFWPLITG-CRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA----ACTSLRRLFSGGEAL 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 367 DEPTASWVSNTL-DVPVIDNYWQTESGWPIMAIARGLDDRptrLGSP-GVPMYGYNVQLLN-EVTGEPCGVneKGMLVVE 443
Cdd:PRK05691 1401 PAELRNRVLQRLpQVQLHNRYGPTETAINVTHWQCQAEDG---ERSPiGRPLGNVLCRVLDaELNLLPPGV--AGELCIG 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 444 GPlppGCIQTIWGDDG----RFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPG 519
Cdd:PRK05691 1476 GA---GLARGYLGRPAltaeRFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128320 520 VAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRdvahsqekaIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRR 596
Cdd:PRK05691 1553 VAQAAVLVREGAAGAQLVGYYTGEAGQEAEAER---------LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
349-591 |
7.26e-03 |
|
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: 38.82 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 349 RKHDLSSLEVLylAGEPLDEPTASwVSNTLDVPVIDNYWQTESGWPIMAIARGLDDrptrLGSPGVPMYGYNVQLLNEvT 428
Cdd:cd17636 109 GLYDLSSLRSS--PAAPEWNDMAT-VDTSPWGRKPGGYGQTEVMGLATFAALGGGA----IGGAGRPSPLVQVRILDE-D 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 429 GEPCGVNEKGMLVVEGP-LPPGciqtIWGDDG----RFVKTYWSlfsrpvyaTFDWGIRDADGYHFILGRTDDVINVAGH 503
Cdd:cd17636 181 GREVPDGEVGEIVARGPtVMAG----YWNRPEvnarRTRGGWHH--------TNDLGRREPDGSLSFVGPKTRMIKSGAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128320 504 RLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEdrdvahsqEKAIMALVDSQIGNFGRPAHVWFVS 583
Cdd:cd17636 249 NIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVT--------EAELIEHCRARIASYKKPKSVEFAD 320
|
....*...
gi 16128320 584 QLPKTRSG 591
Cdd:cd17636 321 ALPRTAGG 328
|
|
| |
